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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) (mUBC9) (Ubiquitin carrier protein I) (Ubiquitin-conjugating enzyme E2 I) (Ubiquitin-protein ligase I)

 UBC9_MOUSE              Reviewed;         158 AA.
P63280; P50550; Q15698; Q6RUT3; Q86VB3;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
23-MAY-2018, entry version 150.
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;
Short=mUBC9;
AltName: Full=Ubiquitin carrier protein I;
AltName: Full=Ubiquitin-conjugating enzyme E2 I;
AltName: Full=Ubiquitin-protein ligase I;
Name=Ube2i; Synonyms=Ubc9, Ubce2i, Ubce9;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=MDF1; TISSUE=Promyelocytic leukemia;
PubMed=8839844;
Scott L.M., Mueller L., Collins S.J.;
"E3, a hematopoietic-specific transcript directly regulated by the
retinoic acid receptor alpha.";
Blood 88:2517-2530(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ADENOVIRUS TYPE 5 AND
TYPE 12 E1A.
PubMed=8824223; DOI=10.1074/jbc.271.42.25906;
Hateboer G., Hijmans E.M., Nooij J.B.D., Schlenker S., Jentsch S.,
Bernards R.;
"mUBC9, a novel adenovirus E1A-interacting protein that complements a
yeast cell cycle defect.";
J. Biol. Chem. 271:25906-25911(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=8610150; DOI=10.1073/pnas.93.7.2958;
Kovalenko O.V., Plug A.W., Haaf T., Gonda D.K., Ashley T., Ward D.C.,
Radding C.M., Golub E.I.;
"Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51
recombination protein and localizes in synaptonemal complexes.";
Proc. Natl. Acad. Sci. U.S.A. 93:2958-2963(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
TCF3.
STRAIN=BALB/cJ; TISSUE=Fibroblast;
PubMed=9409784; DOI=10.1016/S0378-1119(97)00444-7;
Loveys D.A., Streiff M.B., Schaefer T.S., Kato G.J.;
"The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A
transcription factors.";
Gene 201:169-177(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=B-cell lymphoma;
PubMed=9223278; DOI=10.1073/pnas.94.15.7862;
Tashiro K., Pando M.P., Kanegae Y., Wamsley P.M., Inoue S.,
Verma I.M.;
"Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in
the degradation of IkappaBalpha.";
Proc. Natl. Acad. Sci. U.S.A. 94:7862-7867(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=PJS1;
Weber B.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=BALB/cJ, C57BL/6J, and NOD;
TISSUE=Bone marrow, Head, Heart, Kidney, Liver, Lung, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[9]
INTERACTION WITH HIPK1 AND HIPK2.
PubMed=10535925; DOI=10.1073/pnas.96.22.12350;
Kim Y.H., Choi C.Y., Kim Y.;
"Covalent modification of the homeodomain-interacting protein kinase 2
(HIPK2) by the ubiquitin-like protein SUMO-1.";
Proc. Natl. Acad. Sci. U.S.A. 96:12350-12355(1999).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16326389; DOI=10.1016/j.devcel.2005.10.007;
Nacerddine K., Lehembre F., Bhaumik M., Artus J., Cohen-Tannoudji M.,
Babinet C., Pandolfi P.P., Dejean A.;
"The SUMO pathway is essential for nuclear integrity and chromosome
segregation in mice.";
Dev. Cell 9:769-779(2005).
[11]
INTERACTION WITH PPM1J.
PubMed=12633878; DOI=10.1016/S0014-5793(03)00153-4;
Kashiwaba M., Katsura K., Ohnishi M., Sasaki M., Tanaka H.,
Nishimune Y., Kobayashi T., Tamura S.;
"A novel protein phosphatase 2C family member (PP2Czeta) is able to
associate with ubiquitin conjugating enzyme 9.";
FEBS Lett. 538:197-202(2003).
[12]
INTERACTION WITH MOMLV CA.
PubMed=16352559; DOI=10.1128/JVI.80.1.342-352.2006;
Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K.,
Pu S.-Y., Goff S.P.;
"Interaction of moloney murine leukemia virus capsid with Ubc9 and
PIASy mediates SUMO-1 addition required early in infection.";
J. Virol. 80:342-352(2006).
[13]
INTERACTION WITH NR2C1, AND FUNCTION IN NR2C1 SUMOYLATION.
PubMed=17187077; DOI=10.1038/nsmb1185;
Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.;
"SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4
expression in stem cells.";
Nat. Struct. Mol. Biol. 14:68-75(2007).
[14]
SUBCELLULAR LOCATION.
PubMed=18681895; DOI=10.1111/j.1365-2443.2008.01216.x;
Kuwata T., Nakamura T.;
"BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes
in its nuclear body.";
Genes Cells 13:931-940(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
FUNCTION, AND INTERACTION WITH PRKRA AND TP53.
PubMed=22214662; DOI=10.4161/cc.11.2.18999;
Bennett R.L., Pan Y., Christian J., Hui T., May W.S. Jr.;
"The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and
activation, leading to G(1) arrest.";
Cell Cycle 11:407-417(2012).
[17]
INTERACTION WITH CPEB3.
PubMed=26074071; DOI=10.1016/j.celrep.2015.04.061;
Drisaldi B., Colnaghi L., Fioriti L., Rao N., Myers C., Snyder A.M.,
Metzger D.J., Tarasoff J., Konstantinov E., Fraser P.E., Manley J.L.,
Kandel E.R.;
"SUMOylation is an inhibitory constraint that regulates the prion-like
aggregation and activity of CPEB3.";
Cell Rep. 11:1694-1702(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=9261152; DOI=10.1074/jbc.272.34.21381;
Tong H., Hateboer G., Perrakis A., Bernards R., Sixma T.K.;
"Crystal structure of murine/human Ubc9 provides insight into the
variability of the ubiquitin-conjugating system.";
J. Biol. Chem. 272:21381-21387(1997).
-!- FUNCTION: Accepts the ubiquitin-like proteins SUMO1, SUMO2 and
SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their
covalent attachment to other proteins with the help of an E3
ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation
of poly-SUMO chains. Essential for nuclear architecture,
chromosome segregation and embryonic viability. Necessary for
sumoylation of FOXL2 and KAT5 (By similarity). Sumoylates p53/TP53
at 'Lys-386'. {ECO:0000250|UniProtKB:P63279,
ECO:0000269|PubMed:16326389, ECO:0000269|PubMed:17187077,
ECO:0000269|PubMed:22214662}.
-!- 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: Forms a tight complex with RANGAP1 and RANBP2. Interacts
with SIAH1 and PARP. Interacts with various transcription factors
such as TFAP2A, TFAP2B, TFAP2C, AR, ETS1 and SOX4. Interacts with
RASD2. Interacts with RWDD3; the interaction enhances the
sumoylation of a number of proteins such as HIF1A and I-kappa-B.
Interacts with FOXL2. Forms a complex with SENP6 and UBE2I in
response to UV irradiation. Interacts with DNM1L (via its GTPase
and B domains); the interaction promotes sumoylation of DNM1L,
mainly in the B domain (By similarity). Interacts with HIPK1,
HIPK2, PPM1J and TCF3. Interacts with Moloney murine leukemia
virus CA and adenovirus type 5 and type 12 E1A. Interacts with
NR2C1; the interaction promotes its sumoylation. Interacts with
NFATC2IP; this inhibits formation of poly-SUMO chains. Interacts
with FHIT (By similarity). Interacts with PRKRA and p53/TP53.
Interacts with UHRF2. Interacts with NR3C1 and this interaction is
enhanced in the presence of RWDD3. Interacts with MTA1 (By
similarity). Interacts with ZNF451. Identified in a complex with
SUMO2 and UBC9, where one ZNF451 interacts with one UBC9 and two
SUMO2 chains, one bound to the UBC9 active site and the other to
another region of the same UBC9 molecule. Interacts with SETX (By
similarity). Interacts with CPEB3 (PubMed:26074071).
{ECO:0000250|UniProtKB:P63279, ECO:0000269|PubMed:26074071}.
-!- INTERACTION:
P08152:Egr2; NbExp=2; IntAct=EBI-80180, EBI-7070449;
Q505F1:Nr2c1; NbExp=3; IntAct=EBI-80180, EBI-15617004;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear. In
spermatocytes, localizes in synaptonemal complexes. Recruited by
BCL11A into the nuclear body.
-!- TISSUE SPECIFICITY: Present in spleen, kidney, lung, brain, heart
and testis (at protein level). {ECO:0000269|PubMed:9409784}.
-!- PTM: Phosphorylation at Ser-71 significantly enhances SUMOylation
activity. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Death prior to E7.5 due to major defects in
nuclear organization. {ECO:0000269|PubMed:16326389}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
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EMBL; U94402; AAB52424.1; -; mRNA.
EMBL; X99739; CAA68072.1; -; mRNA.
EMBL; U31934; AAB02182.1; -; mRNA.
EMBL; U76416; AAB18790.1; -; mRNA.
EMBL; U82627; AAB48446.1; -; mRNA.
EMBL; X97575; CAA66188.1; -; mRNA.
EMBL; AK003141; BAB22599.1; -; mRNA.
EMBL; AK005058; BAB23783.1; -; mRNA.
EMBL; AK011239; BAB27487.1; -; mRNA.
EMBL; AK012282; BAB28140.1; -; mRNA.
EMBL; AK088508; BAC40395.1; -; mRNA.
EMBL; AK150575; BAE29670.1; -; mRNA.
EMBL; AK160014; BAE35560.1; -; mRNA.
EMBL; AK160988; BAE36134.1; -; mRNA.
EMBL; AK165606; BAE38290.1; -; mRNA.
EMBL; AK165615; BAE38295.1; -; mRNA.
EMBL; AK166016; BAE38521.1; -; mRNA.
EMBL; AK166657; BAE38922.1; -; mRNA.
EMBL; AK166930; BAE39124.1; -; mRNA.
EMBL; AK167162; BAE39303.1; -; mRNA.
EMBL; AK168212; BAE40170.1; -; mRNA.
EMBL; AK168706; BAE40548.1; -; mRNA.
EMBL; AK168766; BAE40602.1; -; mRNA.
EMBL; AY491413; AAS21651.1; -; Genomic_DNA.
CCDS; CCDS28513.1; -.
RefSeq; NP_001171080.1; NM_001177609.1.
RefSeq; NP_001171081.1; NM_001177610.1.
RefSeq; NP_035795.1; NM_011665.4.
RefSeq; XP_006524111.1; XM_006524048.3.
RefSeq; XP_006524112.1; XM_006524049.3.
UniGene; Mm.240044; -.
UniGene; Mm.384234; -.
UniGene; Mm.442797; -.
PDB; 1U9A; X-ray; 2.00 A; A=1-158.
PDB; 1U9B; X-ray; 2.00 A; A=1-158.
PDB; 2UYZ; X-ray; 1.40 A; A=1-158.
PDB; 2VRR; X-ray; 2.22 A; A=1-158.
PDBsum; 1U9A; -.
PDBsum; 1U9B; -.
PDBsum; 2UYZ; -.
PDBsum; 2VRR; -.
ProteinModelPortal; P63280; -.
SMR; P63280; -.
BioGrid; 204408; 82.
DIP; DIP-29276N; -.
IntAct; P63280; 56.
MINT; P63280; -.
STRING; 10090.ENSMUSP00000055714; -.
iPTMnet; P63280; -.
PhosphoSitePlus; P63280; -.
EPD; P63280; -.
MaxQB; P63280; -.
PaxDb; P63280; -.
PeptideAtlas; P63280; -.
PRIDE; P63280; -.
TopDownProteomics; P63280; -.
Ensembl; ENSMUST00000049911; ENSMUSP00000055714; ENSMUSG00000015120.
Ensembl; ENSMUST00000172618; ENSMUSP00000134169; ENSMUSG00000015120.
Ensembl; ENSMUST00000173084; ENSMUSP00000134261; ENSMUSG00000015120.
Ensembl; ENSMUST00000173713; ENSMUSP00000134491; ENSMUSG00000015120.
Ensembl; ENSMUST00000174001; ENSMUSP00000134450; ENSMUSG00000015120.
Ensembl; ENSMUST00000174031; ENSMUSP00000134350; ENSMUSG00000015120.
GeneID; 22196; -.
KEGG; mmu:22196; -.
UCSC; uc008bai.2; mouse.
CTD; 7329; -.
MGI; MGI:107365; Ube2i.
eggNOG; KOG0424; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00550000075088; -.
HOGENOM; HOG000233454; -.
HOVERGEN; HBG063308; -.
InParanoid; P63280; -.
KO; K10577; -.
OMA; KCKFTPP; -.
OrthoDB; EOG091G0NAK; -.
PhylomeDB; P63280; -.
TreeFam; TF101122; -.
Reactome; R-MMU-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-MMU-3232118; SUMOylation of transcription factors.
Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-MMU-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
UniPathway; UPA00886; -.
ChiTaRS; Ube2i; mouse.
EvolutionaryTrace; P63280; -.
PRO; PR:P63280; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000015120; -.
CleanEx; MM_UBE2I; -.
ExpressionAtlas; P63280; baseline and differential.
Genevisible; P63280; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0016605; C:PML body; ISO:MGI.
GO; GO:1990356; C:sumoylated E2 ligase complex; ISO:MGI.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:1990234; C:transferase complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0043398; F:HLH domain binding; IPI:UniProtKB.
GO; GO:0071535; F:RING-like zinc finger domain binding; ISO:MGI.
GO; GO:0044388; F:small protein activating enzyme binding; ISO:MGI.
GO; GO:0061656; F:SUMO conjugating enzyme activity; ISO:MGI.
GO; GO:0019789; F:SUMO transferase activity; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
GO; GO:0033145; P:positive regulation of intracellular steroid hormone receptor signaling pathway; IEA:Ensembl.
GO; GO:1903755; P:positive regulation of SUMO transferase activity; ISO:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0016925; P:protein sumoylation; ISO:MGI.
GO; GO:0010469; P:regulation of signaling receptor activity; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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;
3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
Chromosome partition; Complete proteome; Cytoplasm;
Developmental protein; Host-virus interaction; Isopeptide bond;
Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P63279}.
CHAIN 2 158 SUMO-conjugating enzyme UBC9.
/FTId=PRO_0000082456.
REGION 13 18 Interaction with SUMO1. {ECO:0000250}.
ACT_SITE 93 93 Glycyl thioester intermediate.
SITE 4 4 Interaction with RANBP2. {ECO:0000250}.
SITE 25 25 Interaction with RANBP2. {ECO:0000250}.
SITE 57 57 Interaction with RANBP2. {ECO:0000250}.
SITE 100 101 Substrate binding. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P63279}.
MOD_RES 65 65 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63279}.
MOD_RES 71 71 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:P63279}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P63279}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P63279}.
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P63279}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P63279}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P63279}.
CROSSLNK 101 101 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P63279}.
HELIX 4 18 {ECO:0000244|PDB:2UYZ}.
STRAND 25 30 {ECO:0000244|PDB:2UYZ}.
STRAND 36 46 {ECO:0000244|PDB:2UYZ}.
TURN 52 55 {ECO:0000244|PDB:2UYZ}.
STRAND 57 63 {ECO:0000244|PDB:2UYZ}.
TURN 66 69 {ECO:0000244|PDB:2UYZ}.
STRAND 74 79 {ECO:0000244|PDB:2UYZ}.
STRAND 90 92 {ECO:0000244|PDB:2UYZ}.
HELIX 95 97 {ECO:0000244|PDB:2UYZ}.
TURN 99 102 {ECO:0000244|PDB:2UYZ}.
HELIX 109 121 {ECO:0000244|PDB:2UYZ}.
HELIX 131 139 {ECO:0000244|PDB:2UYZ}.
HELIX 141 154 {ECO:0000244|PDB:2UYZ}.
SEQUENCE 158 AA; 18007 MW; E2C826E9C8D0683D CRC64;
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS


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