GenomeNet

Database: UniProt
Entry: P63279
LinkDB: P63279
Original site: P63279 
ID   UBC9_HUMAN              Reviewed;         158 AA.
AC   P63279; D3DU69; P50550; Q15698; Q59GX1; Q86VB3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   29-SEP-2021, entry version 191.
DE   RecName: Full=SUMO-conjugating enzyme UBC9;
DE            EC=2.3.2.- {ECO:0000269|PubMed:26524494};
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-protein ligase I;
DE   AltName: Full=p18;
GN   Name=UBE2I; Synonyms=UBC9, UBCE9;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=8668529; DOI=10.1093/nar/24.11.2005;
RA   Yasugi T., Howley P.M.;
RT   "Identification of the structural and functional human homolog of the yeast
RT   ubiquitin conjugating enzyme UBC9.";
RL   Nucleic Acids Res. 24:2005-2010(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9067428; DOI=10.1159/000134487;
RA   Tachibana M., Iwata N., Watanabe A., Nobukuni Y., Ploplis B., Kajigaya S.;
RT   "Assignment of the gene for a ubiquitin-conjugating enzyme (UBE2I) to human
RT   chromosome band 16p13.3 by in situ hybridization.";
RL   Cytogenet. Cell Genet. 75:222-223(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=8565643; DOI=10.1159/000134169;
RA   Watanabe T.K., Fujiwara T., Kawai A., Shimizu F., Takami S., Hirano H.,
RA   Okuno S., Ozaki K., Takeda S., Shimada Y., Nagata M., Takaichi A.,
RA   Takahashi E., Nakamura Y., Shin S.;
RT   "Cloning, expression, and mapping of UBE2I, a novel gene encoding a human
RT   homologue of yeast ubiquitin-conjugating enzymes which are critical for
RT   regulating the cell cycle.";
RL   Cytogenet. Cell Genet. 72:86-89(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PARP.
RX   PubMed=9197546; DOI=10.1016/s0378-1119(97)00015-2;
RA   Masson M., Menissier-de Murcia J., Mattei M.-G., de Murcia G.M.,
RA   Niedergang C.P.;
RT   "Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin
RT   conjugating enzyme: hUbc9.";
RL   Gene 190:287-296(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8668125; DOI=10.1007/bf02172913;
RA   Jiang W., Koltin Y.;
RT   "Two-hybrid interaction of a human UBC9 homolog with centromere proteins of
RT   Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 251:153-160(1996).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=8798754; DOI=10.1074/jbc.271.40.24811;
RA   Wang Z.-Y., Qiu Q., Seufert W., Taguchi T., Testa J.R., Whitmore S.A.,
RA   Callen D.F., Welsh D., Shenk T., Deuel T.F.;
RT   "Molecular cloning of the cDNA and chromosome localization of the gene for
RT   human ubiquitin-conjugating enzyme 9.";
RL   J. Biol. Chem. 271:24811-24816(1996).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shen Z.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ETS1.
RX   PubMed=9333025; DOI=10.1038/sj.onc.1201301;
RA   Hahn S.L., Criqui-Filipe P., Wasylyk B.;
RT   "Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-
RT   conjugating enzyme.";
RL   Oncogene 15:1489-1495(1997).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA   Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA   Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT   "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT   the short arm of human chromosome 16.";
RL   Hum. Mol. Genet. 10:339-352(2001).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [16]
RP   INTERACTION WITH ADENOVIRUS E1A (MICROBIAL INFECTION).
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   [17]
RP   INTERACTION WITH SIAH1.
RX   PubMed=9334332; DOI=10.1101/gad.11.20.2701;
RA   Hu G., Zhang S., Vidal M., Baer J.L., Xu T., Fearon E.R.;
RT   "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-
RT   proteasome pathway.";
RL   Genes Dev. 11:2701-2714(1997).
RN   [18]
RP   INTERACTION WITH AR.
RX   PubMed=10383460; DOI=10.1074/jbc.274.27.19441;
RA   Poukka H., Aarnisalo P., Karvonen U., Palvimo J.J., Jaenne O.A.;
RT   "Ubc9 interacts with the androgen receptor and activates receptor-dependent
RT   transcription.";
RL   J. Biol. Chem. 274:19441-19446(1999).
RN   [19]
RP   INTERACTION WITH FHIT.
RX   PubMed=11085938; DOI=10.1042/bj3520443;
RA   Shi Y., Zou M., Farid N.R., Paterson M.C.;
RT   "Association of FHIT (fragile histidine triad), a candidate tumour
RT   suppressor gene, with the ubiquitin-conjugating enzyme hUBC9.";
RL   Biochem. J. 352:443-448(2000).
RN   [20]
RP   FUNCTION.
RX   PubMed=11451954; DOI=10.1074/jbc.m104214200;
RA   Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H.,
RA   Naismith J.H., Hay R.T.;
RT   "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates
RT   by SAE1/SAE2 and Ubc9.";
RL   J. Biol. Chem. 276:35368-35374(2001).
RN   [21]
RP   INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C.
RX   PubMed=12072434; DOI=10.1074/jbc.m202780200;
RA   Eloranta J.J., Hurst H.C.;
RT   "Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9
RT   and is sumolated in vivo.";
RL   J. Biol. Chem. 277:30798-30804(2002).
RN   [22]
RP   MUTAGENESIS OF 100-ASP-LYS-101.
RX   PubMed=12641448; DOI=10.1021/bi026861x;
RA   Tatham M.H., Chen Y., Hay R.T.;
RT   "Role of two residues proximal to the active site of Ubc9 in substrate
RT   recognition by the Ubc9.SUMO-1 thiolester complex.";
RL   Biochemistry 42:3168-3179(2003).
RN   [23]
RP   INTERACTION WITH SUMO1; SUMO2; SUMO3 AND THE UBLE1A-UBLE1B E1 COMPLEX, AND
RP   MUTAGENESIS OF 13-ARG-LYS-14 AND 17-ARG-LYS-18.
RX   PubMed=12924945; DOI=10.1021/bi0345283;
RA   Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J., Rodriguez M.S.,
RA   Hay R.T., Chen Y.;
RT   "Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and
RT   conjugation.";
RL   Biochemistry 42:9959-9969(2003).
RN   [24]
RP   INTERACTION WITH RANBP2.
RX   PubMed=15378033; DOI=10.1038/nsmb834;
RA   Pichler A., Knipscheer P., Saitoh H., Sixma T.K., Melchior F.;
RT   "The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type.";
RL   Nat. Struct. Mol. Biol. 11:984-991(2004).
RN   [25]
RP   INTERACTION WITH THE PML-RARALPHA ONCOPROTEIN, AND FUNCTION.
RX   PubMed=15809060; DOI=10.1016/j.bbrc.2005.03.052;
RA   Kim Y.E., Kim D.Y., Lee J.M., Kim S.T., Han T.H., Ahn J.H.;
RT   "Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for
RT   localization, sumoylation, and inhibition of monocyte differentiation.";
RL   Biochem. Biophys. Res. Commun. 330:746-754(2005).
RN   [26]
RP   INTERACTION WITH RANBP2, AND MUTAGENESIS OF PHE-22; VAL-25; VAL-27; GLU-42;
RP   LYS-48; GLU-54; LEU-57; LYS-59 AND ARG-61.
RX   PubMed=15608651; DOI=10.1038/nsmb878;
RA   Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.;
RT   "Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism
RT   for SUMO paralog selection.";
RL   Nat. Struct. Mol. Biol. 12:67-74(2005).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16620772; DOI=10.1016/j.abb.2006.03.002;
RA   Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H.,
RA   Chock P.B.;
RT   "A general approach for investigating enzymatic pathways and substrates for
RT   ubiquitin-like modifiers.";
RL   Arch. Biochem. Biophys. 453:70-74(2006).
RN   [28]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH SOX4.
RX   PubMed=16631117; DOI=10.1016/j.bbrc.2006.03.194;
RA   Pan X., Li H., Zhang P., Jin B., Man J., Tian L., Su G., Zhao J., Li W.,
RA   Liu H., Gong W., Zhou T., Zhang X.;
RT   "Ubc9 interacts with SOX4 and represses its transcriptional activity.";
RL   Biochem. Biophys. Res. Commun. 344:727-734(2006).
RN   [29]
RP   INTERACTION WITH HERPESVIRUS 6 IE2 (MICROBIAL INFECTION).
RX   PubMed=17005699; DOI=10.1128/jvi.00375-06;
RA   Tomoiu A., Gravel A., Tanguay R.M., Flamand L.;
RT   "Functional interaction between human herpesvirus 6 immediate-early 2
RT   protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation.";
RL   J. Virol. 80:10218-10228(2006).
RN   [30]
RP   INTERACTION WITH RWDD3, AND SUBCELLULAR LOCATION.
RX   PubMed=17956732; DOI=10.1016/j.cell.2007.07.044;
RA   Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M.,
RA   Silberstein S., Stalla G.K., Holsboer F., Arzt E.;
RT   "RSUME, a small RWD-containing protein, enhances SUMO conjugation and
RT   stabilizes HIF-1alpha during hypoxia.";
RL   Cell 131:309-323(2007).
RN   [31]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION OF KAT5-UBE2I-SENP6
RP   COMPLEX.
RX   PubMed=17704809; DOI=10.1038/sj.onc.1210710;
RA   Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z.,
RA   Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M., Liang S.,
RA   Wu Q., Reddy S.E., Hu R., Huang H., Jin C., Yao X.;
RT   "Functional characterization of TIP60 sumoylation in UV-irradiated DNA
RT   damage response.";
RL   Oncogene 27:931-941(2008).
RN   [32]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [33]
RP   INTERACTION WITH DNMT1.
RX   PubMed=19450230; DOI=10.1042/bj20090142;
RA   Lee B., Muller M.T.;
RT   "SUMOylation enhances DNA methyltransferase 1 activity.";
RL   Biochem. J. 421:449-461(2009).
RN   [34]
RP   INTERACTION WITH FOXL2, ROLE IN FOXL2 SUMOYLATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=19744555; DOI=10.1016/j.cellsig.2009.09.001;
RA   Kuo F.T., Bentsi-Barnes I.K., Barlow G.M., Bae J., Pisarska M.D.;
RT   "Sumoylation of forkhead L2 by Ubc9 is required for its activity as a
RT   transcriptional repressor of the steroidogenic acute regulatory gene.";
RL   Cell. Signal. 21:1935-1944(2009).
RN   [35]
RP   INTERACTION WITH DNM1L, AND FUNCTION IN DNM1L SUMOYLATION.
RX   PubMed=19638400; DOI=10.1096/fj.09-136630;
RA   Figueroa-Romero C., Iniguez-Lluhi J.A., Stadler J., Chang C.R., Arnoult D.,
RA   Keller P.J., Hong Y., Blackstone C., Feldman E.L.;
RT   "SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple
RT   nonconsensus sites within the B domain and is linked to its activity
RT   cycle.";
RL   FASEB J. 23:3917-3927(2009).
RN   [36]
RP   INTERACTION WITH EBOLAVIRUS VP35 (MICROBIAL INFECTION).
RX   PubMed=19557165; DOI=10.1371/journal.ppat.1000493;
RA   Chang T.H., Kubota T., Matsuoka M., Jones S., Bradfute S.B., Bray M.,
RA   Ozato K.;
RT   "Ebola Zaire virus blocks type I interferon production by exploiting the
RT   host SUMO modification machinery.";
RL   PLoS Pathog. 5:e1000493-e1000493(2009).
RN   [37]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [38]
RP   INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN (MICROBIAL INFECTION).
RX   PubMed=20543865; DOI=10.1038/onc.2010.226;
RA   Yousef A.F., Fonseca G.J., Pelka P., Ablack J.N., Walsh C., Dick F.A.,
RA   Bazett-Jones D.P., Shaw G.S., Mymryk J.S.;
RT   "Identification of a molecular recognition feature in the E1A oncoprotein
RT   that binds the SUMO conjugase UBC9 and likely interferes with
RT   polySUMOylation.";
RL   Oncogene 29:4693-4704(2010).
RN   [39]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [40]
RP   INTERACTION WITH MTA1.
RX   PubMed=21965678; DOI=10.1074/jbc.m111.267237;
RA   Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
RT   "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1
RT   (MTA1) synergistically regulate its transcriptional repressor function.";
RL   J. Biol. Chem. 286:43793-43808(2011).
RN   [41]
RP   INTERACTION WITH EPSTEIN-BARR VIRUS LMP1 (MICROBIAL INFECTION).
RX   PubMed=21795333; DOI=10.1128/jvi.05035-11;
RA   Bentz G.L., Whitehurst C.B., Pagano J.S.;
RT   "Epstein-Barr virus latent membrane protein 1 (LMP1) C-terminal-activating
RT   region 3 contributes to LMP1-mediated cellular migration via its
RT   interaction with Ubc9.";
RL   J. Virol. 85:10144-10153(2011).
RN   [42]
RP   SUBCELLULAR LOCATION.
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   [43]
RP   PHOSPHORYLATION AT SER-71.
RX   PubMed=22509284; DOI=10.1371/journal.pone.0034250;
RA   Su Y.F., Yang T., Huang H., Liu L.F., Hwang J.;
RT   "Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity.";
RL   PLoS ONE 7:E34250-E34250(2012).
RN   [44]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [45]
RP   INTERACTION WITH SETX.
RX   PubMed=24105744; DOI=10.1101/gad.224923.113;
RA   Richard P., Feng S., Manley J.L.;
RT   "A SUMO-dependent interaction between Senataxin and the exosome, disrupted
RT   in the neurodegenerative disease AOA2, targets the exosome to sites of
RT   transcription-induced DNA damage.";
RL   Genes Dev. 27:2227-2232(2013).
RN   [46]
RP   INTERACTION WITH UHRF2.
RX   PubMed=23404503; DOI=10.1074/jbc.m112.438234;
RA   Oh Y., Chung K.C.;
RT   "UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3
RT   ligase for zinc finger protein 131.";
RL   J. Biol. Chem. 288:9102-9111(2013).
RN   [47]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [48]
RP   INTERACTION WITH NR3C1.
RX   PubMed=23508108; DOI=10.1128/mcb.01470-12;
RA   Druker J., Liberman A.C., Antunica-Noguerol M., Gerez J., Paez-Pereda M.,
RA   Rein T., Iniguez-Lluhi J.A., Holsboer F., Arzt E.;
RT   "RSUME enhances glucocorticoid receptor SUMOylation and transcriptional
RT   activity.";
RL   Mol. Cell. Biol. 33:2116-2127(2013).
RN   [49]
RP   INTERACTION WITH RWDD3.
RX   PubMed=23469069; DOI=10.1371/journal.pone.0057795;
RA   Gerez J., Fuertes M., Tedesco L., Silberstein S., Sevlever G.,
RA   Paez-Pereda M., Holsboer F., Turjanski A.G., Arzt E.;
RT   "In silico structural and functional characterization of the RSUME splice
RT   variants.";
RL   PLoS ONE 8:E57795-E57795(2013).
RN   [50]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [51]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [52]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [53]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [54]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-49, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [55]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [56]
RP   FUNCTION.
RX   PubMed=26620705; DOI=10.1074/jbc.m115.683235;
RA   Sin Y., Tanaka K., Saijo M.;
RT   "The C-terminal Region and SUMOylation of Cockayne Syndrome Group B Protein
RT   Play Critical Roles in Transcription-coupled Nucleotide Excision Repair.";
RL   J. Biol. Chem. 291:1387-1397(2016).
RN   [57]
RP   INTERACTION WITH ZBED1, AND SUBCELLULAR LOCATION.
RX   PubMed=27068747; DOI=10.1074/jbc.m115.713370;
RA   Yamashita D., Moriuchi T., Osumi T., Hirose F.;
RT   "Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2alpha.";
RL   J. Biol. Chem. 291:11619-11634(2016).
RN   [58]
RP   INTERACTION WITH SUMO1P1/SUMO5.
RX   PubMed=27211601; DOI=10.1038/srep26509;
RA   Liang Y.C., Lee C.C., Yao Y.L., Lai C.C., Schmitz M.L., Yang W.M.;
RT   "SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies.";
RL   Sci. Rep. 6:26509-26509(2016).
RN   [59]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-48; LYS-49 AND LYS-101,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [60]
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).
RN   [61]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH RANGAP1.
RX   PubMed=11853669; DOI=10.1016/s0092-8674(02)00630-x;
RA   Bernier-Villamor V., Sampson D.A., Matunis M.J., Lima C.D.;
RT   "Structural basis for E2-mediated SUMO conjugation revealed by a complex
RT   between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.";
RL   Cell 108:345-356(2002).
RN   [62]
RP   X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SUMO1; RANGAP1 AND
RP   RANBP2.
RX   PubMed=15931224; DOI=10.1038/nature03588;
RA   Reverter D., Lima C.D.;
RT   "Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358
RT   complex.";
RL   Nature 435:687-692(2005).
RN   [63]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH RANGAP1, AND
RP   MUTAGENESIS OF ASN-85; TYR-87 AND ASP-127.
RX   PubMed=16732283; DOI=10.1038/nsmb1104;
RA   Yunus A.A., Lima C.D.;
RT   "Lysine activation and functional analysis of E2-mediated conjugation in
RT   the SUMO pathway.";
RL   Nat. Struct. Mol. Biol. 13:491-499(2006).
RN   [64]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUMO1, INTERACTION
RP   WITH SUMO1; SUMO2 AND SUMO3, AND FUNCTION.
RX   PubMed=17466333; DOI=10.1016/j.jmb.2007.04.006;
RA   Capili A.D., Lima C.D.;
RT   "Structure and analysis of a complex between SUMO and Ubc9 illustrates
RT   features of a conserved E2-Ubl interaction.";
RL   J. Mol. Biol. 369:608-618(2007).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH NFATC2IP/NIP45,
RP   INTERACTION WITH NFATC2IP, AND FUNCTION.
RX   PubMed=20077568; DOI=10.1002/prot.22667;
RA   Sekiyama N., Arita K., Ikeda Y., Hashiguchi K., Ariyoshi M., Tochio H.,
RA   Saitoh H., Shirakawa M.;
RT   "Structural basis for regulation of poly-SUMO chain by a SUMO-like domain
RT   of Nip45.";
RL   Proteins 78:1491-1502(2010).
RN   [66]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH IPO13.
RX   PubMed=21139563; DOI=10.1038/emboj.2010.320;
RA   Grunwald M., Bono F.;
RT   "Structure of Importin13-Ubc9 complex: nuclear import and release of a key
RT   regulator of sumoylation.";
RL   EMBO J. 30:427-438(2011).
RN   [67]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH RWDD3, AND
RP   INTERACTION WITH RWDD3.
RX   PubMed=25918163; DOI=10.1074/jbc.m115.644047;
RA   Alontaga A.Y., Ambaye N.D., Li Y.J., Vega R., Chen C.H., Bzymek K.P.,
RA   Williams J.C., Hu W., Chen Y.;
RT   "RWD domain as an E2 (Ubc9)-interaction module.";
RL   J. Biol. Chem. 290:16550-16559(2015).
RN   [68]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZNF451 AND SUMO2,
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH ZNF451 AND
RP   SUMO2.
RX   PubMed=26524494; DOI=10.1038/nsmb.3116;
RA   Cappadocia L., Pichler A., Lima C.D.;
RT   "Structural basis for catalytic activation by the human ZNF451 SUMO E3
RT   ligase.";
RL   Nat. Struct. Mol. Biol. 22:968-975(2015).
CC   -!- FUNCTION: Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3,
CC       SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes
CC       their covalent attachment to other proteins with the help of an E3
CC       ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of
CC       poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5.
CC       Essential for nuclear architecture and chromosome segregation.
CC       Sumoylates p53/TP53 at 'Lys-386'. Mediates sumoylation of ERCC6 which
CC       is essential for its transcription-coupled nucleotide excision repair
CC       activity (PubMed:26620705). {ECO:0000269|PubMed:11451954,
CC       ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:17466333,
CC       ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:19744555,
CC       ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:26524494,
CC       ECO:0000269|PubMed:26620705, ECO:0000269|PubMed:27211601,
CC       ECO:0000269|PubMed:8668529}.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000269|PubMed:26524494}.
CC   -!- SUBUNIT: Forms a complex with SENP6 and UBE2I in response to UV
CC       irradiation (PubMed:17704809). Forms a tight complex with RANGAP1 and
CC       RANBP2 (PubMed:15378033, PubMed:15608651, PubMed:11853669,
CC       PubMed:15931224, PubMed:16732283). Identified in a complex with SUMO2
CC       and UBE2I, where one ZNF451 interacts with one UBE2I and two SUMO2
CC       chains, one bound to the UBE2I active site and the other to another
CC       region of the same UBE2I molecule (PubMed:12924945, PubMed:26524494).
CC       Interacts with SETX (PubMed:24105744). Interacts with HIPK1 and HIPK2
CC       (By similarity). Interacts with PPM1J (By similarity). Interacts with
CC       RASD2 (By similarity). Interacts with TCF3 (By similarity). Interacts
CC       with NR2C1; the interaction promotes its sumoylation (By similarity).
CC       Interacts with SIAH1 (PubMed:9334332). Interacts with PARP
CC       (PubMed:9197546). Interacts with various transcription factors such as
CC       TFAP2A, TFAP2B, and TFAP2C (PubMed:12072434). Interacts with AR
CC       (PubMed:10383460). Interacts with ETS1 (PubMed:9333025). Interacts with
CC       SOX4 (PubMed:16631117). Interacts with RWDD3; the interaction enhances
CC       the sumoylation of a number of proteins such as HIF1A and I-kappa-B
CC       (PubMed:17956732, PubMed:23469069). Interacts with FOXL2
CC       (PubMed:19744555). Interacts with DNM1l (via its GTPase and B domains);
CC       the interaction promotes sumoylation of DNM1L, mainly in its B domain
CC       (PubMed:19638400). Interacts with NFATC2IP; this inhibits formation of
CC       poly-SUMO chains (PubMed:20077568). Interacts with FHIT
CC       (PubMed:11085938). Interacts with PRKRA and p53/TP53 (By similarity).
CC       Interacts with UHRF2 (PubMed:23404503). Interacts with NR3C1 and this
CC       interaction is enhanced in the presence of RWDD3 (PubMed:23508108,
CC       PubMed:25918163). Interacts with MTA1 (PubMed:21965678). Interacts with
CC       ZNF451 (PubMed:26524494). Interacts with CPEB3 (By similarity).
CC       Interacts with SUMO1, SUMO2 and SUMO3 (PubMed:17466333). Interacts with
CC       IPO13 (PubMed:21139563). Interacts with DNMT1 (PubMed:19450230).
CC       Interacts with SUMO1P1/SUMO5 (PubMed:27211601). Interacts with PML-RARA
CC       oncoprotein (via the coiled-colied domain); the interaction is required
CC       for sumoylation of the PML-RARA oncoprotein (PubMed:15809060).
CC       Interacts with ZBED1/hDREF (PubMed:27068747).
CC       {ECO:0000250|UniProtKB:P63280, ECO:0000250|UniProtKB:P63281,
CC       ECO:0000269|PubMed:10383460, ECO:0000269|PubMed:11085938,
CC       ECO:0000269|PubMed:11853669, ECO:0000269|PubMed:12072434,
CC       ECO:0000269|PubMed:12924945, ECO:0000269|PubMed:15378033,
CC       ECO:0000269|PubMed:15608651, ECO:0000269|PubMed:15809060,
CC       ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:16631117,
CC       ECO:0000269|PubMed:16732283, ECO:0000269|PubMed:17466333,
CC       ECO:0000269|PubMed:17704809, ECO:0000269|PubMed:17956732,
CC       ECO:0000269|PubMed:19450230, ECO:0000269|PubMed:19638400,
CC       ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:20077568,
CC       ECO:0000269|PubMed:21139563, ECO:0000269|PubMed:21965678,
CC       ECO:0000269|PubMed:23404503, ECO:0000269|PubMed:23469069,
CC       ECO:0000269|PubMed:23508108, ECO:0000269|PubMed:24105744,
CC       ECO:0000269|PubMed:25918163, ECO:0000269|PubMed:26524494,
CC       ECO:0000269|PubMed:27068747, ECO:0000269|PubMed:27211601,
CC       ECO:0000269|PubMed:9197546, ECO:0000269|PubMed:9333025,
CC       ECO:0000269|PubMed:9334332, ECO:0000305}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human herpesvirus 6 IE2.
CC       {ECO:0000269|PubMed:17005699}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus early
CC       E1A protein; this interaction interferes with polysumoylation.
CC       {ECO:0000269|PubMed:20543865, ECO:0000269|PubMed:8824223}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Epstein-barr virus
CC       protein LMP1. {ECO:0000269|PubMed:21795333}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus VP35; this
CC       interaction mediates the sumoylation of IRF7 and contributes to the
CC       viral inhibition of IFN-type I production.
CC       {ECO:0000269|PubMed:19557165}.
CC   -!- INTERACTION:
CC       P63279; P54253: ATXN1; NbExp=7; IntAct=EBI-80168, EBI-930964;
CC       P63279; O14503: BHLHE40; NbExp=3; IntAct=EBI-80168, EBI-711810;
CC       P63279; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-80168, EBI-749627;
CC       P63279; Q9UER7: DAXX; NbExp=3; IntAct=EBI-80168, EBI-77321;
CC       P63279; Q9UBC3: DNMT3B; NbExp=3; IntAct=EBI-80168, EBI-80125;
CC       P63279; Q8WWZ3: EDARADD; NbExp=3; IntAct=EBI-80168, EBI-2949647;
CC       P63279; P19419: ELK1; NbExp=7; IntAct=EBI-80168, EBI-726632;
CC       P63279; Q96IK5: GMCL1; NbExp=4; IntAct=EBI-80168, EBI-2548508;
CC       P63279; Q08379: GOLGA2; NbExp=4; IntAct=EBI-80168, EBI-618309;
CC       P63279; P56524: HDAC4; NbExp=3; IntAct=EBI-80168, EBI-308629;
CC       P63279; P42858: HTT; NbExp=3; IntAct=EBI-80168, EBI-466029;
CC       P63279; O94829: IPO13; NbExp=6; IntAct=EBI-80168, EBI-747310;
CC       P63279; O75928: PIAS2; NbExp=8; IntAct=EBI-80168, EBI-348555;
CC       P63279; P49792: RANBP2; NbExp=3; IntAct=EBI-80168, EBI-973138;
CC       P63279; P46060: RANGAP1; NbExp=12; IntAct=EBI-80168, EBI-396091;
CC       P63279; Q6ZNA4: RNF111; NbExp=5; IntAct=EBI-80168, EBI-2129175;
CC       P63279; Q9Y265: RUVBL1; NbExp=3; IntAct=EBI-80168, EBI-353675;
CC       P63279; Q9Y3V2: RWDD3; NbExp=5; IntAct=EBI-80168, EBI-1549885;
CC       P63279; Q7Z333: SETX; NbExp=3; IntAct=EBI-80168, EBI-1220123;
CC       P63279; Q13485: SMAD4; NbExp=6; IntAct=EBI-80168, EBI-347263;
CC       P63279; P56693: SOX10; NbExp=2; IntAct=EBI-80168, EBI-1167533;
CC       P63279; P63165: SUMO1; NbExp=11; IntAct=EBI-80168, EBI-80140;
CC       P63279; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-80168, EBI-10175576;
CC       P63279; P61956: SUMO2; NbExp=7; IntAct=EBI-80168, EBI-473220;
CC       P63279; P05549: TFAP2A; NbExp=4; IntAct=EBI-80168, EBI-347351;
CC       P63279; Q92754: TFAP2C; NbExp=5; IntAct=EBI-80168, EBI-937309;
CC       P63279; Q12800: TFCP2; NbExp=4; IntAct=EBI-80168, EBI-717422;
CC       P63279; P04637: TP53; NbExp=3; IntAct=EBI-80168, EBI-366083;
CC       P63279; P22314: UBA1; NbExp=2; IntAct=EBI-80168, EBI-709688;
CC       P63279; Q9UBT2: UBA2; NbExp=6; IntAct=EBI-80168, EBI-718569;
CC       P63279; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-80168, EBI-3918996;
CC       P63279; Q8N3Z6: ZCCHC7; NbExp=3; IntAct=EBI-80168, EBI-7265024;
CC       P63279; Q9Y4E5: ZNF451; NbExp=4; IntAct=EBI-80168, EBI-747230;
CC       P63279; P03116: E1; Xeno; NbExp=2; IntAct=EBI-80168, EBI-7015985;
CC       P63279; P03230: LMP1; Xeno; NbExp=5; IntAct=EBI-80168, EBI-6973030;
CC       P63279; P59595: N; Xeno; NbExp=12; IntAct=EBI-80168, EBI-7602718;
CC       P63279; PRO_0000037946 [P29991]; Xeno; NbExp=3; IntAct=EBI-80168, EBI-8826488;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16631117,
CC       ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:22214662,
CC       ECO:0000269|PubMed:27068747}. Cytoplasm {ECO:0000269|PubMed:22214662}.
CC       Note=Mainly nuclear (By similarity). In spermatocytes, localizes in
CC       synaptonemal complexes (PubMed:8610150). Recruited by BCL11A into the
CC       nuclear body (By similarity). {ECO:0000250|UniProtKB:P63280,
CC       ECO:0000269|PubMed:8610150}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, pancreas,
CC       kidney, liver, lung, placenta and brain. Also expressed in testis and
CC       thymus. {ECO:0000269|PubMed:8610150}.
CC   -!- PTM: Phosphorylation at Ser-71 significantly enhances SUMOylation
CC       activity. {ECO:0000269|PubMed:22509284}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH51289.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD92225.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X96427; CAA65287.1; -; mRNA.
DR   EMBL; U45328; AAA86662.1; -; mRNA.
DR   EMBL; D45050; BAA08091.1; -; mRNA.
DR   EMBL; U29092; AAC51361.1; -; mRNA.
DR   EMBL; U31933; AAB02181.1; -; mRNA.
DR   EMBL; U31882; AAC50603.1; -; mRNA.
DR   EMBL; U66867; AAC50716.1; -; mRNA.
DR   EMBL; U66818; AAC50715.1; -; mRNA.
DR   EMBL; U38785; AAB09410.1; -; mRNA.
DR   EMBL; AJ002385; CAA05359.1; -; mRNA.
DR   EMBL; BT006932; AAP35578.1; -; mRNA.
DR   EMBL; AB208988; BAD92225.1; ALT_INIT; mRNA.
DR   EMBL; AE006466; AAK61274.1; -; Genomic_DNA.
DR   EMBL; AL031714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471112; EAW85673.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85676.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85677.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85678.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85679.1; -; Genomic_DNA.
DR   EMBL; BC000427; AAH00427.1; -; mRNA.
DR   EMBL; BC004429; AAH04429.1; -; mRNA.
DR   EMBL; BC051289; AAH51289.3; ALT_INIT; mRNA.
DR   CCDS; CCDS10433.1; -.
DR   PIR; JC6056; JC6056.
DR   RefSeq; NP_003336.1; NM_003345.4.
DR   RefSeq; NP_919235.1; NM_194259.2.
DR   RefSeq; NP_919236.1; NM_194260.2.
DR   RefSeq; NP_919237.1; NM_194261.2.
DR   RefSeq; XP_016879129.1; XM_017023640.1.
DR   PDB; 1A3S; X-ray; 2.80 A; A=1-158.
DR   PDB; 1KPS; X-ray; 2.50 A; A/C=1-158.
DR   PDB; 1Z5Q; Model; -; A=1-158.
DR   PDB; 1Z5S; X-ray; 3.01 A; A=1-158.
DR   PDB; 2GRN; X-ray; 1.80 A; A=1-158.
DR   PDB; 2GRO; X-ray; 1.70 A; A=1-158.
DR   PDB; 2GRP; X-ray; 2.05 A; A=1-158.
DR   PDB; 2GRQ; X-ray; 1.70 A; A=1-158.
DR   PDB; 2GRR; X-ray; 1.30 A; A=1-158.
DR   PDB; 2O25; X-ray; 2.60 A; C/D=1-158.
DR   PDB; 2PE6; X-ray; 2.40 A; A=1-158.
DR   PDB; 2PX9; NMR; -; B=1-158.
DR   PDB; 2XWU; X-ray; 2.80 A; A=1-158.
DR   PDB; 3A4S; X-ray; 2.70 A; A/B=1-158.
DR   PDB; 3UIN; X-ray; 2.60 A; A=1-158.
DR   PDB; 3UIO; X-ray; 2.60 A; A=1-158.
DR   PDB; 3UIP; X-ray; 2.29 A; A=1-158.
DR   PDB; 4W5V; X-ray; 2.50 A; A=1-158.
DR   PDB; 4Y1L; X-ray; 2.70 A; A/B=1-158.
DR   PDB; 5D2M; X-ray; 2.40 A; A/D=1-158.
DR   PDB; 5F6D; X-ray; 1.55 A; A=2-158.
DR   PDB; 5F6E; X-ray; 1.12 A; A=2-158.
DR   PDB; 5F6U; X-ray; 1.55 A; A=2-158.
DR   PDB; 5F6V; X-ray; 1.49 A; A=2-158.
DR   PDB; 5F6W; X-ray; 1.70 A; A=2-158.
DR   PDB; 5F6X; X-ray; 1.56 A; A=2-158.
DR   PDB; 5F6Y; X-ray; 1.14 A; A=2-158.
DR   PDB; 5FQ2; X-ray; 2.20 A; A=1-158.
DR   PDB; 6SYF; X-ray; 1.90 A; A/B/C/D=2-158.
DR   PDBsum; 1A3S; -.
DR   PDBsum; 1KPS; -.
DR   PDBsum; 1Z5Q; -.
DR   PDBsum; 1Z5S; -.
DR   PDBsum; 2GRN; -.
DR   PDBsum; 2GRO; -.
DR   PDBsum; 2GRP; -.
DR   PDBsum; 2GRQ; -.
DR   PDBsum; 2GRR; -.
DR   PDBsum; 2O25; -.
DR   PDBsum; 2PE6; -.
DR   PDBsum; 2PX9; -.
DR   PDBsum; 2XWU; -.
DR   PDBsum; 3A4S; -.
DR   PDBsum; 3UIN; -.
DR   PDBsum; 3UIO; -.
DR   PDBsum; 3UIP; -.
DR   PDBsum; 4W5V; -.
DR   PDBsum; 4Y1L; -.
DR   PDBsum; 5D2M; -.
DR   PDBsum; 5F6D; -.
DR   PDBsum; 5F6E; -.
DR   PDBsum; 5F6U; -.
DR   PDBsum; 5F6V; -.
DR   PDBsum; 5F6W; -.
DR   PDBsum; 5F6X; -.
DR   PDBsum; 5F6Y; -.
DR   PDBsum; 5FQ2; -.
DR   PDBsum; 6SYF; -.
DR   BMRB; P63279; -.
DR   SMR; P63279; -.
DR   BioGRID; 113177; 635.
DR   ComplexPortal; CPX-4747; E3 ligase (RANBP2) complex.
DR   CORUM; P63279; -.
DR   DIP; DIP-29078N; -.
DR   ELM; P63279; -.
DR   IntAct; P63279; 207.
DR   MINT; P63279; -.
DR   STRING; 9606.ENSP00000348056; -.
DR   BindingDB; P63279; -.
DR   ChEMBL; CHEMBL1741191; -.
DR   MoonDB; P63279; Predicted.
DR   TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
DR   GlyGen; P63279; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P63279; -.
DR   PhosphoSitePlus; P63279; -.
DR   SwissPalm; P63279; -.
DR   BioMuta; UBE2I; -.
DR   DMDM; 54039791; -.
DR   CPTAC; CPTAC-1469; -.
DR   CPTAC; CPTAC-1470; -.
DR   CPTAC; CPTAC-1471; -.
DR   CPTAC; CPTAC-3261; -.
DR   CPTAC; CPTAC-711; -.
DR   EPD; P63279; -.
DR   jPOST; P63279; -.
DR   MassIVE; P63279; -.
DR   MaxQB; P63279; -.
DR   PaxDb; P63279; -.
DR   PeptideAtlas; P63279; -.
DR   PRIDE; P63279; -.
DR   ProteomicsDB; 12715; -.
DR   ProteomicsDB; 57517; -.
DR   TopDownProteomics; P63279; -.
DR   ABCD; P63279; 1 sequenced antibody.
DR   Antibodypedia; 1138; 524 antibodies.
DR   CPTC; P63279; 1 antibody.
DR   DNASU; 7329; -.
DR   Ensembl; ENST00000325437; ENSP00000324897; ENSG00000103275.
DR   Ensembl; ENST00000355803; ENSP00000348056; ENSG00000103275.
DR   Ensembl; ENST00000397514; ENSP00000380649; ENSG00000103275.
DR   Ensembl; ENST00000397515; ENSP00000380650; ENSG00000103275.
DR   Ensembl; ENST00000403747; ENSP00000385009; ENSG00000103275.
DR   Ensembl; ENST00000406620; ENSP00000384568; ENSG00000103275.
DR   Ensembl; ENST00000562470; ENSP00000490882; ENSG00000103275.
DR   Ensembl; ENST00000566587; ENSP00000457064; ENSG00000103275.
DR   Ensembl; ENST00000567074; ENSP00000455893; ENSG00000103275.
DR   Ensembl; ENST00000567383; ENSP00000456188; ENSG00000103275.
DR   GeneID; 7329; -.
DR   KEGG; hsa:7329; -.
DR   UCSC; uc002clc.2; human.
DR   CTD; 7329; -.
DR   DisGeNET; 7329; -.
DR   GeneCards; UBE2I; -.
DR   HGNC; HGNC:12485; UBE2I.
DR   HPA; ENSG00000103275; Low tissue specificity.
DR   MIM; 601661; gene.
DR   neXtProt; NX_P63279; -.
DR   OpenTargets; ENSG00000103275; -.
DR   PharmGKB; PA37134; -.
DR   VEuPathDB; HostDB:ENSG00000103275; -.
DR   eggNOG; KOG0424; Eukaryota.
DR   GeneTree; ENSGT00550000075088; -.
DR   InParanoid; P63279; -.
DR   OMA; QEPAWRA; -.
DR   OrthoDB; 1110467at2759; -.
DR   PhylomeDB; P63279; -.
DR   TreeFam; TF101122; -.
DR   BRENDA; 2.3.2.23; 2681.
DR   PathwayCommons; P63279; -.
DR   Reactome; R-HSA-1221632; Meiotic synapsis.
DR   Reactome; R-HSA-196791; Vitamin D (calciferol) metabolism.
DR   Reactome; R-HSA-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR   Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-HSA-3108232; SUMO E3 ligases SUMOylate target proteins.
DR   Reactome; R-HSA-3232118; SUMOylation of transcription factors.
DR   Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR   Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR   Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR   Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins.
DR   Reactome; R-HSA-4755510; SUMOylation of immune response proteins.
DR   Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-HSA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR   Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   Reactome; R-HSA-9683610; Maturation of nucleoprotein.
DR   Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR   SignaLink; P63279; -.
DR   SIGNOR; P63279; -.
DR   UniPathway; UPA00886; -.
DR   BioGRID-ORCS; 7329; 795 hits in 1033 CRISPR screens.
DR   ChiTaRS; UBE2I; human.
DR   EvolutionaryTrace; P63279; -.
DR   GeneWiki; UBE2I; -.
DR   GenomeRNAi; 7329; -.
DR   Pharos; P63279; Tbio.
DR   PRO; PR:P63279; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P63279; protein.
DR   Bgee; ENSG00000103275; Expressed in oocyte and 246 other tissues.
DR   ExpressionAtlas; P63279; baseline and differential.
DR   Genevisible; P63279; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR   GO; GO:1990356; C:sumoylated E2 ligase complex; IDA:CAFA.
DR   GO; GO:0000795; C:synaptonemal complex; TAS:ProtInc.
DR   GO; GO:1990234; C:transferase complex; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0043398; F:HLH domain binding; IEA:Ensembl.
DR   GO; GO:0071535; F:RING-like zinc finger domain binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0044388; F:small protein activating enzyme binding; IPI:CAFA.
DR   GO; GO:0061656; F:SUMO conjugating enzyme activity; IDA:BHF-UCL.
DR   GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR   GO; GO:0001221; F:transcription coregulator binding; IPI:ARUK-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0007084; P:mitotic nuclear membrane reassembly; TAS:Reactome.
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; IDA:BHF-UCL.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR   GO; GO:1903755; P:positive regulation of SUMO transferase activity; IDA:BHF-UCL.
DR   GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
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; Host-virus interaction; Isopeptide bond;
KW   Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..158
FT                   /note="SUMO-conjugating enzyme UBC9"
FT                   /id="PRO_0000082454"
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   ACT_SITE        93
FT                   /note="Glycyl thioester intermediate"
FT   SITE            4
FT                   /note="Interaction with RANBP2"
FT   SITE            25
FT                   /note="Interaction with RANBP2"
FT   SITE            57
FT                   /note="Interaction with RANBP2"
FT   SITE            100..101
FT                   /note="Substrate binding"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         65
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         71
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000269|PubMed:22509284,
FT                   ECO:0007744|PubMed:23186163"
FT   CROSSLNK        18
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        18
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT   CROSSLNK        48
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        49
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        49
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211,
FT                   ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        101
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   MUTAGEN         13..14
FT                   /note="RK->AA: Impairs binding to SUMO1 and catalytic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:12924945"
FT   MUTAGEN         17..18
FT                   /note="RK->AA: Impairs binding to SUMO1 and catalytic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:12924945"
FT   MUTAGEN         22
FT                   /note="F->A: Impairs binding to RANBP2."
FT                   /evidence="ECO:0000269|PubMed:15608651"
FT   MUTAGEN         25
FT                   /note="V->A: Impairs binding to RANBP2."
FT                   /evidence="ECO:0000269|PubMed:15608651"
FT   MUTAGEN         27
FT                   /note="V->A: Impairs binding to RANBP2."
FT                   /evidence="ECO:0000269|PubMed:15608651"
FT   MUTAGEN         42
FT                   /note="E->A: Slightly impairs binding to RANBP2."
FT                   /evidence="ECO:0000269|PubMed:15608651"
FT   MUTAGEN         48
FT                   /note="K->A: Slightly impairs binding to RANBP2."
FT                   /evidence="ECO:0000269|PubMed:15608651"
FT   MUTAGEN         54
FT                   /note="E->A: Slightly impairs binding to RANBP2."
FT                   /evidence="ECO:0000269|PubMed:15608651"
FT   MUTAGEN         57
FT                   /note="L->A: Impairs binding to RANBP2."
FT                   /evidence="ECO:0000269|PubMed:15608651"
FT   MUTAGEN         59
FT                   /note="K->A: Impairs binding to RANBP2."
FT                   /evidence="ECO:0000269|PubMed:15608651"
FT   MUTAGEN         61
FT                   /note="R->A: Slightly impairs binding to RANBP2."
FT                   /evidence="ECO:0000269|PubMed:15608651"
FT   MUTAGEN         85
FT                   /note="N->Q: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:16732283"
FT   MUTAGEN         87
FT                   /note="Y->A: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:16732283"
FT   MUTAGEN         93
FT                   /note="C->S: Loss of enhancement of sumoylation by RWDD3.
FT                   No effect on RWDD3 protein levels."
FT   MUTAGEN         100..101
FT                   /note="DK->AA: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:12641448"
FT   MUTAGEN         127
FT                   /note="D->A: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:16732283"
FT   MUTAGEN         127
FT                   /note="D->S: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:16732283"
FT   CONFLICT        18
FT                   /note="K -> P (in Ref. 6; AAC50603)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86..89
FT                   /note="VYPS -> GVPF (in Ref. 6; AAC50603)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..18
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:2PE6"
FT   STRAND          36..46
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   TURN            52..55
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   STRAND          57..63
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   TURN            66..69
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   TURN            99..102
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   HELIX           109..121
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   HELIX           131..139
FT                   /evidence="ECO:0007829|PDB:5F6E"
FT   HELIX           141..154
FT                   /evidence="ECO:0007829|PDB:5F6E"
SQ   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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