source: EMBL

source: Proteomes

value: Vacuole membrane protein 1

name: a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out)

name: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out)

name: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out)

value: Endoplasmic reticulum

value: Vacuole membrane

value: Multi-pass membrane protein

value: Belongs to the VMP1 family

type: Transmembrane

description: Helical

description: Helical

description: Helical

description: Helical

description: KMS1 N-terminal

description: Vacuole membrane protein 1 C-terminal helical

description: Disordered

description: Disordered

description: Polar residues

description: Basic and acidic residues

description: Polar residues

description: Basic 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.

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.

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 posterior terminal follicle cell in ovary and 257 other cell types or tissues


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

proteinExistence: 3: Inferred from homology

value: Probable tRNA-splicing endonuclease subunit sen15

value: tRNA-intron endonuclease sen15

value: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body (By similarity)

commentType: FUNCTION

value: tRNA splicing endonuclease is a heterotetramer composed of sen2, sen15, sen34 and sen54. Interacts directly with sen34 (By similarity)

commentType: SUBUNIT

value: Belongs to the SEN15 family

commentType: SIMILARITY

type: Chain

modifier: EXACT

Reference proteome

category: Technical term

tRNA processing

category: Biological process

citationType: journal article

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.

database: PubMed

database: DOI

title: The genome sequence of Schizosaccharomyces pombe.

journal: Nature

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

type: STRAIN

database: EMBL

key: ProteinId

key: Status

key: MoleculeType

database: RefSeq

key: NucleotideSequenceId

database: AlphaFoldDB

key: Description

database: SMR

database: BioGRID

key: Interactions

database: FunCoup

key: Number of interactors

database: STRING

database: PaxDb

database: GeneID

database: KEGG

database: PomBase

key: GeneName

database: VEuPathDB

database: eggNOG

key: ToxonomicScope

value: Eukaryota

database: HOGENOM

database: InParanoid

database: OMA

key: Fingerprint

database: PhylomeDB

database: PRO

database: Proteomes

key: Component

value: Chromosome I

database: GO

key: GoTerm

key: GoEvidenceType

source: PubMed

value: C:tRNA-intron endonuclease complex

value: F:nucleic acid binding

value: P:tRNA-type intron splice site recognition and cleavage

key: EntryName

key: MatchStatus

database: InterPro

database: PANTHER

value: TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN15

database: Pfam

database: SUPFAM

value: tRNA-intron endonuclease catalytic domain-like


proteinExistence: 1: Evidence at protein level

value: SAGA complex subunit Sus1

source: HAMAP-Rule

value: Transcription and mRNA export factor sus1

source: UniProtKB

value: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs). Within the SAGA complex, participates in a subcomplex with SGF11, SGF73 and UBP8 required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery

value: Component of the 1.8 MDa SAGA (Spt-Ada-Gcn5 acetyltransferase) complex, which is composed of 19 subunits tra1, spt7, taf5, ngg1/ada3, sgf73, spt20, spt8, taf12, taf6, hfi1/ada1, ubp8, gcn5, ada2, spt3, sgf29, taf10, taf9, sgf11 and sus1 (PubMed:19056896). The SAGA complex is composed of 4 modules, namely the HAT (histone acetyltransferase) module (gcn5, ada2, ngg1/ada3 and sgf29), the DUB (deubiquitinating) module (ubp8, sgf11, sgf73 and sus1), the core or TAF (TBP-associated factor) module (taf5, taf6, taf9, taf10 and taf12), and the Tra1 or SPT (Suppressor of Ty) module (tra1, hfi1/ada1, spt3, spt7, spt8 and spt20). The Tra1/SPT module binds activators, the core module recruits TBP (TATA-binding protein), the HAT module contains the histone H3 acetyltransferase gcn5, and the DUB module comprises the histone H2B deubiquitinase ubp8 (By similarity). Component of the nuclear pore complex (NPC)-associated TREX-2 complex (transcription and export complex 2), composed of at least sus1, sac3, thp1, sem1, and cdc31. TREX-2 contains 2 sus1 chains. The TREX-2 complex interacts with the mRNA export factors mex67, mtr2 and sub2, and the nucleoporin nup1 (By similarity)

commentType: SUBCELLULAR LOCATION

value: Nucleus, nucleoplasm

value: Cytoplasm, P-body

value: Belongs to the ENY2 family

description: SAGA complex subunit Sus1

Activator

category: Molecular function

Cytoplasm

category: Cellular component

database: PubMed

database: DOI

authors:
Helmlinger D.
Marguerat S.
Villen J.
Gygi S.P.
Bahler J.
Winston F.

title: The S. pombe SAGA complex controls the switch from proliferation to sexual differentiation through the opposing roles of its subunits Gcn5 and Spt8.

journal: Genes Dev.

referencePositions:
IDENTIFICATION IN THE SAGA COMPLEX
IDENTIFICATION BY MASS SPECTROMETRY

database: EMBL

database: RefSeq

database: AlphaFoldDB

database: SMR

database: BioGRID

database: ComplexPortal

value: SAGA complex

database: FunCoup

database: IntAct

database: MINT

database: STRING

database: iPTMnet

database: PaxDb

value: Chromosome II

value: C:DUBm complex

value: C:nuclear pore

value: P:positive regulation of transcription by RNA polymerase II

value: P:regulation of transcription by RNA polymerase II

value: P:transcription elongation by RNA polymerase II

value: P:transcription initiation-coupled chromatin remodeling

value: ENHANCER OF YELLOW 2 TRANSCRIPTION FACTOR


entryType: UniProtKB unreviewed (TrEMBL)

scientificName: Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / CCUG 213 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / MK)

lineage: Bacteria Pseudomonadati Pseudomonadota Betaproteobacteria Neisseriales Chromobacteriaceae Chromobacterium

proteinExistence: 4: Predicted

value: Probable transcriptional regulator, MarR family

type: Domain

description: HTH marR-type

source: PROSITE

type: DNA binding

description: H-T-H motif

source: PROSITE-ProRule

authors:
Vasconcelos A.T.R.
de Almeida D.F.
Almeida F.C.
de Almeida L.G.P.
de Almeida R.
Goncalves J.A.A.
Andrade E.M.
Antonio R.V.
Araripe J.
de Araujo M.F.F.
Filho S.A.
Azevedo V.
Batista A.J.
Bataus L.A.M.
Batista J.S.
Belo A.
vander Berg C.
Blamey J.
Bogo M.
Bonato S.
Bordignon J.
Brito C.A.
Brocchi M.
Burity H.A.
Camargo A.A.
Cardoso D.D.P.
Carneiro N.P.
Carraro D.M.
Carvalho C.M.B.
Cascardo J.C.M.
Cavada B.S.
Chueire L.M.O.
Pasa T.B.C.
Duran N.
Fagundes N.
Falcao C.L.
Fantinatti F.
Farias I.P.
Felipe M.S.S.
Ferrari L.P.
Ferro J.A.
Ferro M.I.T.
Franco G.R.
Freitas N.S.A.
Furlan L.R.
Gazzinelli R.T.
Gomes E.A.
Goncalves P.R.
Grangeiro T.B.
Grattapaglia D.
Grisard E.C.
Guimaraes C.T.
Hanna E.S.
Hungria M.
Jardim S.N.
Laurino J.
Leoi L.C.T.
Fassarella L.
Lima A.
Loureiro M.F.
Lyra M.C.P.
Macedo M.
Madeira H.M.F.
Manfio G.P.
Maranhao A.Q.
Martins W.S.
di Mauro S.M.Z.
de Medeiros S.R.B.
Meissner R.D.V.
Menck C.F.M.
Moreira M.A.M.
Nascimento F.F.
Nicolas M.F.
Oliveira J.G.
Oliveira S.C.
Paixao R.F.C.
Parente J.A.
Pedrosa F.O.
Pena S.J.D.
Perreira J.O.
Perreira M.
Pinto L.S.R.C.
Pinto L.S.
Porto J.I.R.
Potrich D.P.
Neto C.E.R.
Reis A.M.M.
Rigo L.U.
Rondinelli E.
dos Santos E.B.P.
Santos F.R.
Schneider M.P.C.
Seuanez H.N.
Silva A.M.R.
da Silva A.L.C.
Silva D.W.
Silva R.
Simoes I.C.
Simon D.
Soares C.M.A.
Soares R.B.A.
Souza E.M.
Souza K.R.L.
Souza R.C.
Steffens M.B.R.
Steindel M.
Teixeira S.R.
Urmenyi T.
Vettore A.
Wassem R.
Zaha A.
Simpson A.J.G.

title: The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability.

journal: Proc. Natl. Acad. Sci. U.S.A.

database: GeneID

database: KEGG

database: eggNOG

value: Bacteria

database: HOGENOM

database: OrthoDB

database: Proteomes

value: Chromosome

database: GO

value: F:DNA-binding transcription factor activity

value: P:response to stress

value: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

database: InterPro

value: MarR/SlyA-like

database: PANTHER

value: HTH-TYPE TRANSCRIPTIONAL REPRESSOR YETL

value: TRANSCRIPTIONAL REGULATOR, MARR FAMILY

database: SMART

value: Winged helix' DNA-binding domain

database: PROSITE


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: SPX domain-containing protein

source: ARBA

value: Membrane

value: Multi-pass membrane protein

description: Helical

source: SAM

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: Helical

description: SPX

type: Region

description: Disordered

type: Compositional bias

description: Polar residues

description: Basic residues

Transmembrane

category: Domain

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.

database: PubMed

database: DOI

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

database: EMBL

value: F:phosphate transmembrane transporter activity

value: LOW-AFFINITY PHOSPHATE TRANSPORTER PHO91


value: Serine/threonine-protein

commentType: CATALYTIC ACTIVITY

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

database: Rhea

database: ChEBI

directionType: left-to-right

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

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

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

description: Protein kinase

description: Disordered

description: Polar residues

description: Low complexity

description: Pro residues

description: Low complexity

description: Low complexity

description: Polar residues

type: Active site

description: Proton acceptor

type: Binding site

value: P:positive regulation of calcium-mediated signaling

value: P:regulation of fungal-type cell wall organization

value: DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE DSOR1-LIKE PROTEIN

value: MITOGEN-ACTIVATED PROTEIN KINASE KINAE MKK2


source: RuleBase

value: Small nuclear ribonucleoprotein G

value: snRNP-G

value: Plays a role in pre-mRNA splicing

value: Nucleus

value: Belongs to the snRNP Sm proteins family

description: Sm

database: RefSeq

database: AlphaFoldDB

database: SMR

database: FunCoup

database: STRING

database: PaxDb

database: VEuPathDB

database: InParanoid

database: OMA

value: Chromosome 1, Linkage Group I

value: C:catalytic step 2 spliceosome

value: C:post-mRNA release spliceosomal complex

value: C:precatalytic spliceosome

value: C:SMN-Sm protein complex


value: glycerol kinase

value: ATP:glycerol 3-phosphotransferase

value: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1

commentType: PATHWAY

value: Belongs to the FGGY kinase family

description: Carbohydrate kinase FGGY N-terminal

source: Pfam

description: Carbohydrate kinase FGGY C-terminal

ATP-binding

category: Ligand

database: GeneID

database: KEGG

database: HOGENOM

database: OrthoDB

database: UniPathway

key: RectionId

database: Proteomes

value: Chromosome 5, Linkage Group VI

database: GO

value: F:glycerol kinase activity

value: P:glycerol catabolic process

value: P:triglyceride metabolic process

database: CDD


source: PIRNR

value: AP complex subunit beta

value: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration

value: Endomembrane system

value: Belongs to the adaptor complexes large subunit family

description: Clathrin/coatomer adaptor adaptin-like N-terminal

description: Disordered

description: Low complexity

database: PubMed

database: DOI

database: EMBL

database: RefSeq

value: Chromosome 7, Linkage Group VII

value: C:AP-1 adaptor complex

value: F:clathrin binding

value: P:intracellular protein transport

database: FunFam

value: Leucine-rich Repeat Variant

value: ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER


value: Large ribosomal subunit protein eL39

value: 60S ribosomal protein L39

value: Belongs to the eukaryotic ribosomal protein eL39 family

description: Disordered

description: Basic residues

source: PDB

authors:
Shen L.
Su Z.
Yang K.
Wu C.
Becker T.
Bell-Pedersen D.
Zhang J.
Sachs M.S.

title: Structure of the translating Neurospora ribosome arrested by cycloheximide.

referencePositions: STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS)

database: PDB

key: Method

value: EM

key: Resolution

key: Chains

database: AlphaFoldDB

database: EMDB

database: SMR

database: FunCoup

database: STRING

database: PaxDb

value: Chromosome 3, Linkage Group III

value: C:cytosolic large ribosomal subunit

value: F:structural constituent of ribosome

value: P:cytoplasmic translation

value: 60S ribosomal protein-like L39


value: BAR adaptor protein RVS167

description: BAR

description: Disordered

type: Coiled coil

description: Low complexity

description: Low complexity

Phosphoprotein

category: PTM

key: ProteinId

key: Status

key: MoleculeType

database: GeneID

database: KEGG

database: VEuPathDB

database: HOGENOM

database: InParanoid

database: OrthoDB

value: Chromosome 2, Linkage Group V

value: C:actin cortical patch

value: C:actin cytoskeleton

value: C:mating projection tip

value: C:medial cortex

value: C:Rvs161p-Rvs167p complex

value: Arfaptin homology (AH) domain/BAR domain

value: REDUCED VIABILITY UPON STARVATION PROTEIN 167


error: HTTPSConnectionPool(host='rest.uniprot.org', port=443): Read timed out. (read timeout=90)


value: Ribosome production factor 2 homolog

value: Ribosome biogenesis protein RPF2 homolog

value: Nucleus, nucleolus

value: Belongs to the RPF2 family

description: Brix

description: Disordered

description: Basic residues

database: PubMed

database: DOI

key: NucleotideSequenceId

key: Description

database: OMA

database: Proteomes

value: Chromosome 1, Linkage Group I

database: GO

value: F:rRNA binding

value: P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

value: P:ribosomal large subunit assembly

database: InterPro

value: Brix

database: PANTHER

value: BRIX DOMAIN CONTAINING PROTEIN

value: RIBOSOME PRODUCTION FACTOR 2 HOMOLOG


value: Transcriptional activator HAP2

value: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes

value: Heterotrimer

value: Nucleus

value: Belongs to the NFYA/HAP2 subunit family

description: Disordered

description: Disordered

description: Disordered

description: Disordered

type: Motif

description: Subunit association domain (SAD)

description: Polar residues

description: Polar residues

description: Polar residues

description: Pro residues

description: Basic and acidic residues

description: Polar residues

database: EMBL

database: RefSeq

database: AlphaFoldDB

value: F:DNA-binding transcription factor activity, RNA polymerase II-specific

value: P:regulation of transcription by RNA polymerase II


scientificName: Homo sapiens

commonName: Human

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

source: HGNC

value: Shieldin complex subunit 2

value: Protein FAM35A

value: RINN1-REV7-interacting novel NHEJ regulator 2

value: Shield complex subunit 2

value: Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs) (PubMed:29656893, PubMed:29789392). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection (PubMed:29656893, PubMed:29789392). Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres (PubMed:29656893)

value: Component of the shieldin complex, consisting of SHLD1, SHLD2, SHLD3 and MAD2L2/REV7 (PubMed:29656893, PubMed:29789392). Within the complex, SHLD2 forms a scaffold which interacts with a SHLD3-MAD2L2 subcomplex via its N-terminus, and with SHLD1 via its C-terminus (PubMed:29656893). Interacts with TP53BP1 (PubMed:29789392). Interacts with RIF1 (PubMed:29789392). Interacts with ASTE1 (PubMed:34354233)

commentType: INTERACTION

value: Localizes to nuclear foci in response to DNA damage

value: Chromosome

commentType: ALTERNATIVE PRODUCTS

isoformSequenceStatus: Displayed

isoformSequenceStatus: Described

value: In BRCA1-deficient cells, function of the shieldin complex is necessary for sensitivity to camptothecin and the PARP inhibitor olaparib

commentType: MISCELLANEOUS

value: Belongs to the SHLD2 family

description: Shieldin complex subunit 2

description: Interaction with ASTE1

description: Sufficient for interaction with SHLD3 and MAD2L2

description: Mediates interaction with SHLD1

type: Alternative sequence

description: in isoform 2

source: Reference

originalSequence: K

type: Natural variant

description: in dbSNP:rs3129520

database: dbSNP

originalSequence: F

description: in dbSNP:rs11202365

originalSequence: S

description: in dbSNP:rs11816168

originalSequence: R

type: Mutagenesis

description: Fails to interact with SHLD3 or MAD2L2.

type: Sequence conflict

description: in Ref. 4; AAD20041

originalSequence: SQLL

description: in Ref. 1; BAB14342

type: Beta strand

Alternative splicing

category: Coding sequence diversity

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 1)

authors:
Deloukas P.
Earthrowl M.E.
Grafham D.V.
Rubenfield M.
French L.
Steward C.A.
Sims S.K.
Jones M.C.
Searle S.
Scott C.
Howe K.
Hunt S.E.
Andrews T.D.
Gilbert J.G.R.
Swarbreck D.
Ashurst J.L.
Taylor A.
Battles J.
Bird C.P.
Ainscough R.
Almeida J.P.
Ashwell R.I.S.
Ambrose K.D.
Babbage A.K.
Bagguley C.L.
Bailey J.
Banerjee R.
Bates K.
Beasley H.
Bray-Allen S.
Brown A.J.
Brown J.Y.
Burford D.C.
Burrill W.
Burton J.
Cahill P.
Camire D.
Carter N.P.
Chapman J.C.
Clark S.Y.
Clarke G.
Clee C.M.
Clegg S.
Corby N.
Coulson A.
Dhami P.
Dutta I.
Dunn M.
Faulkner L.
Frankish A.
Frankland J.A.
Garner P.
Garnett J.
Gribble S.
Griffiths C.
Grocock R.
Gustafson E.
Hammond S.
Harley J.L.
Hart E.
Heath P.D.
Ho T.P.
Hopkins B.
Horne J.
Howden P.J.
Huckle E.
Hynds C.
Johnson C.
Johnson D.
Kana A.
Kay M.
Kimberley A.M.
Kershaw J.K.
Kokkinaki M.
Laird G.K.
Lawlor S.
Lee H.M.
Leongamornlert D.A.
Laird G.
Lloyd C.
Lloyd D.M.
Loveland J.
Lovell J.
McLaren S.
McLay K.E.
McMurray A.
Mashreghi-Mohammadi M.
Matthews L.
Milne S.
Nickerson T.
Nguyen M.
Overton-Larty E.
Palmer S.A.
Pearce A.V.
Peck A.I.
Pelan S.
Phillimore B.
Porter K.
Rice C.M.
Rogosin A.
Ross M.T.
Sarafidou T.
Sehra H.K.
Shownkeen R.
Skuce C.D.
Smith M.
Standring L.
Sycamore N.
Tester J.
Thorpe A.
Torcasso W.
Tracey A.
Tromans A.
Tsolas J.
Wall M.
Walsh J.
Wang H.
Weinstock K.
West A.P.
Willey D.L.
Whitehead S.L.
Wilming L.
Wray P.W.
Young L.
Chen Y.
Lovering R.C.
Moschonas N.K.
Siebert R.
Fechtel K.
Bentley D.
Durbin R.M.
Hubbard T.
Doucette-Stamm L.
Beck S.
Smith D.R.
Rogers J.

title: The DNA sequence and comparative analysis of human chromosome 10.

