scientificName: Drosophila melanogaster

value: Menage a trois, isoform A

source: FlyBase

value: metro

value: met

value: Metro

value: Belongs to the MAGUK family

description: PDZ

description: Guanylate kinase-like

description: Disordered

description: Basic and acidic residues

authors:
Adams M.D.
Celniker S.E.
Holt R.A.
Evans C.A.
Gocayne J.D.
Amanatides P.G.
Scherer S.E.
Li P.W.
Hoskins R.A.
Galle R.F.
George R.A.
Lewis S.E.
Richards S.
Ashburner M.
Henderson S.N.
Sutton G.G.
Wortman J.R.
Yandell M.D.
Zhang Q.
Chen L.X.
Brandon R.C.
Rogers Y.H.
Blazej R.G.
Champe M.
Pfeiffer B.D.
Wan K.H.
Doyle C.
Baxter E.G.
Helt G.
Nelson C.R.
Gabor G.L.
Abril J.F.
Agbayani A.
An H.J.
Andrews-Pfannkoch C.
Baldwin D.
Ballew R.M.
Basu A.
Baxendale J.
Bayraktaroglu L.
Beasley E.M.
Beeson K.Y.
Benos P.V.
Berman B.P.
Bhandari D.
Bolshakov S.
Borkova D.
Botchan M.R.
Bouck J.
Brokstein P.
Brottier P.
Burtis K.C.
Busam D.A.
Butler H.
Cadieu E.
Center A.
Chandra I.
Cherry J.M.
Cawley S.
Dahlke C.
Davenport L.B.
Davies P.
de Pablos B.
Delcher A.
Deng Z.
Mays A.D.
Dew I.
Dietz S.M.
Dodson K.
Doup L.E.
Downes M.
Dugan-Rocha S.
Dunkov B.C.
Dunn P.
Durbin K.J.
Evangelista C.C.
Ferraz C.
Ferriera S.
Fleischmann W.
Fosler C.
Gabrielian A.E.
Garg N.S.
Gelbart W.M.
Glasser K.
Glodek A.
Gong F.
Gorrell J.H.
Gu Z.
Guan P.
Harris M.
Harris N.L.
Harvey D.
Heiman T.J.
Hernandez J.R.
Houck J.
Hostin D.
Houston K.A.
Howland T.J.
Wei M.H.
Ibegwam C.
Jalali M.
Kalush F.
Karpen G.H.
Ke Z.
Kennison J.A.
Ketchum K.A.
Kimmel B.E.
Kodira C.D.
Kraft C.
Kravitz S.
Kulp D.
Lai Z.
Lasko P.
Lei Y.
Levitsky A.A.
Li J.
Li Z.
Liang Y.
Lin X.
Liu X.
Mattei B.
McIntosh T.C.
McLeod M.P.
McPherson D.
Merkulov G.
Milshina N.V.
Mobarry C.
Morris J.
Moshrefi A.
Mount S.M.
Moy M.
Murphy B.
Murphy L.
Muzny D.M.
Nelson D.L.
Nelson D.R.
Nelson K.A.
Nixon K.
Nusskern D.R.
Pacleb J.M.
Palazzolo M.
Pittman G.S.
Pan S.
Pollard J.
Puri V.
Reese M.G.
Reinert K.
Remington K.
Saunders R.D.
Scheeler F.
Shen H.
Shue B.C.
Siden-Kiamos I.
Simpson M.
Skupski M.P.
Smith T.
Spier E.
Spradling A.C.
Stapleton M.
Strong R.
Sun E.
Svirskas R.
Tector C.
Turner R.
Venter E.
Wang A.H.
Wang X.
Wang Z.Y.
Wassarman D.A.
Weinstock G.M.
Weissenbach J.
Williams S.M.
WoodageT
Worley K.C.
Wu D.
Yang S.
Yao Q.A.
Ye J.
Yeh R.F.
Zaveri J.S.
Zhan M.
Zhang G.
Zhao Q.
Zheng L.
Zheng X.H.
Zhong F.N.
Zhong W.
Zhou X.
Zhu S.
Zhu X.
Smith H.O.
Gibbs R.A.
Myers E.W.
Rubin G.M.
Venter J.C.

database: PubMed

title: The genome sequence of Drosophila melanogaster.

value: Berkeley

authors:
Celniker S.E.
Wheeler D.A.
Kronmiller B.
Carlson J.W.
Halpern A.
Patel S.
Adams M.
Champe M.
Dugan S.P.
Frise E.
Hodgson A.
George R.A.
Hoskins R.A.
Laverty T.
Muzny D.M.
Nelson C.R.
Pacleb J.M.
Park S.
Pfeiffer B.D.
Richards S.
Sodergren E.J.
Svirskas R.
Tabor P.E.
Wan K.
Stapleton M.
Sutton G.G.
Venter C.
Weinstock G.
Scherer S.E.
Myers E.W.
Gibbs R.A.
Rubin G.M.

title: Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence.

authors:
Misra S.
Crosby M.A.
Mungall C.J.
Matthews B.B.
Campbell K.S.
Hradecky P.
Huang Y.
Kaminker J.S.
Millburn G.H.
Prochnik S.E.
Smith C.D.
Tupy J.L.
Whitfied E.J.
Bayraktaroglu L.
Berman B.P.
Bettencourt B.R.
Celniker S.E.
de Grey A.D.
Drysdale R.A.
Harris N.L.
Richter J.
Russo S.
Schroeder A.J.
Shu S.Q.
Stapleton M.
Yamada C.
Ashburner M.
Gelbart W.M.
Rubin G.M.
Lewis S.E.

title: Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.

authors:
Kaminker J.S.
Bergman C.M.
Kronmiller B.
Carlson J.
Svirskas R.
Patel S.
Frise E.
Wheeler D.A.
Lewis S.E.
Rubin G.M.
Ashburner M.
Celniker S.E.

title: The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective.

authors:
Hoskins R.A.
Smith C.D.
Carlson J.W.
Carvalho A.B.
Halpern A.
Kaminker J.S.
Kennedy C.
Mungall C.J.
Sullivan B.A.
Sutton G.G.
Yasuhara J.C.
Wakimoto B.T.
Myers E.W.
Celniker S.E.
Rubin G.M.
Karpen G.H.

title: Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.

authors:
Quesneville H.
Bergman C.M.
Andrieu O.
Autard D.
Nouaud D.
Ashburner M.
Anxolabehere D.

title: Combined evidence annotation of transposable elements in genome sequences.

authors:
Smith C.D.
Shu S.
Mungall C.J.
Karpen G.H.

title: The Release 5.1 annotation of Drosophila melanogaster heterochromatin.

authors:
Hoskins R.A.
Carlson J.W.
Kennedy C.
Acevedo D.
Evans-Holm M.
Frise E.
Wan K.H.
Park S.
Mendez-Lago M.
Rossi F.
Villasante A.
Dimitri P.
Karpen G.H.
Celniker S.E.

title: Sequence finishing and mapping of Drosophila melanogaster heterochromatin.

authors:
Matthews B.B.
Dos Santos G.
Crosby M.A.
Emmert D.B.
St Pierre S.E.
Gramates L.S.
Zhou P.
Schroeder A.J.
Falls K.
Strelets V.
Russo S.M.
Gelbart W.M.

title: Gene Model Annotations for Drosophila melanogaster: Impact of High-Throughput Data.

authors:
Crosby M.A.
Gramates L.S.
Dos Santos G.
Matthews B.B.
St Pierre S.E.
Zhou P.
Schroeder A.J.
Falls K.
Emmert D.B.
Russo S.M.
Gelbart W.M.

title: Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.

authors:
Hoskins R.A.
Carlson J.W.
Wan K.H.
Park S.
Mendez I.
Galle S.E.
Booth B.W.
Pfeiffer B.D.
George R.A.
Svirskas R.
Krzywinski M.
Schein J.
Accardo M.C.
Damia E.
Messina G.
Mendez-Lago M.
de Pablos B.
Demakova O.V.
Andreyeva E.N.
Boldyreva L.V.
Marra M.
Carvalho A.B.
Dimitri P.
Villasante A.
Zhimulev I.F.
Rubin G.M.
Karpen G.H.
Celniker S.E.

title: The Release 6 reference sequence of the Drosophila melanogaster genome.

value: Expressed in cyst progenitor cell (Drosophila) in testis and 137 other cell types or tissues

value: P:regulation of synaptic assembly at neuromuscular junction

value: P-loop containing nucleotide triphosphate hydrolases

value: MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK

value: P-loop containing nucleoside triphosphate hydrolases


entryType: UniProtKB unreviewed (TrEMBL)

scientificName: Trichomonas vaginalis (strain ATCC PRA-98 / G3)

source: EMBL

source: Proteomes

lineage: Eukaryota Metamonada Parabasalia Trichomonadida Trichomonadidae Trichomonas

proteinExistence: 4: Predicted

source: PROSITE

value: KilA-N domain-containing protein

type: Domain

modifier: EXACT

description: KilA-N

Reference proteome

category: Technical term

citationType: submission

authors:
Amadeo P.
Zhao Q.
Wortman J.
Fraser-Liggett C.
Carlton J.

submissionDatabase: EMBL/GenBank/DDBJ databases

type: STRAIN

citationType: journal article

authors:
Carlton J.M.
Hirt R.P.
Silva J.C.
Delcher A.L.
Schatz M.
Zhao Q.
Wortman J.R.
Bidwell S.L.
Alsmark U.C.M.
Besteiro S.
Sicheritz-Ponten T.
Noel C.J.
Dacks J.B.
Foster P.G.
Simillion C.
Van de Peer Y.
Miranda-Saavedra D.
Barton G.J.
Westrop G.D.
Mueller S.
Dessi D.
Fiori P.L.
Ren Q.
Paulsen I.
Zhang H.
Bastida-Corcuera F.D.
Simoes-Barbosa A.
Brown M.T.
Hayes R.D.
Mukherjee M.
Okumura C.Y.
Schneider R.
Smith A.J.
Vanacova S.
Villalvazo M.
Haas B.J.
Pertea M.
Feldblyum T.V.
Utterback T.R.
Shu C.L.
Osoegawa K.
de Jong P.J.
Hrdy I.
Horvathova L.
Zubacova Z.
Dolezal P.
Malik S.B.
Logsdon J.M. Jr.
Henze K.
Gupta A.
Wang C.C.
Dunne R.L.
Upcroft J.A.
Upcroft P.
White O.
Salzberg S.L.
Tang P.
Chiu C.-H.
Lee Y.-S.
Embley T.M.
Coombs G.H.
Mottram J.C.
Tachezy J.
Fraser-Liggett C.M.
Johnson P.J.

database: DOI

title: Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis.

journal: Science

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

value: ATCC PRA-98 / G3

database: EMBL

key: ProteinId

key: Status

key: MoleculeType

database: AlphaFoldDB

key: Description

database: VEuPathDB

database: Proteomes

key: Component

value: Unassembled WGS sequence

database: InterPro

key: EntryName

database: Pfam

value: KilA-N

key: MatchStatus

database: SMART

database: PROSITE


commonName: Fruit fly

lineage: Eukaryota Metazoa Ecdysozoa Arthropoda Altocrustacea Allotriocarida Hexapoda Insecta Pterygota Neoptera Eumetabola Endopterygota Aparaglossata Panorpida Diptera Brachycera Muscomorpha Ephydroidea Drosophilidae Drosophila Sophophora

proteinExistence: 3: Inferred from homology

source: PIRNR

value: Phospholipase

value: Pld

value: dPLD

value: dPld

value: MitoPLD

value: PC-Pld

value: phospholipase D

value: PLD

value: pld

commentType: CATALYTIC ACTIVITY

name: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+)

database: Rhea

database: ChEBI

source: ARBA

commentType: SUBCELLULAR LOCATION

value: Endomembrane system

value: Lipid-anchor

value: Belongs to the phospholipase D family

commentType: SIMILARITY

description: PX

description: PLD phosphodiesterase

description: PLD phosphodiesterase

type: Region

description: Disordered

source: SAM

description: Disordered

description: Disordered

type: Compositional bias

description: Acidic residues

description: Low complexity

description: Basic and acidic residues

type: Active site

source: PROSITE-ProRule

value: Expressed in enterocyte of anterior adult midgut epithelium in digestive tract and 129 other cell types or tissues

value: P:gastrulation involving germ band extension

value: P:phosphatidic acid biosynthetic process

value: P:positive regulation of Golgi vesicle fusion to target membrane

value: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)


scientificName: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

lineage: Eukaryota Fungi Dikarya Ascomycota Pezizomycotina Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Neurospora

value: DUF890 domain-containing protein

description: Disordered

description: Disordered

description: Basic and acidic residues

description: Polar residues

Methyltransferase

category: Molecular function

authors:
Galagan J.E.
Calvo S.E.
Borkovich K.A.
Selker E.U.
Read N.D.
Jaffe D.
FitzHugh W.
Ma L.J.
Smirnov S.
Purcell S.
Rehman B.
Elkins T.
Engels R.
Wang S.
Nielsen C.B.
Butler J.
Endrizzi M.
Qui D.
Ianakiev P.
Bell-Pedersen D.
Nelson M.A.
Werner-Washburne M.
Selitrennikoff C.P.
Kinsey J.A.
Braun E.L.
Zelter A.
Schulte U.
Kothe G.O.
Jedd G.
Mewes W.
Staben C.
Marcotte E.
Greenberg D.
Roy A.
Foley K.
Naylor J.
Stange-Thomann N.
Barrett R.
Gnerre S.
Kamal M.
Kamvysselis M.
Mauceli E.
Bielke C.
Rudd S.
Frishman D.
Krystofova S.
Rasmussen C.
Metzenberg R.L.
Perkins D.D.
Kroken S.
Cogoni C.
Macino G.
Catcheside D.
Li W.
Pratt R.J.
Osmani S.A.
DeSouza C.P.
Glass L.
Orbach M.J.
Berglund J.A.
Voelker R.
Yarden O.
Plamann M.
Seiler S.
Dunlap J.
Radford A.
Aramayo R.
Natvig D.O.
Alex L.A.
Mannhaupt G.
Ebbole D.J.
Freitag M.
Paulsen I.
Sachs M.S.
Lander E.S.
Nusbaum C.
Birren B.

title: The genome sequence of the filamentous fungus Neurospora crassa.

journal: Nature

database: RefSeq

key: NucleotideSequenceId

database: SMR

database: STRING

database: PaxDb

database: GeneID

database: KEGG

database: HOGENOM

database: InParanoid

database: OMA

key: Fingerprint

database: OrthoDB

value: Chromosome 4, Linkage Group IV

database: GO

key: GoTerm

value: F:23S rRNA (adenine(1618)-N(6))-methyltransferase activity

key: GoEvidenceType

value: P:rRNA base methylation

database: CDD

database: FunFam

value: DUF890 domain protein (AFU_orthologue AFUA_7G05590)

value: Vaccinia Virus protein VP39

database: PANTHER

value: SAM-DEPENDENT METHYLTRANSFERASE

database: SUPFAM


proteinExistence: 1: Evidence at protein level

value: GFAT

value: Gfat

value: gfat

value: zep

value: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1

commentType: PATHWAY

description: SIS

description: SIS

Carbohydrate metabolism

category: Biological process

Phosphoprotein

category: PTM

Proteomics identification

source: PeptideAtlas

Repeat

category: Domain

database: PubMed

database: DOI

value: Berkeley

journal: Genome Biol.

journal: PLoS Comput. Biol.

value: F:L-glutamine:D-fructose-6-phosphate transaminase (isomerizing) activity

value: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

value: Glucose-6-phosphate isomerase like protein, domain 1

value: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

value: N-terminal nucleophile aminohydrolases (Ntn hydrolases)


scientificName: Rattus norvegicus

commonName: Rat

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Rattus

proteinExistence: 2: Evidence at transcript level

value: Pnkd protein

source: RGD

value: Pnkd

commentType: COFACTOR

database: ChEBI

value: Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family

description: Metallo-beta-lactamase

source: SMART

description: Disordered

description: Disordered

description: Polar residues

Metal-binding

category: Ligand

authors:
Gerhard D.S.
Wagner L.
Feingold E.A.
Shenmen C.M.
Grouse L.H.
Schuler G.
Klein S.L.
Old S.
Rasooly R.
Good P.
Guyer M.
Peck A.M.
Derge J.G.
Lipman D.
Collins F.S.
Jang W.
Sherry S.
Feolo M.
Misquitta L.
Lee E.
Rotmistrovsky K.
Greenhut S.F.
Schaefer C.F.
Buetow K.
Bonner T.I.
Haussler D.
Kent J.
Kiekhaus M.
Furey T.
Brent M.
Prange C.
Schreiber K.
Shapiro N.
Bhat N.K.
Hopkins R.F.
Hsie F.
Driscoll T.
Soares M.B.
Casavant T.L.
Scheetz T.E.
Brown-stein M.J.
Usdin T.B.
Toshiyuki S.
Carninci P.
Piao Y.
Dudekula D.B.
Ko M.S.
Kawakami K.
Suzuki Y.
Sugano S.
Gruber C.E.
Smith M.R.
Simmons B.
Moore T.
Waterman R.
Johnson S.L.
Ruan Y.
Wei C.L.
Mathavan S.
Gunaratne P.H.
Wu J.
Garcia A.M.
Hulyk S.W.
Fuh E.
Yuan Y.
Sneed A.
Kowis C.
Hodgson A.
Muzny D.M.
McPherson J.
Gibbs R.A.
Fahey J.
Helton E.
Ketteman M.
Madan A.
Rodrigues S.
Sanchez A.
Whiting M.
Madari A.
Young A.C.
Wetherby K.D.
Granite S.J.
Kwong P.N.
Brinkley C.P.
Pearson R.L.
Bouffard G.G.
Blakesly R.W.
Green E.D.
Dickson M.C.
Rodriguez A.C.
Grimwood J.
Schmutz J.
Myers R.M.
Butterfield Y.S.
Griffith M.
Griffith O.L.
Krzywinski M.I.
Liao N.
Morin R.
Morrin R.
Palmquist D.
Petrescu A.S.
Skalska U.
Smailus D.E.
Stott J.M.
Schnerch A.
Schein J.E.
Jones S.J.
Holt R.A.
Baross A.
Marra M.A.
Clifton S.
Makowski K.A.
Bosak S.
Malek J.

title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

journal: Genome Res.

value: Spleen

type: TISSUE

database: EMBL

value: mRNA

database: RefSeq

database: AlphaFoldDB

database: AGR

database: CTD

database: RGD

key: GeneName

database: GeneTree

database: Bgee

key: ExpressionPatterns

value: Expressed in heart and 19 other cell types or tissues

value: P:methylglyoxal catabolic process

database: InterPro

value: Metallo-B-lactamas


scientificName: Drosophila virilis

lineage: Eukaryota Metazoa Ecdysozoa Arthropoda Altocrustacea Allotriocarida Hexapoda Insecta Pterygota Neoptera Eumetabola Endopterygota Aparaglossata Panorpida Diptera Brachycera Muscomorpha Ephydroidea Drosophilidae Drosophila

value: Uncharacterized protein, isoform A

value: Uncharacterized protein, isoform B

value: Belongs to the exportin family

description: Importin N-terminal

source: Pfam

description: Exportin-5 C-terminal

description: Disordered

description: Polar residues

authors:
Clark A.G.
Eisen M.B.
Smith D.R.
Bergman C.M.
Oliver B.
Markow T.A.
Kaufman T.C.
Kellis M.
Gelbart W.
Iyer V.N.
Pollard D.A.
Sackton T.B.
Larracuente A.M.
Singh N.D.
Abad J.P.
Abt D.N.
Adryan B.
Aguade M.
Akashi H.
Anderson W.W.
Aquadro C.F.
Ardell D.H.
Arguello R.
Artieri C.G.
Barbash D.A.
Barker D.
Barsanti P.
Batterham P.
Batzoglou S.
Begun D.
Bhutkar A.
Blanco E.
Bosak S.A.
Bradley R.K.
Brand A.D.
Brent M.R.
Brooks A.N.
Brown R.H.
Butlin R.K.
Caggese C.
Calvi B.R.
Bernardo de Carvalho A.
Caspi A.
Castrezana S.
Celniker S.E.
Chang J.L.
Chapple C.
Chatterji S.
Chinwalla A.
Civetta A.
Clifton S.W.
Comeron J.M.
Costello J.C.
Coyne J.A.
Daub J.
David R.G.
Delcher A.L.
Delehaunty K.
Do C.B.
Ebling H.
Edwards K.
Eickbush T.
Evans J.D.
Filipski A.
Findeiss S.
Freyhult E.
Fulton L.
Fulton R.
Garcia A.C.
Gardiner A.
Garfield D.A.
Garvin B.E.
Gibson G.
Gilbert D.
Gnerre S.
Godfrey J.
Good R.
Gotea V.
Gravely B.
Greenberg A.J.
Griffiths-Jones S.
Gross S.
Guigo R.
Gustafson E.A.
Haerty W.
Hahn M.W.
Halligan D.L.
Halpern A.L.
Halter G.M.
Han M.V.
Heger A.
Hillier L.
Hinrichs A.S.
Holmes I.
Hoskins R.A.
Hubisz M.J.
Hultmark D.
Huntley M.A.
Jaffe D.B.
Jagadeeshan S.
Jeck W.R.
Johnson J.
Jones C.D.
Jordan W.C.
Karpen G.H.
Kataoka E.
Keightley P.D.
Kheradpour P.
Kirkness E.F.
Koerich L.B.
Kristiansen K.
Kudrna D.
Kulathinal R.J.
Kumar S.
Kwok R.
Lander E.
Langley C.H.
Lapoint R.
Lazzaro B.P.
Lee S.J.
Levesque L.
Li R.
Lin C.F.
Lin M.F.
Lindblad-Toh K.
Llopart A.
Long M.
Low L.
Lozovsky E.
Lu J.
Luo M.
Machado C.A.
Makalowski W.
Marzo M.
Matsuda M.
Matzkin L.
McAllister B.
McBride C.S.
McKernan B.
McKernan K.
Mendez-Lago M.
Minx P.
Mollenhauer M.U.
Montooth K.
Mount S.M.
Mu X.
Myers E.
Negre B.
Newfeld S.
Nielsen R.
Noor M.A.
O'Grady P.
Pachter L.
Papaceit M.
Parisi M.J.
Parisi M.
Parts L.
Pedersen J.S.
Pesole G.
Phillippy A.M.
Ponting C.P.
Pop M.
Porcelli D.
Powell J.R.
Prohaska S.
Pruitt K.
Puig M.
Quesneville H.
Ram K.R.
Rand D.
Rasmussen M.D.
Reed L.K.
Reenan R.
Reily A.
Remington K.A.
Rieger T.T.
Ritchie M.G.
Robin C.
Rogers Y.H.
Rohde C.
Rozas J.
Rubenfield M.J.
Ruiz A.
Russo S.
Salzberg S.L.
Sanchez-Gracia A.
Saranga D.J.
Sato H.
Schaeffer S.W.
Schatz M.C.
Schlenke T.
Schwartz R.
Segarra C.
Singh R.S.
Sirot L.
Sirota M.
Sisneros N.B.
Smith C.D.
Smith T.F.
Spieth J.
Stage D.E.
Stark A.
Stephan W.
Strausberg R.L.
Strempel S.
Sturgill D.
Sutton G.
Sutton G.G.
Tao W.
Teichmann S.
Tobari Y.N.
Tomimura Y.
Tsolas J.M.
Valente V.L.
Venter E.
Venter J.C.
Vicario S.
Vieira F.G.
Vilella A.J.
Villasante A.
Walenz B.
Wang J.
Wasserman M.
Watts T.
Wilson D.
Wilson R.K.
Wing R.A.
Wolfner M.F.
Wong A.
Wong G.K.
Wu C.I.
Wu G.
Yamamoto D.
Yang H.P.
Yang S.P.
Yorke J.A.
Yoshida K.
Zdobnov E.
Zhang P.
Zhang Y.
Zimin A.V.
Baldwin J.
Abdouelleil A.
Abdulkadir J.
Abebe A.
Abera B.
Abreu J.
Acer S.C.
Aftuck L.
Alexander A.
An P.
Anderson E.
Anderson S.
Arachi H.
Azer M.
Bachantsang P.
Barry A.
Bayul T.
Berlin A.
Bessette D.
Bloom T.
Blye J.
Boguslavskiy L.
Bonnet C.
Boukhgalter B.
Bourzgui I.
Brown A.
Cahill P.
Channer S.
Cheshatsang Y.
Chuda L.
Citroen M.
Collymore A.
Cooke P.
Costello M.
D'Aco K.
Daza R.
De Haan G.
DeGray S.
DeMaso C.
Dhargay N.
Dooley K.
Dooley E.
Doricent M.
Dorje P.
Dorjee K.
Dupes A.
Elong R.
Falk J.
Farina A.
Faro S.
Ferguson D.
Fisher S.
Foley C.D.
Franke A.
Friedrich D.
Gadbois L.
Gearin G.
Gearin C.R.
Giannoukos G.
Goode T.
Graham J.
Grandbois E.
Grewal S.
Gyaltsen K.
Hafez N.
Hagos B.
Hall J.
Henson C.
Hollinger A.
Honan T.
Huard M.D.
Hughes L.
Hurhula B.
Husby M.E.
Kamat A.
Kanga B.
Kashin S.
Khazanovich D.
Kisner P.
Lance K.
Lara M.
Lee W.
Lennon N.
Letendre F.
LeVine R.
Lipovsky A.
Liu X.
Liu J.
Liu S.
Lokyitsang T.
Lokyitsang Y.
Lubonja R.
Lui A.
MacDonald P.
Magnisalis V.
Maru K.
Matthews C.
McCusker W.
McDonough S.
Mehta T.
Meldrim J.
Meneus L.
Mihai O.
Mihalev A.
Mihova T.
Mittelman R.
Mlenga V.
Montmayeur A.
Mulrain L.
Navidi A.
Naylor J.
Negash T.
Nguyen T.
Nguyen N.
Nicol R.
Norbu C.
Norbu N.
Novod N.
O'Neill B.
Osman S.
Markiewicz E.
Oyono O.L.
Patti C.
Phunkhang P.
Pierre F.
Priest M.
Raghuraman S.
Rege F.
Reyes R.
Rise C.
Rogov P.
Ross K.
Ryan E.
Settipalli S.
Shea T.
Sherpa N.
Shi L.
Shih D.
Sparrow T.
Spaulding J.
Stalker J.
Stange-Thomann N.
Stavropoulos S.
Stone C.
Strader C.
Tesfaye S.
Thomson T.
Thoulutsang Y.
Thoulutsang D.
Topham K.
Topping I.
Tsamla T.
Vassiliev H.
Vo A.
Wangchuk T.
Wangdi T.
Weiand M.
Wilkinson J.
Wilson A.
Yadav S.
Young G.
Yu Q.
Zembek L.
Zhong D.
Zimmer A.
Zwirko Z.
Jaffe D.B.
Alvarez P.
Brockman W.
Butler J.
Chin C.
Gnerre S.
Grabherr M.
Kleber M.
Mauceli E.
MacCallum I.

title: Evolution of genes and genomes on the Drosophila phylogeny.

authors:
Zimin A.V.
Smith D.R.
Sutton G.
Yorke J.A.

title: Assembly reconciliation.

journal: Bioinformatics

database: STRING

database: KEGG

database: eggNOG

key: ToxonomicScope

value: Eukaryota

database: HOGENOM

database: OMA

database: OrthoDB

database: Proteomes

value: Unassembled WGS sequence

database: GO

value: C:RNA nuclear export complex

value: F:nuclear export signal receptor activity


scientificName: Phaeodactylum tricornutum (strain CCAP 1055/1)

lineage: Eukaryota Sar Stramenopiles Ochrophyta Bacillariophyta Bacillariophyceae Bacillariophycidae Naviculales Phaeodactylaceae Phaeodactylum

value: Heat shock protein Hsp20

source: RuleBase

value: Belongs to the small heat shock protein (HSP20) family

description: SHSP

description: Disordered

authors:
Bowler C.
Allen A.E.
Badger J.H.
Grimwood J.
Jabbari K.
Kuo A.
Maheswari U.
Martens C.
Maumus F.
Otillar R.P.
Rayko E.
Salamov A.
Vandepoele K.
Beszteri B.
Gruber A.
Heijde M.
Katinka M.
Mock T.
Valentin K.
Verret F.
Berges J.A.
Brownlee C.
Cadoret J.P.
Chiovitti A.
Choi C.J.
Coesel S.
De Martino A.
Detter J.C.
Durkin C.
Falciatore A.
Fournet J.
Haruta M.
Huysman M.J.
Jenkins B.D.
Jiroutova K.
Jorgensen R.E.
Joubert Y.
Kaplan A.
Kroger N.
Kroth P.G.
La Roche J.
Lindquist E.
Lommer M.
Martin-Jezequel V.
Lopez P.J.
Lucas S.
Mangogna M.
McGinnis K.
Medlin L.K.
Montsant A.
Oudot-Le Secq M.P.
Napoli C.
Obornik M.
Parker M.S.
Petit J.L.
Porcel B.M.
Poulsen N.
Robison M.
Rychlewski L.
Rynearson T.A.
Schmutz J.
Shapiro H.
Siaut M.
Stanley M.
Sussman M.R.
Taylor A.R.
Vardi A.
von Dassow P.
Vyverman W.
Willis A.
Wyrwicz L.S.
Rokhsar D.S.
Weissenbach J.
Armbrust E.V.
Green B.R.
Van de Peer Y.
Grigoriev I.V.

database: PubMed

database: DOI

title: The Phaeodactylum genome reveals the evolutionary history of diatom genomes.

authors:
Grigoriev I.
Grimwood J.
Kuo A.
Otillar R.P.
Salamov A.
Detter J.C.
Lindquist E.
Shapiro H.
Lucas S.
Glavina del Rio T.
Pitluck S.
Rokhsar D.
Bowler C.

database: EMBL

database: PaxDb

database: GeneID

database: InParanoid

value: Chromosome 7

database: CDD

database: PANTHER

value: HEAT-SHOCK PROTEIN 20 FAMILY MEMBER

database: Pfam

database: SUPFAM

value: HSP20-like chaperones

database: PROSITE

value: SHSP


value: Fibrinogen C-terminal domain-containing protein

value: Lacks conserved residue(s) required for the propagation of feature annotation

commentType: CAUTION

type: Signal

type: Chain

description: Fibrinogen C-terminal

description: Disordered

type: Disulfide bond

authors:
Adams M.D.
Celniker S.E.
Holt R.A.
Evans C.A.
Gocayne J.D.
Amanatides P.G.
Scherer S.E.
Li P.W.
Hoskins R.A.
Galle R.F.
George R.A.
Lewis S.E.
Richards S.
Ashburner M.
Henderson S.N.
Sutton G.G.
Wortman J.R.
Yandell M.D.
Zhang Q.
Chen L.X.
Brandon R.C.
Rogers Y.H.
Blazej R.G.
Champe M.
Pfeiffer B.D.
Wan K.H.
Doyle C.
Baxter E.G.
Helt G.
Nelson C.R.
Gabor G.L.
Abril J.F.
Agbayani A.
An H.J.
Andrews-Pfannkoch C.
Baldwin D.
Ballew R.M.
Basu A.
Baxendale J.
Bayraktaroglu L.
Beasley E.M.
Beeson K.Y.
Benos P.V.
Berman B.P.
Bhandari D.
Bolshakov S.
Borkova D.
Botchan M.R.
Bouck J.
Brokstein P.
Brottier P.
Burtis K.C.
Busam D.A.
Butler H.
Cadieu E.
Center A.
Chandra I.
Cherry J.M.
Cawley S.
Dahlke C.
Davenport L.B.
Davies P.
de Pablos B.
Delcher A.
Deng Z.
Mays A.D.
Dew I.
Dietz S.M.
Dodson K.
Doup L.E.
Downes M.
Dugan-Rocha S.
Dunkov B.C.
Dunn P.
Durbin K.J.
Evangelista C.C.
Ferraz C.
Ferriera S.
Fleischmann W.
Fosler C.
Gabrielian A.E.
Garg N.S.
Gelbart W.M.
Glasser K.
Glodek A.
Gong F.
Gorrell J.H.
Gu Z.
Guan P.
Harris M.
Harris N.L.
Harvey D.
Heiman T.J.
Hernandez J.R.
Houck J.
Hostin D.
Houston K.A.
Howland T.J.
Wei M.H.
Ibegwam C.
Jalali M.
Kalush F.
Karpen G.H.
Ke Z.
Kennison J.A.
Ketchum K.A.
Kimmel B.E.
Kodira C.D.
Kraft C.
Kravitz S.
Kulp D.
Lai Z.
Lasko P.
Lei Y.
Levitsky A.A.
Li J.
Li Z.
Liang Y.
Lin X.
Liu X.
Mattei B.
McIntosh T.C.
McLeod M.P.
McPherson D.
Merkulov G.
Milshina N.V.
Mobarry C.
Morris J.
Moshrefi A.
Mount S.M.
Moy M.
Murphy B.
Murphy L.
Muzny D.M.
Nelson D.L.
Nelson D.R.
Nelson K.A.
Nixon K.
Nusskern D.R.
Pacleb J.M.
Palazzolo M.
Pittman G.S.
Pan S.
Pollard J.
Puri V.
Reese M.G.
Reinert K.
Remington K.
Saunders R.D.
Scheeler F.
Shen H.
Shue B.C.
Siden-Kiamos I.
Simpson M.
Skupski M.P.
Smith T.
Spier E.
Spradling A.C.
Stapleton M.
Strong R.
Sun E.
Svirskas R.
Tector C.
Turner R.
Venter E.
Wang A.H.
Wang X.
Wang Z.Y.
Wassarman D.A.
Weinstock G.M.
Weissenbach J.
Williams S.M.
WoodageT
Worley K.C.
Wu D.
Yang S.
Yao Q.A.
Ye J.
Yeh R.F.
Zaveri J.S.
Zhan M.
Zhang G.
Zhao Q.
Zheng L.
Zheng X.H.
Zhong F.N.
Zhong W.
Zhou X.
Zhu S.
Zhu X.
Smith H.O.
Gibbs R.A.
Myers E.W.
Rubin G.M.
Venter J.C.

value: Berkeley

authors:
Celniker S.E.
Wheeler D.A.
Kronmiller B.
Carlson J.W.
Halpern A.
Patel S.
Adams M.
Champe M.
Dugan S.P.
Frise E.
Hodgson A.
George R.A.
Hoskins R.A.
Laverty T.
Muzny D.M.
Nelson C.R.
Pacleb J.M.
Park S.
Pfeiffer B.D.
Richards S.
Sodergren E.J.
Svirskas R.
Tabor P.E.
Wan K.
Stapleton M.
Sutton G.G.
Venter C.
Weinstock G.
Scherer S.E.
Myers E.W.
Gibbs R.A.
Rubin G.M.

authors:
Misra S.
Crosby M.A.
Mungall C.J.
Matthews B.B.
Campbell K.S.
Hradecky P.
Huang Y.
Kaminker J.S.
Millburn G.H.
Prochnik S.E.
Smith C.D.
Tupy J.L.
Whitfied E.J.
Bayraktaroglu L.
Berman B.P.
Bettencourt B.R.
Celniker S.E.
de Grey A.D.
Drysdale R.A.
Harris N.L.
Richter J.
Russo S.
Schroeder A.J.
Shu S.Q.
Stapleton M.
Yamada C.
Ashburner M.
Gelbart W.M.
Rubin G.M.
Lewis S.E.

value: Assembly of active LPL and LIPC lipase complexes

value: Expressed in hemocyte (sensu Nematoda and Protostomia) in imaginal disc-derived wing and 60 other cell types or tissues

value: P:G protein-coupled receptor signaling pathway


scientificName: Oryza sativa subsp. indica

commonName: Rice

lineage:
Eukaryota
Viridiplantae
Streptophyta
Embryophyta
Tracheophyta
Spermatophyta
Magnoliopsida
Liliopsida
Poales
Poaceae
BOP clade
Oryzoideae
Oryzeae
Oryzinae
Oryza
Oryza sativa

value: BURP domain-containing protein

description: BURP domain-containing protein

description: BURP

authors:
Yu J.
Wang J.
Lin W.
Li S.
Li H.
Zhou J.
Ni P.
Dong W.
Hu S.
Zeng C.
Zhang J.
Zhang Y.
Li R.
Xu Z.
Li S.
Li X.
Zheng H.
Cong L.
Lin L.
Yin J.
Geng J.
Li G.
Shi J.
Liu J.
Lv H.
Li J.
Wang J.
Deng Y.
Ran L.
Shi X.
Wang X.
Wu Q.
Li C.
Ren X.
Wang J.
Wang X.
Li D.
Liu D.
Zhang X.
Ji Z.
Zhao W.
Sun Y.
Zhang Z.
Bao J.
Han Y.
Dong L.
Ji J.
Chen P.
Wu S.
Liu J.
Xiao Y.
Bu D.
Tan J.
Yang L.
Ye C.
Zhang J.
Xu J.
Zhou Y.
Yu Y.
Zhang B.
Zhuang S.
Wei H.
Liu B.
Lei M.
Yu H.
Li Y.
Xu H.
Wei S.
He X.
Fang L.
Zhang Z.
Zhang Y.
Huang X.
Su Z.
Tong W.
Li J.
Tong Z.
Li S.
Ye J.
Wang L.
Fang L.
Lei T.
Chen C.
Chen H.
Xu Z.
Li H.
Huang H.
Zhang F.
Xu H.
Li N.
Zhao C.
Li S.
Dong L.
Huang Y.
Li L.
Xi Y.
Qi Q.
Li W.
Zhang B.
Hu W.
Zhang Y.
Tian X.
Jiao Y.
Liang X.
Jin J.
Gao L.
Zheng W.
Hao B.
Liu S.
Wang W.
Yuan L.
Cao M.
McDermott J.
Samudrala R.
Wang J.
Wong G.K.
Yang H.

title: The genomes of Oryza sativa: a history of duplications.

journal: PLoS Biol.

database: AlphaFoldDB

database: STRING

database: Gramene

key: GeneId

value: Chromosome 8

database: InterPro

value: POLYGALACTURONASE 1 BETA-LIKE PROTEIN 2

value: BURP

database: SMART


value: Inr-a

description: CID

authors:
Carlson J.
Booth B.
Frise E.
Sandler J.
Wan K.
Yu C.
Celniker S.

value: mRNA

database: RefSeq

database: SMR

database: IntAct

key: Interactions

database: PeptideAtlas

database: DNASU

database: AGR

database: CTD

database: FlyBase

database: VEuPathDB

database: HOGENOM

database: OrthoDB

database: BioGRID-ORCS

key: hits

value: 1 hit in 1 CRISPR screen

database: Bgee

value: Expressed in indirect flight muscle cell (Drosophila) in body wall and 279 other cell types or tissues

database: GO

value: F:mRNA binding

value: F:RNA binding

source: PubMed

value: F:RNA polymerase II complex binding

value: P:mRNA 3'-end processing

value: P:termination of RNA polymerase II transcription

value: PRE-MRNA CLEAVAGE COMPLEX 2 PROTEIN PCF11

value: PRE-MRNA CLEAVAGE COMPLEX II

value: ENTH/VHS domain

value: CID


scientificName: Glycine max

commonName: Soybean

lineage:
Eukaryota
Viridiplantae
Streptophyta
Embryophyta
Tracheophyta
Spermatophyta
Magnoliopsida
eudicotyledons
Gunneridae
Pentapetalae
rosids
fabids
Fabales
Fabaceae
Papilionoideae
50 kb inversion clade
NPAAA clade
indigoferoid/millettioid clade
Phaseoleae
Glycine
Glycine subgen. Soja

value: C2H2-Zn transcription factor

description: Disordered

description: Disordered

description: Acidic residues

authors:
Cheung F.
Xiao Y.
Chan A.
Moskal W.
Town C.D.

authors:
Chai C.
Wang Y.
Joshi T.
Valliyodan B.
Prince S.
Michel L.
Xu D.
Nguyen H.T.

database: PubMed

database: DOI

title: Soybean transcription factor ORFeome associated with drought resistance: a valuable resource to accelerate research on abiotic stress resistance.

journal: BMC Genomics

database: EMBL

key: ProteinId

database: AlphaFoldDB

database: STRING

database: PaxDb

database: Gramene

database: KEGG

database: eggNOG

value: Eukaryota

database: OMA

value: Classic Zinc Finger

database: PANTHER

value: C2H2-TYPE DOMAIN-CONTAINING PROTEIN

value: ZINC FINGER PROTEIN 4-LIKE

database: SUPFAM

value: beta-beta-alpha zinc fingers

database: PROSITE


entryType: UniProtKB reviewed (Swiss-Prot)

scientificName: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

commonName: Fission yeast

lineage: Eukaryota Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces

value: Sporulation-specific protein 2

value: Involved in sporulation. Plays a significant role in modification of the spindle pole body prior to spore formation and is required for initiating forespore membrane formation. Assists in the localization of spo13 to the outer surface of the SPB

commentType: FUNCTION

value: Interacts with spo13 and spo15

commentType: SUBUNIT

value: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body

value: Induced during meiosis by the transcription factor mei4. Protein levels rapidly increase during meiosis and then decline

commentType: INDUCTION

value: The sequence is 100 percent identical to the C-terminus of vps13b

commentType: MISCELLANEOUS

value: Belongs to the VPS13 family

description: Sporulation-specific protein 2

Cytoplasm

category: Cellular component

authors:
Wood V.
Gwilliam R.
Rajandream M.A.
Lyne M.H.
Lyne R.
Stewart A.
Sgouros J.G.
Peat N.
Hayles J.
Baker S.G.
Basham D.
Bowman S.
Brooks K.
Brown D.
Brown S.
Chillingworth T.
Churcher C.M.
Collins M.
Connor R.
Cronin A.
Davis P.
Feltwell T.
Fraser A.
Gentles S.
Goble A.
Hamlin N.
Harris D.E.
Hidalgo J.
Hodgson G.
Holroyd S.
Hornsby T.
Howarth S.
Huckle E.J.
Hunt S.
Jagels K.
James K.D.
Jones L.
Jones M.
Leather S.
McDonald S.
McLean J.
Mooney P.
Moule S.
Mungall K.L.
Murphy L.D.
Niblett D.
Odell C.
Oliver K.
O'Neil S.
Pearson D.
Quail M.A.
Rabbinowitsch E.
Rutherford K.M.
Rutter S.
Saunders D.
Seeger K.
Sharp S.
Skelton J.
Simmonds M.N.
Squares R.
Squares S.
Stevens K.
Taylor K.
Taylor R.G.
Tivey A.
Walsh S.V.
Warren T.
Whitehead S.
Woodward J.R.
Volckaert G.
Aert R.
Robben J.
Grymonprez B.
Weltjens I.
Vanstreels E.
Rieger M.
Schaefer M.
Mueller-Auer S.
Gabel C.
Fuchs M.
Duesterhoeft A.
Fritzc C.
Holzer E.
Moestl D.
Hilbert H.
Borzym K.
Langer I.
Beck A.
Lehrach H.
Reinhardt R.
Pohl T.M.
Eger P.
Zimmermann W.
Wedler H.
Wambutt R.
Purnelle B.
Goffeau A.
Cadieu E.
Dreano S.
Gloux S.
Lelaure V.
Mottier S.
Galibert F.
Aves S.J.
Xiang Z.
Hunt C.
Moore K.
Hurst S.M.
Lucas M.
Rochet M.
Gaillardin C.
Tallada V.A.
Garzon A.
Thode G.
Daga R.R.
Cruzado L.
Jimenez J.
Sanchez M.
del Rey F.
Benito J.
Dominguez A.
Revuelta J.L.
Moreno S.
Armstrong J.
Forsburg S.L.
Cerutti L.
Lowe T.
McCombie W.R.
Paulsen I.
Potashkin J.
Shpakovski G.V.
Ussery D.
Barrell B.G.
Nurse P.

title: The genome sequence of Schizosaccharomyces pombe.

authors:
Nakase Y.
Nakamura-Kubo M.
Ye Y.
Hirata A.
Shimoda C.
Nakamura T.

title: Meiotic spindle pole bodies acquire the ability to assemble the spore plasma membrane by sequential recruitment of sporulation-specific components in fission yeast.

