UBC9_CAEEL
ID UBC9_CAEEL Reviewed; 166 AA.
AC Q95017; Q9GYI5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=SUMO-conjugating enzyme UBC9;
DE EC=2.3.2.-;
DE AltName: Full=RING-type E3 SUMO transferase UBC9;
DE AltName: Full=SUMO-protein ligase;
DE AltName: Full=Ubiquitin carrier protein 9;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 9;
DE AltName: Full=Ubiquitin-protein ligase 9;
GN Name=ubc-9 {ECO:0000312|WormBase:F29B9.6};
GN ORFNames=F29B9.6 {ECO:0000312|WormBase:F29B9.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SMO-1.
RC STRAIN=Bristol N2;
RA Li T., Sun B., Lee M.-K., Teo T.-S.;
RT "Ubc-9 of Caenorhabditis elegans: identification, characterization and
RT interaction with smt-3.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND INTERACTION WITH SOP-2.
RX PubMed=11806825; DOI=10.1186/gb-2001-3-1-research0002;
RA Jones D., Crowe E., Stevens T.A., Candido E.P.M.;
RT "Functional and phylogenetic analysis of the ubiquitylation system in
RT Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating
RT enzymes, and ubiquitin-like proteins.";
RL Genome Biol. 3:RESEARCH0002.1-RESEARCH0002.15(2002).
RN [4]
RP FUNCTION, INTERACTION WITH BRD-1 AND RAD-51, AND DISRUPTION PHENOTYPE.
RX PubMed=14711411; DOI=10.1016/j.cub.2003.11.029;
RA Boulton S.J., Martin J.S., Polanowska J., Hill D.E., Gartner A., Vidal M.;
RT "BRCA1/BARD1 orthologs required for DNA repair in Caenorhabditis elegans.";
RL Curr. Biol. 14:33-39(2004).
RN [5]
RP FUNCTION.
RX PubMed=15107848; DOI=10.1038/ng1336;
RA Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S.,
RA Haber D.A.;
RT "SUMO modification is required for in vivo Hox gene regulation by the
RT Caenorhabditis elegans Polycomb group protein SOP-2.";
RL Nat. Genet. 36:507-511(2004).
RN [6]
RP FUNCTION.
RX PubMed=15689373; DOI=10.1242/dev.01664;
RA Leight E.R., Glossip D., Kornfeld K.;
RT "Sumoylation of LIN-1 promotes transcriptional repression and inhibition of
RT vulval cell fates.";
RL Development 132:1047-1056(2005).
RN [7]
RP FUNCTION.
RX PubMed=15990876; DOI=10.1038/sj.emboj.7600726;
RA Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J.;
RT "Chromatin regulation and sumoylation in the inhibition of Ras-induced
RT vulval development in Caenorhabditis elegans.";
RL EMBO J. 24:2613-2623(2005).
RN [8]
RP FUNCTION.
RX PubMed=16701625; DOI=10.1016/j.ydbio.2006.04.001;
RA Roy Chowdhuri S., Crum T., Woollard A., Aslam S., Okkema P.G.;
RT "The T-box factor TBX-2 and the SUMO conjugating enzyme UBC-9 are required
RT for ABa-derived pharyngeal muscle in C. elegans.";
RL Dev. Biol. 295:664-677(2006).
RN [9]
RP INTERACTION WITH BET-1.
RX PubMed=24349540; DOI=10.1371/journal.pone.0083659;
RA Gee F., Fisher K., Klemstein U., Poulin G.B.;
RT "An RNAi-based dimorphic genetic screen identified the double bromodomain
RT protein BET-1 as a sumo-dependent attenuator of RAS-mediated signalling.";
RL PLoS ONE 8:E83659-E83659(2013).
RN [10]
RP FUNCTION, INTERACTION WITH XBP-1, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24933177; DOI=10.1016/j.biocel.2014.06.005;
RA Lim Y., Lee D., Kalichamy K., Hong S.E., Michalak M., Ahnn J., Kim D.H.,
RA Lee S.K.;
RT "Sumoylation regulates ER stress response by modulating calreticulin gene
RT expression in XBP-1-dependent mode in Caenorhabditis elegans.";
RL Int. J. Biochem. Cell Biol. 53:399-408(2014).
RN [11]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25475837; DOI=10.1038/ncomms6485;
RA Pelisch F., Sonneville R., Pourkarimi E., Agostinho A., Blow J.J.,
RA Gartner A., Hay R.T.;
RT "Dynamic SUMO modification regulates mitotic chromosome assembly and cell
RT cycle progression in Caenorhabditis elegans.";
RL Nat. Commun. 5:5485-5485(2014).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=25873636; DOI=10.1534/g3.115.018101;
RA Milton A.C., Okkema P.G.;
RT "Caenorhabditis elegans TBX-2 Directly Regulates Its Own Expression in a
RT Negative Autoregulatory Loop.";
RL G3 (Bethesda) 5:1177-1186(2015).
CC -!- FUNCTION: Accepts the ubiquitin-like protein smo-1 from the aos-1-uba-2
CC E1 complex and catalyzes its covalent attachment to other proteins with
CC the help of an E3 ligase such as gei-17. Required to sumoylate the ETS
CC transcription factor lin-1, Polycomb protein sop-2, and intermediate
CC filament proteins, such as ifb-1 (PubMed:15107848, PubMed:15689373,
CC PubMed:24933177). Required for embryonic development, fertility, vulval
CC morphogenesis, inhibition of vulval cell fates, lifespan, and
CC neuromuscular activity (PubMed:24933177). {ECO:0000269|PubMed:11806825,
CC ECO:0000269|PubMed:14711411, ECO:0000269|PubMed:15107848,
CC ECO:0000269|PubMed:15689373, ECO:0000269|PubMed:15990876,
CC ECO:0000269|PubMed:16701625, ECO:0000269|PubMed:24933177}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with brd-1 and rad-51 (PubMed:14711411). Interacts
CC with smo-1 and sop-2 (Ref.1, PubMed:15107848). Interacts with bet-1
CC (via BROMO domain 2) (PubMed:24349540). Interacts with isoforms 1 and 2
CC of X-box-binding protein xbp-1. {ECO:0000269|PubMed:14711411,
CC ECO:0000269|PubMed:24349540, ECO:0000269|PubMed:24933177,
CC ECO:0000269|Ref.1}.
CC -!- INTERACTION:
CC Q95017; Q21209: brd-1; NbExp=4; IntAct=EBI-328938, EBI-3895480;
CC Q95017; Q95Q25: rad-51; NbExp=4; IntAct=EBI-328938, EBI-321895;
CC Q95017; P55853: smo-1; NbExp=5; IntAct=EBI-328938, EBI-313647;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:25475837}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed throughout development (at
CC protein level) (PubMed:24933177). Expressed in early embryos in utero,
CC in the pharynx and body-wall muscles during larval stages, becoming
CC prominent in coelomocytes and the male tail in young adults
CC (PubMed:24933177). {ECO:0000269|PubMed:24933177}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in sterility,
CC embryonic lethality and sensitivity to radiation (PubMed:14711411,
CC PubMed:25873636). RNAi-mediated knockdown causes a number of defects
CC during the first embryonic mitotic division including loss of smo-1
CC from metaphase chromosomes, chromosome misalignment at metaphase,
CC diminished spindle pole separation, slow chromosome segregation,
CC decreased distance between chromosomes afer anaphase onset and
CC increased air-2 levels in the spindle midzone (PubMed:25475837). RNAi-
CC mediated knockdown results in ectopic tbx-2 expression in seam cells,
CC the gut and in the syncytial hypodermis (PubMed:25873636). Exhibits
CC abnormal localization and structure of intermediate filament protein
CC ifb-1, such as altered filaments and aggregates, resulting in
CC elongation defects of embryos. {ECO:0000269|PubMed:14711411,
CC ECO:0000269|PubMed:24933177, ECO:0000269|PubMed:25475837,
CC ECO:0000269|PubMed:25873636}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AF106565; AAC97374.1; -; mRNA.
DR EMBL; BX284604; CCD70229.1; -; Genomic_DNA.
DR PIR; T29929; T29929.
DR RefSeq; NP_001023158.1; NM_001027987.3.
DR AlphaFoldDB; Q95017; -.
DR SMR; Q95017; -.
DR BioGRID; 533085; 30.
DR DIP; DIP-25778N; -.
DR IntAct; Q95017; 10.
DR MINT; Q95017; -.
DR STRING; 6239.F29B9.6; -.
DR MoonDB; Q95017; Predicted.
DR EPD; Q95017; -.
DR PaxDb; Q95017; -.
DR PeptideAtlas; Q95017; -.
DR EnsemblMetazoa; F29B9.6.1; F29B9.6.1; WBGene00006706.
DR GeneID; 3565767; -.
DR KEGG; cel:CELE_F29B9.6; -.
DR UCSC; F29B9.6.1; c. elegans.
DR CTD; 3565767; -.
DR WormBase; F29B9.6; CE09784; WBGene00006706; ubc-9.
DR eggNOG; KOG0424; Eukaryota.
DR GeneTree; ENSGT00550000075088; -.
DR HOGENOM; CLU_030988_12_0_1; -.
DR InParanoid; Q95017; -.
DR OMA; QEPAWRA; -.
DR OrthoDB; 1522509at2759; -.
DR PhylomeDB; Q95017; -.
DR Reactome; R-CEL-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-CEL-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-CEL-3232118; SUMOylation of transcription factors.
DR Reactome; R-CEL-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-CEL-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-CEL-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-CEL-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-CEL-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-CEL-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR SignaLink; Q95017; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:Q95017; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006706; Expressed in embryo and 4 other tissues.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0032093; F:SAM domain binding; IPI:WormBase.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; IDA:WormBase.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0043282; P:pharyngeal muscle development; IMP:WormBase.
DR GO; GO:0016925; P:protein sumoylation; IDA:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..166
FT /note="SUMO-conjugating enzyme UBC9"
FT /id="PRO_0000082517"
FT DOMAIN 4..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 93
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 166 AA; 19115 MW; E5A5AFA773DE286C CRC64;
MSGIAAGRLA EERKHWRKDH PFGFIAKPVK NADGTLNLFN WECAIPGRKD TIWEGGLYRI
RMLFKDDFPS TPPKCKFEPP LFHPNVYPSG TVCLSLLDEN KDWKPSISIK QLLIGIQDLL
NHPNIEDPAQ AEAYQIYCQN RAEYEKRVKK EAVKYAAELV QKQMLE