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

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 529-835 (ISOFORM 2)

authors:
Gupta R.
Somyajit K.
Narita T.
Maskey E.
Stanlie A.
Kremer M.
Typas D.
Lammers M.
Mailand N.
Nussenzweig A.
Lukas J.
Choudhary C.

title: DNA repair network analysis reveals shieldin as a key regulator of NHEJ and PARP inhibitor sensitivity.

referencePositions: INTERACTION WITH SHLD1; SHLD3 AND MAD2L2

authors:
Tomida J.
Takata K.I.
Bhetawal S.
Person M.D.
Chao H.P.
Tang D.G.
Wood R.D.

title: FAM35A associates with REV7 and modulates DNA damage responses of normal and BRCA1-defective cells.

referencePositions: INTERACTION WITH MAD2L2; TP53BP1 AND RIF1

authors:
Zhao F.
Kim W.
Gao H.
Liu C.
Zhang Y.
Chen Y.
Deng M.
Zhou Q.
Huang J.
Hu Q.
Chen S.H.
Nowsheen S.
Kloeber J.A.
Qin B.
Yin P.
Tu X.
Guo G.
Qin S.
Zhang C.
Gao M.
Luo K.
Liu Y.
Lou Z.
Yuan J.

title: ASTE1 promotes shieldin-complex-mediated DNA repair by attenuating end resection.

value: 3 GO annotations based on evolutionary models

value: Expressed in calcaneal tendon and 106 other cell types or tissues

value: P:negative regulation of double-strand break repair via homologous recombination

value: P:positive regulation of double-strand break repair via nonhomologous end joining

value: P:positive regulation of isotype switching

value: P:regulation of double-strand break repair via homologous recombination

value: P:somatic diversification of immunoglobulins involved in immune response

value: P:telomere maintenance in response to DNA damage


scientificName: Drosophila melanogaster

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

source: SMART

value: CHK kinase-like domain-containing protein

source: FlyBase

description: CHK kinase-like

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.

title: The genome sequence of Drosophila melanogaster.

journal: Science

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.

journal: Genome Biol.

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.

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

journal: PLoS Comput. Biol.

journal: G3 (Bethesda)

value: Expressed in early-mid elongation-stage spermatid (Drosophila) in testis and 22 other cell types or tissues


source: EMBL

value: Oo18 RNA-binding protein, isoform C

value: Oo18 RNA-binding protein, isoform E

value: orb

value: ORB

value: Orb

value: Cytoplasm

value: Belongs to the RRM CPEB family

description: RRM

description: Disordered

description: Low complexity

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

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

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.

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

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: Expressed in mid-late elongation-stage spermatid (Drosophila) in testis and 144 other cell types or tissues

value: P:dorsal/ventral axis specification, ovarian follicular epithelium

value: P:oocyte anterior/posterior axis specification

value: P:oocyte dorsal/ventral axis specification

value: Putative Cytoplasmic polyadenylation element-binding protein 1

value: Cytoplasmic polyadenylation element-binding protein, ZZ domain

value: CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN CPEB

value: CYTOPLASMIC POLYADENYLATION ELEMENT-BINDING PROTEIN 1


source: Proteomes

value: Glorund, isoform C

value: glo

value: Glo

description: RRM

description: Disordered

description: Low complexity

Proteomics identification

source: PeptideAtlas

value: Berkeley

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 T neuron T5b (Drosophila) in embryonic/larval optic lobe (Drosophila) and 288 other cell types or tissues

value: P:intracellular mRNA localization involved in pattern specification process

value: P:maternal specification of dorsal/ventral axis, oocyte, germ-line encoded


value: Peptidase S1 domain-containing protein

value: Belongs to the peptidase S1 family. CLIP subfamily

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

commentType: CAUTION

type: Signal

description: Peptidase S1 domain-containing protein

description: Peptidase S1

value: Expressed in arthropod fat body and 3 other cell types or tissues

value: P:positive regulation of hemocyte proliferation


value: Uncharacterized protein

value: Expressed in fat body cell in dorsal vessel heart and 12 other cell types or tissues


value: Male specific transcript 27D, isoform A

value: Male specific transcript 27D, isoform B

description: Calponin-homology (CH)

description: Disordered

description: Disordered

description: Disordered

description: Polar residues

description: Polar residues

value: Expressed in early elongation stage spermatid (Drosophila) in testis and 37 other cell types or tissues

value: P:regulation of microtubule polymerization or depolymerization

value: MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER


value: Chymotrypsin

name: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.

description: Chymotrypsin

description: Peptidase S1

description: Charge relay system

description: Charge relay system

description: Charge relay system

type: Disulfide bond


value: RRM domain-containing protein

value: Nucleus, nucleolus

value: Belongs to the ESF2/ABP1 family

description: RRM

description: Disordered

description: Basic and acidic residues

value: Berkeley

value: Expressed in spermatocyte in testis and 56 other cell types or tissues

value: P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

value: P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

value: P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA)


value: Palmitoyltransferase ZDHHC23

source: PubMed

value: Zinc finger DHHC domain-containing protein 23

value: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes (Probable). Palmitoyltransferase that mediates palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane. May be involved in NOS1 regulation and targeting to the synaptic membrane

name: L-cysteinyl-[protein] + hexadecanoyl-CoA = S-hexadecanoyl-L-cysteinyl-[protein] + CoA

database: Rhea

database: ChEBI

value: Interacts with NOS1

value: Golgi apparatus membrane

value: Multi-pass membrane protein

value: Golgi apparatus, trans-Golgi network membrane

value: The DHHC domain is required for palmitoyltransferase activity

commentType: DOMAIN

value: Belongs to the DHHC palmitoyltransferase family

type: Chain

description: Palmitoyltransferase ZDHHC23

type: Topological domain

description: Cytoplasmic

type: Transmembrane

description: Helical

description: Lumenal

description: Helical

description: Cytoplasmic

description: Helical

description: Lumenal

description: Helical

description: Cytoplasmic

description: Helical

description: Lumenal

description: Helical

description: Cytoplasmic

description: Helical

description: Lumenal

description: DHHC

description: Disordered

description: S-palmitoyl cysteine intermediate

description: in dbSNP:rs17853401

description: in dbSNP:rs17853402

description: in dbSNP:rs11921691

description: in dbSNP:rs17857054

authors:
Muzny D.M.
Scherer S.E.
Kaul R.
Wang J.
Yu J.
Sudbrak R.
Buhay C.J.
Chen R.
Cree A.
Ding Y.
Dugan-Rocha S.
Gill R.
Gunaratne P.
Harris R.A.
Hawes A.C.
Hernandez J.
Hodgson A.V.
Hume J.
Jackson A.
Khan Z.M.
Kovar-Smith C.
Lewis L.R.
Lozado R.J.
Metzker M.L.
Milosavljevic A.
Miner G.R.
Morgan M.B.
Nazareth L.V.
Scott G.
Sodergren E.
Song X.-Z.
Steffen D.
Wei S.
Wheeler D.A.
Wright M.W.
Worley K.C.
Yuan Y.
Zhang Z.
Adams C.Q.
Ansari-Lari M.A.
Ayele M.
Brown M.J.
Chen G.
Chen Z.
Clendenning J.
Clerc-Blankenburg K.P.
Chen R.
Chen Z.
Davis C.
Delgado O.
Dinh H.H.
Dong W.
Draper H.
Ernst S.
Fu G.
Gonzalez-Garay M.L.
Garcia D.K.
Gillett W.
Gu J.
Hao B.
Haugen E.
Havlak P.
He X.
Hennig S.
Hu S.
Huang W.
Jackson L.R.
Jacob L.S.
Kelly S.H.
Kube M.
Levy R.
Li Z.
Liu B.
Liu J.
Liu W.
Lu J.
Maheshwari M.
Nguyen B.-V.
Okwuonu G.O.
Palmeiri A.
Pasternak S.
Perez L.M.
Phelps K.A.
Plopper F.J.
Qiang B.
Raymond C.
Rodriguez R.
Saenphimmachak C.
Santibanez J.
Shen H.
Shen Y.
Subramanian S.
Tabor P.E.
Verduzco D.
Waldron L.
Wang J.
Wang J.
Wang Q.
Williams G.A.
Wong G.K.-S.
Yao Z.
Zhang J.
Zhang X.
Zhao G.
Zhou J.
Zhou Y.
Nelson D.
Lehrach H.
Reinhardt R.
Naylor S.L.
Yang H.
Olson M.
Weinstock G.
Gibbs R.A.

title: The DNA sequence, annotation and analysis of human chromosome 3.

authors:
Mural R.J.
Istrail S.
Sutton G.G.
Florea L.
Halpern A.L.
Mobarry C.M.
Lippert R.
Walenz B.
Shatkay H.
Dew I.
Miller J.R.
Flanigan M.J.
Edwards N.J.
Bolanos R.
Fasulo D.
Halldorsson B.V.
Hannenhalli S.
Turner R.
Yooseph S.
Lu F.
Nusskern D.R.
Shue B.C.
Zheng X.H.
Zhong F.
Delcher A.L.
Huson D.H.
Kravitz S.A.
Mouchard L.
Reinert K.
Remington K.A.
Clark A.G.
Waterman M.S.
Eichler E.E.
Adams M.D.
Hunkapiller M.W.
Myers E.W.
Venter J.C.

referencePositions:
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
VARIANTS ASN-132; ALA-221 AND ARG-274

authors:
Tian L.
McClafferty H.
Knaus H.G.
Ruth P.
Shipston M.J.

title: Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels.

referencePositions:
FUNCTION
CATALYTIC ACTIVITY
SUBCELLULAR LOCATION

value: 5 GO annotations based on evolutionary models

value: Expressed in sperm and 133 other cell types or tissues

value: P:protein localization to plasma membrane

value: ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN


value: Chymotrypsin

value: Belongs to the peptidase S1 family. CLIP subfamily

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

description: Chymotrypsin

type: Domain

description: Peptidase S1

description: Charge relay system

description: Charge relay system

description: Charge relay system

value: Berkeley

type: STRAIN

value: Expressed in fat body cell in dorsal vessel heart and 11 other cell types or tissues


proteinExistence: 2: Evidence at transcript level

value: Tubulin beta chain

value: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin

commentType: COFACTOR

value: Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells

value: Cytoplasm, cytoskeleton

value: Belongs to the tubulin family

description: Tubulin/FtsZ GTPase

description: Tubulin/FtsZ 2-layer sandwich

type: Region

description: Disordered

type: Compositional bias

description: Acidic residues

citationType: submission

authors:
Stapleton M.
Brokstein P.
Hong L.
Agbayani A.
Carlson J.
Champe M.
Chavez C.
Dorsett V.
Dresnek D.
Farfan D.
Frise E.
George R.
Gonzalez M.
Guarin H.
Kronmiller B.
Li P.
Liao G.
Miranda A.
Mungall C.J.
Nunoo J.
Pacleb J.
Paragas V.
Park S.
Patel S.
Phouanenavong S.
Wan K.
Yu C.
Lewis S.E.
Rubin G.M.
Celniker S.

submissionDatabase: EMBL/GenBank/DDBJ databases

value: mRNA

database: SMR

database: IntAct

key: Interactions

database: STRING

database: PaxDb

database: PeptideAtlas

database: DNASU

database: GeneID

database: KEGG

database: AGR

database: CTD

database: FlyBase

key: GeneName

database: VEuPathDB

value: HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand

value: COPI-independent Golgi-to-ER retrograde traffic

value: Expressed in capitellum (Drosophila) and 106 other cell types or tissues

value: F:structural constituent of cytoskeleton


description: Helical

database: EMBL

database: RefSeq

database: UCSC

key: OrganismName

value: d. melanogaster

database: eggNOG

key: ToxonomicScope

value: Eukaryota

database: HOGENOM

database: OMA

key: Fingerprint

database: BioGRID-ORCS

key: hits

value: 0 hits in 1 CRISPR screen

database: Bgee

key: ExpressionPatterns

value: Expressed in mid-late elongation-stage spermatid (Drosophila) in testis and 21 other cell types or tissues


value: AFAP1-like protein 2

value: May play a role in a signaling cascade by enhancing the kinase activity of SRC. Contributes to SRC-regulated transcription activation

value: Interacts with SRC. Interacts with LCK when tyrosine phosphorylated

value: Cytoplasm

value: Detected in spleen and thyroid, and at lower levels in kidney, brain, lung and pancreas

commentType: TISSUE SPECIFICITY

value: Tyrosine phosphorylated (by SRC)

commentType: PTM

commentType: SEQUENCE CAUTION

sequenceCautionType: Erroneous initiation

description: PH 1

description: PH 2

description: Disordered

description: Disordered

description: Disordered

description: Polar residues

description: Acidic residues

type: Modified residue

description: Phosphotyrosine

source: UniProtKB

description: Phosphoserine

description: Phosphotyrosine

description: Phosphoserine

description: in isoform 3

description: in isoform 4

originalSequence: N

description: in isoform 2 and isoform 4

description: in isoform 3

originalSequence: EWEKKGAS

description: in dbSNP:rs11196689

database: dbSNP

originalSequence: G

description: in dbSNP:rs7075067

description: in dbSNP:rs2781806

description: in dbSNP:rs11599051

description: Reduced interaction with SRC.

description: in Ref. 4; BAF84401

description: in Ref. 4; BAF84401

description: in Ref. 4; BAB55135

description: in Ref. 4; BAB55135

description: in Ref. 4; BAB55135

description: in Ref. 1; AAQ05765

description: in Ref. 4; BAF84401

description: in Ref. 1; AAQ05765

title: XB130, a novel adaptor protein for Src binding and activation.

title: Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins.

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

authors:
Deloukas P.
Earthrowl M.E.
Grafham D.V.
Rubenfield M.
French L.
Steward C.A.
Sims S.K.
Jones M.C.
Searle S.
Scott C.
Howe K.
Hunt S.E.
Andrews T.D.
Gilbert J.G.R.
Swarbreck D.
Ashurst J.L.
Taylor A.
Battles J.
Bird C.P.
Ainscough R.
Almeida J.P.
Ashwell R.I.S.
Ambrose K.D.
Babbage A.K.
Bagguley C.L.
Bailey J.
Banerjee R.
Bates K.
Beasley H.
Bray-Allen S.
Brown A.J.
Brown J.Y.
Burford D.C.
Burrill W.
Burton J.
Cahill P.
Camire D.
Carter N.P.
Chapman J.C.
Clark S.Y.
Clarke G.
Clee C.M.
Clegg S.
Corby N.
Coulson A.
Dhami P.
Dutta I.
Dunn M.
Faulkner L.
Frankish A.
Frankland J.A.
Garner P.
Garnett J.
Gribble S.
Griffiths C.
Grocock R.
Gustafson E.
Hammond S.
Harley J.L.
Hart E.
Heath P.D.
Ho T.P.
Hopkins B.
Horne J.
Howden P.J.
Huckle E.
Hynds C.
Johnson C.
Johnson D.
Kana A.
Kay M.
Kimberley A.M.
Kershaw J.K.
Kokkinaki M.
Laird G.K.
Lawlor S.
Lee H.M.
Leongamornlert D.A.
Laird G.
Lloyd C.
Lloyd D.M.
Loveland J.
Lovell J.
McLaren S.
McLay K.E.
McMurray A.
Mashreghi-Mohammadi M.
Matthews L.
Milne S.
Nickerson T.
Nguyen M.
Overton-Larty E.
Palmer S.A.
Pearce A.V.
Peck A.I.
Pelan S.
Phillimore B.
Porter K.
Rice C.M.
Rogosin A.
Ross M.T.
Sarafidou T.
Sehra H.K.
Shownkeen R.
Skuce C.D.
Smith M.
Standring L.
Sycamore N.
Tester J.
Thorpe A.
Torcasso W.
Tracey A.
Tromans A.
Tsolas J.
Wall M.
Walsh J.
Wang H.
Weinstock K.
West A.P.
Willey D.L.
Whitehead S.L.
Wilming L.
Wray P.W.
Young L.
Chen Y.
Lovering R.C.
Moschonas N.K.
Siebert R.
Fechtel K.
Bentley D.
Durbin R.M.
Hubbard T.
Doucette-Stamm L.
Beck S.
Smith D.R.
Rogers J.

title: The DNA sequence and comparative analysis of human chromosome 10.

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] (ISOFORMS 1 AND 4)

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

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2)

authors:
Xu J.
Bai X.-H.
Lodyga M.
Han B.
Xiao H.
Keshavjee S.
Hu J.
Zhang H.
Yang B.B.
Liu M.

title: XB130, a novel adaptor protein for signal transduction.

referencePositions:
FUNCTION
INTERACTION WITH SRC
SUBCELLULAR LOCATION
TISSUE SPECIFICITY
MUTAGENESIS OF TYR-4
PHOSPHORYLATION

authors:
Emaduddin M.
Edelmann M.J.
Kessler B.M.
Feller S.M.

title: Odin (ANKS1A) is a Src family kinase target in colorectal cancer cells.

referencePositions:
PHOSPHORYLATION
INTERACTION WITH LCK
IDENTIFICATION BY MASS SPECTROMETRY

authors:
Burkard T.R.
Planyavsky M.
Kaupe I.
Breitwieser F.P.
Buerckstuemmer T.
Bennett K.L.
Superti-Furga G.
Colinge J.

title: Initial characterization of the human central proteome.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

authors:
Bian Y.
Song C.
Cheng K.
Dong M.
Wang F.
Huang J.
Sun D.
Wang L.
Ye M.
Zou H.

title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

authoringGroup: RIKEN structural genomics initiative (RSGI)

title: Solution structure of the C-terminal PH domain of hypothetical protein KIAA1914 from human.

value: Tissue enhanced (lymphoid tissue, parathyroid gland, thyroid gland)

value: 6 GO annotations based on evolutionary models

value: Expressed in sural nerve and 145 other cell types or tissues

value: F:protein tyrosine kinase activator activity

value: P:positive regulation of DNA-templated transcription

value: P:positive regulation of epidermal growth factor receptor signaling pathway

value: P:positive regulation of interleukin-8 production

value: P:regulation of interleukin-6 production

value: Actin filament-associated protein 1-like 2 isoform 1

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

value: ACTIN FILAMENT-ASSOCIATED PROTEIN 1 FAMILY MEMBER

value: ACTIN FILAMENT-ASSOCIATED PROTEIN 1-LIKE 2


scientificName: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)

lineage: Bacteria Pseudomonadati Pseudomonadota Gammaproteobacteria Lysobacterales Lysobacteraceae Xanthomonas

value: Glutathione peroxidase

value: btuE

value: Belongs to the glutathione peroxidase family

type: Active site

source: PIRSR

authors:
da Silva A.C.
Ferro J.A.
Reinach F.C.
Farah C.S.
Furlan L.R.
Quaggio R.B.
Monteiro-Vitorello C.B.
Van Sluys M.A.
Almeida N.F.
Alves L.M.
do Amaral A.M.
Bertolini M.C.
Camargo L.E.
Camarotte G.
Cannavan F.
Cardozo J.
Chambergo F.
Ciapina L.P.
Cicarelli R.M.
Coutinho L.L.
Cursino-Santos J.R.
El-Dorry H.
Faria J.B.
Ferreira A.J.
Ferreira R.C.
Ferro M.I.
Formighieri E.F.
Franco M.C.
Greggio C.C.
Gruber A.
Katsuyama A.M.
Kishi L.T.
Leite R.P.
Lemos E.G.
Lemos M.V.
Locali E.C.
Machado M.A.
Madeira A.M.
Martinez-Rossi N.M.
Martins E.C.
Meidanis J.
Menck C.F.
Miyaki C.Y.
Moon D.H.
Moreira L.M.
Novo M.T.
Okura V.K.
Oliveira M.C.
Oliveira V.R.
Pereira H.A.
Rossi A.
Sena J.A.
Silva C.
de Souza R.F.
Spinola L.A.
Takita M.A.
Tamura R.E.
Teixeira E.C.
Tezza R.I.
Trindade dos Santos M.
Truffi D.
Tsai S.M.
White F.F.
Setubal J.C.
Kitajima J.P.

database: PubMed

database: DOI

title: Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.

database: AlphaFoldDB

database: STRING

database: EnsemblBacteria

key: GeneId

database: PATRIC

key: GeneDesignation

value: Bacteria

database: OrthoDB

database: Proteomes

key: Component

value: Chromosome

database: GO

key: GoTerm

value: F:peroxidase activity

key: GoEvidenceType

value: P:cellular response to oxidative stress

database: CDD

key: EntryName

key: MatchStatus

database: FunFam

value: Glutaredoxin

database: InterPro

database: PANTHER

value: GLUTATHIONE PEROXIDASE

value: THIOREDOXIN_GLUTATHIONE PEROXIDASE BTUE

database: Pfam

value: GSHPx

database: PIRSF

database: PRINTS


value: Belongs to the NDRG family

description: Disordered

description: Disordered

authors:
Stapleton M.
Brokstein P.
Hong L.
Agbayani A.
Carlson J.
Champe M.
Chavez C.
Dorsett V.
Farfan D.
Frise E.
George R.
Gonzalez M.
Guarin H.
Li P.
Liao G.
Miranda A.
Mungall C.J.
Nunoo J.
Pacleb J.
Paragas V.
Park S.
Phouanenavong S.
Wan K.
Yu C.
Lewis S.E.
Rubin G.M.
Celniker S.

value: Berkeley

database: EMBL

key: ProteinId

key: Status

key: MoleculeType

value: mRNA

database: RefSeq

database: SMR

database: IntAct

database: ESTHER

key: FamilyName

database: PeptideAtlas

database: DNASU

database: GeneID

database: UCSC

value: d. melanogaster

database: AGR

database: CTD

database: FlyBase

database: VEuPathDB

database: OMA

database: BioGRID-ORCS

value: 0 hits in 3 CRISPR screens

database: Bgee

value: Expressed in adult Malpighian tubule tiny cell (Drosophila) in Malpighian tubule and 290 other cell types or tissues

value: protein NDRG3 isoform X8

value: alpha/beta hydrolase

value: NDRG

value: N-MYC DOWNSTREAM REGULATED


value: Gem-associated protein 5

value: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:16857593, PubMed:18984161, PubMed:20513430, PubMed:33963192). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate (PubMed:18984161). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN5 recognizes and delivers the small nuclear RNAs (snRNAs) to the SMN complex (PubMed:11714716, PubMed:16314521, PubMed:16857593, PubMed:19377484, PubMed:19750007, PubMed:20513430, PubMed:27834343, PubMed:27881600, PubMed:27881601). Binds to the 7-methylguanosine cap of RNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref.27). Binds to the 3'-UTR of SMN1 mRNA and regulates its translation; does not affect mRNA stability (PubMed:25911097). May play a role in the regulation of protein synthesis via its interaction with ribosomes (PubMed:27507887)

value: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:16314521, PubMed:17178713, PubMed:19377484, PubMed:20513430, PubMed:27507887). Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:11714716, PubMed:16314521, PubMed:20513430). Interacts with GEMIN2; the interaction is direct (PubMed:17178713). Interacts with SMN1, SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE; the interaction is direct (PubMed:11714716). Interacts with cytosolic DDX20/GEMIN3 and GEMIN4 (PubMed:19750007, PubMed:27507887, PubMed:33963192). Interacts with SNRNP70 and HNRNPU (PubMed:27507887). Identified in a complex with 80S ribosomes; binds to the 60S large ribosomal subunit (PubMed:27507887). Interacts with the ribosomal subunits RPL3 and RPL4 (PubMed:27507887)

geneName: SNRPE

value: Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm

value: Nucleus, nucleoplasm

value: Nucleus, gem

value: Cytoplasm

value: The WD repeat domain mediates binding to U1 snRNA and to U4 snRNA (PubMed:19377484, PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601). The WD repeat domain also mediates binding to the 7-methylguanosine cap that is found both on mRNA and snRNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref.27). The regions that bind snRNA molecules and the isolated 7-methylguanosine cap overlap at least partially (PubMed:27834343, PubMed:27881600, PubMed:27881601). Besides, the WD repeat domain mediates interaction with the 60S large ribosomal subunit (PubMed:27507887)

commentType: DISEASE

diseaseId: Neurodevelopmental disorder with cerebellar atrophy and motor dysfunction

acronym: NEDCAM

description: An autosomal recessive disorder characterized by global developmental delay with predominantly motor abnormalities, axial hypotonia with decreased or absent reflexes, gait ataxia and appendicular spasticity. Affected individuals have cognitive impairment and speech delay. Brain imaging shows cerebellar atrophy.

database: MIM

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

value: Belongs to the WD repeat gemin-5 family

note: Extended N-terminus.

description: Gem-associated protein 5

type: Repeat

description: WD 1

description: WD 2

description: WD 3

description: WD 4

description: WD 5

description: WD 6

description: WD 7

description: WD 8

description: WD 9

description: WD 10

description: WD 11

description: WD 12

description: WD 13

description: Important for interaction with U1 snRNA

description: Interaction with U4 snRNA

description: Disordered

description: Disordered

description: Disordered

description: Basic residues

description: Polar residues

description: Interaction with U4 snRNA

description: Interaction with U4 snRNA

description: Interaction with U4 snRNA

description: Interaction with U4 snRNA

description: Interaction with U4 snRNA

description: Interaction with U4 snRNA

description: Interaction with U4 snRNA

description: Interaction with U4 snRNA

description: Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA molecules

description: Interaction with U4 snRNA

description: Interaction with U4 snRNA

description: Phosphoserine

description: Phosphothreonine

description: Phosphoserine

description: Phosphothreonine

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: Phosphoserine

description: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

description: in NEDCAM; uncertain significance

description: in NEDCAM

description: in NEDCAM; uncertain significance; dbSNP:rs1764284051

description: in NEDCAM; uncertain significance; dbSNP:rs1333297702

description: in NEDCAM; uncertain significance

description: in NEDCAM

description: in NEDCAM

description: in NEDCAM; uncertain significance; dbSNP:rs374532509

description: in dbSNP:rs1974777

description: in NEDCAM; uncertain significance

description: in NEDCAM; impaired function in spliceosomal snRNP assembly; decreased protein abundance; decreased protein stability; decreased interaction with DDX20; decreased interaction with GEMIN4; dbSNP:rs2113468939

description: in NEDCAM; uncertain significance; dbSNP:rs1763488906

description: in NEDCAM; uncertain significance

description: in NEDCAM; uncertain significance

description: in NEDCAM; dbSNP:rs760029026

description: in NEDCAM; uncertain significance; dbSNP:rs1763459819

description: in NEDCAM; uncertain significance

description: in NEDCAM; uncertain significance

description: in NEDCAM; impaired function in spliceosomal snRNP assembly; decreased protein abundance; decreased protein stability; decreased interaction with DDX20; decreased interaction with GEMIN4; dbSNP:rs371174241

description: in NEDCAM; uncertain significance; dbSNP:rs2113459584

description: in dbSNP:rs6865950

description: in NEDCAM; uncertain significance; dbSNP:rs748292248

description: in NEDCAM; dbSNP:rs780303963

description: in NEDCAM; dbSNP:rs2113452099

description: in NEDCAM; uncertain significance

description: in NEDCAM; uncertain significance; dbSNP:rs200680023

description: Abolishes interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. No effect on interaction with 80S ribosomes.

description: Abolishes interaction with U4 snRNA.

description: Abolishes interaction with U4 snRNA.

description: No effect in interaction with U4 snRNA. No effect on interaction with SMN complex.

description: Abolishes interaction with U4 snRNA. Abolishes interaction with the 7-methylguanosine cap of RNA molecules. No effect on interaction with SMN complex.

description: Abolishes interaction with U4 snRNA.

description: Abolishes interaction with U4 snRNA.

description: Strongly decreases interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. Abolishes interaction with 80S ribosomes.

description: Abolishes interaction with U4 snRNA.

description: Abolishes interaction with U4 snRNA.

description: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules.

description: in Ref. 5; BAB14222

description: in Ref. 5; BAB14222

authors:
Gubitz A.K.
Mourelatos Z.
Abel L.
Rappsilber J.
Mann M.
Dreyfuss G.

title: Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins.

referencePositions: INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE

authors:
Jikuya H.
Takano J.
Nomura N.
Kikuno R.
Nagase T.
Ohara O.

title: The nucleotide sequence of a long cDNA clone isolated from human spleen.

referencePositions:
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
VARIANT GLN-682

authors:
Schmutz J.
Martin J.
Terry A.
Couronne O.
Grimwood J.
Lowry S.
Gordon L.A.
Scott D.
Xie G.
Huang W.
Hellsten U.
Tran-Gyamfi M.
She X.
Prabhakar S.
Aerts A.
Altherr M.
Bajorek E.
Black S.
Branscomb E.
Caoile C.
Challacombe J.F.
Chan Y.M.
Denys M.
Detter J.C.
Escobar J.
Flowers D.
Fotopulos D.
Glavina T.
Gomez M.
Gonzales E.
Goodstein D.
Grigoriev I.
Groza M.
Hammon N.
Hawkins T.
Haydu L.
Israni S.
Jett J.
Kadner K.
Kimball H.
Kobayashi A.
Lopez F.
Lou Y.
Martinez D.
Medina C.
Morgan J.
Nandkeshwar R.
Noonan J.P.
Pitluck S.
Pollard M.
Predki P.
Priest J.
Ramirez L.
Retterer J.
Rodriguez A.
Rogers S.
Salamov A.
Salazar A.
Thayer N.
Tice H.
Tsai M.
Ustaszewska A.
Vo N.
Wheeler J.
Wu K.
Yang J.
Dickson M.
Cheng J.-F.
Eichler E.E.
Olsen A.
Pennacchio L.A.
Rokhsar D.S.
Richardson P.
Lucas S.M.
Myers R.M.
Rubin E.M.

title: The DNA sequence and comparative analysis of human chromosome 5.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-737

authors:
Bechtel S.
Rosenfelder H.
Duda A.
Schmidt C.P.
Ernst U.
Wellenreuther R.
Mehrle A.
Schuster C.
Bahr A.
Bloecker H.
Heubner D.
Hoerlein A.
Michel G.
Wedler H.
Koehrer K.
Ottenwaelder B.
Poustka A.
Wiemann S.
Schupp I.

title: The full-ORF clone resource of the German cDNA consortium.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1508

title: Specific sequence features, recognized by the SMN complex, identify snRNAs and determine their fate as snRNPs.

referencePositions:
FUNCTION
IDENTIFICATION IN THE SMN COMPLEX
IDENTIFICATION IN SMN-SM COMPLEX

authors:
Olsen J.V.
Blagoev B.
Gnad F.
Macek B.
Kumar C.
Mortensen P.
Mann M.

title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-778

authors:
Battle D.J.
Lau C.-K.
Wan L.
Deng H.
Lotti F.
Dreyfuss G.

title: The Gemin5 protein of the SMN complex identifies snRNAs.

authors:
Otter S.
Grimmler M.
Neuenkirchen N.
Chari A.
Sickmann A.
Fischer U.

title: A comprehensive interaction map of the human survival of motor neuron (SMN) complex.

referencePositions:
IDENTIFICATION IN THE SMN COMPLEX
INTERACTION WITH GEMIN2

authors:
Chari A.
Golas M.M.
Klingenhager M.
Neuenkirchen N.
Sander B.
Englbrecht C.
Sickmann A.
Stark H.
Fischer U.

title: An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs.

referencePositions:
FUNCTION IN SNRNP BIOGENESIS
IDENTIFICATION IN SMN-SM COMPLEX

authors:
Daub H.
Olsen J.V.
Bairlein M.
Gnad F.
Oppermann F.S.
Korner R.
Greff Z.
Keri G.
Stemmann O.
Mann M.

title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-751; SER-770; SER-778 AND SER-847

authors:
Dephoure N.
Zhou C.
Villen J.
Beausoleil S.A.
Bakalarski C.E.
Elledge S.J.
Gygi S.P.

title: A quantitative atlas of mitotic phosphorylation.

title: Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains.

referencePositions: MUTAGENESIS OF 271-LYS--ARG-273; TRP-286 AND HIS-290

title: Identification of gemin5 as a novel 7-methylguanosine cap-binding protein.

referencePositions:
FUNCTION
SUBCELLULAR LOCATION
IDENTIFICATION BY MASS SPECTROMETRY
INTERACTION WITH DDX20 AND GEMIN4
MUTAGENESIS OF TRP-286

authors:
Yong J.
Kasim M.
Bachorik J.L.
Wan L.
Dreyfuss G.

title: Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis.

authors:
Olsen J.V.
Vermeulen M.
Santamaria A.
Kumar C.
Miller M.L.
Jensen L.J.
Gnad F.
Cox J.
Jensen T.S.
Nigg E.A.
Brunak S.
Mann M.

title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

authors:
Rigbolt K.T.
Prokhorova T.A.
Akimov V.
Henningsen J.
Johansen P.T.
Kratchmarova I.
Kassem M.
Mann M.
Olsen J.V.
Blagoev B.

title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757 AND SER-778

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.

referencePositions: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-51; SER-624; SER-757 AND SER-778

authors:
Workman E.
Kalda C.
Patel A.
Battle D.J.

title: Gemin5 binds to the survival motor neuron mRNA to regulate SMN expression.

authors:
Francisco-Velilla R.
Fernandez-Chamorro J.
Ramajo J.
Martinez-Salas E.

title: The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation.

referencePositions: INTERACTION WITH RIBOSOME SUBUNITS RPL3 AND RPL4; SNRNP70; HNRNPU; DDX20 AND GEMIN4

referencePositions: MUTAGENESIS OF TRP-14; TYR-15 AND PHE-381

authors:
Hendriks I.A.
Lyon D.
Young C.
Jensen L.J.
Vertegaal A.C.
Nielsen M.L.

title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

referencePositions: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-754

authors:
Tang X.
Bharath S.R.
Piao S.
Tan V.Q.
Bowler M.W.
Song H.

title: Structural basis for specific recognition of pre-snRNA by Gemin5.

referencePositions: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-740 IN COMPLEXES WITH 7-METHYLGUANOSINE CAP AND SNRNA ANALOGS

referencePositions: MUTAGENESIS OF TRP-14; TYR-15; PHE-381; TYR-474; LYS-641; TYR-660 AND ARG-684

authors:
Xu C.
Ishikawa H.
Izumikawa K.
Li L.
He H.
Nobe Y.
Yamauchi Y.
Shahjee H.M.
Wu X.H.
Yu Y.T.
Isobe T.
Takahashi N.
Min J.

title: Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-739 IN COMPLEXES WITH SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP

referencePositions: MUTAGENESIS OF TRP-14; TYR-15; GLU-197; PHE-381; TYR-474 AND LYS-641

authors:
Jin W.
Wang Y.
Liu C.P.
Yang N.
Jin M.
Cong Y.
Wang M.
Xu R.M.

title: Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-726 IN COMPLEXES WITH U4 SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP

referencePositions: MUTAGENESIS OF TRP-14; TYR-15; ARG-33; ARG-335; ARG-359; PHE-381 AND TRP-422

authors:
Chao X.
Tempel W.
Bian C.
He H.
Cerovina T.
Bountra C.
Arrowsmith C.H.
Edwards A.M.
Min J.

title: Crystal structure of Gemin5 WD40 repeats in complex with m7GpppG.

referencePositions: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-739 IN COMPLEX WITH 7-METHYLGUANOSINE CAP

authors:
Kour S.
Rajan D.S.
Fortuna T.R.
Anderson E.N.
Ward C.
Lee Y.
Lee S.
Shin Y.B.
Chae J.H.
Choi M.
Siquier K.
Cantagrel V.
Amiel J.
Stolerman E.S.
Barnett S.S.
Cousin M.A.
Castro D.
McDonald K.
Kirmse B.
Nemeth A.H.
Rajasundaram D.
Innes A.M.
Lynch D.
Frosk P.
Collins A.
Gibbons M.
Yang M.
Desguerre I.
Boddaert N.
Gitiaux C.
Rydning S.L.
Selmer K.K.
Urreizti R.
Garcia-Oguiza A.
Osorio A.N.
Verdura E.
Pujol A.
McCurry H.R.
Landers J.E.
Agnihotri S.
Andriescu E.C.
Moody S.B.
Phornphutkul C.
Sacoto M.J.G.
Begtrup A.
Houlden H.
Kirschner J.
Schorling D.
Rudnik-Schoeneborn S.
Strom T.M.
Leiz S.
Juliette K.
Richardson R.
Yang Y.
Zhang Y.
Wang M.
Wang J.
Wang X.
Platzer K.
Donkervoort S.
Boennemann C.G.
Wagner M.
Issa M.Y.
Elbendary H.M.
Stanley V.
Maroofian R.
Gleeson J.G.
Zaki M.S.
Senderek J.
Pandey U.B.

title: Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder.

referencePositions: CHARACTERIZATION OF VARIANTS NEDCAM ARG-913 AND PRO-1068

value: Osteosarcoma (U2OS) cell map - Chromosome segregation and DNA repair (56 proteins)

value: Autosomal recessive non-syndromic intellectual disability

value: 4 GO annotations based on evolutionary models

value: SARS-CoV-2 modulates host translation machinery

value: Expressed in oocyte and 166 other cell types or tissues

value: YVTN repeat-like/Quinoprotein amine dehydrogenase


value: Dynein light chain Tctex-type protein 2B

value: Tctex1 domain-containing protein 2

value: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system. Required for proper retrograde ciliary transport

value: Light chain of the cytoplasmic dynein complex 2, a multisubunit complex composed at least of eleven different proteins (PubMed:25205765, PubMed:26044572). The cytoplasmic dynein 2 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs). Among them, a heavy chain (DYNC2H1), two intermediate chains (DYNC2I2 and DYNC2I1), a light intermediate chain (DYNC2LI1), and a light chain (DYNLT2B) are unique to the dynein-2 complex, but a subset of the light chains are also shared by dynein-1 and dynein-2 complexes (PubMed:25205765, PubMed:26044572). Interacts with DYNC2I1 (PubMed:26044572). The dimer DYNLT2B-DYNLT1/DYNLT3 interacts with DYNC2I1; this interaction is crucial for retrograde trafficking of ciliary proteins (PubMed:26044572, PubMed:29742051)

value: Dynein axonemal particle

diseaseId: Short-rib thoracic dysplasia 17 with or without polydactyly

description: A form of short-rib thoracic dysplasia, a group of autosomal recessive ciliopathies that are characterized by a constricted thoracic cage, short ribs, shortened tubular bones, and a 'trident' appearance of the acetabular roof. Polydactyly is variably present. Non-skeletal involvement can include cleft lip/palate as well as anomalies of major organs such as the brain, eye, heart, kidneys, liver, pancreas, intestines, and genitalia. Some forms of the disease are lethal in the neonatal period due to respiratory insufficiency secondary to a severely restricted thoracic cage, whereas others are compatible with life. Disease spectrum encompasses Ellis-van Creveld syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino syndrome, and short rib-polydactyly syndrome.

value: Belongs to the dynein light chain Tctex-type family

description: in SRTD17

description: in Ref. 2; AAH21177

originalSequence: E

type: Helix

type: Turn

Ciliopathy

category: Disease

authors:
Muzny D.M.
Scherer S.E.
Kaul R.
Wang J.
Yu J.
Sudbrak R.
Buhay C.J.
Chen R.
Cree A.
Ding Y.
Dugan-Rocha S.
Gill R.
Gunaratne P.
Harris R.A.
Hawes A.C.
Hernandez J.
Hodgson A.V.
Hume J.
Jackson A.
Khan Z.M.
Kovar-Smith C.
Lewis L.R.
Lozado R.J.
Metzker M.L.
Milosavljevic A.
Miner G.R.
Morgan M.B.
Nazareth L.V.
Scott G.
Sodergren E.
Song X.-Z.
Steffen D.
Wei S.
Wheeler D.A.
Wright M.W.
Worley K.C.
Yuan Y.
Zhang Z.
Adams C.Q.
Ansari-Lari M.A.
Ayele M.
Brown M.J.
Chen G.
Chen Z.
Clendenning J.
Clerc-Blankenburg K.P.
Chen R.
Chen Z.
Davis C.
Delgado O.
Dinh H.H.
Dong W.
Draper H.
Ernst S.
Fu G.
Gonzalez-Garay M.L.
Garcia D.K.
Gillett W.
Gu J.
Hao B.
Haugen E.
Havlak P.
He X.
Hennig S.
Hu S.
Huang W.
Jackson L.R.
Jacob L.S.
Kelly S.H.
Kube M.
Levy R.
Li Z.
Liu B.
Liu J.
Liu W.
Lu J.
Maheshwari M.
Nguyen B.-V.
Okwuonu G.O.
Palmeiri A.
Pasternak S.
Perez L.M.
Phelps K.A.
Plopper F.J.
Qiang B.
Raymond C.
Rodriguez R.
Saenphimmachak C.
Santibanez J.
Shen H.
Shen Y.
Subramanian S.
Tabor P.E.
Verduzco D.
Waldron L.
Wang J.
Wang J.
Wang Q.
Williams G.A.
Wong G.K.-S.
Yao Z.
Zhang J.
Zhang X.
Zhao G.
Zhou J.
Zhou Y.
Nelson D.
Lehrach H.
Reinhardt R.
Naylor S.L.
Yang H.
Olson M.
Weinstock G.
Gibbs R.A.

database: PubMed

database: DOI

title: The DNA sequence, annotation and analysis of human chromosome 3.

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

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

journal: Genome Res.

value: Testis

type: TISSUE

authors:
Asante D.
Stevenson N.L.
Stephens D.J.

title: Subunit composition of the human cytoplasmic dynein-2 complex.

journal: J. Cell Sci.

referencePositions: IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 2 COMPLEX

authors:
Schmidts M.
Hou Y.
Cortes C.R.
Mans D.A.
Huber C.
Boldt K.
Patel M.
van Reeuwijk J.
Plaza J.M.
van Beersum S.E.
Yap Z.M.
Letteboer S.J.
Taylor S.P.
Herridge W.
Johnson C.A.
Scambler P.J.
Ueffing M.
Kayserili H.
Krakow D.
King S.M.
Beales P.L.
Al-Gazali L.
Wicking C.
Cormier-Daire V.
Roepman R.
Mitchison H.M.
Witman G.B.

title: TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dystrophy with impaired retrograde intraflagellar transport.

journal: Nat. Commun.

referencePositions:
FUNCTION
INTERACTION WITH DYNC2I1
INVOLVEMENT IN SRTD17
VARIANT SRTD17 88-ARG--TYR-142 DEL
SUBUNIT

authors:
Hamada Y.
Tsurumi Y.
Nozaki S.
Katoh Y.
Nakayama K.

title: Interaction of WDR60 intermediate chain with TCTEX1D2 light chain of the dynein-2 complex is crucial for ciliary protein trafficking.

referencePositions:
SUBUNIT
FUNCTION
INTERACTION WITH DYNC2I1

value: Expressed in right uterine tube and 97 other cell types or tissues

value: P:regulation of intraciliary retrograde transport

value: DYNEIN LIGHT CHAIN TCTEX-TYPE PROTEIN 2B

value: T-COMPLEX-ASSOCIATED-TESTIS-EXPRESSED 1/ DYNEIN LIGHT CHAIN


value: Calcyphosin-like protein

value: CAPSL

value: Cytoplasm

note: Truncated N-terminus.

description: Calcyphosin-like protein

description: EF-hand 1

source: PROSITE-ProRule

description: EF-hand 2

description: EF-hand 3

description: EF-hand 4

type: Binding site

database: ChEBI

type: Natural variant

description: in dbSNP:rs1445898

database: dbSNP

description: in dbSNP:rs1345826

originalSequence: M

type: Sequence conflict

description: in Ref. 2; AAH17586

originalSequence: D

authors:
Schmutz J.
Martin J.
Terry A.
Couronne O.
Grimwood J.
Lowry S.
Gordon L.A.
Scott D.
Xie G.
Huang W.
Hellsten U.
Tran-Gyamfi M.
She X.
Prabhakar S.
Aerts A.
Altherr M.
Bajorek E.
Black S.
Branscomb E.
Caoile C.
Challacombe J.F.
Chan Y.M.
Denys M.
Detter J.C.
Escobar J.
Flowers D.
Fotopulos D.
Glavina T.
Gomez M.
Gonzales E.
Goodstein D.
Grigoriev I.
Groza M.
Hammon N.
Hawkins T.
Haydu L.
Israni S.
Jett J.
Kadner K.
Kimball H.
Kobayashi A.
Lopez F.
Lou Y.
Martinez D.
Medina C.
Morgan J.
Nandkeshwar R.
Noonan J.P.
Pitluck S.
Pollard M.
Predki P.
Priest J.
Ramirez L.
Retterer J.
Rodriguez A.
Rogers S.
Salamov A.
Salazar A.
Thayer N.
Tice H.
Tsai M.
Ustaszewska A.
Vo N.
Wheeler J.
Wu K.
Yang J.
Dickson M.
Cheng J.-F.
Eichler E.E.
Olsen A.
Pennacchio L.A.
Rokhsar D.S.
Richardson P.
Lucas S.M.
Myers R.M.
Rubin E.M.

title: The DNA sequence and comparative analysis of human chromosome 5.

value: Group enriched (choroid plexus, fallopian tube)

value: 0 GO annotations based on evolutionary models

value: Expressed in bronchial epithelial cell and 95 other cell types or tissues


value: Growth hormone secretagogue receptor type 1

value: GHS-R

value: GH-releasing peptide receptor

value: GHRP

value: Ghrelin receptor

value: GHSR

value: G protein-coupled receptor specific to ghrelin, an appetite-regulating peptide hormone commonly found in stomach (PubMed:35027551, PubMed:39833471). Upon activation, stimulates appetite and promotes growth hormone secretion (PubMed:10604470, PubMed:11322507, PubMed:35027551, PubMed:39833471). Ghrelin binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as phospholipase C (By similarity). GHSR is coupled to G(q) G proteins and mediates production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (By similarity). Also binds other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692, 429, MK-0677, adenosine) (PubMed:10604470, PubMed:11322507). Also plays a role in synaptic plasticity independently of ghrelin by forming a heteromer with the dopamine receptors DRD1 and DRD2 in neurons (By similarity). Following DRD1 activation by dopamine in hippocampal neurons, GHSR acts as a coreceptor, resulting in DRD1 coupling to G(q) at the expense of G(s), initiating hippocampal synaptic plasticity involved in memory and learning (By similarity). Following DRD2 activation by dopamine in lumbosacral defecation centers, GHSR acts as a coreceptor, resulting in DRD1 coupling to G(q) at the expense of G(i)/G(o), regulating defecation (By similarity)

value: Activated by octanoylated ghrelin; octanoylation is essential for full activation of the receptor (PubMed:35027551). Stimulated by anamorelin, which binds to the same binding sites as ghrelin (PubMed:39833471)

commentType: ACTIVITY REGULATION

value: Interacts with the heterotrimeric G protein complex composed of 3 units, alpha, beta and gamma; this complex may consist of GNB1 and GNG2 (PubMed:35027551, PubMed:39833471). Interacts with DRD1; forms a heteromer with DRD1 in hippocampal neurons (By similarity). Interacts with DRD2; forms a heteromer with DRD2 in neurons (By similarity)

geneName: GHSR

value: Cell membrane

value: Multi-pass membrane protein

value: Pituitary and hypothalamus

diseaseId: Growth hormone deficiency, isolated partial

acronym: GHDP

description: A disorder characterized by partial growth hormone deficiency resulting in growth delay and short stature, sometimes associated with recurrent episodes of abdominal pain, vomiting, ketosis and hypoglycemia.

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

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

description: Growth hormone secretagogue receptor type 1

description: Extracellular

description: Helical; Name=1

description: Cytoplasmic

description: Helical; Name=2

description: Extracellular

description: Helical; Name=3

description: Cytoplasmic

description: Helical; Name=4

description: Extracellular

description: Helical; Name=5

description: Cytoplasmic

description: Helical; Name=6

description: Extracellular

description: Helical; Name=7

description: Cytoplasmic

description: N-linked (GlcNAc...) asparagine

description: N-linked (GlcNAc...) asparagine

description: in isoform 1B

description: in isoform 1B

description: in dbSNP:rs2232165

description: in GHDP; affects cell-surface expression; impairs constitutive activity; does not affect the ability to respond to ghrelin; dbSNP:rs121917883

description: in GHDP; results in partial loss of constitutive activity of the receptor; does not affect response to ghrelin; does not affect receptor cell-surface expression; dbSNP:rs199588904

description: Abolishes receptor activity stimulated by anamorelin. Abolishes receptor activity stimulated by ghrelin.

description: Impairs receptor activity stimulated by anamorelin. Impairs receptor activity stimulated by ghrelin.

description: Abolishes receptor activity stimulated by anamorelin. Impairs receptor activity stimulated by ghrelin.

description: Impairs receptor activity stimulated by anamorelin. Abolishes receptor activity stimulated by ghrelin.

authors:
Howard A.D.
Feighner S.D.
Cully D.F.
Arena J.P.
Liberator P.A.
Rosenblum C.I.
Hamelin M.
Hreniuk D.L.
Palyha O.C.
Anderson J.
Paress P.S.
Diaz C.
Chou M.
Liu K.K.
McKee K.K.
Pong S.-S.
Chaung L.-Y.
Elbrecht A.
Dashkevicz M.
Heavens R.
Rigby M.
Sirinathsinghji D.J.S.
Dean D.C.
Melillo D.G.
Patchett A.A.
Nargund R.
Griffin P.R.
Demartino J.A.
Gupta S.K.
Schaeffer J.M.
Smith R.G.
van der Ploeg L.H.T.

title: A receptor in pituitary and hypothalamus that functions in growth hormone release.

referencePositions: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B)

authors:
Petersenn S.
Rasch A.C.
Penshorn M.
Beil F.U.
Schulte H.M.

title: Genomic structure and transcriptional regulation of the human growth hormone secretagogue receptor.

referencePositions: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A AND 1B)

title: cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org).

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B)

authors:
Mural R.J.
Istrail S.
Sutton G.G.
Florea L.
Halpern A.L.
Mobarry C.M.
Lippert R.
Walenz B.
Shatkay H.
Dew I.
Miller J.R.
Flanigan M.J.
Edwards N.J.
Bolanos R.
Fasulo D.
Halldorsson B.V.
Hannenhalli S.
Turner R.
Yooseph S.
Lu F.
Nusskern D.R.
Shue B.C.
Zheng X.H.
Zhong F.
Delcher A.L.
Huson D.H.
Kravitz S.A.
Mouchard L.
Reinert K.
Remington K.A.
Clark A.G.
Waterman M.S.
Eichler E.E.
Adams M.D.
Hunkapiller M.W.
Myers E.W.
Venter J.C.

authors:
Smith R.G.
Leonard R.
Bailey A.R.T.
Palyha O.C.
Feighner S.D.
Tan C.P.
Mckee K.K.
Pong S.-S.
Griffin P.R.
Howard A.D.

title: Growth hormone secretagogue receptor family members and ligands.

authors:
Kojima M.
Hosoda H.
Date Y.
Nakazato M.
Matsuo H.
Kangawa K.

title: Ghrelin is a growth-hormone-releasing acylated peptide from stomach.

authors:
Qin J.
Cai Y.
Xu Z.
Ming Q.
Ji S.Y.
Wu C.
Zhang H.
Mao C.
Shen D.D.
Hirata K.
Ma Y.
Yan W.
Zhang Y.
Shao Z.

title: Molecular mechanism of agonism and inverse agonism in ghrelin receptor.

referencePositions: STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH OCTANOYLATED GHRELIN; GNB1 AND GNG2

referencePositions: MUTAGENESIS OF GLU-124; LEU-210; TRP-276; PHE-279; ARG-283; PHE-286; GLN-302; ASN-305 AND PHE-312

authors:
Shiimura Y.
Im D.
Tany R.
Asada H.
Kise R.
Kurumiya E.
Wakasugi-Masuho H.
Yasuda S.
Matsui K.
Kishikawa J.I.
Kato T.
Murata T.
Kojima M.
Iwata S.
Masuho I.

title: The structure and function of the ghrelin receptor coding for drug actions.

referencePositions: STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 2-366 IN COMPLEX WITH ANAMORELIN; GNB1 AND GNG2

authors:
Pantel J.
Legendre M.
Cabrol S.
Hilal L.
Hajaji Y.
Morisset S.
Nivot S.
Vie-Luton M.-P.
Grouselle D.
de Kerdanet M.
Kadiri A.
Epelbaum J.
Le Bouc Y.
Amselem S.

title: Loss of constitutive activity of the growth hormone secretagogue receptor in familial short stature.

referencePositions: CHARACTERIZATION OF VARIANT GHDP GLU-204

authors:
Pantel J.
Legendre M.
Nivot S.
Morisset S.
Vie-Luton M.P.
le Bouc Y.
Epelbaum J.
Amselem S.

title: Recessive isolated growth hormone deficiency and mutations in the ghrelin receptor.

referencePositions: CHARACTERIZATION OF VARIANT GHDP TRP-237

value: the g-protein-coupled receptor (gpcr) family

value: 4 GO annotations based on evolutionary models

value: Expressed in pituitary gland and 20 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:cellular response to insulin-like growth factor stimulus

value: P:cellular response to lipopolysaccharide

value: P:cellular response to thyroid hormone stimulus

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 locomotion involved in locomotory behavior

value: P:negative regulation of macrophage apoptotic process

value: P:negative regulation of norepinephrine secretion

value: P:negative regulation of tumor necrosis factor production

value: P:phospholipase C-activating G protein-coupled receptor signaling pathway

value: P:positive regulation of eating behavior

value: P:positive regulation of fatty acid metabolic process

value: P:positive regulation of multicellular organism growth

value: P:positive regulation of small intestinal transit

value: P:positive regulation of small intestine smooth muscle contraction

value: P:positive regulation of sprouting angiogenesis

value: P:positive regulation of vascular endothelial cell proliferation

value: P:postsynaptic modulation of chemical synaptic transmission

value: P:regulation of growth hormone secretion

value: P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane

value: P:regulation of postsynapse organization

value: P:regulation of transmission of nerve impulse

value: P:response to follicle-stimulating hormone

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