entryType: UniProtKB unreviewed (TrEMBL)

proteinExistence: 5: Uncertain

source: Google

value: UBC core

value: domain

value: UBC core domain-containing protein

commentType: SUBCELLULAR LOCATION

value: Nucleus

citationType: unpublished observations

database: GO

key: GoTerm

key: GoEvidenceType

value: P:protein ubiquitination

scientificName: Homo sapiens

commonName: Human

source: Ensembl

source: Proteomes

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

proteinExistence: 1: Evidence at protein level

value: Ubiquitin conjugating enzyme E2 F (putative)

source: PROSITE-ProRule

value: Belongs to the ubiquitin-conjugating enzyme family

commentType: SIMILARITY

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

commentType: CAUTION

type: Domain

modifier: EXACT

description: UBC core

source: PROSITE

type: Region

description: Disordered

source: SAM

Proteomics identification

source: PeptideAtlas

source: ProteomicsDB

category: Technical term

citationType: journal article

authoringGroup: International Human Genome Sequencing Consortium

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

database: PubMed

database: DOI

title: Initial sequencing and analysis of the human genome.

journal: Nature

referencePositions: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

title: Finishing the euchromatic sequence of the human genome.

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

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

citationType: submission

submissionDatabase: UniProtKB

database: EMBL

key: ProteinId

key: Status

key: MoleculeType

database: AlphaFoldDB

key: Description

database: SMR

database: MassIVE

database: ProteomicsDB

database: Ensembl

key: GeneId

database: UCSC

key: OrganismName

value: human

database: HGNC

key: GeneName

database: VEuPathDB

database: GeneTree

database: OrthoDB

database: Proteomes

key: Component

value: Chromosome 2

database: Bgee

key: ExpressionPatterns

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


value: Uncharacterized protein

value: Component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins

commentType: FUNCTION

value: F:4 iron, 4 sulfur cluster binding

source: ARBA

value: Nuclear prelamin A recognition factor

value: Iron-only hydrogenase-like protein 2

value: NARF

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

commentType: SUBUNIT

value: Belongs to the NARF family

description: Iron hydrogenase large subunit C-terminal

source: Pfam

description: Disordered

type: Compositional bias

description: Basic and acidic residues

Nucleus

category: Cellular component

Phosphoprotein

category: PTM

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

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

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

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

journal: J. Proteome Res.

referencePositions: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

source: PubMed

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

value: Cytosolic Fe-S cluster assembly factor NAR1


value: D-tyrosyl-tRNA(Tyr) deacylase

value: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality

source: RuleBase

value: D-aminoacyl-tRNA deacylase

commentType: CATALYTIC ACTIVITY

name: a D-aminoacyl-tRNA + H2O = a tRNA + a D-alpha-amino acid + H(+)

database: Rhea

database: ChEBI

name: glycyl-tRNA(Ala) + H2O = tRNA(Ala) + glycine + H(+)

value: Homodimer. Interacts with CDC45 and TOPBP1

value: Cytoplasm

value: Belongs to the DTD family

Hydrolase

category: Molecular function

authors:
Deloukas P.
Matthews L.H.
Ashurst J.
Burton J.
Gilbert J.G.
Jones M.
Stavrides G.
Almeida J.P.
Babbage A.K.
Bagguley C.L.
Bailey J.
Barlow K.F.
Bates K.N.
Beard L.M.
Beare D.M.
Beasley O.P.
Bird C.P.
Blakey S.E.
Bridgeman A.M.
Brown A.J.
Buck D.
Burrill W.
Butler A.P.
Carder C.
Carter N.P.
Chapman J.C.
Clamp M.
Clark G.
Clark L.N.
Clark S.Y.
Clee C.M.
Clegg S.
Cobley V.E.
Collier R.E.
Connor R.
Corby N.R.
Coulson A.
Coville G.J.
Deadman R.
Dhami P.
Dunn M.
Ellington A.G.
Frankland J.A.
Fraser A.
French L.
Garner P.
Grafham D.V.
Griffiths C.
Griffiths M.N.
Gwilliam R.
Hall R.E.
Hammond S.
Harley J.L.
Heath P.D.
Ho S.
Holden J.L.
Howden P.J.
Huckle E.
Hunt A.R.
Hunt S.E.
Jekosch K.
Johnson C.M.
Johnson D.
Kay M.P.
Kimberley A.M.
King A.
Knights A.
Laird G.K.
Lawlor S.
Lehvaslaiho M.H.
Leversha M.
Lloyd C.
Lloyd D.M.
Lovell J.D.
Marsh V.L.
Martin S.L.
McConnachie L.J.
McLay K.
McMurray A.A.
Milne S.
Mistry D.
Moore M.J.
Mullikin J.C.
Nickerson T.
Oliver K.
Parker A.
Patel R.
Pearce T.A.
Peck A.I.
Phillimore B.J.
Prathalingam S.R.
Plumb R.W.
Ramsay H.
Rice C.M.
Ross M.T.
Scott C.E.
Sehra H.K.
Shownkeen R.
Sims S.
Skuce C.D.
Smith M.L.
Soderlund C.
Steward C.A.
Sulston J.E.
Swann M.
Sycamore N.
Taylor R.
Tee L.
Thomas D.W.
Thorpe A.
Tracey A.
Tromans A.C.
Vaudin M.
Wall M.
Wallis J.M.
Whitehead S.L.
Whittaker P.
Willey D.L.
Williams L.
Williams S.A.
Wilming L.
Wray P.W.
Hubbard T.
Durbin R.M.
Bentley D.R.
Beck S.
Rogers J.

title: The DNA sequence and comparative analysis of human chromosome 20.

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

title: Initial characterization of the human central proteome.

journal: BMC Syst. Biol.

authors:
Van Damme P.
Lasa M.
Polevoda B.
Gazquez C.
Elosegui-Artola A.
Kim D.S.
De Juan-Pardo E.
Demeyer K.
Hole K.
Larrea E.
Timmerman E.
Prieto J.
Arnesen T.
Sherman F.
Gevaert K.
Aldabe R.

title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

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

value: Expressed in gingival epithelium and 195 other cell types or tissues


value: domain

value: Acyl-CoA dehydrogenase/oxidase C-terminal domain-containing protein

value: Mitochondrion matrix

database: GO

value: P:carboxylic acid catabolic process

value: long-chain-acyl-CoA dehydrogenase

name: (11Z)-eicosenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,11Z)-eicosadienoyl-CoA + reduced [electron-transfer flavoprotein]

directionType: left-to-right

name: (11Z)-octadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,11Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z)-decenoyl-CoA(4-) + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z)-decadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z)-tetradecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z)-tetradecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z,7Z)-decadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z,7Z)-decatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z,7Z,10Z)-hexadecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z,7Z,10Z)-hexadecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (4Z,7Z,10Z,13Z)-hexadecatetraenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,4Z,7Z,10Z,13Z)-hexadecapentaenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z)-dodecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z)-dodecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z)-tetradecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z)-tetradecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z,8Z)-tetradecadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z,8Z)-tetradecatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (5Z,8Z,11Z)-tetradecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,5Z,8Z,11Z)-tetradecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z)-dodecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z)-dodecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z)-octadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z,9Z)-dodecadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z,9Z)-dodecatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z,9Z,12Z)-octadecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z,9Z,12Z)-octadecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,6Z,9Z,12Z,15Z)-octadecapentaenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z)-octadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z)-tetradecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z)-tetradecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z,10Z)-hexadecadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z,10Z)-hexadecatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (7Z,10Z,13Z)-hexadecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,7Z,10Z,13Z)-hexadecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: (9Z)-eicosenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,9Z)-eicosadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (9Z)-hexadecenoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,9Z)-hexadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (9Z,12Z)-octadecadienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,9Z,12Z)-octadecatrienoyl-CoA + reduced [electron-transfer flavoprotein]

name: (9Z,12Z,15Z)-octadecatrienoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E,9Z,12Z,15Z)-octadecatetraenoyl-CoA + reduced [electron-transfer flavoprotein]

name: a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]

name: dodecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: eicosanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]

name: octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: oxidized [electron-transfer flavoprotein] + (9Z)-octadecenoyl-CoA + H(+) = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-transfer flavoprotein]

name: oxidized [electron-transfer flavoprotein] + hexadecanoyl-CoA + H(+) = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]

name: tetradecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-tetradecenoyl-CoA + reduced [electron-transfer flavoprotein]

value: Belongs to the acyl-CoA dehydrogenase family

description: Acyl-CoA dehydrogenase/oxidase N-terminal

description: Acyl-CoA dehydrogenase/oxidase middle

description: Disordered

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.
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.

value: Expressed in upper arm skin and 178 other cell types or tissues

value: F:long-chain fatty acyl-CoA dehydrogenase activity

value: acyl-CoA dehydrogenase family member 9, mitochondrial

value: very long-chain specific acyl-CoA dehydrogenase, mitochondrial

value: Very long-chain-specific acyl-CoA dehydrogenase, mitochondrial

value: Acyl-CoA dehydrogenase/oxidase, N-terminal domain

value: Butyryl-CoA Dehydrogenase, subunit A, domain 2

value: Butyryl-CoA Dehydrogenase, subunit A, domain 3

value: COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL

value: Acyl-CoA dehydrogenase C-terminal domain-like


value: Cell division control protein 42 homolog

value: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins

value: GO

value: Membrane

value: small monomeric GTPase

value: RHOJ

commentType: COFACTOR

value: Belongs to the small GTPase superfamily. Rab family

description: Switch-I

description: Switch-II

description: Disordered

description: Basic and acidic residues

GTP-binding

category: Ligand

database: PubMed

database: DOI

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

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

database: SwissPalm

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

value: P:small GTPase-mediated signal transduction

value: P-loop containing nucleotide triphosphate hydrolases

value: P-loop containing nucleoside triphosphate hydrolases


value: Signal peptidase complex subunit 2 homolog (S. cerevisiae)

value: substring

value: Signal peptidase complex subunit 2

value: Endoplasmic reticulum membrane

value: F:peptidase activity

value: hydrated

value: P:signal peptide processing

value: C:signal peptidase complex

scientificName: Mus musculus

commonName: Mouse

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

source: MGI

description: Disordered

description: Gly residues

description: Basic and acidic residues

description: Basic residues

authors:
Trinidad J.C.
Specht C.G.
Thalhammer A.
Schoepfer R.
Burlingame A.L.

title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.

journal: Mol. Cell. Proteomics

authors:
Church D.M.
Goodstadt L.
Hillier L.W.
Zody M.C.
Goldstein S.
She X.
Bult C.J.
Agarwala R.
Cherry J.L.
DiCuccio M.
Hlavina W.
Kapustin Y.
Meric P.
Maglott D.
Birtle Z.
Marques A.C.
Graves T.
Zhou S.
Teague B.
Potamousis K.
Churas C.
Place M.
Herschleb J.
Runnheim R.
Forrest D.
Amos-Landgraf J.
Schwartz D.C.
Cheng Z.
Lindblad-Toh K.
Eichler E.E.
Ponting C.P.

title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

journal: PLoS Biol.

type: STRAIN

authors:
Church D.M.
Schneider V.A.
Graves T.
Auger K.
Cunningham F.
Bouk N.
Chen H.C.
Agarwala R.
McLaren W.M.
Ritchie G.R.
Albracht D.
Kremitzki M.
Rock S.
Kotkiewicz H.
Kremitzki C.
Wollam A.
Trani L.
Fulton L.
Fulton R.
Matthews L.
Whitehead S.
Chow W.
Torrance J.
Dunn M.
Harden G.
Threadgold G.
Wood J.
Collins J.
Heath P.
Griffiths G.
Pelan S.
Grafham D.
Eichler E.E.
Weinstock G.
Mardis E.R.
Wilson R.K.
Howe K.
Flicek P.
Hubbard T.

title: Modernizing reference genome assemblies.

database: AlphaFoldDB

database: SMR

database: jPOST

database: Antibodypedia

key: antibodies

value: 125 antibodies from 21 providers

database: AGR

database: MGI

value: Expressed in lacrimal gland and 260 other cell types or tissues


value: PANTHER

value: Succinate dehydrogenase assembly factor 2, mitochondrial

value: Mitochondrion matrix

value: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SDHA of the SDH catalytic dimer

value: P:protein-FAD linkage

value: C:mitochondrial matrix

value: P:mitochondrial electron transport, succinate to ubiquinone

value: Succinate dehydrogenase complex assembly factor 2

value: 57 antibodies from 24 providers

database: Ensembl

database: VEuPathDB

value: Chromosome 19

value: Expressed in otic placode and 261 other cell types or tissues

database: ExpressionAtlas

value: baseline and differential

value: P:negative regulation of canonical Wnt signaling pathway

value: P:negative regulation of epithelial to mesenchymal transition

value: SUCCINATE DEHYDROGENASE ASSEMBLY FACTOR 2, MITOCHONDRIAL


value: Receptor ligand binding region

value: domain

value: Receptor ligand binding region domain-containing protein

value: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity

proteinExistence: 4: Predicted

value: Vomeronasal 2, receptor 73

value: Cell membrane

value: Multi-pass membrane protein

type: Signal

type: Chain

description: Receptor ligand binding region

description: GPCR family 3 nine cysteines

Signal

category: Domain

database: GeneTree

database: Proteomes

value: Chromosome 7


value: Metallo-beta-lactamase

value: Mitochondrion matrix

value: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid

scientificName: Rattus norvegicus

commonName: Rat

source: EMBL

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

proteinExistence: 2: Evidence at transcript level

value: Pnkd protein

source: RGD

value: Pnkd

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

description: Metallo-beta-lactamase

source: SMART

description: Disordered

description: Disordered

description: Polar residues

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

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

journal: Genome Res.

value: Spleen

type: TISSUE

database: EMBL

value: mRNA

database: RefSeq

key: NucleotideSequenceId

database: STRING

database: PaxDb

database: GeneID

database: KEGG

database: CTD

database: RGD

database: OrthoDB

database: Bgee

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

value: P:methylglyoxal catabolic process

database: CDD

key: EntryName

key: MatchStatus


value: Myotubularin phosphatase

value: domain

value: Myotubularin phosphatase domain-containing protein

value: keyword

value: hydrated

value: Membrane

database: GO

value: Cytoplasm

value: Myotubularin-related protein 12

value: Inactive phosphatidylinositol 3-phosphatase 12

value: Acts as an adapter for the myotubularin-related phosphatases. Regulates phosphatase MTM1 protein stability and possibly its intracellular location. By stabilizing MTM1 protein levels, required for skeletal muscle maintenance but not for myogenesis

value: Heterodimer with lipid phosphatase MTM1. Heterodimer with lipid phosphatase MTMR2

value: Cytoplasm, myofibril, sarcomere

value: Sarcoplasmic reticulum

value: Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily

description: Myotubularin-related protein 12

description: Myotubularin phosphatase

description: Disordered

description: Basic residues

description: Polar residues

authors:
Doris P.A.
Kalbfleisch T.
Li K.
Howe K.
Wood J.

title: GRCr8: a new rat reference genome assembly contstructed from accurate long reads and long range scaffolding.

submissionDatabase: EMBL/GenBank/DDBJ databases

value: Brown Norway

database: AlphaFoldDB

value: Chromosome 2

value: baseline and differential

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

value: (Phosphotyrosine protein) phosphatases II


value: PANTHER

value: Inactive tyrosine-protein kinase 7

value: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons

proteinExistence: 3: Inferred from homology

value: Protein-tyrosine kinase 7

value: Pseudo tyrosine kinase receptor 7

value: Tyrosine-protein kinase-like 7

value: Inactive tyrosine kinase involved in the Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathways. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis. Does not bind ATP

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

database: Rhea

database: ChEBI

value: Interacts with CTNNB1

value: Cell junction

value: Cell membrane

value: Single-pass type I membrane protein

value: Belongs to the protein kinase superfamily. Tyr protein kinase family

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

type: Transmembrane

description: Helical

description: Ig-like

description: Ig-like

description: Ig-like

description: Ig-like

description: Ig-like

description: Ig-like

description: Ig-like

description: Protein kinase

description: Disordered

description: Disordered

type: Active site

description: Proton acceptor

Cell adhesion

category: Biological process

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

value: P:establishment of epithelial cell apical/basal polarity

value: P:positive regulation of canonical Wnt signaling pathway

value: P:positive regulation of neuron projection development

value: Putative inactive tyrosine-protein kinase 7


value: Dolichol-phosphate mannosyltransferase subunit 1

value: substring

value: Dolichol-phosphate mannosyltransferase

value: GO

value: Membrane

value: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins

scientificName: Caenorhabditis elegans

lineage: Eukaryota Metazoa Ecdysozoa Nematoda Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis

source: WormBase

authors:
Sulson J.E.
Waterston R.

database: PubMed

database: DOI

title: Genome sequence of the nematode C. elegans: a platform for investigating biology.

journal: Science

value: Bristol N2

database: PeptideAtlas

database: AGR

database: WormBase

database: HOGENOM

value: Chromosome IV

value: Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues

database: ExpressionAtlas

value: baseline and differential

database: InterPro

database: PANTHER

value: DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE SUBUNIT 1


source: Google

value: PANTHER

value: DDB1- and CUL4-associated factor 11

value: Nucleus

value: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex

value: F:translation regulator activity

value: F:ribosome binding

source: PIRNR

value: DDB1- and CUL4-associated factor 11 homolog

value: Involved in regulation of lifespan. Required for dopaminergic CEP neuron degeneration in response to Mn(2+)

value: Belongs to the WD repeat LEC14B family

type: Repeat

description: WD

description: WD

description: WD

database: EMBL

database: RefSeq

database: SMR

database: GeneID

database: CTD

database: Proteomes

value: Chromosome I

value: DDB1-and CUL4-associated factor 11 homolog

value: YVTN repeat-like/Quinoprotein amine dehydrogenase


value: Serpin B10

value: Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen

value: Secreted

database: GO

value: P:negative regulation of peptidase activity

value: F:serine-type endopeptidase inhibitor activity

source: Proteomes

value: Serpin domain-containing protein

description: Serpin

value: Bristol N2

database: PIR

database: AlphaFoldDB

database: FunCoup

key: Number of interactors

database: STRING

database: PaxDb

database: KEGG

database: UCSC

value: c. elegans

database: eggNOG

key: ToxonomicScope

value: Eukaryota

database: InParanoid

database: OMA

key: Fingerprint

database: OrthoDB

database: PhylomeDB

database: Reactome

key: PathwayName

value: Platelet degranulation

value: Collagen biosynthesis and modifying enzymes

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

value: Regulation of FXIIa and plasma kallikrein activity


value: AAA+ ATPase

value: domain

value: AAA+ ATPase domain-containing protein

value: Chloroplast membrane

value: Plastid

value: Probable ATP-dependent zinc metallopeptidase

scientificName: Arabidopsis thaliana

commonName: Mouse-ear cress

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

value: FTSH protease 12

source: TAIR

value: EMBRYO DEFECTIVE 1047

value: EMBRYO DEFECTIVE 156

value: EMBRYO DEFECTIVE 36

source: Araport

database: ChEBI

value: In the C-terminal section; belongs to the peptidase M41 family

value: In the N-terminal section; belongs to the AAA ATPase family

description: Helical

description: Helical

description: AAA+ ATPase

authors:
Theologis A.
Ecker J.R.
Palm C.J.
Federspiel N.A.
Kaul S.
White O.
Alonso J.
Altafi H.
Araujo R.
Bowman C.L.
Brooks S.Y.
Buehler E.
Chan A.
Chao Q.
Chen H.
Cheuk R.F.
Chin C.W.
Chung M.K.
Conn L.
Conway A.B.
Conway A.R.
Creasy T.H.
Dewar K.
Dunn P.
Etgu P.
Feldblyum T.V.
Feng J.
Fong B.
Fujii C.Y.
Gill J.E.
Goldsmith A.D.
Haas B.
Hansen N.F.
Hughes B.
Huizar L.
Hunter J.L.
Jenkins J.
Johnson-Hopson C.
Khan S.
Khaykin E.
Kim C.J.
Koo H.L.
Kremenetskaia I.
Kurtz D.B.
Kwan A.
Lam B.
Langin-Hooper S.
Lee A.
Lee J.M.
Lenz C.A.
Li J.H.
Li Y.
Lin X.
Liu S.X.
Liu Z.A.
Luros J.S.
Maiti R.
Marziali A.
Militscher J.
Miranda M.
Nguyen M.
Nierman W.C.
Osborne B.I.
Pai G.
Peterson J.
Pham P.K.
Rizzo M.
Rooney T.
Rowley D.
Sakano H.
Salzberg S.L.
Schwartz J.R.
Shinn P.
Southwick A.M.
Sun H.
Tallon L.J.
Tambunga G.
Toriumi M.J.
Town C.D.
Utterback T.
Van Aken S.
Vaysberg M.
Vysotskaia V.S.
Walker M.
Wu D.
Yu G.
Fraser C.M.
Venter J.C.
Davis R.W.

database: PubMed

database: DOI

title: Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.

value: cv. Columbia

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

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

journal: Plant J.

value: ATP-dependent zinc metalloprotease FTSH 12, chloroplastic

value: P-loop containing nucleotide triphosphate hydrolases

value: ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 12, CHLOROPLASTIC

value: P-loop containing nucleoside triphosphate hydrolases


value: DNA damage-binding protein CMR1

value: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC

value: GO

value: Nucleus

value: WD repeat-containing protein 76

value: DROUGHT SENSITIVE 1

value: Belongs to the WD repeat DDB2/WDR76 family

description: WD

source: PROSITE-ProRule

description: Disordered

source: SAM

description: Polar residues

database: EMBL

key: ProteinId

database: RefSeq

database: SMR

database: ProteomicsDB

database: GeneID

database: Araport

database: TAIR

value: YVTN repeat-like/Quinoprotein amine dehydrogenase


value: Phosphoglycerate mutase-like protein

database: GO

key: GoTerm

value: F:catalytic activity

key: GoEvidenceType

value: Uncharacterized protein At4g38370

authors:
Totoki Y.
Seki M.
Ishida J.
Nakajima M.
Enju A.
Morosawa T.
Kamiya A.
Narusaka M.
Shin-i T.
Nakagawa M.
Sakamoto N.
Oishi K.
Kohara Y.
Kobayashi M.
Toyoda A.
Sakaki Y.
Sakurai T.
Iida K.
Akiyama K.
Satou M.
Toyoda T.
Konagaya A.
Carninci P.
Kawai J.
Hayashizaki Y.
Shinozaki K.

title: Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.

authors:
Bienvenut W.V.
Sumpton D.
Martinez A.
Lilla S.
Espagne C.
Meinnel T.
Giglione C.

title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

key: Status

value: mRNA

database: AlphaFoldDB

database: STRING

database: PaxDb

database: KEGG

value: Eukaryota

database: HOGENOM

database: CDD

database: FunFam

value: Phosphoglycerate mutase family protein

value: Phosphoglycerate mutase-like

database: InterPro

database: PANTHER

value: PHOSPHOGLYCERATE MUTASE FAMILY PROTEIN

database: Pfam

database: SMART

value: PGAM

database: SUPFAM


value: Uncharacterized protein

value: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis

value: F:oxidoreductase activity

value: hydrated

scientificName: Danio rerio

commonName: Zebrafish

lineage: Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Actinopterygii Neopterygii Teleostei Ostariophysi Cypriniformes Danionidae Danioninae Danio

value: Dicarbonyl/L-xylulose reductase

source: ZFIN

value: dcxr

value: Homotetramer

value: Belongs to the short-chain dehydrogenases/reductases (SDR) family

description: Proton acceptor

authoringGroup: NIH - Zebrafish Gene Collection (ZGC) project

value: Ovary

database: EMBL

key: MoleculeType

database: RefSeq

key: Description

database: SMR

database: PeptideAtlas

database: AGR

database: CTD

database: ZFIN

database: eggNOG

database: GeneTree

database: OMA

database: OrthoDB

database: Reactome

value: Formation of xylulose-5-phosphate

database: Bgee

value: Expressed in mature ovarian follicle and 26 other cell types or tissues

value: F:carbonyl reductase (NADPH) activity

value: F:L-xylulose reductase (NADPH) activity

value: P:glucose metabolic process

value: P:xylulose metabolic process


database: GO

value: F:DNA binding

value: GO

value: P:regulation of DNA-templated transcription

value: F:protein dimerization activity

value: Hairy and enhancer of split 6 (Drosophila)

value: Hairy-related 13.2

commentType: INTERACTION

source: ARBA

value: Nucleus

description: BHLH

source: PROSITE

description: Orange

description: Disordered

description: Helix-loop-helix motif

description: Disordered

description: Basic and acidic residues

description: Low complexity

value: Embryo

authors:
Kawamura A.
Koshida S.
Hijikata H.
Sakaguchi T.
Kondoh H.
Takada S.

database: PubMed

database: DOI

title: Zebrafish hairy/enhancer of split protein links FGF signaling to cyclic gene expression in the periodic segmentation of somites.

journal: Genes Dev.

value: mRNA

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

value: F:RNA polymerase II cis-regulatory region sequence-specific DNA binding

value: P:negative regulation of DNA-templated transcription

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

value: BASIC HELIX-LOOP-HELIX TRANSCRIPTION FACTOR, HES-RELATED

value: HLH, helix-loop-helix DNA-binding domain


value: Uncharacterized protein

value: UTP--glucose-1-phosphate uridylyltransferase catalyzing the conversion of glucose-1-phosphate into UDP-glucose, a crucial precursor for the production of glycogen

scientificName: Xenopus laevis

commonName: African clawed frog

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

value: Uap1-prov protein

source: Xenbase

value: Belongs to the UDPGP type 1 family

authoringGroup: NIH - Xenopus Gene Collection (XGC) project

database: AlphaFoldDB

database: GeneID

database: KEGG

database: Xenbase

key: GeneName

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

database: CDD

database: FunFam

value: UDP-N-acetylhexosamine pyrophosphorylase isoform X2

value: Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A

database: InterPro

database: PANTHER

value: UDP- GLUCOSE PYROPHOSPHORYLASE

database: Pfam

value: UDPGP

database: SUPFAM

value: Nucleotide-diphospho-sugar transferases