journal: Mol. Biol. Cell

referencePositions:
FUNCTION
INDUCTION
SUBCELLULAR LOCATION
INTERACTION WITH SPO13 AND SPO15

key: Status

database: SMR

database: BioGRID

database: PomBase

database: VEuPathDB

database: HOGENOM

database: InParanoid

database: PRO

database: Proteomes

value: Chromosome II

value: C:meiotic spindle pole body

value: P:ascospore formation

value: P:ascospore-type prospore-specific spindle pole body remodeling


scientificName: Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 / AN6)

lineage: Bacteria Pseudomonadati Pseudomonadota Gammaproteobacteria Enterobacterales Morganellaceae Xenorhabdus

value: Cysteine transport protein (ABC superfamily, peri_bind)

value: fliY

value: Cell envelope

value: Belongs to the bacterial solute-binding protein 3 family

description: Solute-binding protein family 3/N-terminal

authors:
Chaston J.M.
Suen G.
Tucker S.L.
Andersen A.W.
Bhasin A.
Bode E.
Bode H.B.
Brachmann A.O.
Cowles C.E.
Cowles K.N.
Darby C.
de Leon L.
Drace K.
Du Z.
Givaudan A.
Herbert Tran E.E.
Jewell K.A.
Knack J.J.
Krasomil-Osterfeld K.C.
Kukor R.
Lanois A.
Latreille P.
Leimgruber N.K.
Lipke C.M.
Liu R.
Lu X.
Martens E.C.
Marri P.R.
Medigue C.
Menard M.L.
Miller N.M.
Morales-Soto N.
Norton S.
Ogier J.C.
Orchard S.S.
Park D.
Park Y.
Qurollo B.A.
Sugar D.R.
Richards G.R.
Rouy Z.
Slominski B.
Slominski K.
Snyder H.
Tjaden B.C.
van der Hoeven R.
Welch R.D.
Wheeler C.
Xiang B.
Barbazuk B.
Gaudriault S.
Goodner B.
Slater S.C.
Forst S.
Goldman B.S.
Goodrich-Blair H.

database: PubMed

database: DOI

title: The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus: convergent lifestyles from divergent genomes.

journal: PLoS ONE

database: EMBL

key: MoleculeType

database: RefSeq

database: AlphaFoldDB

database: STRING

database: GeneID

value: Bacteria

value: Chromosome

database: GO

value: C:outer membrane-bounded periplasmic space

database: CDD

value: Periplasmic binding protein-like II

database: InterPro

value: ABC TRANSPORTER EXTRACELLULAR-BINDING PROTEIN YCKB-RELATED

value: MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F

database: Pfam

database: SMART

value: PBPb


value: ttv

value: ttv-RA

value: Protein modification; protein glycosylation

value: Endoplasmic reticulum membrane

value: Single-pass type II membrane protein

value: Belongs to the glycosyltransferase 47 family

description: Glycosyl transferase 64

description: Disordered

description: Polar residues

value: mRNA

key: Description

database: SMR

database: PeptideAtlas

database: AGR

database: CTD

database: FlyBase

database: VEuPathDB

database: OrthoDB

database: BioGRID-ORCS

value: 1 hit in 3 CRISPR screens

database: Bgee

value: Expressed in dorsal appendage forming follicle cell in ovary and 276 other cell types or tissues

value: C:endoplasmic reticulum membrane

value: F:glycosyltransferase activity

value: P:glycoprotein biosynthetic process

database: FunFam

value: Tout-velu, isoform B

value: Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A


scientificName: Bos taurus

commonName: Bovine

source: Ensembl

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos

value: Xin actin binding repeat containing 2

source: VGNC

value: Cell junction

value: Xin repeats bind F-actin

commentType: DOMAIN

value: Belongs to the Xin family

type: Repeat

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Xin

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Basic and acidic residues

description: Basic and acidic residues

description: Basic and acidic residues

description: Low complexity

description: Basic and acidic residues

description: Polar residues

description: Polar residues

description: Low complexity

description: Pro residues

description: Pro residues

description: Low complexity

description: Basic and acidic residues

description: Basic and acidic residues

description: Polar residues

description: Polar residues

description: Basic and acidic residues

description: Polar residues

description: Basic and acidic residues

description: Basic and acidic residues

description: Polar residues

description: Basic and acidic residues

description: Polar residues

authors:
Rosen B.D.
Bickhart D.M.
Koren S.
Schnabel R.D.
Hall R.
Zimin A.
Dreischer C.
Schultheiss S.
Schroeder S.G.
Elsik C.G.
Couldrey C.
Liu G.E.
Van Tassell C.P.
Phillippy A.M.
Smith T.P.L.
Medrano J.F.

title: ARS-UCD1.2.

value: Expressed in rectus femoris and 30 other cell types or tissues

value: P:positive regulation of protein localization

value: P:regulation of actin filament organization

value: XIN ACTIN-BINDING REPEAT-CONTAINING PROTEIN 2


name: sn-glycerol 3-phosphate + NAD(+) = dihydroxyacetone phosphate + NADH + H(+)

database: Rhea

database: ChEBI

value: Lipid metabolism

value: Phospholipid metabolism; alpha-glycerophosphate cycle

value: Homodimer

value: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family

description: Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal

description: Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Polar residues

description: Polar residues

description: Basic and acidic residues

description: Basic and acidic residues

description: Basic and acidic residues

description: Basic residues

description: Basic and acidic residues

title: The genome sequence of Drosophila melanogaster.

title: Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence.

title: Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.

authors:
Kaminker J.S.
Bergman C.M.
Kronmiller B.
Carlson J.
Svirskas R.
Patel S.
Frise E.
Wheeler D.A.
Lewis S.E.
Rubin G.M.
Ashburner M.
Celniker S.E.

title: The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective.

authors:
Hoskins R.A.
Smith C.D.
Carlson J.W.
Carvalho A.B.
Halpern A.
Kaminker J.S.
Kennedy C.
Mungall C.J.
Sullivan B.A.
Sutton G.G.
Yasuhara J.C.
Wakimoto B.T.
Myers E.W.
Celniker S.E.
Rubin G.M.
Karpen G.H.

title: Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.

authors:
Quesneville H.
Bergman C.M.
Andrieu O.
Autard D.
Nouaud D.
Ashburner M.
Anxolabehere D.

authors:
Smith C.D.
Shu S.
Mungall C.J.
Karpen G.H.

authors:
Hoskins R.A.
Carlson J.W.
Kennedy C.
Acevedo D.
Evans-Holm M.
Frise E.
Wan K.H.
Park S.
Mendez-Lago M.
Rossi F.
Villasante A.
Dimitri P.
Karpen G.H.
Celniker S.E.

authors:
Matthews B.B.
Dos Santos G.
Crosby M.A.
Emmert D.B.
St Pierre S.E.
Gramates L.S.
Zhou P.
Schroeder A.J.
Falls K.
Strelets V.
Russo S.M.
Gelbart W.M.

authors:
Crosby M.A.
Gramates L.S.
Dos Santos G.
Matthews B.B.
St Pierre S.E.
Zhou P.
Schroeder A.J.
Falls K.
Emmert D.B.
Russo S.M.
Gelbart W.M.

authors:
Hoskins R.A.
Carlson J.W.
Wan K.H.
Park S.
Mendez I.
Galle S.E.
Booth B.W.
Pfeiffer B.D.
George R.A.
Svirskas R.
Krzywinski M.
Schein J.
Accardo M.C.
Damia E.
Messina G.
Mendez-Lago M.
de Pablos B.
Demakova O.V.
Andreyeva E.N.
Boldyreva L.V.
Marra M.
Carvalho A.B.
Dimitri P.
Villasante A.
Zhimulev I.F.
Rubin G.M.
Karpen G.H.
Celniker S.E.

value: Expressed in early-mid elongation-stage spermatid (Drosophila) in testis and 66 other cell types or tissues

value: F:glycerol-3-phosphate dehydrogenase (NAD+) activity

value: N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2

value: 6-phosphogluconate dehydrogenase C-terminal domain-like


value: phenylalanine 4-monooxygenase

value: Hn

value: Hn-RB

source: PIRSR

value: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family

description: Biopterin-dependent aromatic amino acid hydroxylase family profile

type: Binding site

authors:
Carlson J.
Booth B.
Frise E.
Park S.
Wan K.
Yu C.
Celniker S.

value: Berkeley

database: EMBL

value: mRNA

database: RefSeq

database: AlphaFoldDB

database: DNASU

database: GeneID

database: HOGENOM

database: OMA

value: 0 hits in 3 CRISPR screens

value: Expressed in head capsule and 71 other cell types or tissues

database: GO

value: F:iron ion binding

value: Aromatic amino acid hydroxylase

value: Aromatic aminoacid monoxygenases, catalytic and oligomerization domains


scientificName: Arabidopsis thaliana

commonName: Mouse-ear cress

lineage: Eukaryota Viridiplantae Streptophyta Embryophyta Tracheophyta Spermatophyta Magnoliopsida eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis

value: ROP-interactive CRIB motif-containing protein 7

source: TAIR

source: Araport

value: Membrane

value: Single-pass type I membrane protein

value: Belongs to the RLP family

Proteomics identification

source: ProteomicsDB

authoringGroup: CSHL and WU Arabidopsis Sequencing Project

authors:
Mayer K.
Schuller C.
Wambutt R.
Murphy G.
Volckaert G.
Pohl T.
Dusterhoft A.
Stiekema W.
Entian K.D.
Terryn N.
Harris B.
Ansorge W.
Brandt P.
Grivell L.
Rieger M.
Weichselgartner M.
de Simone V.
Obermaier B.
Mache R.
Muller M.
Kreis M.
Delseny M.
Puigdomenech P.
Watson M.
Schmidtheini T.
Reichert B.
Portatelle D.
Perez-Alonso M.
Boutry M.
Bancroft I.
Vos P.
Hoheisel J.
Zimmermann W.
Wedler H.
Ridley P.
Langham S.A.
McCullagh B.
Bilham L.
Robben J.
Van der Schueren J.
Grymonprez B.
Chuang Y.J.
Vandenbussche F.
Braeken M.
Weltjens I.
Voet M.
Bastiaens I.
Aert R.
Defoor E.
Weitzenegger T.
Bothe G.
Ramsperger U.
Hilbert H.
Braun M.
Holzer E.
Brandt A.
Peters S.
van Staveren M.
Dirske W.
Mooijman P.
Klein Lankhorst R.
Rose M.
Hauf J.
Kotter P.
Berneiser S.
Hempel S.
Feldpausch M.
Lamberth S.
Van den Daele H.
De Keyser A.
Buysshaert C.
Gielen J.
Villarroel R.
De Clercq R.
Van Montagu M.
Rogers J.
Cronin A.
Quail M.
Bray-Allen S.
Clark L.
Doggett J.
Hall S.
Kay M.
Lennard N.
McLay K.
Mayes R.
Pettett A.
Rajandream M.A.
Lyne M.
Benes V.
Rechmann S.
Borkova D.
Blocker H.
Scharfe M.
Grimm M.
Lohnert T.H.
Dose S.
de Haan M.
Maarse A.
Schafer M.
Muller-Auer S.
Gabel C.
Fuchs M.
Fartmann B.
Granderath K.
Dauner D.
Herzl A.
Neumann S.
Argiriou A.
Vitale D.
Liguori R.
Piravandi E.
Massenet O.
Quigley F.
Clabauld G.
Mundlein A.
Felber R.
Schnabl S.
Hiller R.
Schmidt W.
Lecharny A.
Aubourg S.
Chefdor F.
Cooke R.
Berger C.
Montfort A.
Casacuberta E.
Gibbons T.
Weber N.
Vandenbol M.
Bargues M.
Terol J.
Torres A.
Perez-Perez A.
Purnelle B.
Bent E.
Johnson S.
Tacon D.
Jesse T.
Heijnen L.
Schwarz S.
Scholler P.
Heber S.
Francs P.
Bielke C.
Frishman D.
Haase D.
Lemcke K.
Mewes H.W.
Stocker S.
Zaccaria P.
Bevan M.
Wilson R.K.
de la Bastide M.
Habermann K.
Parnell L.
Dedhia N.
Gnoj L.
Schutz K.
Huang E.
Spiegel L.
Sehkon M.
Murray J.
Sheet P.
Cordes M.
Abu-Threideh J.
Stoneking T.
Kalicki J.
Graves T.
Harmon G.
Edwards J.
Latreille P.
Courtney L.
Cloud J.
Abbott A.
Scott K.
Johnson D.
Minx P.
Bentley D.
Fulton B.
Miller N.
Greco T.
Kemp K.
Kramer J.
Fulton L.
Mardis E.
Dante M.
Pepin K.
Hillier L.
Nelson J.
Spieth J.
Ryan E.
Andrews S.
Geisel C.
Layman D.
Du H.
Ali J.
Berghoff A.
Jones K.
Drone K.
Cotton M.
Joshu C.
Antonoiu B.
Zidanic M.
Strong C.
Sun H.
Lamar B.
Yordan C.
Ma P.
Zhong J.
Preston R.
Vil D.
Shekher M.
Matero A.
Shah R.
Swaby I.K.
O'Shaughnessy A.
Rodriguez M.
Hoffmann J.
Till S.
Granat S.
Shohdy N.
Hasegawa A.
Hameed A.
Lodhi M.
Johnson A.
Chen E.
Marra M.
Martienssen R.
McCombie W.R.

database: PubMed

database: DOI

title: Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.

value: cv. Columbia

authors:
Cheng C.Y.
Krishnakumar V.
Chan A.P.
Thibaud-Nissen F.
Schobel S.
Town C.D.

title: Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.

journal: Plant J.

database: SMR

database: FunCoup

key: Number of interactors

database: STRING

database: PaxDb

database: ProteomicsDB

database: KEGG

database: Araport

database: TAIR

database: eggNOG

value: Eukaryota

database: InParanoid

value: LRR receptor-like serine/threonine-protein kinase ERECTA


scientificName: Triticum aestivum

commonName: Wheat

source: EnsemblPlants

source: Proteomes

lineage:
Eukaryota
Viridiplantae
Streptophyta
Embryophyta
Tracheophyta
Spermatophyta
Magnoliopsida
Liliopsida
Poales
Poaceae
BOP clade
Pooideae
Triticodae
Triticeae
Triticinae
Triticum

value: Protein phosphatase 2A structural subunit

value: Belongs to the phosphatase 2A regulatory subunit A family

description: HEAT

description: HEAT

description: HEAT

description: HEAT

description: Phosphatase PP2A regulatory subunit A/Splicing factor 3B subunit 1-like HEAT repeat

description: HEAT

description: HEAT

description: HEAT

description: HEAT

description: HEAT

description: HEAT

description: HEAT

description: HEAT

value: cv. Chinese Spring

submissionDatabase: UniProtKB

database: RefSeq

database: AlphaFoldDB

database: EnsemblPlants

database: Gramene

value: F:protein phosphatase regulator activity

value: Serine/threonine-protein phosphatase 2A regulatory subunit A alpha isoform

value: PROTEIN PHOSPHATASE 2 (FORMERLY 2A), REGULATORY SUBUNIT A, BETA ISOFORM-RELATED

value: SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A 65 KDA REGULATORY SUBUNIT


scientificName: Equus caballus

commonName: Horse

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Laurasiatheria Perissodactyla Equidae Equus

source: ARBA

value: Growth hormone secretagogue receptor type 1

value: GH-releasing peptide receptor

value: Ghrelin receptor

value: GHSR

value: Interacts with the heterotrimeric G protein complex composed of 3 units, alpha, beta and gamma; this complex may consist of GNB1 and GNG2

value: Cell membrane

value: Multi-pass membrane protein

value: Belongs to the G protein-coupled receptor 1 family

value: Lacks conserved residue(s) required for the propagation of feature annotation

type: Transmembrane

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: G-protein coupled receptors family 1 profile

source: PROSITE

authoringGroup: Broad Institute Genome Sequencing Platform

authoringGroup: Broad Institute Whole Genome Assembly Team

authors:
Wade C.M.
Giulotto E.
Sigurdsson S.
Zoli M.
Gnerre S.
Imsland F.
Lear T.L.
Adelson D.L.
Bailey E.
Bellone R.R.
Bloecker H.
Distl O.
Edgar R.C.
Garber M.
Leeb T.
Mauceli E.
MacLeod J.N.
Penedo M.C.T.
Raison J.M.
Sharpe T.
Vogel J.
Andersson L.
Antczak D.F.
Biagi T.
Binns M.M.
Chowdhary B.P.
Coleman S.J.
Della Valle G.
Fryc S.
Guerin G.
Hasegawa T.
Hill E.W.
Jurka J.
Kiialainen A.
Lindgren G.
Liu J.
Magnani E.
Mickelson J.R.
Murray J.
Nergadze S.G.
Onofrio R.
Pedroni S.
Piras M.F.
Raudsepp T.
Rocchi M.
Roeed K.H.
Ryder O.A.
Searle S.
Skow L.
Swinburne J.E.
Syvaenen A.C.
Tozaki T.
Valberg S.J.
Vaudin M.
White J.R.
Zody M.C.
Lander E.S.
Lindblad-Toh K.

title: Genome sequence, comparative analysis, and population genetics of the domestic horse.

value: Thoroughbred

value: Expressed in inner cell mass and 5 other cell types or tissues

value: F:growth hormone secretagogue receptor activity

value: F:growth hormone-releasing hormone receptor activity

value: P:actin polymerization or depolymerization

value: P:G protein-coupled receptor signaling pathway

value: P:negative regulation of inflammatory response

value: P:negative regulation of interleukin-1 beta production

value: P:negative regulation of interleukin-6 production

value: P:negative regulation of tumor necrosis factor production

value: P:positive regulation of multicellular organism growth

value: growth hormone secretagogue receptor type 1

value: Rhodopsin 7-helix transmembrane proteins

value: GROWTH HORMONE SECRETAGOGUE RECEPTOR TYPE 1

value: Family A G protein-coupled receptor-like


value: Sirtuin 5

source: PROSITE-ProRule

description: Deacetylase sirtuin-type

database: Ensembl

database: VGNC

database: GeneTree

database: HOGENOM

database: Proteomes

key: Component

value: Chromosome 20

database: Bgee

value: Expressed in muscle tissue and 23 other cell types or tissues

database: ExpressionAtlas

value: baseline

database: GO

value: F:NAD+ binding

key: EntryName

value: TPP-binding domain

database: InterPro

value: Sirtuin

database: PANTHER

value: NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED

database: Pfam

database: SUPFAM

value: DHS-like NAD/FAD-binding domain

database: PROSITE

value: SIRTUIN


value: Cholesterol 25-hydroxylase

value: Membrane

description: Helical

source: SAM

description: Helical

description: Helical

description: Helical

description: Fatty acid hydroxylase

database: PubMed

database: DOI

value: Thoroughbred

database: RefSeq

key: NucleotideSequenceId

database: STRING

database: PaxDb

database: GeneID

database: KEGG

database: CTD

database: InParanoid

database: OMA

database: OrthoDB

database: BRENDA

key: OrganismId

value: Chromosome 1

value: Expressed in synovial membrane of synovial joint and 17 other cell types or tissues

value: P:cholesterol biosynthetic process via desmosterol

value: P:negative regulation of cholesterol metabolic process

value: P:negative regulation of fusion of virus membrane with host plasma membrane


source: PIRNR

value: Wee1-like protein kinase

value: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation

name: L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)

database: Rhea

database: ChEBI

name: L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)

name: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)

directionType: left-to-right

value: Binds 2 magnesium ions per subunit.

value: Nucleus

value: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily

description: Protein kinase

description: Disordered

description: Disordered

description: Disordered

type: Coiled coil

description: Acidic residues

description: Proton acceptor

value: Expressed in inner cell mass and 23 other cell types or tissues

value: F:non-membrane spanning protein tyrosine kinase activity

value: P:negative regulation of G2/M transition of mitotic cell cycle

value: EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED


scientificName: Xenopus tropicalis

commonName: Western clawed frog

source: RefSeq

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Silurana

value: ADP-ribosylation factor-like protein 5A

source: Xenbase

value: Belongs to the small GTPase superfamily. Arf family

value: Nigerian

value: Liver and blood

database: AlphaFoldDB

database: AGR

database: Xenbase

database: eggNOG

value: Eukaryota

database: GeneTree

key: Fingerprint

database: Proteomes

value: Chromosome 9

database: Bgee

value: Expressed in testis and 12 other cell types or tissues

database: GO

key: GoTerm

value: C:trans-Golgi network

value: F:GTP binding

value: P:protein localization to Golgi membrane

value: P-loop containing nucleotide triphosphate hydrolases

value: P-loop containing nucleoside triphosphate hydrolases


value: 60 kDa heat shock protein, mitochondrial

value: 60 kDa chaperonin

value: Chaperonin 60

value: Heat shock protein 60

value: Mitochondrial matrix protein P1

value: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein

name: ATP + H2O + an unfolded polypeptide = ADP + phosphate + a folded polypeptide.

value: Homoheptamer arranged in a ring structure. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. Interacts with 2 heptameric Hsp10 rings to form the symmetrical football complex. Interacts with HRAS. Interacts with ATAD3A. Interacts with ETFBKMT and EEF1AKMT3. Interacts with MFHAS1

value: Mitochondrion matrix

value: Belongs to the TCP-1 chaperonin family

value: Belongs to the chaperonin (HSP60) family

source: PeptideAtlas

database: PubMed

database: DOI

value: Thoroughbred

database: FunCoup

database: STRING

database: PaxDb

database: Ensembl

database: VGNC

key: GeneName

database: HOGENOM

value: Chromosome 18

value: Expressed in trophectoderm and 23 other cell types or tissues

database: ExpressionAtlas

value: baseline

value: C:chaperonin-containing T-complex

key: GoEvidenceType

value: C:mitochondrial matrix

value: F:ATP binding

value: F:ATP-dependent protein folding chaperone

value: P:positive regulation of cytokine production

value: Chaperonin 60 subunit alpha 2 chloroplastic

value: 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL


value: CTD small phosphatase 2

description: Disordered

description: Low complexity

database: AlphaFoldDB

database: InParanoid

value: Chromosome 6

key: ExpressionPatterns

value: Expressed in synovial membrane of synovial joint and 23 other cell types or tissues


value: TNF receptor-associated factor

name: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.

value: Protein modification; protein ubiquitination

value: Cytoplasm

value: Belongs to the TNF receptor-associated factor family. A subfamily

description: RING-type

description: TRAF-type

description: TRAF-type

description: MATH

type: Zinc finger

description: TRAF-type

description: TRAF-type

value: Expressed in leukocyte and 22 other cell types or tissues

value: F:tumor necrosis factor receptor binding

value: P:positive regulation of canonical NF-kappaB signal transduction

value: P:positive regulation of gene expression

value: P:regulation of production of molecular mediator of immune response

value: P:tumor necrosis factor-mediated signaling pathway

value: Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2, Chain A

value: Zinc/RING finger domain, C3HC4 (zinc finger)


scientificName: Homo sapiens

commonName: Human

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo

value: Ubiquitin conjugating enzyme E2 F (putative)

value: Belongs to the ubiquitin-conjugating enzyme family

value: Lacks conserved residue(s) required for the propagation of feature annotation

description: UBC core

description: Disordered

authoringGroup: International Human Genome Sequencing Consortium

authors:
Lander E.S.
Linton L.M.
Birren B.
Nusbaum C.
Zody M.C.
Baldwin J.
Devon K.
Dewar K.
Doyle M.
FitzHugh W.
Funke R.
Gage D.
Harris K.
Heaford A.
Howland J.
Kann L.
Lehoczky J.
LeVine R.
McEwan P.
McKernan K.
Meldrim J.
Mesirov J.P.
Miranda C.
Morris W.
Naylor J.
Raymond C.
Rosetti M.
Santos R.
Sheridan A.
Sougnez C.
Stange-Thomann N.
Stojanovic N.
Subramanian A.
Wyman D.
Rogers J.
Sulston J.
Ainscough R.
Beck S.
Bentley D.
Burton J.
Clee C.
Carter N.
Coulson A.
Deadman R.
Deloukas P.
Dunham A.
Dunham I.
Durbin R.
French L.
Grafham D.
Gregory S.
Hubbard T.
Humphray S.
Hunt A.
Jones M.
Lloyd C.
McMurray A.
Matthews L.
Mercer S.
Milne S.
Mullikin J.C.
Mungall A.
Plumb R.
Ross M.
Shownkeen R.
Sims S.
Waterston R.H.
Wilson R.K.
Hillier L.W.
McPherson J.D.
Marra M.A.
Mardis E.R.
Fulton L.A.
Chinwalla A.T.
Pepin K.H.
Gish W.R.
Chissoe S.L.
Wendl M.C.
Delehaunty K.D.
Miner T.L.
Delehaunty A.
Kramer J.B.
Cook L.L.
Fulton R.S.
Johnson D.L.
Minx P.J.
Clifton S.W.
Hawkins T.
Branscomb E.
Predki P.
Richardson P.
Wenning S.
Slezak T.
Doggett N.
Cheng J.F.
Olsen A.
Lucas S.
Elkin C.
Uberbacher E.
Frazier M.
Gibbs R.A.
Muzny D.M.
Scherer S.E.
Bouck J.B.
Sodergren E.J.
Worley K.C.
Rives C.M.
Gorrell J.H.
Metzker M.L.
Naylor S.L.
Kucherlapati R.S.
Nelson D.L.
Weinstock G.M.
Sakaki Y.
Fujiyama A.
Hattori M.
Yada T.
Toyoda A.
Itoh T.
Kawagoe C.
Watanabe H.
Totoki Y.
Taylor T.
Weissenbach J.
Heilig R.
Saurin W.
Artiguenave F.
Brottier P.
Bruls T.
Pelletier E.
Robert C.
Wincker P.
Smith D.R.
Doucette-Stamm L.
Rubenfield M.
Weinstock K.
Lee H.M.
Dubois J.
Rosenthal A.
Platzer M.
Nyakatura G.
Taudien S.
Rump A.
Yang H.
Yu J.
Wang J.
Huang G.
Gu J.
Hood L.
Rowen L.
Madan A.
Qin S.
Davis R.W.
Federspiel N.A.
Abola A.P.
Proctor M.J.
Myers R.M.
Schmutz J.
Dickson M.
Grimwood J.
Cox D.R.
Olson M.V.
Kaul R.
Raymond C.
Shimizu N.
Kawasaki K.
Minoshima S.
Evans G.A.
Athanasiou M.
Schultz R.
Roe B.A.
Chen F.
Pan H.
Ramser J.
Lehrach H.
Reinhardt R.
McCombie W.R.
de la Bastide M.
Dedhia N.
Blocker H.
Hornischer K.
Nordsiek G.
Agarwala R.
Aravind L.
Bailey J.A.
Bateman A.
Batzoglou S.
Birney E.
Bork P.
Brown D.G.
Burge C.B.
Cerutti L.
Chen H.C.
Church D.
Clamp M.
Copley R.R.
Doerks T.
Eddy S.R.
Eichler E.E.
Furey T.S.
Galagan J.
Gilbert J.G.
Harmon C.
Hayashizaki Y.
Haussler D.
Hermjakob H.
Hokamp K.
Jang W.
Johnson L.S.
Jones T.A.
Kasif S.
Kaspryzk A.
Kennedy S.
Kent W.J.
Kitts P.
Koonin E.V.
Korf I.
Kulp D.
Lancet D.
Lowe T.M.
McLysaght A.
Mikkelsen T.
Moran J.V.
Mulder N.
Pollara V.J.
Ponting C.P.
Schuler G.
Schultz J.
Slater G.
Smit A.F.
Stupka E.
Szustakowski J.
Thierry-Mieg D.
Thierry-Mieg J.
Wagner L.
Wallis J.
Wheeler R.
Williams A.
Wolf Y.I.
Wolfe K.H.
Yang S.P.
Yeh R.F.
Collins F.
Guyer M.S.
Peterson J.
Felsenfeld A.
Wetterstrand K.A.
Patrinos A.
Morgan M.J.
de Jong P.
Catanese J.J.
Osoegawa K.
Shizuya H.
Choi S.
Chen Y.J.

title: Initial sequencing and analysis of the human genome.

title: Finishing the euchromatic sequence of the human genome.

authors:
Hillier L.W.
Graves T.A.
Fulton R.S.
Fulton L.A.
Pepin K.H.
Minx P.
Wagner-McPherson C.
Layman D.
Wylie K.
Sekhon M.
Becker M.C.
Fewell G.A.
Delehaunty K.D.
Miner T.L.
Nash W.E.
Kremitzki C.
Oddy L.
Du H.
Sun H.
Bradshaw-Cordum H.
Ali J.
Carter J.
Cordes M.
Harris A.
Isak A.
van Brunt A.
Nguyen C.
Du F.
Courtney L.
Kalicki J.
Ozersky P.
Abbott S.
Armstrong J.
Belter E.A.
Caruso L.
Cedroni M.
Cotton M.
Davidson T.
Desai A.
Elliott G.
Erb T.
Fronick C.
Gaige T.
Haakenson W.
Haglund K.
Holmes A.
Harkins R.
Kim K.
Kruchowski S.S.
Strong C.M.
Grewal N.
Goyea E.
Hou S.
Levy A.
Martinka S.
Mead K.
McLellan M.D.
Meyer R.
Randall-Maher J.
Tomlinson C.
Dauphin-Kohlberg S.
Kozlowicz-Reilly A.
Shah N.
Swearengen-Shahid S.
Snider J.
Strong J.T.
Thompson J.
Yoakum M.
Leonard S.
Pearman C.
Trani L.
Radionenko M.
Waligorski J.E.
Wang C.
Rock S.M.
Tin-Wollam A.M.
Maupin R.
Latreille P.
Wendl M.C.
Yang S.P.
Pohl C.
Wallis J.W.
Spieth J.
Bieri T.A.
Berkowicz N.
Nelson J.O.
Osborne J.
Ding L.
Meyer R.
Sabo A.
Shotland Y.
Sinha P.
Wohldmann P.E.
Cook L.L.
Hickenbotham M.T.
Eldred J.
Williams D.
Jones T.A.
She X.
Ciccarelli F.D.
Izaurralde E.
Taylor J.
Schmutz J.
Myers R.M.
Cox D.R.
Huang X.
McPherson J.D.
Mardis E.R.
Clifton S.W.
Warren W.C.
Chinwalla A.T.
Eddy S.R.
Marra M.A.
Ovcharenko I.
Furey T.S.
Miller W.
Eichler E.E.
Bork P.
Suyama M.
Torrents D.
Waterston R.H.
Wilson R.K.

title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.

database: EMBL

database: SMR

database: MassIVE

database: ProteomicsDB

key: GeneId

database: UCSC

key: OrganismName

value: human

database: HGNC

database: VEuPathDB

database: OrthoDB

value: Chromosome 2

value: Expressed in body of pancreas and 189 other cell types or tissues

value: baseline and differential

database: CDD

key: MatchStatus

value: Ubiquitin Conjugating Enzyme

database: InterPro

value: UBC

database: SUPFAM

value: UBC-like

database: PROSITE


scientificName: Oryctolagus cuniculus

commonName: Rabbit

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Lagomorpha Leporidae Oryctolagus

value: E2 ubiquitin-conjugating enzyme

name: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.

source: RuleBase

description: UBC core

description: Glycyl thioester intermediate

authors:
Lindblad-Toh K.
Garber M.
Zuk O.
Lin M.F.
Parker B.J.
Washietl S.
Kheradpour P.
Ernst J.
Jordan G.
Mauceli E.
Ward L.D.
Lowe C.B.
Holloway A.K.
Clamp M.
Gnerre S.
Alfoldi J.
Beal K.
Chang J.
Clawson H.
Cuff J.
Di Palma F.
Fitzgerald S.
Flicek P.
Guttman M.
Hubisz M.J.
Jaffe D.B.
Jungreis I.
Kent W.J.
Kostka D.
Lara M.
Martins A.L.
Massingham T.
Moltke I.
Raney B.J.
Rasmussen M.D.
Robinson J.
Stark A.
Vilella A.J.
Wen J.
Xie X.
Zody M.C.
Baldwin J.
Bloom T.
Chin C.W.
Heiman D.
Nicol R.
Nusbaum C.
Young S.
Wilkinson J.
Worley K.C.
Kovar C.L.
Muzny D.M.
Gibbs R.A.
Cree A.
Dihn H.H.
Fowler G.
Jhangiani S.
Joshi V.
Lee S.
Lewis L.R.
Nazareth L.V.
Okwuonu G.
Santibanez J.
Warren W.C.
Mardis E.R.
Weinstock G.M.
Wilson R.K.
Delehaunty K.
Dooling D.
Fronik C.
Fulton L.
Fulton B.
Graves T.
Minx P.
Sodergren E.
Birney E.
Margulies E.H.
Herrero J.
Green E.D.
Haussler D.
Siepel A.
Goldman N.
Pollard K.S.
Pedersen J.S.
Lander E.S.
Kellis M.

database: PubMed

database: DOI

title: A high-resolution map of human evolutionary constraint using 29 mammals.

value: Thorbecke inbred

value: Thorbecke

key: ProteinId

database: RefSeq

database: FunCoup

database: STRING

database: PaxDb

database: Ensembl

database: GeneID

database: KEGG

database: CTD

database: eggNOG

key: ToxonomicScope

value: Eukaryota

database: GeneTree

database: Proteomes

value: Chromosome 1

database: Bgee

value: Expressed in blood and 20 other cell types or tissues


source: Ensembl

value: small monomeric GTPase

value: RHOJ

GTP + H2O = GDP + phosphate + H(+)

database: Rhea

database: ChEBI

value: Belongs to the small GTPase superfamily. Rab family

description: Switch-I

description: Switch-II

description: Disordered

description: Basic and acidic residues

authors:
Heilig R.
Eckenberg R.
Petit J.L.
Fonknechten N.
Da Silva C.
Cattolico L.
Levy M.
Barbe V.
de Berardinis V.
Ureta-Vidal A.
Pelletier E.
Vico V.
Anthouard V.
Rowen L.
Madan A.
Qin S.
Sun H.
Du H.
Pepin K.
Artiguenave F.
Robert C.
Cruaud C.
Bruls T.
Jaillon O.
Friedlander L.
Samson G.
Brottier P.
Cure S.
Segurens B.
Aniere F.
Samain S.
Crespeau H.
Abbasi N.
Aiach N.
Boscus D.
Dickhoff R.
Dors M.
Dubois I.
Friedman C.
Gouyvenoux M.
James R.
Madan A.
Mairey-Estrada B.
Mangenot S.
Martins N.
Menard M.
Oztas S.
Ratcliffe A.
Shaffer T.
Trask B.
Vacherie B.
Bellemere C.
Belser C.
Besnard-Gonnet M.
Bartol-Mavel D.
Boutard M.
Briez-Silla S.
Combette S.
Dufosse-Laurent V.
Ferron C.
Lechaplais C.
Louesse C.
Muselet D.
Magdelenat G.
Pateau E.
Petit E.
Sirvain-Trukniewicz P.
Trybou A.
Vega-Czarny N.
Bataille E.
Bluet E.
Bordelais I.
Dubois M.
Dumont C.
Guerin T.
Haffray S.
Hammadi R.
Muanga J.
Pellouin V.
Robert D.
Wunderle E.
Gauguet G.
Roy A.
Sainte-Marthe L.
Verdier J.
Verdier-Discala C.
Hillier L.
Fulton L.
McPherson J.
Matsuda F.
Wilson R.
Scarpelli C.
Gyapay G.
Wincker P.
Saurin W.
Quetier F.
Waterston R.
Hood L.
Weissenbach J.

title: The DNA sequence and analysis of human chromosome 14.

database: EMBL

key: Status

key: MoleculeType

database: AlphaFoldDB

database: SMR

database: SwissPalm

database: MassIVE

database: ProteomicsDB

database: UCSC

database: HGNC

value: Expressed in tendon of biceps brachii and 162 other cell types or tissues

value: P:small GTPase-mediated signal transduction

value: P-loop containing nucleotide triphosphate hydrolases

value: P-loop containing nucleoside triphosphate hydrolases


scientificName: Drosophila melanogaster

source: EMBL

source: FlyBase

description: Disordered

description: Disordered

description: Basic and acidic residues

description: Low complexity

description: Low complexity

description: Basic and acidic residues

description: Acidic residues

value: mRNA

database: RefSeq

key: Description

database: DNASU

database: GeneID

database: AGR

database: FlyBase

database: VEuPathDB

database: HOGENOM

database: OMA

database: OrthoDB

database: BioGRID-ORCS

key: hits

value: 0 hits in 1 CRISPR screen

value: Expressed in posterior terminal follicle cell in ovary and 115 other cell types or tissues

database: CDD

database: InterPro

database: PANTHER

value: RIBOSOMAL L1 DOMAIN-CONTAINING PROTEIN CG13096

database: Pfam

database: SUPFAM

value: Ribosomal protein L1


value: Nuclear prelamin A recognition factor

value: Iron-only hydrogenase-like protein 2

value: NARF

value: Interacts with LMNA and binds to the farnesylated C-terminal domain

value: Nucleus

value: Belongs to the NARF family

description: Iron hydrogenase large subunit C-terminal

source: Pfam

description: Disordered

description: Basic and acidic residues

database: PubMed

database: DOI

authors:
Zody M.C.
Garber M.
Adams D.J.
Sharpe T.
Harrow J.
Lupski J.R.
Nicholson C.
Searle S.M.
Wilming L.
Young S.K.
Abouelleil A.
Allen N.R.
Bi W.
Bloom T.
Borowsky M.L.
Bugalter B.E.
Butler J.
Chang J.L.
Chen C.K.
Cook A.
Corum B.
Cuomo C.A.
de Jong P.J.
DeCaprio D.
Dewar K.
FitzGerald M.
Gilbert J.
Gibson R.
Gnerre S.
Goldstein S.
Grafham D.V.
Grocock R.
Hafez N.
Hagopian D.S.
Hart E.
Norman C.H.
Humphray S.
Jaffe D.B.
Jones M.
Kamal M.
Khodiyar V.K.
LaButti K.
Laird G.
Lehoczky J.
Liu X.
Lokyitsang T.
Loveland J.
Lui A.
Macdonald P.
Major J.E.
Matthews L.
Mauceli E.
McCarroll S.A.
Mihalev A.H.
Mudge J.
Nguyen C.
Nicol R.
O'Leary S.B.
Osoegawa K.
Schwartz D.C.
Shaw-Smith C.
Stankiewicz P.
Steward C.
Swarbreck D.
Venkataraman V.
Whittaker C.A.
Yang X.
Zimmer A.R.
Bradley A.
Hubbard T.
Birren B.W.
Rogers J.
Lander E.S.
Nusbaum C.

title: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.

authors:
Zhou H.
Di Palma S.
Preisinger C.
Peng M.
Polat A.N.
Heck A.J.
Mohammed S.

title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

journal: J. Proteome Res.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

source: PubMed

database: EMBL

database: AlphaFoldDB

database: SMR

database: MassIVE

database: Ensembl

database: UCSC

value: human

database: GeneTree

database: ChiTaRS

database: Proteomes

key: Component

value: Expressed in left testis and 198 other cell types or tissues

value: Cytosolic Fe-S cluster assembly factor NAR1


value: EFHB C-terminal EF-hand domain-containing protein

description: EFHB C-terminal EF-hand

authors:
Adams M.D.
Celniker S.E.
Holt R.A.
Evans C.A.
Gocayne J.D.
Amanatides P.G.
Scherer S.E.
Li P.W.
Hoskins R.A.
Galle R.F.
George R.A.
Lewis S.E.
Richards S.
Ashburner M.
Henderson S.N.
Sutton G.G.
Wortman J.R.
Yandell M.D.
Zhang Q.
Chen L.X.
Brandon R.C.
Rogers Y.H.
Blazej R.G.
Champe M.
Pfeiffer B.D.
Wan K.H.
Doyle C.
Baxter E.G.
Helt G.
Nelson C.R.
Gabor G.L.
Abril J.F.
Agbayani A.
An H.J.
Andrews-Pfannkoch C.
Baldwin D.
Ballew R.M.
Basu A.
Baxendale J.
Bayraktaroglu L.
Beasley E.M.
Beeson K.Y.
Benos P.V.
Berman B.P.
Bhandari D.
Bolshakov S.
Borkova D.
Botchan M.R.
Bouck J.
Brokstein P.
Brottier P.
Burtis K.C.
Busam D.A.
Butler H.
Cadieu E.
Center A.
Chandra I.
Cherry J.M.
Cawley S.
Dahlke C.
Davenport L.B.
Davies P.
de Pablos B.
Delcher A.
Deng Z.
Mays A.D.
Dew I.
Dietz S.M.
Dodson K.
Doup L.E.
Downes M.
Dugan-Rocha S.
Dunkov B.C.
Dunn P.
Durbin K.J.
Evangelista C.C.
Ferraz C.
Ferriera S.
Fleischmann W.
Fosler C.
Gabrielian A.E.
Garg N.S.
Gelbart W.M.
Glasser K.
Glodek A.
Gong F.
Gorrell J.H.
Gu Z.
Guan P.
Harris M.
Harris N.L.
Harvey D.
Heiman T.J.
Hernandez J.R.
Houck J.
Hostin D.
Houston K.A.
Howland T.J.
Wei M.H.
Ibegwam C.
Jalali M.
Kalush F.
Karpen G.H.
Ke Z.
Kennison J.A.
Ketchum K.A.
Kimmel B.E.
Kodira C.D.
Kraft C.
Kravitz S.
Kulp D.
Lai Z.
Lasko P.
Lei Y.
Levitsky A.A.
Li J.
Li Z.
Liang Y.
Lin X.
Liu X.
Mattei B.
McIntosh T.C.
McLeod M.P.
McPherson D.
Merkulov G.
Milshina N.V.
Mobarry C.
Morris J.
Moshrefi A.
Mount S.M.
Moy M.
Murphy B.
Murphy L.
Muzny D.M.
Nelson D.L.
Nelson D.R.
Nelson K.A.
Nixon K.
Nusskern D.R.
Pacleb J.M.
Palazzolo M.
Pittman G.S.
Pan S.
Pollard J.
Puri V.
Reese M.G.
Reinert K.
Remington K.
Saunders R.D.
Scheeler F.
Shen H.
Shue B.C.
Siden-Kiamos I.
Simpson M.
Skupski M.P.
Smith T.
Spier E.
Spradling A.C.
Stapleton M.
Strong R.
Sun E.
Svirskas R.
Tector C.
Turner R.
Venter E.
Wang A.H.
Wang X.
Wang Z.Y.
Wassarman D.A.
Weinstock G.M.
Weissenbach J.
Williams S.M.
WoodageT
Worley K.C.
Wu D.
Yang S.
Yao Q.A.
Ye J.
Yeh R.F.
Zaveri J.S.
Zhan M.
Zhang G.
Zhao Q.
Zheng L.
Zheng X.H.
Zhong F.N.
Zhong W.
Zhou X.
Zhu S.
Zhu X.
Smith H.O.
Gibbs R.A.
Myers E.W.
Rubin G.M.
Venter J.C.

value: Berkeley

authors:
Celniker S.E.
Wheeler D.A.
Kronmiller B.
Carlson J.W.
Halpern A.
Patel S.
Adams M.
Champe M.
Dugan S.P.
Frise E.
Hodgson A.
George R.A.
Hoskins R.A.
Laverty T.
Muzny D.M.
Nelson C.R.
Pacleb J.M.
Park S.
Pfeiffer B.D.
Richards S.
Sodergren E.J.
Svirskas R.
Tabor P.E.
Wan K.
Stapleton M.
Sutton G.G.
Venter C.
Weinstock G.
Scherer S.E.
Myers E.W.
Gibbs R.A.
Rubin G.M.

authors:
Misra S.
Crosby M.A.
Mungall C.J.
Matthews B.B.
Campbell K.S.
Hradecky P.
Huang Y.
Kaminker J.S.
Millburn G.H.
Prochnik S.E.
Smith C.D.
Tupy J.L.
Whitfied E.J.
Bayraktaroglu L.
Berman B.P.
Bettencourt B.R.
Celniker S.E.
de Grey A.D.
Drysdale R.A.
Harris N.L.
Richter J.
Russo S.
Schroeder A.J.
Shu S.Q.
Stapleton M.
Yamada C.
Ashburner M.
Gelbart W.M.
Rubin G.M.
Lewis S.E.

authors:
Kaminker J.S.
Bergman C.M.
Kronmiller B.
Carlson J.
Svirskas R.
Patel S.
Frise E.
Wheeler D.A.
Lewis S.E.
Rubin G.M.
Ashburner M.
Celniker S.E.

authors:
Hoskins R.A.
Smith C.D.
Carlson J.W.
Carvalho A.B.
Halpern A.
Kaminker J.S.
Kennedy C.
Mungall C.J.
Sullivan B.A.
Sutton G.G.
Yasuhara J.C.
Wakimoto B.T.
Myers E.W.
Celniker S.E.
Rubin G.M.
Karpen G.H.

title: Combined evidence annotation of transposable elements in genome sequences.

title: The Release 5.1 annotation of Drosophila melanogaster heterochromatin.

title: Sequence finishing and mapping of Drosophila melanogaster heterochromatin.

title: Gene Model Annotations for Drosophila melanogaster: Impact of High-Throughput Data.

journal: G3 (Bethesda)

title: Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.

title: The Release 6 reference sequence of the Drosophila melanogaster genome.

value: Expressed in mid-late elongation-stage spermatid (Drosophila) in testis and 20 other cell types or tissues


value: Nuclear hormone receptor FTZ-F1

value: Nuclear receptor subfamily 5 group A member 3

value: beta FTZ-F1

value: beta Ftz-f1

value: FTZ-Fl

value: Belongs to the nuclear hormone receptor family. NR5 subfamily

description: Nuclear receptor

description: NR LBD

type: DNA binding

description: Nuclear receptor

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Low complexity

description: Basic residues

description: Low complexity

description: Gly residues

description: Low complexity

description: Gly residues

description: Gly residues

description: Low complexity

description: Gly residues

title: The genome sequence of Drosophila melanogaster.

title: Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence.

title: Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.

title: The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective.

title: Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.

authors:
Quesneville H.
Bergman C.M.
Andrieu O.
Autard D.
Nouaud D.
Ashburner M.
Anxolabehere D.

authors:
Smith C.D.
Shu S.
Mungall C.J.
Karpen G.H.

authors:
Hoskins R.A.
Carlson J.W.
Kennedy C.
Acevedo D.
Evans-Holm M.
Frise E.
Wan K.H.
Park S.
Mendez-Lago M.
Rossi F.
Villasante A.
Dimitri P.
Karpen G.H.
Celniker S.E.

authors:
Matthews B.B.
Dos Santos G.
Crosby M.A.
Emmert D.B.
St Pierre S.E.
Gramates L.S.
Zhou P.
Schroeder A.J.
Falls K.
Strelets V.
Russo S.M.
Gelbart W.M.

authors:
Crosby M.A.
Gramates L.S.
Dos Santos G.
Matthews B.B.
St Pierre S.E.
Zhou P.
Schroeder A.J.
Falls K.
Emmert D.B.
Russo S.M.
Gelbart W.M.

value: Expressed in adult Malpighian tubule stellate cell of main segment in Malpighian tubule and 285 other cell types or tissues

value: Erythroid Transcription Factor GATA-1, subunit A

value: Glucocorticoid receptor-like (DNA-binding domain)


value: Cyclin A, isoform C

value: CycA

value: Cyc A

value: CYCA

value: cycA

value: CYCLIN A

value: cyclin A

value: CyclinA

value: dCycA

value: DmcycA

value: hari

value: Belongs to the cyclin family

description: Cyclin-like

source: SMART

description: Cyclin C-terminal

description: Cyclin-like

description: Disordered

authors:
Hoskins R.A.
Carlson J.W.
Wan K.H.
Park S.
Mendez I.
Galle S.E.
Booth B.W.
Pfeiffer B.D.
George R.A.
Svirskas R.
Krzywinski M.
Schein J.
Accardo M.C.
Damia E.
Messina G.
Mendez-Lago M.
de Pablos B.
Demakova O.V.
Andreyeva E.N.
Boldyreva L.V.
Marra M.
Carvalho A.B.
Dimitri P.
Villasante A.
Zhimulev I.F.
Rubin G.M.
Karpen G.H.
Celniker S.E.

value: Expressed in egg cell and 109 other cell types or tissues


source: Google

value: Transmembrane protein 268

description: Helical

description: Helical

description: Disordered

description: Disordered

description: Basic and acidic residues

description: Polar residues

description: Low complexity

description: Low complexity

description: Low complexity

value: Berkeley

value: Expressed in spermatocyte cyst cell (Drosophila) in testis and 119 other cell types or tissues


source: Proteomes

value: Serine incorporator, isoform C

value: Serinc

value: DmSERINC

value: SERINC

value: Membrane

value: Multi-pass membrane protein

value: Belongs to the TDE1 family

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Disordered

description: Basic and acidic residues

value: Expressed in oviduct (Drosophila) and 257 other cell types or tissues


value: Regeneration, isoform B

value: Regeneration, isoform C

value: rgn

value: RGN

value: Lacks conserved residue(s) required for the propagation of feature annotation

description: C-type lectin

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Disordered

description: Basic residues

description: Polar residues

description: Basic and acidic residues

description: Low complexity

description: Basic and acidic residues

description: Basic and acidic residues

authors:
Celniker S.
Carlson J.
Wan K.
Frise E.
Hoskins R.
Park S.
Svirskas R.
Rubin G.

authors:
Celniker S.
Carlson J.
Wan K.
Pfeiffer B.
Frise E.
George R.
Hoskins R.
Stapleton M.
Pacleb J.
Park S.
Svirskas R.
Smith E.
Yu C.
Rubin G.

title: Drosophila melanogaster release 4 sequence.

value: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)

value: Retrograde transport at the Trans-Golgi-Network

value: Cargo recognition for clathrin-mediated endocytosis

value: Expressed in peripheral glial cell (Drosophila) in proboscis and 258 other cell types or tissues

value: TRANS-GOLGI NETWORK INTEGRAL MEMBRANE PROTEIN 2

value: TRANS-GOLGI NETWORK INTEGRAL MEMBRANE PROTEIN TGN38


value: Krev interaction trapped protein 1

value: Krev interaction trapped 1

value: Cerebral cavernous malformations 1 protein

source: UniProtKB

value: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Microtubule-associated protein that binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes in a GTP-bound RAP1-dependent manner. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels. May play a role in the regulation of macroautophagy through the down-regulation of the mTOR pathway (PubMed:26417067)

value: Interacts with CDH5 (PubMed:20332120). Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (via C-terminus FERM domain) with RAP1A (active GTP-bound form preferentially); the interaction does not induce the opening conformation of KRIT1. Interacts (via FERM domain) with RAP1B. Interacts (via N-terminus NPXY motif) with ITGB1BP1; the interaction induces the opening conformation of KRIT1 and competes with ITGB1 for ITGB1BP1 interaction. Interacts with HEG1 and CCM2; greatly facilitates CCM2-binding to HEG1. Associates (via N-terminus and C-terminus regions) with microtubules; the interaction is inhibited in presence of ITGB1BP1 and active GTP-bound RAP1A

commentType: INTERACTION

value: KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Association with RAP1 relocalizes KRIT1 from microtubules to cell junction membranes. Translocates from the cytoplasm along microtubules to the cell membrane in a ITGB1BP1-dependent manner

value: Cytoplasm, cytoskeleton

value: Cell membrane

value: Peripheral membrane protein

value: Cell junction

commentType: ALTERNATIVE PRODUCTS

isoformSequenceStatus: Displayed

isoformSequenceStatus: Described

value: Low levels in brain. Very weak expression found in heart and muscle

commentType: TISSUE SPECIFICITY

value: The FERM domain mediates binding to RAP1A and RAP1B and is necessary for binding to phosphatidylinositol 4,5-bisphosphate (PIP2)

value: The N-terminal domain has structural similarity to the nudix hydrolase domain, despite the absence of a nudix box and low sequence similarity with nudix hydrolase domains. The N-terminus and the C-terminus part associate together via the NPAY binding motif and adopt a lose conformation that is disrupted by ITGB1BP1, but not by RAP1A

value: Contains 4 ANK repeats that precede the FERM domain

commentType: DISEASE

diseaseId: Cerebral cavernous malformations 1

description: A form of cerebral cavernous malformations, a congenital vascular anomaly of the central nervous system that can result in hemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. The lesions are characterized by grossly enlarged blood vessels consisting of a single layer of endothelium and without any intervening neural tissue, ranging in diameter from a few millimeters to several centimeters. CCM1 inheritance is autosomal dominant.

database: MIM

value: The disease is caused by variants affecting the gene represented in this entry

description: Krev interaction trapped protein 1

description: ANK 1

description: ANK 2

description: ANK 3

description: ANK 4

description: FERM

description: N-terminal domain similar to Nudix hydrolase domain

description: Interaction with ITGB1BP1

description: Interaction with RAP1B

type: Alternative sequence

description: in isoform 2

description: in isoform 3

type: Natural variant

description: in CCM1

originalSequence: F

description: in CCM1

originalSequence: K

type: Mutagenesis

description: Reduces interaction with microtubules, but not with ITGB1BP1.

originalSequence: KKRK

description: Strongly reduces ITGB1BP1 binding; when associated with D-182.

description: Strongly reduces ITGB1BP1 binding; when associated with A-179.

description: Strongly reduces ITGB1BP1 binding; when associated with D-176.

description: Reduces interaction with ITGB1BP1.

description: Reduces ITGB1BP1 binding; when associated with A-195.

description: Reduces ITGB1BP1 binding; when associated with A-192.

description: Impairs interaction with RAP1B.

description: Impairs interaction with RAP1B.

description: 40-fold-reduced affinity for Rap1A.

description: Impairs interaction with RAP1B.

description: Strongly reduced affinity for HEG1; when associated with A-721.

description: Strongly reduced affinity for HEG1; when associated with A-717.

description: in Ref. 5; AAQ94072

description: in Ref. 1; AAB58582

description: in Ref. 1; AAB58582, 2; AAG47774 and 5; AAQ94072

authors:
Serebriiskii I.
Estojak J.
Sonoda G.
Testa J.R.
Golemis E.A.

title: Association of Krev-1/rap1a with Krit1, a novel ankyrin repeat-containing protein encoded by a gene mapping to 7q21-22.

referencePositions:
NUCLEOTIDE SEQUENCE [GENOMIC DNA]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)
TISSUE SPECIFICITY
INTERACTION WITH RAP1A

authors:
Zhang J.
Clatterbuck R.E.
Rigamonti D.
Dietz H.C.

title: Cloning of the murine Krit1 cDNA reveals novel mammalian 5' coding exons.

authors:
Sahoo T.
Goenaga-Diaz E.
Serebriiskii I.G.
Thomas J.W.
Kotova E.
Cuellar J.G.
Peloquin J.M.
Golemis E.
Beitinjaneh F.
Green E.D.
Johnson E.W.
Marchuk D.A.

title: Computational and experimental analyses reveal previously undetected coding exons of the KRIT1 (CCM1) gene.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
ALTERNATIVE SPLICING

authors:
Kehrer-Sawatzki H.
Wilda M.
Braun V.M.
Richter H.-P.
Hameister H.

title: Mutation and expression analysis of the KRIT1 gene associated with cerebral cavernous malformations (CCM1).

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
ALTERNATIVE SPLICING
VARIANTS CCM1 SER-97 AND GLU-569

authors:
Ferrera L.
Marini V.
Dorcaratto A.
Pigatto F.
Alberti F.
Forni M.
Cama A.
Viale G.
Origone P.
Mareni C.
Garre' C.

title: Four novel and three known KRIT1 mutations in CCM Italian patients: Characterization at mRNA and protein level.

authors:
Ota T.
Suzuki Y.
Nishikawa T.
Otsuki T.
Sugiyama T.
Irie R.
Wakamatsu A.
Hayashi K.
Sato H.
Nagai K.
Kimura K.
Makita H.
Sekine M.
Obayashi M.
Nishi T.
Shibahara T.
Tanaka T.
Ishii S.
Yamamoto J.
Saito K.
Kawai Y.
Isono Y.
Nakamura Y.
Nagahari K.
Murakami K.
Yasuda T.
Iwayanagi T.
Wagatsuma M.
Shiratori A.
Sudo H.
Hosoiri T.
Kaku Y.
Kodaira H.
Kondo H.
Sugawara M.
Takahashi M.
Kanda K.
Yokoi T.
Furuya T.
Kikkawa E.
Omura Y.
Abe K.
Kamihara K.
Katsuta N.
Sato K.
Tanikawa M.
Yamazaki M.
Ninomiya K.
Ishibashi T.
Yamashita H.
Murakawa K.
Fujimori K.
Tanai H.
Kimata M.
Watanabe M.
Hiraoka S.
Chiba Y.
Ishida S.
Ono Y.
Takiguchi S.
Watanabe S.
Yosida M.
Hotuta T.
Kusano J.
Kanehori K.
Takahashi-Fujii A.
Hara H.
Tanase T.-O.
Nomura Y.
Togiya S.
Komai F.
Hara R.
Takeuchi K.
Arita M.
Imose N.
Musashino K.
Yuuki H.
Oshima A.
Sasaki N.
Aotsuka S.
Yoshikawa Y.
Matsunawa H.
Ichihara T.
Shiohata N.
Sano S.
Moriya S.
Momiyama H.
Satoh N.
Takami S.
Terashima Y.
Suzuki O.
Nakagawa S.
Senoh A.
Mizoguchi H.
Goto Y.
Shimizu F.
Wakebe H.
Hishigaki H.
Watanabe T.
Sugiyama A.
Takemoto M.
Kawakami B.
Yamazaki M.
Watanabe K.
Kumagai A.
Itakura S.
Fukuzumi Y.
Fujimori Y.
Komiyama M.
Tashiro H.
Tanigami A.
Fujiwara T.
Ono T.
Yamada K.
Fujii Y.
Ozaki K.
Hirao M.
Ohmori Y.
Kawabata A.
Hikiji T.
Kobatake N.
Inagaki H.
Ikema Y.
Okamoto S.
Okitani R.
Kawakami T.
Noguchi S.
Itoh T.
Shigeta K.
Senba T.
Matsumura K.
Nakajima Y.
Mizuno T.
Morinaga M.
Sasaki M.
Togashi T.
Oyama M.
Hata H.
Watanabe M.
Komatsu T.
Mizushima-Sugano J.
Satoh T.
Shirai Y.
Takahashi Y.
Nakagawa K.
Okumura K.
Nagase T.
Nomura N.
Kikuchi H.
Masuho Y.
Yamashita R.
Nakai K.
Yada T.
Nakamura Y.
Ohara O.
Isogai T.
Sugano S.

title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3)

authors:
Hillier L.W.
Fulton R.S.
Fulton L.A.
Graves T.A.
Pepin K.H.
Wagner-McPherson C.
Layman D.
Maas J.
Jaeger S.
Walker R.
Wylie K.
Sekhon M.
Becker M.C.
O'Laughlin M.D.
Schaller M.E.
Fewell G.A.
Delehaunty K.D.
Miner T.L.
Nash W.E.
Cordes M.
Du H.
Sun H.
Edwards J.
Bradshaw-Cordum H.
Ali J.
Andrews S.
Isak A.
Vanbrunt A.
Nguyen C.
Du F.
Lamar B.
Courtney L.
Kalicki J.
Ozersky P.
Bielicki L.
Scott K.
Holmes A.
Harkins R.
Harris A.
Strong C.M.
Hou S.
Tomlinson C.
Dauphin-Kohlberg S.
Kozlowicz-Reilly A.
Leonard S.
Rohlfing T.
Rock S.M.
Tin-Wollam A.-M.
Abbott A.
Minx P.
Maupin R.
Strowmatt C.
Latreille P.
Miller N.
Johnson D.
Murray J.
Woessner J.P.
Wendl M.C.
Yang S.-P.
Schultz B.R.
Wallis J.W.
Spieth J.
Bieri T.A.
Nelson J.O.
Berkowicz N.
Wohldmann P.E.
Cook L.L.
Hickenbotham M.T.
Eldred J.
Williams D.
Bedell J.A.
Mardis E.R.
Clifton S.W.
Chissoe S.L.
Marra M.A.
Raymond C.
Haugen E.
Gillett W.
Zhou Y.
James R.
Phelps K.
Iadanoto S.
Bubb K.
Simms E.
Levy R.
Clendenning J.
Kaul R.
Kent W.J.
Furey T.S.
Baertsch R.A.
Brent M.R.
Keibler E.
Flicek P.
Bork P.
Suyama M.
Bailey J.A.
Portnoy M.E.
Torrents D.
Chinwalla A.T.
Gish W.R.
Eddy S.R.
McPherson J.D.
Olson M.V.
Eichler E.E.
Green E.D.
Waterston R.H.
Wilson R.K.

title: The DNA sequence of human chromosome 7.

title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)

title: Identification of eight novel 5`-exons in cerebral capillary malformation gene-1 (CCM1) encoding KRIT1.

referencePositions:
NUCLEOTIDE SEQUENCE [MRNA] OF 1-243
ALTERNATIVE SPLICING

authors:
Marini V.
Ferrera L.
Dorcaratto A.
Forni M.
Capra V.
Origone P.
Mareni C.
Garre' C.

title: Six novel and three known KRIT1 mutations in CCM patients: characterization at mRNA level.

referencePositions: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-281

authors:
Zhang J.
Clatterbuck R.E.
Rigamonti D.
Chang D.D.
Dietz H.C.

title: Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation.

referencePositions:
FUNCTION
INTERACTION WITH ITGB1 AND ITGB1BP1
MUTAGENESIS OF ASN-192 AND TYR-195

authors:
Zawistowski J.S.
Serebriiskii I.G.
Lee M.F.
Golemis E.A.
Marchuk D.A.

title: KRIT1 association with the integrin-binding protein ICAP-1: a new direction in the elucidation of cerebral cavernous malformations (CCM1) pathogenesis.

referencePositions:
INTERACTION WITH ITGB1BP1
MUTAGENESIS OF ASN-192 AND TYR-195

authors:
Beraud-Dufour S.
Gautier R.
Albiges-Rizo C.
Chardin P.
Faurobert E.

title: Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1.

referencePositions: IDENTIFICATION IN A COMPLEX WITH ITGB1BP1 AND RAP1A

referencePositions: MUTAGENESIS OF 47-LYS--LYS-50 AND 192-ASN--TYR-195

authors:
Lampugnani M.G.
Orsenigo F.
Rudini N.
Maddaluno L.
Boulday G.
Chapon F.
Dejana E.

title: CCM1 regulates vascular-lumen organization by inducing endothelial polarity.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
INTERACTION WITH CDH5

authors:
Goitre L.
Balzac F.
Degani S.
Degan P.
Marchi S.
Pinton P.
Retta S.F.

title: KRIT1 regulates the homeostasis of intracellular reactive oxygen species.

authors:
Wuestehube J.
Bartol A.
Liebler S.S.
Bruetsch R.
Zhu Y.
Felbor U.
Sure U.
Augustin H.G.
Fischer A.

title: Cerebral cavernous malformation protein CCM1 inhibits sprouting angiogenesis by activating DELTA-NOTCH signaling.

authors:
Liu J.J.
Stockton R.A.
Gingras A.R.
Ablooglu A.J.
Han J.
Bobkov A.A.
Ginsberg M.H.

title: A mechanism of Rap1-induced stabilization of endothelial cell--cell junctions.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
INTERACTION WITH RAP1A
MUTAGENESIS OF ARG-452

authors:
Marchi S.
Corricelli M.
Trapani E.
Bravi L.
Pittaro A.
Delle Monache S.
Ferroni L.
Patergnani S.
Missiroli S.
Goitre L.
Trabalzini L.
Rimessi A.
Giorgi C.
Zavan B.
Cassoni P.
Dejana E.
Retta S.F.
Pinton P.

title: Defective autophagy is a key feature of cerebral cavernous malformations.

authors:
Li X.
Zhang R.
Draheim K.M.
Liu W.
Calderwood D.A.
Boggon T.J.

title: Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1).

referencePositions: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 420-736 IN COMPLEX WITH RAP1B

referencePositions: MUTAGENESIS OF SER-430; ARG-432 AND ARG-452

title: Structural basis of the junctional anchorage of the cerebral cavernous malformations complex.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 417-736 IN COMPLEX WITH HEG1

authors:
Liu W.
Draheim K.M.
Zhang R.
Calderwood D.A.
Boggon T.J.

title: Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 1-198 IN COMPLEX WITH ITGB1BP1

referencePositions: MUTAGENESIS OF ALA-176; ARG-179; PRO-182; ARG-185; ASN-192 AND TYR-195

title: Structural analysis of the KRIT1 ankyrin repeat and FERM domains reveals a conformationally stable ARD-FERM interface.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 259-736

value: Osteosarcoma (U2OS) cell map - Intracellular trafficking and peroxisomes (28 proteins)

value: Familial cerebral cavernous malformation

value: 4 GO annotations based on evolutionary models

value: Expressed in calcaneal tendon and 107 other cell types or tissues

value: P:negative regulation of endothelial cell apoptotic process

value: P:negative regulation of endothelial cell migration

value: P:negative regulation of endothelial cell proliferation

value: P:regulation of establishment of cell polarity

value: P:small GTPase-mediated signal transduction

value: krev interaction trapped protein 1 isoform X1

value: KRIT, N-terminal Nudix domain, NPxY motif-rich region

value: Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1

value: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)


value: Ubiquitin-like-specific protease 2

value: Nucleus

value: Belongs to the peptidase C48 family

description: Ubiquitin-like-specific protease 2

description: Disordered

description: Disordered

description: Disordered

description: Basic and acidic residues

description: Polar residues

description: Low complexity

description: Polar residues

description: Polar residues

description: Acidic residues

type: Modified residue

description: Phosphothreonine

authors:
Wood V.
Gwilliam R.
Rajandream M.A.
Lyne M.H.
Lyne R.
Stewart A.
Sgouros J.G.
Peat N.
Hayles J.
Baker S.G.
Basham D.
Bowman S.
Brooks K.
Brown D.
Brown S.
Chillingworth T.
Churcher C.M.
Collins M.
Connor R.
Cronin A.
Davis P.
Feltwell T.
Fraser A.
Gentles S.
Goble A.
Hamlin N.
Harris D.E.
Hidalgo J.
Hodgson G.
Holroyd S.
Hornsby T.
Howarth S.
Huckle E.J.
Hunt S.
Jagels K.
James K.D.
Jones L.
Jones M.
Leather S.
McDonald S.
McLean J.
Mooney P.
Moule S.
Mungall K.L.
Murphy L.D.
Niblett D.
Odell C.
Oliver K.
O'Neil S.
Pearson D.
Quail M.A.
Rabbinowitsch E.
Rutherford K.M.
Rutter S.
Saunders D.
Seeger K.
Sharp S.
Skelton J.
Simmonds M.N.
Squares R.
Squares S.
Stevens K.
Taylor K.
Taylor R.G.
Tivey A.
Walsh S.V.
Warren T.
Whitehead S.
Woodward J.R.
Volckaert G.
Aert R.
Robben J.
Grymonprez B.
Weltjens I.
Vanstreels E.
Rieger M.
Schaefer M.
Mueller-Auer S.
Gabel C.
Fuchs M.
Duesterhoeft A.
Fritzc C.
Holzer E.
Moestl D.
Hilbert H.
Borzym K.
Langer I.
Beck A.
Lehrach H.
Reinhardt R.
Pohl T.M.
Eger P.
Zimmermann W.
Wedler H.
Wambutt R.
Purnelle B.
Goffeau A.
Cadieu E.
Dreano S.
Gloux S.
Lelaure V.
Mottier S.
Galibert F.
Aves S.J.
Xiang Z.
Hunt C.
Moore K.
Hurst S.M.
Lucas M.
Rochet M.
Gaillardin C.
Tallada V.A.
Garzon A.
Thode G.
Daga R.R.
Cruzado L.
Jimenez J.
Sanchez M.
del Rey F.
Benito J.
Dominguez A.
Revuelta J.L.
Moreno S.
Armstrong J.
Forsburg S.L.
Cerutti L.
Lowe T.
McCombie W.R.
Paulsen I.
Potashkin J.
Shpakovski G.V.
Ussery D.
Barrell B.G.
Nurse P.

title: The genome sequence of Schizosaccharomyces pombe.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

type: STRAIN

authors:
Rhind N.
Chen Z.
Yassour M.
Thompson D.A.
Haas B.J.
Habib N.
Wapinski I.
Roy S.
Lin M.F.
Heiman D.I.
Young S.K.
Furuya K.
Guo Y.
Pidoux A.
Chen H.M.
Robbertse B.
Goldberg J.M.
Aoki K.
Bayne E.H.
Berlin A.M.
Desjardins C.A.
Dobbs E.
Dukaj L.
Fan L.
FitzGerald M.G.
French C.
Gujja S.
Hansen K.
Keifenheim D.
Levin J.Z.
Mosher R.A.
Mueller C.A.
Pfiffner J.
Priest M.
Russ C.
Smialowska A.
Swoboda P.
Sykes S.M.
Vaughn M.
Vengrova S.
Yoder R.
Zeng Q.
Allshire R.
Baulcombe D.
Birren B.W.
Brown W.
Ekwall K.
Kellis M.
Leatherwood J.
Levin H.
Margalit H.
Martienssen R.
Nieduszynski C.A.
Spatafora J.W.
Friedman N.
Dalgaard J.Z.
Baumann P.
Niki H.
Regev A.
Nusbaum C.

title: Comparative functional genomics of the fission yeasts.

authors:
Matsuyama A.
Arai R.
Yashiroda Y.
Shirai A.
Kamata A.
Sekido S.
Kobayashi Y.
Hashimoto A.
Hamamoto M.
Hiraoka Y.
Horinouchi S.
Yoshida M.

title: ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.

journal: Nat. Biotechnol.

referencePositions: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]

authors:
Wilson-Grady J.T.
Villen J.
Gygi S.P.

title: Phosphoproteome analysis of fission yeast.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526

database: PIR

key: EntryName

database: RefSeq

key: NucleotideSequenceId


source: PomBase

value: tRNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in tRNAs at position 49 and 50 (PubMed:30646830). Trm4a and trm4b methylate different sets of tRNAs (PubMed:30646830). Also methylates cytosine to m5C at positions (60, 61 and 62) in tRNA(Asp) (PubMed:23074192)

name: cytidine(49) in tRNA precursor + S-adenosyl-L-methionine = 5-methylcytidine(49) in tRNA precursor + S-adenosyl-L-homocysteine + H(+)

database: Rhea

database: ChEBI

name: cytidine(50) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(50) in tRNA + S-adenosyl-L-homocysteine + H(+)

name: cytidine(60) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(60) in tRNA(Asp) + S-adenosyl-L-homocysteine + H(+)

name: cytidine(61) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(61) in tRNA(Asp) + S-adenosyl-L-homocysteine + H(+)

name: cytidine(62) in tRNA(Asp) + S-adenosyl-L-methionine = 5-methylcytidine(62) in tRNA(Asp) + S-adenosyl-L-homocysteine + H(+)

value: Cells lacking both trm4a and trm4b show a mild resistance to calcium chloride

commentType: DISRUPTION PHENOTYPE

value: Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. TRM4 subfamily

description: Multisite-specific tRNA:(cytosine-C(5))-methyltransferase trm4b

description: Nucleophile

authors:
Becker M.
Muller S.
Nellen W.
Jurkowski T.P.
Jeltsch A.
Ehrenhofer-Murray A.E.

title: Pmt1, a Dnmt2 homolog in Schizosaccharomyces pombe, mediates tRNA methylation in response to nutrient signaling.

authors:
Mueller M.
Samel-Pommerencke A.
Legrand C.
Tuorto F.
Lyko F.
Ehrenhofer-Murray A.E.

title: Division of labour: tRNA methylation by the NSun2 tRNA methyltransferases Trm4a and Trm4b in fission yeast.

referencePositions:
FUNCTION
CATALYTIC ACTIVITY
DISRUPTION PHENOTYPE

value: NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING


value: DNA-directed RNA polymerase, mitochondrial

flag: Precursor

value: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Combines in the mitochondrion with mitochondrial transcription factor mtf1 as a holoenzyme to recognize and initiate transcription at the core mitochondrial promoters

name: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate

source: PROSITE-ProRule

value: Mitochondrion

value: Belongs to the phage and mitochondrial RNA polymerase family

type: Transit peptide

description: Mitochondrion

type: Region

description: Disordered

type: Compositional bias

description: Basic and acidic residues

authors:
Jiang H.
Sun W.
Wang Z.
Zhang J.
Chen D.
Murchie A.I.

title: Identification and characterization of the mitochondrial RNA polymerase and transcription factor in the fission yeast Schizosaccharomyces pombe.

journal: Nucleic Acids Res.

database: BioGRID

key: Interactions

database: FunCoup

key: Number of interactors

database: STRING

database: iPTMnet

database: PaxDb

database: GeneID

database: KEGG

database: PomBase

database: VEuPathDB

database: eggNOG

value: Eukaryota

database: HOGENOM

database: InParanoid

database: OMA

key: Fingerprint

value: C:mitochondrial DNA-directed RNA polymerase complex

value: F:mitochondrial promoter sequence-specific DNA binding

value: P:transcription initiation at mitochondrial promoter

value: 5' to 3' exonuclease, C-terminal subdomain

value: DNA-directed RNA polymerase, N-terminal domain

value: DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL