UBC9_RAT
ID UBC9_RAT Reviewed; 158 AA.
AC P63281; P50550; Q15698; Q86VB3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
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 carrier protein I;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 I;
DE AltName: Full=Ubiquitin-conjugating enzyme UbcE2A {ECO:0000303|PubMed:9013644};
DE AltName: Full=Ubiquitin-protein ligase I;
GN Name=Ube2i; Synonyms=Ubce9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TCF3, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=CD Charles River; TISSUE=Aorta;
RX PubMed=9013644; DOI=10.1074/jbc.272.6.3845;
RA Kho C.-J., Huggins G.S., Endege W.O., Hsieh C.-M., Lee M.-E., Haber E.;
RT "Degradation of E2A proteins through a ubiquitin-conjugating enzyme,
RT UbcE2A.";
RL J. Biol. Chem. 272:3845-3851(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=14739995;
RA Golebiowski F., Szulc A., Sakowicz M., Szutowicz A., Pawelczyk T.;
RT "Expression level of Ubc9 protein in rat tissues.";
RL Acta Biochim. Pol. 50:1065-1073(2003).
RN [4]
RP INTERACTION WITH RASD2.
RX PubMed=19498170; DOI=10.1126/science.1172871;
RA Subramaniam S., Sixt K.M., Barrow R., Snyder S.H.;
RT "Rhes, a striatal specific protein, mediates mutant-huntingtin
RT cytotoxicity.";
RL Science 324:1327-1330(2009).
CC -!- FUNCTION: Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3
CC from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent
CC attachment to other proteins with the help of an E3 ligase such as
CC RANBP2, CBX4 and ZNF451 (By similarity). Can catalyze the formation of
CC poly-SUMO chains (By similarity). Essential for nuclear architecture
CC and chromosome segregation (By similarity). Necessary for sumoylation
CC of FOXL2 and KAT5 (By similarity). Sumoylates p53/TP53 at 'Lys-386' (By
CC similarity). Mediates sumoylation of ERCC6 which is essential for its
CC transcription-coupled nucleotide excision repair activity (By
CC similarity). {ECO:0000250|UniProtKB:P63279}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Forms a complex with SENP6 and UBE2I in response to UV
CC irradiation (By similarity). Forms a tight complex with RANGAP1 and
CC RANBP2 (By similarity). Identified in a complex with SUMO2 and UBE2I,
CC where one ZNF451 interacts with one UBE2I and two SUMO2 chains, one
CC bound to the UBE2I active site and the other to another region of the
CC same UBE2I molecule (By similarity). Interacts with SETX (By
CC similarity). Interacts with HIPK1 and HIPK2 (By similarity). Interacts
CC with PPM1J (By similarity). Interacts with RASD2 (PubMed:19498170).
CC Interacts with TCF3 (PubMed:9013644). Interacts with NR2C1; the
CC interaction promotes its sumoylation (By similarity). Interacts with
CC SIAH1 (By similarity). Interacts with PARP (By similarity). Interacts
CC with various transcription factors such as TFAP2A, TFAP2B, and TFAP2C
CC (By similarity). Interacts with AR (By similarity). Interacts with ETS1
CC (By similarity). Interacts with SOX4 (By similarity). Interacts with
CC RWDD3; the interaction enhances the sumoylation of a number of proteins
CC such as HIF1A and I-kappa-B (By similarity). Interacts with FOXL2 (By
CC similarity). Interacts with DNM1l (via its GTPase and B domains); the
CC interaction promotes sumoylation of DNM1L, mainly in its B domain (By
CC similarity). Interacts with NFATC2IP; this inhibits formation of poly-
CC SUMO chains (By similarity). Interacts with FHIT (By similarity).
CC Interacts with PRKRA and p53/TP53 (By similarity). Interacts with UHRF2
CC (By similarity). Interacts with NR3C1 and this interaction is enhanced
CC in the presence of RWDD3 (By similarity). Interacts with MTA1 (By
CC similarity). Interacts with ZNF451 (By similarity). Interacts with
CC CPEB3 (By similarity). Interacts with SUMO1, SUMO2, and SUMO3 (By
CC similarity). Interacts with IPO13 (By similarity). Interacts with DNMT1
CC (By similarity). {ECO:0000250|UniProtKB:P63279,
CC ECO:0000250|UniProtKB:P63280, ECO:0000269|PubMed:19498170,
CC ECO:0000269|PubMed:9013644}.
CC -!- INTERACTION:
CC P63281; P42260: Grik2; NbExp=3; IntAct=EBI-7974723, EBI-7809795;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9013644}. Cytoplasm
CC {ECO:0000269|PubMed:9013644}. Note=Mainly nuclear (By similarity). In
CC spermatocytes, localizes in synaptonemal complexes (By similarity).
CC Recruited by BCL11A into the nuclear body (By similarity).
CC {ECO:0000250|UniProtKB:P63279, ECO:0000250|UniProtKB:P63280}.
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in spleen
CC and lung (at protein level). {ECO:0000269|PubMed:14739995}.
CC -!- PTM: Phosphorylation at Ser-71 significantly enhances SUMOylation
CC activity. {ECO:0000250|UniProtKB:P63279}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; U54632; AAC98704.1; -; mRNA.
DR EMBL; BC086324; AAH86324.1; -; mRNA.
DR EMBL; BC086592; AAH86592.1; -; mRNA.
DR RefSeq; NP_037182.1; NM_013050.1.
DR RefSeq; XP_006245980.2; XM_006245918.3.
DR RefSeq; XP_006245981.1; XM_006245919.3.
DR RefSeq; XP_006245982.1; XM_006245920.3.
DR RefSeq; XP_008765771.2; XM_008767549.2.
DR RefSeq; XP_017452533.1; XM_017597044.1.
DR AlphaFoldDB; P63281; -.
DR BMRB; P63281; -.
DR SMR; P63281; -.
DR BioGRID; 247604; 13.
DR DIP; DIP-47657N; -.
DR IntAct; P63281; 2.
DR MINT; P63281; -.
DR STRING; 10116.ENSRNOP00000024406; -.
DR iPTMnet; P63281; -.
DR PhosphoSitePlus; P63281; -.
DR jPOST; P63281; -.
DR PaxDb; P63281; -.
DR PRIDE; P63281; -.
DR Ensembl; ENSRNOT00000104064; ENSRNOP00000085922; ENSRNOG00000066579.
DR GeneID; 25573; -.
DR KEGG; rno:25573; -.
DR UCSC; RGD:3926; rat.
DR CTD; 7329; -.
DR RGD; 3926; Ube2i.
DR VEuPathDB; HostDB:ENSRNOG00000017907; -.
DR eggNOG; KOG0424; Eukaryota.
DR GeneTree; ENSGT00550000075088; -.
DR HOGENOM; CLU_030988_12_0_1; -.
DR InParanoid; P63281; -.
DR OMA; QEPAWRA; -.
DR OrthoDB; 1522509at2759; -.
DR PhylomeDB; P63281; -.
DR TreeFam; TF101122; -.
DR Reactome; R-RNO-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-RNO-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-RNO-3232118; SUMOylation of transcription factors.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-RNO-4755510; SUMOylation of immune response proteins.
DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-RNO-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR UniPathway; UPA00886; -.
DR PRO; PR:P63281; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000017907; Expressed in spleen and 19 other tissues.
DR Genevisible; P63281; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0001650; C:fibrillar center; IDA:RGD.
DR GO; GO:0016604; C:nuclear body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0016605; C:PML body; ISO:RGD.
DR GO; GO:0106068; C:SUMO ligase complex; ISO:RGD.
DR GO; GO:1990356; C:sumoylated E2 ligase complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:1990234; C:transferase complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0043398; F:HLH domain binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0071535; F:RING-like zinc finger domain binding; ISO:RGD.
DR GO; GO:0044388; F:small protein activating enzyme binding; ISO:RGD.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; ISO:RGD.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0033145; P:positive regulation of intracellular steroid hormone receptor signaling pathway; IDA:RGD.
DR GO; GO:1903755; P:positive regulation of SUMO transferase activity; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:RGD.
DR GO; GO:0016925; P:protein sumoylation; IDA:RGD.
DR GO; GO:0010469; P:regulation of signaling receptor activity; IDA:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:RGD.
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 Acetylation; ATP-binding; Cell cycle; Cell division; Chromosome partition;
KW Cytoplasm; Isopeptide bond; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CHAIN 2..158
FT /note="SUMO-conjugating enzyme UBC9"
FT /id="PRO_0000082457"
FT DOMAIN 4..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 13..18
FT /note="Interaction with SUMO1"
FT /evidence="ECO:0000250"
FT ACT_SITE 93
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT SITE 4
FT /note="Interaction with RANBP2"
FT /evidence="ECO:0000250"
FT SITE 25
FT /note="Interaction with RANBP2"
FT /evidence="ECO:0000250"
FT SITE 57
FT /note="Interaction with RANBP2"
FT /evidence="ECO:0000250"
FT SITE 100..101
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT MOD_RES 71
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63279"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63279"
SQ SEQUENCE 158 AA; 18007 MW; E2C826E9C8D0683D CRC64;
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS
