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SUMO-conjugating enzyme UBC9 (EC 2.3.2.-) (RING-type E3 SUMO transferase UBC9) (SUMO-protein ligase) (Ubiquitin carrier protein 9) (Ubiquitin-conjugating enzyme E2 9) (Ubiquitin-protein ligase 9)

 UBC9_CAEEL              Reviewed;         166 AA.
Q95017; Q9GYI5;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
12-SEP-2018, entry version 145.
RecName: Full=SUMO-conjugating enzyme UBC9;
EC=2.3.2.-;
AltName: Full=RING-type E3 SUMO transferase UBC9;
AltName: Full=SUMO-protein ligase;
AltName: Full=Ubiquitin carrier protein 9;
AltName: Full=Ubiquitin-conjugating enzyme E2 9;
AltName: Full=Ubiquitin-protein ligase 9;
Name=ubc-9; ORFNames=F29B9.6;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SMO-1.
STRAIN=Bristol N2;
Li T., Sun B., Lee M.-K., Teo T.-S.;
"Ubc-9 of Caenorhabditis elegans: identification, characterization and
interaction with smt-3.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION, AND INTERACTION WITH SOP-2.
PubMed=11806825;
Jones D., Crowe E., Stevens T.A., Candido E.P.M.;
"Functional and phylogenetic analysis of the ubiquitylation system in
Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-
activating enzymes, and ubiquitin-like proteins.";
Genome Biol. 3:RESEARCH0002.1-RESEARCH0002.15(2002).
[4]
FUNCTION, INTERACTION WITH BRD-1 AND RAD-51, AND DISRUPTION PHENOTYPE.
PubMed=14711411; DOI=10.1016/j.cub.2003.11.029;
Boulton S.J., Martin J.S., Polanowska J., Hill D.E., Gartner A.,
Vidal M.;
"BRCA1/BARD1 orthologs required for DNA repair in Caenorhabditis
elegans.";
Curr. Biol. 14:33-39(2004).
[5]
FUNCTION.
PubMed=15107848; DOI=10.1038/ng1336;
Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S.,
Haber D.A.;
"SUMO modification is required for in vivo Hox gene regulation by the
Caenorhabditis elegans Polycomb group protein SOP-2.";
Nat. Genet. 36:507-511(2004).
[6]
FUNCTION.
PubMed=15689373; DOI=10.1242/dev.01664;
Leight E.R., Glossip D., Kornfeld K.;
"Sumoylation of LIN-1 promotes transcriptional repression and
inhibition of vulval cell fates.";
Development 132:1047-1056(2005).
[7]
FUNCTION.
PubMed=15990876; DOI=10.1038/sj.emboj.7600726;
Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J.;
"Chromatin regulation and sumoylation in the inhibition of Ras-induced
vulval development in Caenorhabditis elegans.";
EMBO J. 24:2613-2623(2005).
[8]
FUNCTION.
PubMed=16701625; DOI=10.1016/j.ydbio.2006.04.001;
Roy Chowdhuri S., Crum T., Woollard A., Aslam S., Okkema P.G.;
"The T-box factor TBX-2 and the SUMO conjugating enzyme UBC-9 are
required for ABa-derived pharyngeal muscle in C. elegans.";
Dev. Biol. 295:664-677(2006).
[9]
INTERACTION WITH BET-1.
PubMed=24349540; DOI=10.1371/journal.pone.0083659;
Gee F., Fisher K., Klemstein U., Poulin G.B.;
"An RNAi-based dimorphic genetic screen identified the double
bromodomain protein BET-1 as a sumo-dependent attenuator of RAS-
mediated signalling.";
PLoS ONE 8:E83659-E83659(2013).
[10]
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=25475837; DOI=10.1038/ncomms6485;
Pelisch F., Sonneville R., Pourkarimi E., Agostinho A., Blow J.J.,
Gartner A., Hay R.T.;
"Dynamic SUMO modification regulates mitotic chromosome assembly and
cell cycle progression in Caenorhabditis elegans.";
Nat. Commun. 5:5485-5485(2014).
-!- FUNCTION: Accepts the ubiquitin-like protein smo-1 from the aos-1-
uba-2 E1 complex and catalyzes its covalent attachment to other
proteins with the help of an E3 ligase such as gei-17. Required to
sumoylate the ETS transcription factor lin-1 and the Polycomb
protein sop-2. Required for embryonic development, fertility,
vulval morphogenesis and inhibition of vulval cell fates.
{ECO:0000269|PubMed:11806825, ECO:0000269|PubMed:14711411,
ECO:0000269|PubMed:15107848, ECO:0000269|PubMed:15689373,
ECO:0000269|PubMed:15990876, ECO:0000269|PubMed:16701625}.
-!- CATALYTIC ACTIVITY: SUMOyl-[E2 SUMO-conjugating enzyme]-L-cysteine
+ [acceptor-protein]-L-lysine = [E2 SUMO-conjugating enzyme]-L-
cysteine + N(6)-SUMOyl-[acceptor protein]-L-lysine.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Interacts with brd-1 and rad-51 (PubMed:14711411).
Interacts with smo-1 and sop-2 (Ref.1, PubMed:15107848). Interacts
with bet-1 (via BROMO domain 2) (PubMed:24349540).
{ECO:0000269|PubMed:14711411, ECO:0000269|PubMed:24349540,
ECO:0000269|Ref.1}.
-!- INTERACTION:
Q21209:brd-1; NbExp=4; IntAct=EBI-328938, EBI-3895480;
Q95Q25:rad-51; NbExp=4; IntAct=EBI-328938, EBI-321895;
P55853:smo-1; NbExp=5; IntAct=EBI-328938, EBI-313647;
-!- SUBCELLULAR LOCATION: Nucleus envelope
{ECO:0000269|PubMed:25475837}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in
sterility, embryonic lethality and sensitivity to radiation
(PubMed:14711411). RNAi-mediated knockdown causes a number of
defects during the first embryonic mitotic division including loss
of smo-1 from metaphase chromosomes, chromosome misalignment at
metaphase, diminished spindle pole separation, slow chromosome
segregation, decreased distance between chromosomes afer anaphase
onset and increased air-2 levels in the spindle midzone
(PubMed:25475837). {ECO:0000269|PubMed:14711411,
ECO:0000269|PubMed:25475837}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AF106565; AAC97374.1; -; mRNA.
EMBL; FO081255; CCD70229.1; -; Genomic_DNA.
PIR; T29929; T29929.
RefSeq; NP_001023158.1; NM_001027987.3.
UniGene; Cel.38991; -.
ProteinModelPortal; Q95017; -.
SMR; Q95017; -.
BioGrid; 533085; 8.
DIP; DIP-25778N; -.
IntAct; Q95017; 10.
MINT; Q95017; -.
STRING; 6239.F29B9.6.1; -.
MoonDB; Q95017; Predicted.
EPD; Q95017; -.
PaxDb; Q95017; -.
PeptideAtlas; Q95017; -.
PRIDE; Q95017; -.
EnsemblMetazoa; F29B9.6.1; F29B9.6.1; WBGene00006706.
EnsemblMetazoa; F29B9.6.2; F29B9.6.2; WBGene00006706.
GeneID; 3565767; -.
KEGG; cel:CELE_F29B9.6; -.
UCSC; F29B9.6.1; c. elegans.
CTD; 3565767; -.
WormBase; F29B9.6; CE09784; WBGene00006706; ubc-9.
eggNOG; KOG0424; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00550000075088; -.
HOGENOM; HOG000233454; -.
InParanoid; Q95017; -.
KO; K10577; -.
OMA; KCKFTPP; -.
OrthoDB; EOG091G0NAK; -.
PhylomeDB; Q95017; -.
Reactome; R-CEL-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-CEL-3232118; SUMOylation of transcription factors.
Reactome; R-CEL-3899300; SUMOylation of transcription cofactors.
Reactome; R-CEL-4085377; SUMOylation of SUMOylation proteins.
Reactome; R-CEL-4090294; SUMOylation of intracellular receptors.
Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-CEL-4570464; SUMOylation of RNA binding proteins.
Reactome; R-CEL-4615885; SUMOylation of DNA replication proteins.
Reactome; R-CEL-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-CEL-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
UniPathway; UPA00886; -.
PRO; PR:Q95017; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00006706; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:WormBase.
GO; GO:0032093; F:SAM domain binding; IPI:WormBase.
GO; GO:0061656; F:SUMO conjugating enzyme activity; IDA:WormBase.
GO; GO:0019789; F:SUMO transferase activity; IDA:WormBase.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:WormBase.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
GO; GO:0002119; P:nematode larval development; IMP:WormBase.
GO; GO:0043282; P:pharyngeal muscle development; IMP:WormBase.
GO; GO:0016925; P:protein sumoylation; IDA:WormBase.
GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
GO; GO:1903827; P:regulation of cellular protein localization; IMP:WormBase.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR027230; Ubc9.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
PANTHER; PTHR43927; PTHR43927; 1.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Developmental protein;
Nucleotide-binding; Nucleus; Reference proteome; Transferase;
Ubl conjugation pathway.
CHAIN 1 166 SUMO-conjugating enzyme UBC9.
/FTId=PRO_0000082517.
ACT_SITE 93 93 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
SEQUENCE 166 AA; 19115 MW; E5A5AFA773DE286C CRC64;
MSGIAAGRLA EERKHWRKDH PFGFIAKPVK NADGTLNLFN WECAIPGRKD TIWEGGLYRI
RMLFKDDFPS TPPKCKFEPP LFHPNVYPSG TVCLSLLDEN KDWKPSISIK QLLIGIQDLL
NHPNIEDPAQ AEAYQIYCQN RAEYEKRVKK EAVKYAAELV QKQMLE


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