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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) (Ubiquitin carrier protein I) (Ubiquitin-conjugating enzyme E2 I) (Ubiquitin-protein ligase I) (p18)

 UBC9_HUMAN              Reviewed;         158 AA.
P63279; D3DU69; P50550; Q15698; Q59GX1; Q86VB3;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
22-NOV-2017, entry version 160.
RecName: Full=SUMO-conjugating enzyme UBC9;
EC=2.3.2.- {ECO:0000269|PubMed:26524494};
AltName: Full=RING-type E3 SUMO transferase UBC9;
AltName: Full=SUMO-protein ligase;
AltName: Full=Ubiquitin carrier protein 9;
AltName: Full=Ubiquitin carrier protein I;
AltName: Full=Ubiquitin-conjugating enzyme E2 I;
AltName: Full=Ubiquitin-protein ligase I;
AltName: Full=p18;
Name=UBE2I; Synonyms=UBC9, UBCE9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=8668529; DOI=10.1093/nar/24.11.2005;
Yasugi T., Howley P.M.;
"Identification of the structural and functional human homolog of the
yeast ubiquitin conjugating enzyme UBC9.";
Nucleic Acids Res. 24:2005-2010(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9067428;
Tachibana M., Iwata N., Watanabe A., Nobukuni Y., Ploplis B.,
Kajigaya S.;
"Assignment of the gene for a ubiquitin-conjugating enzyme (UBE2I) to
human chromosome band 16p13.3 by in situ hybridization.";
Cytogenet. Cell Genet. 75:222-223(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal brain;
PubMed=8565643;
Watanabe T.K., Fujiwara T., Kawai A., Shimizu F., Takami S.,
Hirano H., Okuno S., Ozaki K., Takeda S., Shimada Y., Nagata M.,
Takaichi A., Takahashi E., Nakamura Y., Shin S.;
"Cloning, expression, and mapping of UBE2I, a novel gene encoding a
human homologue of yeast ubiquitin-conjugating enzymes which are
critical for regulating the cell cycle.";
Cytogenet. Cell Genet. 72:86-89(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PARP.
PubMed=9197546; DOI=10.1016/S0378-1119(97)00015-2;
Masson M., Menissier-de Murcia J., Mattei M.-G., de Murcia G.M.,
Niedergang C.P.;
"Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin
conjugating enzyme: hUbc9.";
Gene 190:287-296(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8668125; DOI=10.1007/BF02172913;
Jiang W., Koltin Y.;
"Two-hybrid interaction of a human UBC9 homolog with centromere
proteins of Saccharomyces cerevisiae.";
Mol. Gen. Genet. 251:153-160(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8798754; DOI=10.1074/jbc.271.40.24811;
Wang Z.-Y., Qiu Q., Seufert W., Taguchi T., Testa J.R., Whitmore S.A.,
Callen D.F., Welsh D., Shenk T., Deuel T.F.;
"Molecular cloning of the cDNA and chromosome localization of the gene
for human ubiquitin-conjugating enzyme 9.";
J. Biol. Chem. 271:24811-24816(1996).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
Shen Z.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9333025; DOI=10.1038/sj.onc.1201301;
Hahn S.L., Criqui-Filipe P., Wasylyk B.;
"Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-
conjugating enzyme.";
Oncogene 15:1489-1495(1997).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[16]
INTERACTION WITH ADENOVIRUS 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).
[17]
INTERACTION WITH SIAH1.
PubMed=9334332; DOI=10.1101/gad.11.20.2701;
Hu G., Zhang S., Vidal M., Baer J.L., Xu T., Fearon E.R.;
"Mammalian homologs of seven in absentia regulate DCC via the
ubiquitin-proteasome pathway.";
Genes Dev. 11:2701-2714(1997).
[18]
INTERACTION WITH AR.
PubMed=10383460; DOI=10.1074/jbc.274.27.19441;
Poukka H., Aarnisalo P., Karvonen U., Palvimo J.J., Jaenne O.A.;
"Ubc9 interacts with the androgen receptor and activates receptor-
dependent transcription.";
J. Biol. Chem. 274:19441-19446(1999).
[19]
INTERACTION WITH FHIT.
PubMed=11085938; DOI=10.1042/bj3520443;
Shi Y., Zou M., Farid N.R., Paterson M.C.;
"Association of FHIT (fragile histidine triad), a candidate tumour
suppressor gene, with the ubiquitin-conjugating enzyme hUBC9.";
Biochem. J. 352:443-448(2000).
[20]
FUNCTION.
PubMed=11451954; DOI=10.1074/jbc.M104214200;
Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H.,
Naismith J.H., Hay R.T.;
"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein
substrates by SAE1/SAE2 and Ubc9.";
J. Biol. Chem. 276:35368-35374(2001).
[21]
INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C.
PubMed=12072434; DOI=10.1074/jbc.M202780200;
Eloranta J.J., Hurst H.C.;
"Transcription factor AP-2 interacts with the SUMO-conjugating enzyme
UBC9 and is sumolated in vivo.";
J. Biol. Chem. 277:30798-30804(2002).
[22]
MUTAGENESIS OF 100-ASP-LYS-101.
PubMed=12641448; DOI=10.1021/bi026861x;
Tatham M.H., Chen Y., Hay R.T.;
"Role of two residues proximal to the active site of Ubc9 in substrate
recognition by the Ubc9.SUMO-1 thiolester complex.";
Biochemistry 42:3168-3179(2003).
[23]
INTERACTION WITH SUMO1; SUMO2; SUMO3 AND THE UBLE1A-UBLE1B E1 COMPLEX,
AND MUTAGENESIS OF 13-ARG-LYS-14 AND 17-ARG-LYS-18.
PubMed=12924945; DOI=10.1021/bi0345283;
Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J.,
Rodriguez M.S., Hay R.T., Chen Y.;
"Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and
conjugation.";
Biochemistry 42:9959-9969(2003).
[24]
INTERACTION WITH RANBP2.
PubMed=15378033; DOI=10.1038/nsmb834;
Pichler A., Knipscheer P., Saitoh H., Sixma T.K., Melchior F.;
"The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type.";
Nat. Struct. Mol. Biol. 11:984-991(2004).
[25]
INTERACTION WITH THE PML-RARALPHA ONCOPROTEIN, AND FUNCTION.
PubMed=15809060; DOI=10.1016/j.bbrc.2005.03.052;
Kim Y.E., Kim D.Y., Lee J.M., Kim S.T., Han T.H., Ahn J.H.;
"Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for
localization, sumoylation, and inhibition of monocyte
differentiation.";
Biochem. Biophys. Res. Commun. 330:746-754(2005).
[26]
INTERACTION WITH RANBP2, AND MUTAGENESIS OF PHE-22; VAL-25; VAL-27;
GLU-42; LYS-48; GLU-54; LEU-57; LYS-59 AND ARG-61.
PubMed=15608651; DOI=10.1038/nsmb878;
Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.;
"Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a
mechanism for SUMO paralog selection.";
Nat. Struct. Mol. Biol. 12:67-74(2005).
[27]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16620772; DOI=10.1016/j.abb.2006.03.002;
Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H.,
Chock P.B.;
"A general approach for investigating enzymatic pathways and
substrates for ubiquitin-like modifiers.";
Arch. Biochem. Biophys. 453:70-74(2006).
[28]
SUBCELLULAR LOCATION, AND INTERACTION WITH SOX4.
PubMed=16631117; DOI=10.1016/j.bbrc.2006.03.194;
Pan X., Li H., Zhang P., Jin B., Man J., Tian L., Su G., Zhao J.,
Li W., Liu H., Gong W., Zhou T., Zhang X.;
"Ubc9 interacts with SOX4 and represses its transcriptional
activity.";
Biochem. Biophys. Res. Commun. 344:727-734(2006).
[29]
INTERACTION WITH HERPESVIRUS 6 IE2.
PubMed=17005699; DOI=10.1128/JVI.00375-06;
Tomoiu A., Gravel A., Tanguay R.M., Flamand L.;
"Functional interaction between human herpesvirus 6 immediate-early 2
protein and ubiquitin-conjugating enzyme 9 in the absence of
sumoylation.";
J. Virol. 80:10218-10228(2006).
[30]
INTERACTION WITH RWDD3, AND SUBCELLULAR LOCATION.
PubMed=17956732; DOI=10.1016/j.cell.2007.07.044;
Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M.,
Silberstein S., Stalla G.K., Holsboer F., Arzt E.;
"RSUME, a small RWD-containing protein, enhances SUMO conjugation and
stabilizes HIF-1alpha during hypoxia.";
Cell 131:309-323(2007).
[31]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION OF
KAT5-UBE2I-SENP6 COMPLEX.
PubMed=17704809; DOI=10.1038/sj.onc.1210710;
Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z.,
Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M.,
Liang S., Wu Q., Reddy S.E., Hu R., Huang H., Jin C., Yao X.;
"Functional characterization of TIP60 sumoylation in UV-irradiated DNA
damage response.";
Oncogene 27:931-941(2008).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[33]
INTERACTION WITH DNMT1.
PubMed=19450230; DOI=10.1042/BJ20090142;
Lee B., Muller M.T.;
"SUMOylation enhances DNA methyltransferase 1 activity.";
Biochem. J. 421:449-461(2009).
[34]
INTERACTION WITH FOXL2, ROLE IN FOXL2 SUMOYLATION, AND SUBCELLULAR
LOCATION.
PubMed=19744555; DOI=10.1016/j.cellsig.2009.09.001;
Kuo F.T., Bentsi-Barnes I.K., Barlow G.M., Bae J., Pisarska M.D.;
"Sumoylation of forkhead L2 by Ubc9 is required for its activity as a
transcriptional repressor of the steroidogenic acute regulatory
gene.";
Cell. Signal. 21:1935-1944(2009).
[35]
INTERACTION WITH DNM1L, AND FUNCTION IN DNM1L SUMOYLATION.
PubMed=19638400; DOI=10.1096/fj.09-136630;
Figueroa-Romero C., Iniguez-Lluhi J.A., Stadler J., Chang C.R.,
Arnoult D., Keller P.J., Hong Y., Blackstone C., Feldman E.L.;
"SUMOylation of the mitochondrial fission protein Drp1 occurs at
multiple nonconsensus sites within the B domain and is linked to its
activity cycle.";
FASEB J. 23:3917-3927(2009).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[37]
INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
PubMed=20543865; DOI=10.1038/onc.2010.226;
Yousef A.F., Fonseca G.J., Pelka P., Ablack J.N., Walsh C., Dick F.A.,
Bazett-Jones D.P., Shaw G.S., Mymryk J.S.;
"Identification of a molecular recognition feature in the E1A
oncoprotein that binds the SUMO conjugase UBC9 and likely interferes
with polySUMOylation.";
Oncogene 29:4693-4704(2010).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[39]
INTERACTION WITH MTA1.
PubMed=21965678; DOI=10.1074/jbc.M111.267237;
Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
"SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor
antigen 1 (MTA1) synergistically regulate its transcriptional
repressor function.";
J. Biol. Chem. 286:43793-43808(2011).
[40]
INTERACTION WITH EPSTEIN-BARR VIRUS LMP1.
PubMed=21795333; DOI=10.1128/JVI.05035-11;
Bentz G.L., Whitehurst C.B., Pagano J.S.;
"Epstein-Barr virus latent membrane protein 1 (LMP1) C-terminal-
activating region 3 contributes to LMP1-mediated cellular migration
via its interaction with Ubc9.";
J. Virol. 85:10144-10153(2011).
[41]
SUBCELLULAR LOCATION.
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).
[42]
PHOSPHORYLATION AT SER-71.
PubMed=22509284; DOI=10.1371/journal.pone.0034250;
Su Y.F., Yang T., Huang H., Liu L.F., Hwang J.;
"Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity.";
PLoS ONE 7:E34250-E34250(2012).
[43]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[44]
INTERACTION WITH SETX.
PubMed=24105744; DOI=10.1101/gad.224923.113;
Richard P., Feng S., Manley J.L.;
"A SUMO-dependent interaction between Senataxin and the exosome,
disrupted in the neurodegenerative disease AOA2, targets the exosome
to sites of transcription-induced DNA damage.";
Genes Dev. 27:2227-2232(2013).
[45]
INTERACTION WITH UHRF2.
PubMed=23404503; DOI=10.1074/jbc.M112.438234;
Oh Y., Chung K.C.;
"UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier
E3 ligase for zinc finger protein 131.";
J. Biol. Chem. 288:9102-9111(2013).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[47]
INTERACTION WITH NR3C1.
PubMed=23508108; DOI=10.1128/MCB.01470-12;
Druker J., Liberman A.C., Antunica-Noguerol M., Gerez J.,
Paez-Pereda M., Rein T., Iniguez-Lluhi J.A., Holsboer F., Arzt E.;
"RSUME enhances glucocorticoid receptor SUMOylation and
transcriptional activity.";
Mol. Cell. Biol. 33:2116-2127(2013).
[48]
INTERACTION WITH RWDD3.
PubMed=23469069; DOI=10.1371/journal.pone.0057795;
Gerez J., Fuertes M., Tedesco L., Silberstein S., Sevlever G.,
Paez-Pereda M., Holsboer F., Turjanski A.G., Arzt E.;
"In silico structural and functional characterization of the RSUME
splice variants.";
PLoS ONE 8:E57795-E57795(2013).
[49]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[50]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[51]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[52]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[53]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-49, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[54]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[55]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-48; LYS-49 AND
LYS-101, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[56]
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).
[57]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH RANGAP1.
PubMed=11853669; DOI=10.1016/S0092-8674(02)00630-X;
Bernier-Villamor V., Sampson D.A., Matunis M.J., Lima C.D.;
"Structural basis for E2-mediated SUMO conjugation revealed by a
complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.";
Cell 108:345-356(2002).
[58]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SUMO1; RANGAP1
AND RANBP2.
PubMed=15931224; DOI=10.1038/nature03588;
Reverter D., Lima C.D.;
"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-
Nup358 complex.";
Nature 435:687-692(2005).
[59]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH RANGAP1, AND
MUTAGENESIS OF ASN-85; TYR-87 AND ASP-127.
PubMed=16732283; DOI=10.1038/nsmb1104;
Yunus A.A., Lima C.D.;
"Lysine activation and functional analysis of E2-mediated conjugation
in the SUMO pathway.";
Nat. Struct. Mol. Biol. 13:491-499(2006).
[60]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUMO1,
INTERACTION WITH SUMO1; SUMO2 AND SUMO3, AND FUNCTION.
PubMed=17466333; DOI=10.1016/j.jmb.2007.04.006;
Capili A.D., Lima C.D.;
"Structure and analysis of a complex between SUMO and Ubc9 illustrates
features of a conserved E2-Ubl interaction.";
J. Mol. Biol. 369:608-618(2007).
[61]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH NFATC2IP/NIP45,
INTERACTION WITH NFATC2IP, AND FUNCTION.
PubMed=20077568; DOI=10.1002/prot.22667;
Sekiyama N., Arita K., Ikeda Y., Hashiguchi K., Ariyoshi M.,
Tochio H., Saitoh H., Shirakawa M.;
"Structural basis for regulation of poly-SUMO chain by a SUMO-like
domain of Nip45.";
Proteins 78:1491-1502(2010).
[62]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH IPO13.
PubMed=21139563; DOI=10.1038/emboj.2010.320;
Grunwald M., Bono F.;
"Structure of Importin13-Ubc9 complex: nuclear import and release of a
key regulator of sumoylation.";
EMBO J. 30:427-438(2011).
[63]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH RWDD3, AND
INTERACTION WITH RWDD3.
PubMed=25918163; DOI=10.1074/jbc.M115.644047;
Alontaga A.Y., Ambaye N.D., Li Y.J., Vega R., Chen C.H., Bzymek K.P.,
Williams J.C., Hu W., Chen Y.;
"RWD domain as an E2 (Ubc9)-interaction module.";
J. Biol. Chem. 290:16550-16559(2015).
[64]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZNF451 AND
SUMO2, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH
ZNF451 AND SUMO2.
PubMed=26524494; DOI=10.1038/nsmb.3116;
Cappadocia L., Pichler A., Lima C.D.;
"Structural basis for catalytic activation by the human ZNF451 SUMO E3
ligase.";
Nat. Struct. Mol. Biol. 22:968-975(2015).
-!- FUNCTION: Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3
and SUMO4 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. Necessary for sumoylation of FOXL2 and KAT5.
Essential for nuclear architecture and chromosome segregation.
Sumoylates p53/TP53 at 'Lys-386'. {ECO:0000269|PubMed:11451954,
ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:17466333,
ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:19744555,
ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:26524494,
ECO:0000269|PubMed:8668529}.
-!- 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.
{ECO:0000269|PubMed:26524494}.
-!- PATHWAY: Protein modification; protein sumoylation.
{ECO:0000269|PubMed:26524494}.
-!- SUBUNIT: Interacts with SETX (PubMed:24105744). Interacts with
HIPK1, HIPK2, PPM1J, RASD2 and TCF3 Interacts with NR2C1; the
interaction promotes its sumoylation (By similarity). 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 RWDD3; the
interaction enhances the sumoylation of a number of proteins such
as HIF1A and I-kappa-B. Interacts with DNMT1. Interacts with
FOXL2. Forms a complex with SENP6 and UBE2I in response to UV
irradiation. Interacts with human herpesvirus 6 IE2. Interacts
with human adenovirus early E1A protein; this interaction
interferes with polysumoylation (Probable). Interacts with DNM1l
(via its GTPase and B domains); the interaction promotes
sumoylation of DNM1L, mainly in its B domain. Interacts with PML-
RARA oncoprotein (via the coiled-colied domain); the interaction
is required for sumoylation of the PML-RARA oncoprotein. Interacts
with IPO13. Interacts with NFATC2IP; this inhibits formation of
poly-SUMO chains. Interacts with FHIT. Interacts with PRKRA and
p53/TP53 (By similarity). Interacts with UHRF2. Interacts with
NR3C1 and this interaction is enhanced in the presence of RWDD3.
Interacts with MTA1. 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 Epstein-barr virus protein LMP1. Interacts with CPEB3 (By
similarity). {ECO:0000250|UniProtKB:P63280,
ECO:0000269|PubMed:10383460, ECO:0000269|PubMed:11085938,
ECO:0000269|PubMed:11853669, ECO:0000269|PubMed:12072434,
ECO:0000269|PubMed:12924945, ECO:0000269|PubMed:15378033,
ECO:0000269|PubMed:15608651, ECO:0000269|PubMed:15809060,
ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:16631117,
ECO:0000269|PubMed:16732283, ECO:0000269|PubMed:17005699,
ECO:0000269|PubMed:17466333, ECO:0000269|PubMed:17956732,
ECO:0000269|PubMed:19450230, ECO:0000269|PubMed:19638400,
ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:20077568,
ECO:0000269|PubMed:20543865, ECO:0000269|PubMed:21139563,
ECO:0000269|PubMed:21795333, ECO:0000269|PubMed:21965678,
ECO:0000269|PubMed:23404503, ECO:0000269|PubMed:23469069,
ECO:0000269|PubMed:23508108, ECO:0000269|PubMed:24105744,
ECO:0000269|PubMed:25918163, ECO:0000269|PubMed:26524494,
ECO:0000269|PubMed:8824223, ECO:0000269|PubMed:9197546,
ECO:0000269|PubMed:9334332, ECO:0000305}.
-!- INTERACTION:
G2XKQ0:-; NbExp=3; IntAct=EBI-80168, EBI-10175576;
P29991:- (xeno); NbExp=3; IntAct=EBI-80168, EBI-8826488;
O14503:BHLHE40; NbExp=3; IntAct=EBI-80168, EBI-711810;
Q9H444:CHMP4B; NbExp=3; IntAct=EBI-80168, EBI-749627;
Q9UER7:DAXX; NbExp=3; IntAct=EBI-80168, EBI-77321;
Q9UBC3:DNMT3B; NbExp=3; IntAct=EBI-80168, EBI-80125;
P03116:E1 (xeno); NbExp=2; IntAct=EBI-80168, EBI-7015985;
Q8WWZ3:EDARADD; NbExp=3; IntAct=EBI-80168, EBI-2949647;
P19419:ELK1; NbExp=7; IntAct=EBI-80168, EBI-726632;
Q96IK5:GMCL1; NbExp=4; IntAct=EBI-80168, EBI-2548508;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-80168, EBI-618309;
P56524:HDAC4; NbExp=3; IntAct=EBI-80168, EBI-308629;
O94829:IPO13; NbExp=6; IntAct=EBI-80168, EBI-747310;
P03230:LMP1 (xeno); NbExp=5; IntAct=EBI-80168, EBI-6973030;
O75928:PIAS2; NbExp=8; IntAct=EBI-80168, EBI-348555;
P46060:RANGAP1; NbExp=8; IntAct=EBI-80168, EBI-396091;
Q6ZNA4:RNF111; NbExp=5; IntAct=EBI-80168, EBI-2129175;
Q9Y265:RUVBL1; NbExp=3; IntAct=EBI-80168, EBI-353675;
Q9Y3V2:RWDD3; NbExp=5; IntAct=EBI-80168, EBI-1549885;
Q7Z333:SETX; NbExp=3; IntAct=EBI-80168, EBI-1220123;
Q13485:SMAD4; NbExp=4; IntAct=EBI-80168, EBI-347263;
P56693:SOX10; NbExp=2; IntAct=EBI-80168, EBI-1167533;
P63165:SUMO1; NbExp=9; IntAct=EBI-80168, EBI-80140;
P61956:SUMO2; NbExp=6; IntAct=EBI-80168, EBI-473220;
P05549:TFAP2A; NbExp=4; IntAct=EBI-80168, EBI-347351;
Q92754:TFAP2C; NbExp=5; IntAct=EBI-80168, EBI-937309;
Q12800:TFCP2; NbExp=4; IntAct=EBI-80168, EBI-717422;
P22314:UBA1; NbExp=2; IntAct=EBI-80168, EBI-709688;
Q9HCK0:ZBTB26; NbExp=3; IntAct=EBI-80168, EBI-3918996;
Q8N3Z6:ZCCHC7; NbExp=3; IntAct=EBI-80168, EBI-7265024;
Q9Y4E5:ZNF451; NbExp=3; IntAct=EBI-80168, EBI-747230;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear. In
spermatocytes, localizes in synaptonemal complexes. Recruited by
BCL11A into the nuclear body (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, pancreas,
kidney, liver, lung, placenta and brain. Also expressed in testis
and thymus. {ECO:0000269|PubMed:8610150}.
-!- PTM: Phosphorylation at Ser-71 significantly enhances SUMOylation
activity. {ECO:0000269|PubMed:22509284}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SEQUENCE CAUTION:
Sequence=AAH51289.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAD92225.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X96427; CAA65287.1; -; mRNA.
EMBL; U45328; AAA86662.1; -; mRNA.
EMBL; D45050; BAA08091.1; -; mRNA.
EMBL; U29092; AAC51361.1; -; mRNA.
EMBL; U31933; AAB02181.1; -; mRNA.
EMBL; U31882; AAC50603.1; -; mRNA.
EMBL; U66867; AAC50716.1; -; mRNA.
EMBL; U66818; AAC50715.1; -; mRNA.
EMBL; U38785; AAB09410.1; -; mRNA.
EMBL; AJ002385; CAA05359.1; -; mRNA.
EMBL; BT006932; AAP35578.1; -; mRNA.
EMBL; AB208988; BAD92225.1; ALT_INIT; mRNA.
EMBL; AE006466; AAK61274.1; -; Genomic_DNA.
EMBL; AL031714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85673.1; -; Genomic_DNA.
EMBL; CH471112; EAW85676.1; -; Genomic_DNA.
EMBL; CH471112; EAW85677.1; -; Genomic_DNA.
EMBL; CH471112; EAW85678.1; -; Genomic_DNA.
EMBL; CH471112; EAW85679.1; -; Genomic_DNA.
EMBL; BC000427; AAH00427.1; -; mRNA.
EMBL; BC004429; AAH04429.1; -; mRNA.
EMBL; BC051289; AAH51289.3; ALT_INIT; mRNA.
CCDS; CCDS10433.1; -.
PIR; JC6056; JC6056.
RefSeq; NP_003336.1; NM_003345.4.
RefSeq; NP_919235.1; NM_194259.2.
RefSeq; NP_919236.1; NM_194260.2.
RefSeq; NP_919237.1; NM_194261.2.
RefSeq; XP_016879129.1; XM_017023640.1.
UniGene; Hs.302903; -.
PDB; 1A3S; X-ray; 2.80 A; A=1-158.
PDB; 1KPS; X-ray; 2.50 A; A/C=1-158.
PDB; 1Z5Q; Model; -; A=1-158.
PDB; 1Z5S; X-ray; 3.01 A; A=1-158.
PDB; 2GRN; X-ray; 1.80 A; A=1-158.
PDB; 2GRO; X-ray; 1.70 A; A=1-158.
PDB; 2GRP; X-ray; 2.05 A; A=1-158.
PDB; 2GRQ; X-ray; 1.70 A; A=1-158.
PDB; 2GRR; X-ray; 1.30 A; A=1-158.
PDB; 2O25; X-ray; 2.60 A; C/D=1-158.
PDB; 2PE6; X-ray; 2.40 A; A=1-158.
PDB; 2PX9; NMR; -; B=1-158.
PDB; 2XWU; X-ray; 2.80 A; A=1-158.
PDB; 3A4S; X-ray; 2.70 A; A/B=1-158.
PDB; 3UIN; X-ray; 2.60 A; A=1-158.
PDB; 3UIO; X-ray; 2.60 A; A=1-158.
PDB; 3UIP; X-ray; 2.29 A; A=1-158.
PDB; 4W5V; X-ray; 2.50 A; A=1-158.
PDB; 4Y1L; X-ray; 2.70 A; A/B=1-158.
PDB; 5D2M; X-ray; 2.40 A; A/D=1-158.
PDB; 5F6D; X-ray; 1.55 A; A=2-158.
PDB; 5F6E; X-ray; 1.12 A; A=2-158.
PDB; 5F6U; X-ray; 1.55 A; A=2-158.
PDB; 5F6V; X-ray; 1.49 A; A=2-158.
PDB; 5F6W; X-ray; 1.70 A; A=2-158.
PDB; 5F6X; X-ray; 1.56 A; A=2-158.
PDB; 5F6Y; X-ray; 1.14 A; A=2-158.
PDB; 5FQ2; X-ray; 2.20 A; A=1-158.
PDBsum; 1A3S; -.
PDBsum; 1KPS; -.
PDBsum; 1Z5Q; -.
PDBsum; 1Z5S; -.
PDBsum; 2GRN; -.
PDBsum; 2GRO; -.
PDBsum; 2GRP; -.
PDBsum; 2GRQ; -.
PDBsum; 2GRR; -.
PDBsum; 2O25; -.
PDBsum; 2PE6; -.
PDBsum; 2PX9; -.
PDBsum; 2XWU; -.
PDBsum; 3A4S; -.
PDBsum; 3UIN; -.
PDBsum; 3UIO; -.
PDBsum; 3UIP; -.
PDBsum; 4W5V; -.
PDBsum; 4Y1L; -.
PDBsum; 5D2M; -.
PDBsum; 5F6D; -.
PDBsum; 5F6E; -.
PDBsum; 5F6U; -.
PDBsum; 5F6V; -.
PDBsum; 5F6W; -.
PDBsum; 5F6X; -.
PDBsum; 5F6Y; -.
PDBsum; 5FQ2; -.
ProteinModelPortal; P63279; -.
SMR; P63279; -.
BioGrid; 113177; 460.
CORUM; P63279; -.
DIP; DIP-29078N; -.
ELM; P63279; -.
IntAct; P63279; 194.
MINT; MINT-137807; -.
STRING; 9606.ENSP00000324897; -.
BindingDB; P63279; -.
ChEMBL; CHEMBL1741191; -.
TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
iPTMnet; P63279; -.
PhosphoSitePlus; P63279; -.
SwissPalm; P63279; -.
BioMuta; UBE2I; -.
DMDM; 54039791; -.
EPD; P63279; -.
MaxQB; P63279; -.
PaxDb; P63279; -.
PeptideAtlas; P63279; -.
PRIDE; P63279; -.
TopDownProteomics; P63279; -.
DNASU; 7329; -.
Ensembl; ENST00000325437; ENSP00000324897; ENSG00000103275.
Ensembl; ENST00000355803; ENSP00000348056; ENSG00000103275.
Ensembl; ENST00000397514; ENSP00000380649; ENSG00000103275.
Ensembl; ENST00000397515; ENSP00000380650; ENSG00000103275.
Ensembl; ENST00000403747; ENSP00000385009; ENSG00000103275.
Ensembl; ENST00000406620; ENSP00000384568; ENSG00000103275.
Ensembl; ENST00000566587; ENSP00000457064; ENSG00000103275.
GeneID; 7329; -.
KEGG; hsa:7329; -.
UCSC; uc002clc.2; human.
CTD; 7329; -.
DisGeNET; 7329; -.
EuPathDB; HostDB:ENSG00000103275.18; -.
GeneCards; UBE2I; -.
HGNC; HGNC:12485; UBE2I.
HPA; CAB009021; -.
HPA; HPA003909; -.
MIM; 601661; gene.
neXtProt; NX_P63279; -.
OpenTargets; ENSG00000103275; -.
PharmGKB; PA37134; -.
eggNOG; KOG0424; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00550000075088; -.
HOGENOM; HOG000233454; -.
HOVERGEN; HBG063308; -.
InParanoid; P63279; -.
KO; K10577; -.
OMA; KCKFTPP; -.
PhylomeDB; P63279; -.
TreeFam; TF101122; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3232118; SUMOylation of transcription factors.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
SignaLink; P63279; -.
SIGNOR; P63279; -.
UniPathway; UPA00886; -.
ChiTaRS; UBE2I; human.
EvolutionaryTrace; P63279; -.
GeneWiki; UBE2I; -.
GenomeRNAi; 7329; -.
PRO; PR:P63279; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103275; -.
CleanEx; HS_UBE2I; -.
ExpressionAtlas; P63279; baseline and differential.
Genevisible; P63279; HS.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:1990356; C:sumoylated E2 ligase complex; IDA:CAFA.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0000795; C:synaptonemal complex; TAS:ProtInc.
GO; GO:1990234; C:transferase complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0043398; F:HLH domain binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0071535; F:RING-like zinc finger domain binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0044388; F:small protein activating enzyme binding; IPI:CAFA.
GO; GO:0061656; F:SUMO conjugating enzyme activity; IDA:BHF-UCL.
GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
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:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0033145; P:positive regulation of intracellular steroid hormone receptor signaling pathway; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:1903755; P:positive regulation of SUMO transferase activity; IDA:BHF-UCL.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
GO; GO:0010469; P:regulation of receptor activity; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
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;
Host-virus interaction; Isopeptide bond; Mitosis; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 158 SUMO-conjugating enzyme UBC9.
/FTId=PRO_0000082454.
REGION 13 18 Interaction with SUMO1.
ACT_SITE 93 93 Glycyl thioester intermediate.
SITE 4 4 Interaction with RANBP2.
SITE 25 25 Interaction with RANBP2.
SITE 57 57 Interaction with RANBP2.
SITE 100 101 Substrate binding.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 65 65 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 71 71 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22509284}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 101 101 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 13 14 RK->AA: Impairs binding to SUMO1 and
catalytic activity.
{ECO:0000269|PubMed:12924945}.
MUTAGEN 17 18 RK->AA: Impairs binding to SUMO1 and
catalytic activity.
{ECO:0000269|PubMed:12924945}.
MUTAGEN 22 22 F->A: Impairs binding to RANBP2.
{ECO:0000269|PubMed:15608651}.
MUTAGEN 25 25 V->A: Impairs binding to RANBP2.
{ECO:0000269|PubMed:15608651}.
MUTAGEN 27 27 V->A: Impairs binding to RANBP2.
{ECO:0000269|PubMed:15608651}.
MUTAGEN 42 42 E->A: Slightly impairs binding to RANBP2.
{ECO:0000269|PubMed:15608651}.
MUTAGEN 48 48 K->A: Slightly impairs binding to RANBP2.
{ECO:0000269|PubMed:15608651}.
MUTAGEN 54 54 E->A: Slightly impairs binding to RANBP2.
{ECO:0000269|PubMed:15608651}.
MUTAGEN 57 57 L->A: Impairs binding to RANBP2.
{ECO:0000269|PubMed:15608651}.
MUTAGEN 59 59 K->A: Impairs binding to RANBP2.
{ECO:0000269|PubMed:15608651}.
MUTAGEN 61 61 R->A: Slightly impairs binding to RANBP2.
{ECO:0000269|PubMed:15608651}.
MUTAGEN 85 85 N->Q: Impairs catalytic activity.
{ECO:0000269|PubMed:16732283}.
MUTAGEN 87 87 Y->A: Impairs catalytic activity.
{ECO:0000269|PubMed:16732283}.
MUTAGEN 93 93 C->S: Loss of enhancement of sumoylation
by RWDD3. No effect on RWDD3 protein
levels.
MUTAGEN 100 101 DK->AA: Impairs catalytic activity.
{ECO:0000269|PubMed:12641448}.
MUTAGEN 127 127 D->A: Impairs catalytic activity.
{ECO:0000269|PubMed:16732283}.
MUTAGEN 127 127 D->S: No effect on catalytic activity.
{ECO:0000269|PubMed:16732283}.
CONFLICT 18 18 K -> P (in Ref. 6; AAC50603).
{ECO:0000305}.
CONFLICT 86 89 VYPS -> GVPF (in Ref. 6; AAC50603).
{ECO:0000305}.
HELIX 3 18 {ECO:0000244|PDB:5F6E}.
STRAND 25 30 {ECO:0000244|PDB:5F6E}.
STRAND 32 34 {ECO:0000244|PDB:2PE6}.
STRAND 36 46 {ECO:0000244|PDB:5F6E}.
TURN 52 55 {ECO:0000244|PDB:5F6E}.
STRAND 57 63 {ECO:0000244|PDB:5F6E}.
TURN 66 69 {ECO:0000244|PDB:5F6E}.
STRAND 74 79 {ECO:0000244|PDB:5F6E}.
STRAND 90 92 {ECO:0000244|PDB:5F6E}.
HELIX 95 97 {ECO:0000244|PDB:5F6E}.
TURN 99 102 {ECO:0000244|PDB:5F6E}.
HELIX 109 121 {ECO:0000244|PDB:5F6E}.
HELIX 131 139 {ECO:0000244|PDB:5F6E}.
HELIX 141 154 {ECO:0000244|PDB:5F6E}.
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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