UBC9_MOUSE
ID UBC9_MOUSE Reviewed; 158 AA.
AC P63280; P50550; Q15698; Q6RUT3; Q86VB3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 178.
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 Short=mUBC9;
DE AltName: Full=Ubiquitin carrier protein I;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 I;
DE AltName: Full=Ubiquitin-protein ligase I;
GN Name=Ube2i; Synonyms=Ubc9, Ubce2i, Ubce9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=MDF1; TISSUE=Promyelocytic leukemia;
RX PubMed=8839844;
RA Scott L.M., Mueller L., Collins S.J.;
RT "E3, a hematopoietic-specific transcript directly regulated by the retinoic
RT acid receptor alpha.";
RL Blood 88:2517-2530(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ADENOVIRUS TYPE 5 AND TYPE
RP 12 E1A.
RX PubMed=8824223; DOI=10.1074/jbc.271.42.25906;
RA Hateboer G., Hijmans E.M., Nooij J.B.D., Schlenker S., Jentsch S.,
RA Bernards R.;
RT "mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast
RT cell cycle defect.";
RL J. Biol. Chem. 271:25906-25911(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=8610150; DOI=10.1073/pnas.93.7.2958;
RA Kovalenko O.V., Plug A.W., Haaf T., Gonda D.K., Ashley T., Ward D.C.,
RA Radding C.M., Golub E.I.;
RT "Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51
RT recombination protein and localizes in synaptonemal complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2958-2963(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH TCF3.
RC STRAIN=BALB/cJ; TISSUE=Fibroblast;
RX PubMed=9409784; DOI=10.1016/s0378-1119(97)00444-7;
RA Loveys D.A., Streiff M.B., Schaefer T.S., Kato G.J.;
RT "The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A
RT transcription factors.";
RL Gene 201:169-177(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=B-cell lymphoma;
RX PubMed=9223278; DOI=10.1073/pnas.94.15.7862;
RA Tashiro K., Pando M.P., Kanegae Y., Wamsley P.M., Inoue S., Verma I.M.;
RT "Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the
RT degradation of IkappaBalpha.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7862-7867(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PJS1;
RA Weber B.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Head, Heart, Kidney, Liver, Lung, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [9]
RP INTERACTION WITH HIPK1 AND HIPK2.
RX PubMed=10535925; DOI=10.1073/pnas.96.22.12350;
RA Kim Y.H., Choi C.Y., Kim Y.;
RT "Covalent modification of the homeodomain-interacting protein kinase 2
RT (HIPK2) by the ubiquitin-like protein SUMO-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12350-12355(1999).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16326389; DOI=10.1016/j.devcel.2005.10.007;
RA Nacerddine K., Lehembre F., Bhaumik M., Artus J., Cohen-Tannoudji M.,
RA Babinet C., Pandolfi P.P., Dejean A.;
RT "The SUMO pathway is essential for nuclear integrity and chromosome
RT segregation in mice.";
RL Dev. Cell 9:769-779(2005).
RN [11]
RP INTERACTION WITH PPM1J.
RX PubMed=12633878; DOI=10.1016/s0014-5793(03)00153-4;
RA Kashiwaba M., Katsura K., Ohnishi M., Sasaki M., Tanaka H., Nishimune Y.,
RA Kobayashi T., Tamura S.;
RT "A novel protein phosphatase 2C family member (PP2Czeta) is able to
RT associate with ubiquitin conjugating enzyme 9.";
RL FEBS Lett. 538:197-202(2003).
RN [12]
RP INTERACTION WITH MOMLV CA.
RX PubMed=16352559; DOI=10.1128/jvi.80.1.342-352.2006;
RA Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K.,
RA Pu S.-Y., Goff S.P.;
RT "Interaction of moloney murine leukemia virus capsid with Ubc9 and PIASy
RT mediates SUMO-1 addition required early in infection.";
RL J. Virol. 80:342-352(2006).
RN [13]
RP INTERACTION WITH NR2C1, AND FUNCTION IN NR2C1 SUMOYLATION.
RX PubMed=17187077; DOI=10.1038/nsmb1185;
RA Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.;
RT "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4
RT expression in stem cells.";
RL Nat. Struct. Mol. Biol. 14:68-75(2007).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=18681895; DOI=10.1111/j.1365-2443.2008.01216.x;
RA Kuwata T., Nakamura T.;
RT "BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in
RT its nuclear body.";
RL Genes Cells 13:931-940(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP FUNCTION, AND INTERACTION WITH PRKRA AND TP53.
RX PubMed=22214662; DOI=10.4161/cc.11.2.18999;
RA Bennett R.L., Pan Y., Christian J., Hui T., May W.S. Jr.;
RT "The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and
RT activation, leading to G(1) arrest.";
RL Cell Cycle 11:407-417(2012).
RN [17]
RP INTERACTION WITH CPEB3.
RX PubMed=26074071; DOI=10.1016/j.celrep.2015.04.061;
RA Drisaldi B., Colnaghi L., Fioriti L., Rao N., Myers C., Snyder A.M.,
RA Metzger D.J., Tarasoff J., Konstantinov E., Fraser P.E., Manley J.L.,
RA Kandel E.R.;
RT "SUMOylation is an inhibitory constraint that regulates the prion-like
RT aggregation and activity of CPEB3.";
RL Cell Rep. 11:1694-1702(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9261152; DOI=10.1074/jbc.272.34.21381;
RA Tong H., Hateboer G., Perrakis A., Bernards R., Sixma T.K.;
RT "Crystal structure of murine/human Ubc9 provides insight into the
RT variability of the ubiquitin-conjugating system.";
RL J. Biol. Chem. 272:21381-21387(1997).
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. Can catalyze the formation of poly-SUMO
CC chains. Essential for nuclear architecture, chromosome segregation and
CC embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By
CC similarity). Sumoylates p53/TP53 at 'Lys-386'. Mediates sumoylation of
CC ERCC6 which is essential for its transcription-coupled nucleotide
CC excision repair activity (By similarity).
CC {ECO:0000250|UniProtKB:P63279, ECO:0000269|PubMed:16326389,
CC ECO:0000269|PubMed:17187077, ECO:0000269|PubMed:22214662}.
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 (PubMed:10535925).
CC Interacts with PPM1J (PubMed:12633878). Interacts with RASD2 (By
CC similarity). Interacts with TCF3 (PubMed:9409784). Interacts with
CC NR2C1; the interaction promotes its sumoylation (PubMed:17187077).
CC Interacts with SIAH1 (By similarity). Interacts with PARP (By
CC similarity). Interacts with various transcription factors such as
CC TFAP2A, TFAP2B, and TFAP2C (By similarity). Interacts with AR (By
CC similarity). Interacts with ETS1 (By similarity). Interacts with SOX4
CC (By similarity). Interacts with RWDD3; the interaction enhances the
CC sumoylation of a number of proteins such as HIF1A and I-kappa-B (By
CC similarity). Interacts with FOXL2 (By similarity). Interacts with DNM1l
CC (via its GTPase and B domains); the interaction promotes sumoylation of
CC DNM1L, mainly in its B domain (By similarity). Interacts with NFATC2IP;
CC this inhibits formation of poly-SUMO chains (By similarity). Interacts
CC with FHIT (By similarity). Interacts with PRKRA and p53/TP53
CC (PubMed:22214662). Interacts with UHRF2 (By similarity). Interacts with
CC NR3C1 and this interaction is enhanced in the presence of RWDD3 (By
CC similarity). Interacts with MTA1 (By similarity). Interacts with ZNF451
CC (By similarity). Interacts with CPEB3 (PubMed:26074071). Interacts with
CC SUMO1, SUMO2, and SUMO3 (By similarity). Interacts with IPO13 (By
CC similarity). Interacts with DNMT1 (By similarity).
CC {ECO:0000250|UniProtKB:P63279, ECO:0000250|UniProtKB:P63281,
CC ECO:0000269|PubMed:10535925, ECO:0000269|PubMed:12633878,
CC ECO:0000269|PubMed:17187077, ECO:0000269|PubMed:22214662,
CC ECO:0000269|PubMed:26074071, ECO:0000269|PubMed:9409784}.
CC -!- INTERACTION:
CC P63280; P08152: Egr2; NbExp=2; IntAct=EBI-80180, EBI-7070449;
CC P63280; Q505F1: Nr2c1; NbExp=3; IntAct=EBI-80180, EBI-15617004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18681895,
CC ECO:0000269|PubMed:8610150, ECO:0000269|PubMed:9223278}. Cytoplasm
CC {ECO:0000269|PubMed:18681895, ECO:0000269|PubMed:9223278}. Note=Mainly
CC nuclear (PubMed:18681895). In spermatocytes, localizes in synaptonemal
CC complexes (By similarity). Recruited by BCL11A into the nuclear body
CC (PubMed:18681895). {ECO:0000250|UniProtKB:P63279,
CC ECO:0000269|PubMed:18681895}.
CC -!- TISSUE SPECIFICITY: Present in spleen, kidney, lung, brain, heart and
CC testis (at protein level). {ECO:0000269|PubMed:9409784}.
CC -!- PTM: Phosphorylation at Ser-71 significantly enhances SUMOylation
CC activity. {ECO:0000250|UniProtKB:P63279}.
CC -!- DISRUPTION PHENOTYPE: Death prior to E7.5 due to major defects in
CC nuclear organization. {ECO:0000269|PubMed:16326389}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; U94402; AAB52424.1; -; mRNA.
DR EMBL; X99739; CAA68072.1; -; mRNA.
DR EMBL; U31934; AAB02182.1; -; mRNA.
DR EMBL; U76416; AAB18790.1; -; mRNA.
DR EMBL; U82627; AAB48446.1; -; mRNA.
DR EMBL; X97575; CAA66188.1; -; mRNA.
DR EMBL; AK003141; BAB22599.1; -; mRNA.
DR EMBL; AK005058; BAB23783.1; -; mRNA.
DR EMBL; AK011239; BAB27487.1; -; mRNA.
DR EMBL; AK012282; BAB28140.1; -; mRNA.
DR EMBL; AK088508; BAC40395.1; -; mRNA.
DR EMBL; AK150575; BAE29670.1; -; mRNA.
DR EMBL; AK160014; BAE35560.1; -; mRNA.
DR EMBL; AK160988; BAE36134.1; -; mRNA.
DR EMBL; AK165606; BAE38290.1; -; mRNA.
DR EMBL; AK165615; BAE38295.1; -; mRNA.
DR EMBL; AK166016; BAE38521.1; -; mRNA.
DR EMBL; AK166657; BAE38922.1; -; mRNA.
DR EMBL; AK166930; BAE39124.1; -; mRNA.
DR EMBL; AK167162; BAE39303.1; -; mRNA.
DR EMBL; AK168212; BAE40170.1; -; mRNA.
DR EMBL; AK168706; BAE40548.1; -; mRNA.
DR EMBL; AK168766; BAE40602.1; -; mRNA.
DR EMBL; AY491413; AAS21651.1; -; Genomic_DNA.
DR CCDS; CCDS28513.1; -.
DR RefSeq; NP_001171080.1; NM_001177609.1.
DR RefSeq; NP_001171081.1; NM_001177610.1.
DR RefSeq; NP_035795.1; NM_011665.4.
DR RefSeq; XP_006524111.1; XM_006524048.3.
DR RefSeq; XP_006524112.1; XM_006524049.3.
DR PDB; 1U9A; X-ray; 2.00 A; A=1-158.
DR PDB; 1U9B; X-ray; 2.00 A; A=1-158.
DR PDB; 2UYZ; X-ray; 1.40 A; A=1-158.
DR PDB; 2VRR; X-ray; 2.22 A; A=1-158.
DR PDBsum; 1U9A; -.
DR PDBsum; 1U9B; -.
DR PDBsum; 2UYZ; -.
DR PDBsum; 2VRR; -.
DR AlphaFoldDB; P63280; -.
DR BMRB; P63280; -.
DR SMR; P63280; -.
DR BioGRID; 204408; 165.
DR ComplexPortal; CPX-4921; E3 ligase (RANBP2) complex.
DR DIP; DIP-29276N; -.
DR IntAct; P63280; 57.
DR MINT; P63280; -.
DR STRING; 10090.ENSMUSP00000134169; -.
DR iPTMnet; P63280; -.
DR PhosphoSitePlus; P63280; -.
DR SwissPalm; P63280; -.
DR EPD; P63280; -.
DR MaxQB; P63280; -.
DR PaxDb; P63280; -.
DR PeptideAtlas; P63280; -.
DR PRIDE; P63280; -.
DR ProteomicsDB; 297783; -.
DR TopDownProteomics; P63280; -.
DR Antibodypedia; 1138; 529 antibodies from 43 providers.
DR DNASU; 22196; -.
DR Ensembl; ENSMUST00000049911; ENSMUSP00000055714; ENSMUSG00000015120.
DR Ensembl; ENSMUST00000172618; ENSMUSP00000134169; ENSMUSG00000015120.
DR Ensembl; ENSMUST00000173084; ENSMUSP00000134261; ENSMUSG00000015120.
DR Ensembl; ENSMUST00000173713; ENSMUSP00000134491; ENSMUSG00000015120.
DR Ensembl; ENSMUST00000174001; ENSMUSP00000134450; ENSMUSG00000015120.
DR Ensembl; ENSMUST00000174031; ENSMUSP00000134350; ENSMUSG00000015120.
DR GeneID; 22196; -.
DR KEGG; mmu:22196; -.
DR UCSC; uc008bai.2; mouse.
DR CTD; 7329; -.
DR MGI; MGI:107365; Ube2i.
DR VEuPathDB; HostDB:ENSMUSG00000015120; -.
DR eggNOG; KOG0424; Eukaryota.
DR GeneTree; ENSGT00550000075088; -.
DR HOGENOM; CLU_030988_12_0_1; -.
DR InParanoid; P63280; -.
DR OMA; QEPAWRA; -.
DR OrthoDB; 1522509at2759; -.
DR PhylomeDB; P63280; -.
DR TreeFam; TF101122; -.
DR Reactome; R-MMU-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-MMU-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-MMU-3232118; SUMOylation of transcription factors.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-MMU-4755510; SUMOylation of immune response proteins.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 22196; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Ube2i; mouse.
DR EvolutionaryTrace; P63280; -.
DR PRO; PR:P63280; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P63280; protein.
DR Bgee; ENSMUSG00000015120; Expressed in animal zygote and 221 other tissues.
DR ExpressionAtlas; P63280; baseline and differential.
DR Genevisible; P63280; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0106068; C:SUMO ligase complex; ISO:MGI.
DR GO; GO:1990356; C:sumoylated E2 ligase complex; ISO:MGI.
DR GO; GO:1990234; C:transferase complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0043398; F:HLH domain binding; IPI:UniProtKB.
DR GO; GO:0071535; F:RING-like zinc finger domain binding; ISO:MGI.
DR GO; GO:0044388; F:small protein activating enzyme binding; ISO:MGI.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; ISO:MGI.
DR GO; GO:0019789; F:SUMO transferase activity; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
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; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051168; P:nuclear export; IC:ComplexPortal.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:1903755; P:positive regulation of SUMO transferase activity; ISO:MGI.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
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 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Chromosome partition; Cytoplasm; Developmental protein;
KW Host-virus interaction; Isopeptide bond; Mitosis; Nucleotide-binding;
KW Nucleus; 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_0000082456"
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 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"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:2UYZ"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2UYZ"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:2UYZ"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:2UYZ"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:2UYZ"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:2UYZ"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2UYZ"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2UYZ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2UYZ"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:2UYZ"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:2UYZ"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:2UYZ"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:2UYZ"
SQ SEQUENCE 158 AA; 18007 MW; E2C826E9C8D0683D CRC64;
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS
