UBC9_YEAST
ID UBC9_YEAST Reviewed; 157 AA.
AC P50623; D6VRT3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=SUMO-conjugating enzyme UBC9;
DE EC=2.3.2.-;
DE AltName: Full=RING-type E3 SUMO transferase UBC9;
DE AltName: Full=Ubiquitin carrier protein 9;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-18 kDa;
DE AltName: Full=Ubiquitin-protein ligase;
GN Name=UBC9; OrderedLocusNames=YDL064W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7800043; DOI=10.1038/373078a0;
RA Seufert W., Futcher B., Jentsch S.;
RT "Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase
RT cyclins.";
RL Nature 373:78-81(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=9341106; DOI=10.1074/jbc.272.43.26799;
RA Johnson E.S., Blobel G.;
RT "Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p.";
RL J. Biol. Chem. 272:26799-26802(1997).
RN [5]
RP INTERACTION WITH SIZ1, AND FUNCTION.
RX PubMed=11572779; DOI=10.1016/s0092-8674(01)00491-3;
RA Johnson E.S., Gupta A.A.;
RT "An E3-like factor that promotes SUMO conjugation to the yeast septins.";
RL Cell 106:735-744(2001).
RN [6]
RP INTERACTION WITH SIZ1.
RX PubMed=11587849; DOI=10.1016/s0378-1119(01)00662-x;
RA Takahashi Y., Toh-e A., Kikuchi Y.;
RT "A novel factor required for the SUMO1/Smt3 conjugation of yeast septins.";
RL Gene 275:223-231(2001).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: E2 ubiquitin-like--protein ligase mediating SUMO/Smt3
CC attachment to septins and PCNA. Seems to be involved in degradation of
CC S- (CLB5) and M-phase cyclins (CLB2). {ECO:0000269|PubMed:11572779,
CC ECO:0000269|PubMed:9341106}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with SIZ1. {ECO:0000269|PubMed:11572779,
CC ECO:0000269|PubMed:11587849}.
CC -!- INTERACTION:
CC P50623; Q12306: SMT3; NbExp=3; IntAct=EBI-19760, EBI-17490;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; X82538; CAA57888.1; -; Genomic_DNA.
DR EMBL; Z74112; CAA98629.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11793.1; -; Genomic_DNA.
DR PIR; S52414; S52414.
DR RefSeq; NP_010219.1; NM_001180123.1.
DR PDB; 2EKE; X-ray; 1.90 A; A/B=1-157.
DR PDB; 2GJD; X-ray; 1.75 A; A/B/C/D=1-157.
DR PDB; 3ONG; X-ray; 2.30 A; B/D=1-157.
DR PDB; 5JNE; X-ray; 2.85 A; B/F=1-157.
DR PDB; 6Q83; X-ray; 4.53 A; B=2-157.
DR PDB; 7P47; X-ray; 3.31 A; C=1-157.
DR PDBsum; 2EKE; -.
DR PDBsum; 2GJD; -.
DR PDBsum; 3ONG; -.
DR PDBsum; 5JNE; -.
DR PDBsum; 6Q83; -.
DR PDBsum; 7P47; -.
DR AlphaFoldDB; P50623; -.
DR SMR; P50623; -.
DR BioGRID; 31995; 295.
DR DIP; DIP-1531N; -.
DR IntAct; P50623; 8.
DR MINT; P50623; -.
DR STRING; 4932.YDL064W; -.
DR iPTMnet; P50623; -.
DR MaxQB; P50623; -.
DR PaxDb; P50623; -.
DR PRIDE; P50623; -.
DR EnsemblFungi; YDL064W_mRNA; YDL064W; YDL064W.
DR GeneID; 851495; -.
DR KEGG; sce:YDL064W; -.
DR SGD; S000002222; UBC9.
DR VEuPathDB; FungiDB:YDL064W; -.
DR eggNOG; KOG0424; Eukaryota.
DR GeneTree; ENSGT00550000075088; -.
DR HOGENOM; CLU_030988_12_0_1; -.
DR InParanoid; P50623; -.
DR OMA; QEPAWRA; -.
DR BioCyc; YEAST:G3O-29479-MON; -.
DR BRENDA; 2.3.2.23; 984.
DR Reactome; R-SCE-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-SCE-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-SCE-3232118; SUMOylation of transcription factors.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-SCE-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SCE-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR UniPathway; UPA00886; -.
DR EvolutionaryTrace; P50623; -.
DR PRO; PR:P50623; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P50623; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:SGD.
DR GO; GO:0016925; P:protein sumoylation; IDA:SGD.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR027230; Ubc9.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR24067:SF248; PTHR24067:SF248; 1.
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 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; Mitosis;
KW Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..157
FT /note="SUMO-conjugating enzyme UBC9"
FT /id="PRO_0000082556"
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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:2GJD"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2GJD"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:2GJD"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:2GJD"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:2GJD"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:2GJD"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2GJD"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2GJD"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2GJD"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:2GJD"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:2GJD"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:2GJD"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:2GJD"
SQ SEQUENCE 157 AA; 17911 MW; D74EE9845BB677B4 CRC64;
MSSLCLQRLQ EERKKWRKDH PFGFYAKPVK KADGSMDLQK WEAGIPGKEG TNWAGGVYPI
TVEYPNEYPS KPPKVKFPAG FYHPNVYPSG TICLSILNED QDWRPAITLK QIVLGVQDLL
DSPNPNSPAQ EPAWRSFSRN KAEYDKKVLL QAKQYSK
