SUMO1_HUMAN
ID SUMO1_HUMAN Reviewed; 101 AA.
AC P63165; A8MUS8; B2R4I5; P55856; Q6FGG0; Q6NZ62; Q93068;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Small ubiquitin-related modifier 1;
DE Short=SUMO-1;
DE AltName: Full=GAP-modifying protein 1;
DE Short=GMP1;
DE AltName: Full=SMT3 homolog 3;
DE AltName: Full=Sentrin;
DE AltName: Full=Ubiquitin-homology domain protein PIC1;
DE AltName: Full=Ubiquitin-like protein SMT3C;
DE Short=Smt3C;
DE AltName: Full=Ubiquitin-like protein UBL1;
DE Flags: Precursor;
GN Name=SUMO1; Synonyms=SMT3C, SMT3H3, UBL1; ORFNames=OK/SW-cl.43;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9119407; DOI=10.1006/geno.1996.4556;
RA Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F.,
RA Brahe C.;
RT "SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to
RT chromosome 21qter and defines a novel gene family.";
RL Genomics 40:362-367(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
RX PubMed=8806687;
RA Boddy M.N., Howe K., Etkin L.D., Solomon E., Freemont P.S.;
RT "PIC 1, a novel ubiquitin-like protein which interacts with the PML
RT component of a multiprotein complex that is disrupted in acute
RT promyelocytic leukaemia.";
RL Oncogene 13:971-982(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8812453; DOI=10.1006/geno.1996.0462;
RA Shen Z., Pardington-Purtymun P.E., Comeaux J.C., Moyzis R.K., Chen D.J.;
RT "UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52
RT proteins.";
RL Genomics 36:271-279(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=9019411; DOI=10.1016/s0092-8674(00)81862-0;
RA Mahajan R., Delphin C., Guan T., Gerace L., Melchior F.;
RT "A small ubiquitin-related polypeptide involved in targeting RanGAP1 to
RT nuclear pore complex protein RanBP2.";
RL Cell 88:97-107(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8978815; DOI=10.1083/jcb.135.6.1457;
RA Matunis M.J., Coutavas E., Blobel G.;
RT "A novel ubiquitin-like modification modulates the partitioning of the Ran-
RT GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore
RT complex.";
RL J. Cell Biol. 135:1457-1470(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8906799;
RA Okura T., Gong L., Kamitani T., Wada T., Okura I., Wei C.F., Chang H.M.,
RA Yeh E.T.H.;
RT "Protection against Fas/APO-1- and tumor necrosis factor-mediated cell
RT death by a novel protein, sentrin.";
RL J. Immunol. 157:4277-4281(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [12]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=9162015; DOI=10.1074/jbc.272.22.14001;
RA Kamitani T., Nguyen H.P., Yeh E.T.H.;
RT "Preferential modification of nuclear proteins by a novel ubiquitin-like
RT molecule.";
RL J. Biol. Chem. 272:14001-14004(1997).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=10574707; DOI=10.1242/jcs.112.24.4581;
RA Everett R.D., Lomonte P., Sternsdorf T., van Driel R., Orr A.;
RT "Cell cycle regulation of PML modification and ND10 composition.";
RL J. Cell Sci. 112:4581-4588(1999).
RN [16]
RP INTERACTION WITH HIPK3; CHD3; PIAS1; EXOSC9 AND TDG.
RX PubMed=10961991; DOI=10.1074/jbc.m004293200;
RA Minty A., Dumont X., Kaghad M., Caput D.;
RT "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73
RT identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction
RT motif.";
RL J. Biol. Chem. 275:36316-36323(2000).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=12383504; DOI=10.1016/s0378-1119(02)00843-0;
RA Su H.-L., Li S.S.-L.;
RT "Molecular features of human ubiquitin-like SUMO genes and their encoded
RT proteins.";
RL Gene 296:65-73(2002).
RN [18]
RP INTERACTION WITH UBE2I.
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 [19]
RP INTERACTION WITH HIPK2.
RX PubMed=12565818; DOI=10.1016/s0014-4827(02)00025-3;
RA Engelhardt O.G., Boutell C., Orr A., Ullrich E., Haller O., Everett R.D.;
RT "The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through both
RT its kinase domain and a SUMO-1 interaction motif and alters the
RT posttranslational modification of PML.";
RL Exp. Cell Res. 283:36-50(2003).
RN [20]
RP INTERACTION WITH TULA HANTAVIRUS (MICROBIAL INFECTION).
RX PubMed=12606074; DOI=10.1016/s0168-1702(02)00312-x;
RA Kaukinen P., Vaheri A., Plyusnin A.;
RT "Non-covalent interaction between nucleocapsid protein of Tula hantavirus
RT and small ubiquitin-related modifier-1, SUMO-1.";
RL Virus Res. 92:37-45(2003).
RN [21]
RP INTERACTION WITH HANTAAN HANTAVIRUS NUCLEOPROTEIN (MICROBIAL INFECTION).
RX PubMed=12573574; DOI=10.1006/viro.2002.1767;
RA Maeda A., Lee B.H., Yoshimatsu K., Saijo M., Kurane I., Arikawa J.,
RA Morikawa S.;
RT "The intracellular association of the nucleocapsid protein (NP) of hantaan
RT virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating
RT enzyme 9 (Ubc9).";
RL Virology 305:288-297(2003).
RN [22]
RP CLEAVAGE.
RX PubMed=15487983; DOI=10.1042/bj20041210;
RA Xu Z., Au S.W.N.;
RT "Mapping residues of SUMO precursors essential in differential maturation
RT by SUMO-specific protease, SENP1.";
RL Biochem. J. 386:325-330(2005).
RN [23]
RP INTERACTION WITH RANBP2.
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [25]
RP INTERACTION WITH PRKN.
RX PubMed=16955485; DOI=10.1002/jnr.21041;
RA Um J.W., Chung K.C.;
RT "Functional modulation of parkin through physical interaction with SUMO-
RT 1.";
RL J. Neurosci. Res. 84:1543-1554(2006).
RN [26]
RP CHROMOSOMAL TRANSLOCATION, AND INVOLVEMENT IN OFC10.
RX PubMed=16990542; DOI=10.1126/science.1128406;
RA Alkuraya F.S., Saadi I., Lund J.J., Turbe-Doan A., Morton C.C., Maas R.L.;
RT "SUMO1 haploinsufficiency leads to cleft lip and palate.";
RL Science 313:1751-1751(2006).
RN [27]
RP INTERACTION WITH UBE2I AND RWDD3.
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 [28]
RP PHOSPHORYLATION AT SER-2.
RX PubMed=18707152; DOI=10.1021/pr800368m;
RA Matic I., Macek B., Hilger M., Walther T.C., Mann M.;
RT "Phosphorylation of SUMO-1 occurs in vivo and is conserved through
RT evolution.";
RL J. Proteome Res. 7:4050-4057(2008).
RN [29]
RP FUNCTION IN SUMOYLATION OF USP25, AND INTERACTION WITH USP25.
RX PubMed=18538659; DOI=10.1016/j.molcel.2008.03.021;
RA Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.;
RT "Mechanism and consequences for paralog-specific sumoylation of ubiquitin-
RT specific protease 25.";
RL Mol. Cell 30:610-619(2008).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [31]
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=18408734; DOI=10.1038/ncb1716;
RA Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N.,
RA Jaffray E.G., Palvimo J.J., Hay R.T.;
RT "RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-
RT induced PML degradation.";
RL Nat. Cell Biol. 10:538-546(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 FUNCTION IN KCNB1 SUMOYLATION, INTERACTION WITH KCNB1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19223394; DOI=10.1242/jcs.036632;
RA Dai X.Q., Kolic J., Marchi P., Sipione S., Macdonald P.E.;
RT "SUMOylation regulates Kv2.1 and modulates pancreatic beta-cell
RT excitability.";
RL J. Cell Sci. 122:775-779(2009).
RN [34]
RP SUMOYLATION AT LYS-7 AND LYS-25, AND ACETYLATION AT SER-2.
RC TISSUE=Cervix carcinoma;
RX PubMed=20388717; DOI=10.1074/jbc.m110.106955;
RA Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
RA Eriksson J.E., Sistonen L.;
RT "In vivo identification of sumoylation sites by a signature tag and
RT cysteine-targeted affinity purification.";
RL J. Biol. Chem. 285:19324-19329(2010).
RN [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 AND SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [36]
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 [37]
RP FUNCTION, AND 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 [38]
RP INTERACTION WITH BHLHE40/DEC1.
RX PubMed=21829689; DOI=10.1371/journal.pone.0023046;
RA Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X.,
RA Chang A.K., Wu H.;
RT "SUMOylation of DEC1 protein regulates its transcriptional activity and
RT enhances its stability.";
RL PLoS ONE 6:E23046-E23046(2011).
RN [39]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [40]
RP SUBCELLULAR LOCATION.
RX PubMed=22406621; DOI=10.1158/0008-5472.can-11-3159;
RA Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A.,
RA Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J.,
RA Scaglioni P.P.;
RT "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its
RT oncogenic counterpart PML-RARA.";
RL Cancer Res. 72:2275-2284(2012).
RN [41]
RP IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, AND INTERACTION WITH
RP SIMC1; CASP8AP2; RNF111 AND SOBP.
RX PubMed=23086935; DOI=10.1074/jbc.m112.410985;
RA Sun H., Hunter T.;
RT "PolySUMO-binding proteins identified through a string search.";
RL J. Biol. Chem. 287:42071-42083(2012).
RN [42]
RP INTERACTION WITH EPSTEIN-BARR VIRUS BGLF4 (MICROBIAL INFECTION).
RX PubMed=22398289; DOI=10.1128/jvi.00314-12;
RA Li R., Wang L., Liao G., Guzzo C.M., Matunis M.J., Zhu H., Hayward S.D.;
RT "SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for
RT BGLF4 function.";
RL J. Virol. 86:5412-5421(2012).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-32, AND
RP IDENTIFICATION BY 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 [44]
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 [45]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-16 AND LYS-17, AND
RP IDENTIFICATION BY MASS 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 [46]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24651376; DOI=10.1371/journal.pone.0092746;
RA Sun X., Li J., Dong F.N., Dong J.T.;
RT "Characterization of nuclear localization and SUMOylation of the ATBF1
RT transcription factor in epithelial cells.";
RL PLoS ONE 9:E92746-E92746(2014).
RN [47]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-17, AND IDENTIFICATION
RP BY MASS 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 [48]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-37, 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 [49]
RP MUTAGENESIS OF GLY-97.
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 [50]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-16; LYS-17; LYS-23;
RP LYS-37; LYS-39; LYS-45 AND LYS-46, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [51]
RP STRUCTURE BY NMR.
RX PubMed=9654451; DOI=10.1006/jmbi.1998.1839;
RA Bayer P., Arndt A., Metzger S., Mahajan R., Melchior F., Jaenicke R.,
RA Becker J.;
RT "Structure determination of the small ubiquitin-related modifier SUMO-1.";
RL J. Mol. Biol. 280:275-286(1998).
RN [52]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-97 IN COMPLEX WITH SENP2, AND
RP CLEAVAGE.
RX PubMed=15296745; DOI=10.1016/j.str.2004.05.023;
RA Reverter D., Lima C.D.;
RT "A basis for SUMO protease specificity provided by analysis of human Senp2
RT and a Senp2-SUMO complex.";
RL Structure 12:1519-1531(2004).
RN [53]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-97 IN COMPLEX WITH SAE1; SAE2
RP AND ATP.
RX PubMed=15660128; DOI=10.1038/sj.emboj.7600552;
RA Lois L.M., Lima C.D.;
RT "Structures of the SUMO E1 provide mechanistic insights into SUMO
RT activation and E2 recruitment to E1.";
RL EMBO J. 24:439-451(2005).
RN [54]
RP STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH PIAS2, AND MUTAGENESIS OF PHE-36.
RX PubMed=16204249; DOI=10.1074/jbc.m507059200;
RA Song J., Zhang Z., Hu W., Chen Y.;
RT "Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif:
RT a reversal of the bound orientation.";
RL J. Biol. Chem. 280:40122-40129(2005).
RN [55]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 18-97 IN COMPLEX WITH UBE2I;
RP RANGAP1 AND 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 [56]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-97 CONJUGATED TO TDG.
RX PubMed=15959518; DOI=10.1038/nature03634;
RA Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K.,
RA Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.;
RT "Crystal structure of thymine DNA glycosylase conjugated to SUMO-1.";
RL Nature 435:979-982(2005).
RN [57]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-97 CONJUGATED TO HIP2.
RX PubMed=15723079; DOI=10.1038/nsmb903;
RA Pichler A., Knipscheer P., Oberhofer E., van Dijk W.J., Koerner R.,
RA Olsen J.V., Jentsch S., Melchior F., Sixma T.K.;
RT "SUMO modification of the ubiquitin-conjugating enzyme E2-25K.";
RL Nat. Struct. Mol. Biol. 12:264-269(2005).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SENP1.
RX PubMed=16712526; DOI=10.1042/bj20060526;
RA Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N.;
RT "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the
RT hydrolytic mechanism of SUMO-specific protease.";
RL Biochem. J. 398:345-352(2006).
RN [59]
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) IN COMPLEX WITH RANGAP1 AND SENP1.
RX PubMed=17099698; DOI=10.1038/nsmb1172;
RA Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.;
RT "SUMO protease SENP1 induces isomerization of the scissile peptide bond.";
RL Nat. Struct. Mol. Biol. 13:1069-1077(2006).
CC -!- FUNCTION: Ubiquitin-like protein that can be covalently attached to
CC proteins as a monomer or a lysine-linked polymer. Covalent attachment
CC via an isopeptide bond to its substrates requires prior activation by
CC the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be
CC promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-
CC translational modification on lysine residues of proteins plays a
CC crucial role in a number of cellular processes such as nuclear
CC transport, DNA replication and repair, mitosis and signal transduction.
CC Involved for instance in targeting RANGAP1 to the nuclear pore complex
CC protein RANBP2. Covalently attached to the voltage-gated potassium
CC channel KCNB1; this modulates the gating characteristics of KCNB1
CC (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to
CC polyubiquitination which functions as a signal for proteasomal
CC degradation of modified proteins. May also regulate a network of genes
CC involved in palate development. Covalently attached to ZFHX3
CC (PubMed:24651376). {ECO:0000269|PubMed:18408734,
CC ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:19223394,
CC ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24651376,
CC ECO:0000269|PubMed:9019411, ECO:0000269|PubMed:9162015}.
CC -!- SUBUNIT: Covalently attached to KCNB1; UBE2I increases cross-linking
CC with KCNB1 and PIAS1 decreases cross-links with KCNB1 (PubMed:19223394,
CC PubMed:15931224). Interacts with SAE2, RANBP2, PIAS1 and PIAS2
CC (PubMed:10961991, PubMed:15608651, PubMed:15660128, PubMed:16204249,
CC PubMed:15931224). Interacts with PRKN (PubMed:16955485). Covalently
CC attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2,
CC SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG (PubMed:10961991,
CC PubMed:15931224, PubMed:15959518, PubMed:17099698). Also interacts with
CC HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52 (PubMed:10961991,
CC PubMed:12565818). Interacts with USP25 (via ts SIM domain); the
CC interaction weakly sumoylates USP25 (PubMed:18538659). Interacts with
CC SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains) (PubMed:23086935).
CC Interacts with BHLHE40/DEC1 (PubMed:21829689). Interacts with RWDD3
CC (PubMed:17956732). Interacts with UBE2I/UBC9 and this interaction is
CC enhanced in the presence of RWDD3 (PubMed:12924945, PubMed:17956732).
CC Interacts with MTA1 (PubMed:21965678). Interacts with SENP2
CC (PubMed:15296745). Interacts with HINT1 (By similarity).
CC {ECO:0000250|UniProtKB:P63166, ECO:0000269|PubMed:10961991,
CC ECO:0000269|PubMed:12565818, ECO:0000269|PubMed:12924945,
CC ECO:0000269|PubMed:15296745, ECO:0000269|PubMed:15608651,
CC ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:15931224,
CC ECO:0000269|PubMed:15959518, ECO:0000269|PubMed:16204249,
CC ECO:0000269|PubMed:16955485, ECO:0000269|PubMed:17099698,
CC ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:18538659,
CC ECO:0000269|PubMed:19223394, ECO:0000269|PubMed:21829689,
CC ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:23086935}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-barr virus BGLF4.
CC {ECO:0000269|PubMed:22398289}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via N-terminus) with Tula
CC hantavirus nucleoprotein. {ECO:0000269|PubMed:12606074}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via N-terminus) with Hantaan
CC hantavirus nucleoprotein. {ECO:0000269|PubMed:12573574}.
CC -!- INTERACTION:
CC P63165; P10275: AR; NbExp=7; IntAct=EBI-80140, EBI-608057;
CC P63165; P15336: ATF2; NbExp=6; IntAct=EBI-80140, EBI-1170906;
CC P63165; A0A0S2Z4M1: AXIN1; NbExp=6; IntAct=EBI-80140, EBI-16429430;
CC P63165; O15169: AXIN1; NbExp=3; IntAct=EBI-80140, EBI-710484;
CC P63165; P38398: BRCA1; NbExp=3; IntAct=EBI-80140, EBI-349905;
CC P63165; Q9Y2F9: BTBD3; NbExp=3; IntAct=EBI-80140, EBI-311155;
CC P63165; Q96B23: C18orf25; NbExp=7; IntAct=EBI-80140, EBI-742108;
CC P63165; Q9H257: CARD9; NbExp=3; IntAct=EBI-80140, EBI-751319;
CC P63165; O00257: CBX4; NbExp=3; IntAct=EBI-80140, EBI-722425;
CC P63165; P17676-1: CEBPB; NbExp=5; IntAct=EBI-80140, EBI-9997012;
CC P63165; Q9UER7: DAXX; NbExp=7; IntAct=EBI-80140, EBI-77321;
CC P63165; Q05D60: DEUP1; NbExp=3; IntAct=EBI-80140, EBI-748597;
CC P63165; Q9UBC3: DNMT3B; NbExp=5; IntAct=EBI-80140, EBI-80125;
CC P63165; Q86UW9: DTX2; NbExp=3; IntAct=EBI-80140, EBI-740376;
CC P63165; Q8WWZ3: EDARADD; NbExp=5; IntAct=EBI-80140, EBI-2949647;
CC P63165; P06730: EIF4E; NbExp=5; IntAct=EBI-80140, EBI-73440;
CC P63165; P19419: ELK1; NbExp=5; IntAct=EBI-80140, EBI-726632;
CC P63165; P19419-1: ELK1; NbExp=2; IntAct=EBI-80140, EBI-15799641;
CC P63165; A0A0S2Z3N6: ETV6; NbExp=3; IntAct=EBI-80140, EBI-16434659;
CC P63165; Q9BPY3: FAM118B; NbExp=3; IntAct=EBI-80140, EBI-726822;
CC P63165; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-80140, EBI-10244131;
CC P63165; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-80140, EBI-10172181;
CC P63165; O95073: FSBP; NbExp=3; IntAct=EBI-80140, EBI-1059030;
CC P63165; O14964: HGS; NbExp=3; IntAct=EBI-80140, EBI-740220;
CC P63165; Q16665: HIF1A; NbExp=4; IntAct=EBI-80140, EBI-447269;
CC P63165; P07910: HNRNPC; NbExp=6; IntAct=EBI-80140, EBI-357966;
CC P63165; Q00613: HSF1; NbExp=2; IntAct=EBI-80140, EBI-719620;
CC P63165; P42858: HTT; NbExp=3; IntAct=EBI-80140, EBI-466029;
CC P63165; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-80140, EBI-81279;
CC P63165; P10914: IRF1; NbExp=2; IntAct=EBI-80140, EBI-1055781;
CC P63165; O00180: KCNK1; NbExp=3; IntAct=EBI-80140, EBI-3914675;
CC P63165; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-80140, EBI-741424;
CC P63165; Q9UIS9: MBD1; NbExp=3; IntAct=EBI-80140, EBI-867196;
CC P63165; Q02078-1: MEF2A; NbExp=3; IntAct=EBI-80140, EBI-15799584;
CC P63165; P10242: MYB; NbExp=3; IntAct=EBI-80140, EBI-298355;
CC P63165; Q00653: NFKB2; NbExp=2; IntAct=EBI-80140, EBI-307326;
CC P63165; P06748-1: NPM1; NbExp=3; IntAct=EBI-80140, EBI-354150;
CC P63165; P09874: PARP1; NbExp=2; IntAct=EBI-80140, EBI-355676;
CC P63165; O75928: PIAS2; NbExp=8; IntAct=EBI-80140, EBI-348555;
CC P63165; O75928-2: PIAS2; NbExp=3; IntAct=EBI-80140, EBI-348567;
CC P63165; P29590: PML; NbExp=6; IntAct=EBI-80140, EBI-295890;
CC P63165; O75626-2: PRDM1; NbExp=2; IntAct=EBI-80140, EBI-7839538;
CC P63165; O75360: PROP1; NbExp=3; IntAct=EBI-80140, EBI-9027467;
CC P63165; O75475: PSIP1; NbExp=4; IntAct=EBI-80140, EBI-1801773;
CC P63165; Q9Y4B4: RAD54L2; NbExp=6; IntAct=EBI-80140, EBI-948156;
CC P63165; P46060: RANGAP1; NbExp=14; IntAct=EBI-80140, EBI-396091;
CC P63165; P10276: RARA; NbExp=5; IntAct=EBI-80140, EBI-413374;
CC P63165; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-80140, EBI-372094;
CC P63165; P78317: RNF4; NbExp=4; IntAct=EBI-80140, EBI-2340927;
CC P63165; Q9Y3V2: RWDD3; NbExp=2; IntAct=EBI-80140, EBI-1549885;
CC P63165; O43290: SART1; NbExp=2; IntAct=EBI-80140, EBI-607761;
CC P63165; Q01826: SATB1; NbExp=2; IntAct=EBI-80140, EBI-743747;
CC P63165; Q9P0U3: SENP1; NbExp=11; IntAct=EBI-80140, EBI-2822935;
CC P63165; Q9HC62: SENP2; NbExp=2; IntAct=EBI-80140, EBI-714881;
CC P63165; P56693: SOX10; NbExp=2; IntAct=EBI-80140, EBI-1167533;
CC P63165; P48431: SOX2; NbExp=4; IntAct=EBI-80140, EBI-6124081;
CC P63165; P23497: SP100; NbExp=6; IntAct=EBI-80140, EBI-751145;
CC P63165; P23497-2: SP100; NbExp=3; IntAct=EBI-80140, EBI-6589365;
CC P63165; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-80140, EBI-10175576;
CC P63165; Q92844: TANK; NbExp=8; IntAct=EBI-80140, EBI-356349;
CC P63165; Q13569: TDG; NbExp=3; IntAct=EBI-80140, EBI-348333;
CC P63165; Q12800: TFCP2; NbExp=3; IntAct=EBI-80140, EBI-717422;
CC P63165; P04637: TP53; NbExp=3; IntAct=EBI-80140, EBI-366083;
CC P63165; Q12888-1: TP53BP1; NbExp=2; IntAct=EBI-80140, EBI-8022649;
CC P63165; Q12933: TRAF2; NbExp=3; IntAct=EBI-80140, EBI-355744;
CC P63165; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-80140, EBI-3650647;
CC P63165; O00463: TRAF5; NbExp=3; IntAct=EBI-80140, EBI-523498;
CC P63165; Q9UBT2: UBA2; NbExp=9; IntAct=EBI-80140, EBI-718569;
CC P63165; P63279: UBE2I; NbExp=11; IntAct=EBI-80140, EBI-80168;
CC P63165; Q7KZS0: UBE2I; NbExp=6; IntAct=EBI-80140, EBI-10180829;
CC P63165; Q5W0Q7: USPL1; NbExp=5; IntAct=EBI-80140, EBI-2513899;
CC P63165; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-80140, EBI-2515601;
CC P63165; Q9HCK0: ZBTB26; NbExp=8; IntAct=EBI-80140, EBI-3918996;
CC P63165; Q15916: ZBTB6; NbExp=3; IntAct=EBI-80140, EBI-7227791;
CC P63165; Q6PEW1: ZCCHC12; NbExp=6; IntAct=EBI-80140, EBI-748373;
CC P63165; Q8N3Z6: ZCCHC7; NbExp=3; IntAct=EBI-80140, EBI-7265024;
CC P63165; Q96MM3: ZFP42; NbExp=3; IntAct=EBI-80140, EBI-12151755;
CC P63165; Q9UJ78: ZMYM5; NbExp=4; IntAct=EBI-80140, EBI-7228860;
CC P63165; Q59GP6; NbExp=3; IntAct=EBI-80140, EBI-10243413;
CC P63165; Q60636: Prdm1; Xeno; NbExp=3; IntAct=EBI-80140, EBI-7000804;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:10574707,
CC ECO:0000269|PubMed:12383504}. Nucleus speckle
CC {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000269|PubMed:12383504,
CC ECO:0000269|PubMed:9162015}. Nucleus, PML body
CC {ECO:0000269|PubMed:10574707, ECO:0000269|PubMed:12383504,
CC ECO:0000269|PubMed:22406621}. Cell membrane
CC {ECO:0000269|PubMed:19223394}. Nucleus {ECO:0000269|PubMed:24651376,
CC ECO:0000269|PubMed:9162015}. Note=Recruited by BCL11A into the nuclear
CC body (By similarity). In the presence of ZFHX3, sequesterd to nuclear
CC body (NB)-like dots in the nucleus some of which overlap or closely
CC associate with PML body (PubMed:24651376).
CC {ECO:0000250|UniProtKB:P63166, ECO:0000269|PubMed:24651376}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63165-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P63165-2; Sequence=VSP_046756;
CC -!- PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for
CC function. {ECO:0000269|PubMed:15487983}.
CC -!- PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4.
CC {ECO:0000269|PubMed:18408734}.
CC -!- DISEASE: Non-syndromic orofacial cleft 10 (OFC10) [MIM:613705]: A birth
CC defect consisting of cleft lips with or without cleft palate. Cleft
CC lips are associated with cleft palate in two-third of cases. A cleft
CC lip can occur on one or both sides and range in severity from a simple
CC notch in the upper lip to a complete opening in the lip extending into
CC the floor of the nostril and involving the upper gum.
CC {ECO:0000269|PubMed:16990542}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. A chromosomal aberration
CC involving SUMO1 is the cause of OFC10. Translocation
CC t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and
CC resulted in haploinsufficiency confirmed by protein assays.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=SUMO protein entry;
CC URL="https://en.wikipedia.org/wiki/SUMO_protein";
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DR EMBL; X99586; CAA67898.1; -; mRNA.
DR EMBL; U61397; AAB40388.1; -; mRNA.
DR EMBL; U38784; AAC50733.1; -; mRNA.
DR EMBL; U67122; AAC50996.1; -; mRNA.
DR EMBL; U72722; AAB40390.1; -; mRNA.
DR EMBL; U83117; AAB39999.1; -; mRNA.
DR EMBL; AB062294; BAB93477.1; -; mRNA.
DR EMBL; BT006632; AAP35278.1; -; mRNA.
DR EMBL; CR542147; CAG46944.1; -; mRNA.
DR EMBL; CR542156; CAG46953.1; -; mRNA.
DR EMBL; AK311840; BAG34782.1; -; mRNA.
DR EMBL; AC079354; AAY24035.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70304.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70307.1; -; Genomic_DNA.
DR EMBL; BC006462; AAH06462.1; -; mRNA.
DR EMBL; BC053528; AAH53528.1; -; mRNA.
DR EMBL; BC066306; AAH66306.1; -; mRNA.
DR CCDS; CCDS2352.1; -. [P63165-1]
DR CCDS; CCDS46493.1; -. [P63165-2]
DR RefSeq; NP_001005781.1; NM_001005781.1. [P63165-1]
DR RefSeq; NP_001005782.1; NM_001005782.1. [P63165-2]
DR RefSeq; NP_003343.1; NM_003352.4. [P63165-1]
DR PDB; 1A5R; NMR; -; A=1-101.
DR PDB; 1TGZ; X-ray; 2.80 A; B=18-97.
DR PDB; 1WYW; X-ray; 2.10 A; B=1-97.
DR PDB; 1Y8R; X-ray; 2.75 A; C/F=1-97.
DR PDB; 1Z5S; X-ray; 3.01 A; B=18-97.
DR PDB; 2ASQ; NMR; -; A=1-97.
DR PDB; 2BF8; X-ray; 2.30 A; B=21-97.
DR PDB; 2G4D; X-ray; 2.80 A; B/D=20-97.
DR PDB; 2IO2; X-ray; 2.90 A; B=18-97.
DR PDB; 2IY0; X-ray; 2.77 A; B=20-101.
DR PDB; 2IY1; X-ray; 2.46 A; B/D=20-101.
DR PDB; 2KQS; NMR; -; A=1-97.
DR PDB; 2LAS; NMR; -; A=1-101.
DR PDB; 2MW5; NMR; -; A=1-97.
DR PDB; 2N1A; NMR; -; A=1-101.
DR PDB; 2N1V; NMR; -; A=1-97.
DR PDB; 2PE6; X-ray; 2.40 A; B=1-97.
DR PDB; 2UYZ; X-ray; 1.40 A; B=20-97.
DR PDB; 2VRR; X-ray; 2.22 A; B=20-97.
DR PDB; 3KYC; X-ray; 2.45 A; D=1-97.
DR PDB; 3KYD; X-ray; 2.61 A; D=1-94.
DR PDB; 3RZW; X-ray; 2.15 A; C/D=1-97.
DR PDB; 3UIP; X-ray; 2.29 A; B=18-97.
DR PDB; 4WJN; X-ray; 1.50 A; A=17-97.
DR PDB; 4WJO; X-ray; 1.46 A; A=17-97.
DR PDB; 4WJP; X-ray; 1.70 A; A/C=17-97.
DR PDB; 4WJQ; X-ray; 1.35 A; A/C=17-97.
DR PDB; 5AEK; X-ray; 3.00 A; B/D/F/H/J/L/N/P/R/T/V/X=20-97.
DR PDB; 5B7A; NMR; -; A=1-97.
DR PDB; 5ELJ; X-ray; 1.98 A; B=18-97.
DR PDB; 5GHD; NMR; -; A=1-97.
DR PDB; 6EOP; X-ray; 2.40 A; D/E/F=61-68.
DR PDB; 6EOT; X-ray; 3.50 A; C/E/F/H/J/L=61-68.
DR PDB; 6J4I; NMR; -; A=1-97.
DR PDB; 6JXU; NMR; -; A=1-101.
DR PDB; 6JXV; NMR; -; A=1-101.
DR PDB; 6K5T; NMR; -; A=21-97.
DR PDB; 6TRW; X-ray; 3.00 A; D/E/F=61-75.
DR PDB; 6UYO; X-ray; 1.64 A; A/C=17-97.
DR PDB; 6UYP; X-ray; 1.42 A; A=17-97.
DR PDB; 6UYQ; X-ray; 1.50 A; A=17-97.
DR PDB; 6UYR; X-ray; 1.30 A; A=17-97.
DR PDB; 6UYS; X-ray; 1.59 A; A/C=17-97.
DR PDB; 6UYT; X-ray; 1.66 A; A=17-97.
DR PDB; 6UYU; X-ray; 1.66 A; A/C=17-97.
DR PDB; 6UYV; X-ray; 1.40 A; A=17-97.
DR PDB; 6UYX; X-ray; 1.70 A; A/C=17-97.
DR PDB; 6UYY; X-ray; 1.60 A; A=17-97.
DR PDB; 6UYZ; X-ray; 1.40 A; A/C=17-97.
DR PDB; 6V7P; X-ray; 1.40 A; A/C=17-97.
DR PDB; 6V7Q; X-ray; 1.35 A; A/C=17-97.
DR PDB; 6V7R; X-ray; 1.55 A; A/C=17-97.
DR PDB; 6V7S; X-ray; 1.47 A; A/C=17-97.
DR PDB; 6WW3; X-ray; 2.10 A; A/B=2-7.
DR PDB; 6XOG; X-ray; 1.98 A; C=1-101.
DR PDB; 6XOH; X-ray; 2.23 A; C=1-101.
DR PDB; 6XOI; X-ray; 2.00 A; C=1-101.
DR PDBsum; 1A5R; -.
DR PDBsum; 1TGZ; -.
DR PDBsum; 1WYW; -.
DR PDBsum; 1Y8R; -.
DR PDBsum; 1Z5S; -.
DR PDBsum; 2ASQ; -.
DR PDBsum; 2BF8; -.
DR PDBsum; 2G4D; -.
DR PDBsum; 2IO2; -.
DR PDBsum; 2IY0; -.
DR PDBsum; 2IY1; -.
DR PDBsum; 2KQS; -.
DR PDBsum; 2LAS; -.
DR PDBsum; 2MW5; -.
DR PDBsum; 2N1A; -.
DR PDBsum; 2N1V; -.
DR PDBsum; 2PE6; -.
DR PDBsum; 2UYZ; -.
DR PDBsum; 2VRR; -.
DR PDBsum; 3KYC; -.
DR PDBsum; 3KYD; -.
DR PDBsum; 3RZW; -.
DR PDBsum; 3UIP; -.
DR PDBsum; 4WJN; -.
DR PDBsum; 4WJO; -.
DR PDBsum; 4WJP; -.
DR PDBsum; 4WJQ; -.
DR PDBsum; 5AEK; -.
DR PDBsum; 5B7A; -.
DR PDBsum; 5ELJ; -.
DR PDBsum; 5GHD; -.
DR PDBsum; 6EOP; -.
DR PDBsum; 6EOT; -.
DR PDBsum; 6J4I; -.
DR PDBsum; 6JXU; -.
DR PDBsum; 6JXV; -.
DR PDBsum; 6K5T; -.
DR PDBsum; 6TRW; -.
DR PDBsum; 6UYO; -.
DR PDBsum; 6UYP; -.
DR PDBsum; 6UYQ; -.
DR PDBsum; 6UYR; -.
DR PDBsum; 6UYS; -.
DR PDBsum; 6UYT; -.
DR PDBsum; 6UYU; -.
DR PDBsum; 6UYV; -.
DR PDBsum; 6UYX; -.
DR PDBsum; 6UYY; -.
DR PDBsum; 6UYZ; -.
DR PDBsum; 6V7P; -.
DR PDBsum; 6V7Q; -.
DR PDBsum; 6V7R; -.
DR PDBsum; 6V7S; -.
DR PDBsum; 6WW3; -.
DR PDBsum; 6XOG; -.
DR PDBsum; 6XOH; -.
DR PDBsum; 6XOI; -.
DR AlphaFoldDB; P63165; -.
DR BMRB; P63165; -.
DR SMR; P63165; -.
DR BioGRID; 113188; 254.
DR CORUM; P63165; -.
DR DIP; DIP-29080N; -.
DR IntAct; P63165; 190.
DR MINT; P63165; -.
DR STRING; 9606.ENSP00000376077; -.
DR BindingDB; P63165; -.
DR ChEMBL; CHEMBL2146296; -.
DR MoonDB; P63165; Predicted.
DR iPTMnet; P63165; -.
DR MetOSite; P63165; -.
DR PhosphoSitePlus; P63165; -.
DR BioMuta; SUMO1; -.
DR DMDM; 52783799; -.
DR EPD; P63165; -.
DR jPOST; P63165; -.
DR MassIVE; P63165; -.
DR MaxQB; P63165; -.
DR PaxDb; P63165; -.
DR PeptideAtlas; P63165; -.
DR PRIDE; P63165; -.
DR ProteomicsDB; 2128; -.
DR ProteomicsDB; 57500; -. [P63165-1]
DR TopDownProteomics; P63165-1; -. [P63165-1]
DR Antibodypedia; 3793; 1185 antibodies from 45 providers.
DR DNASU; 7341; -.
DR Ensembl; ENST00000392244.7; ENSP00000376075.3; ENSG00000116030.17. [P63165-2]
DR Ensembl; ENST00000392245.5; ENSP00000376076.1; ENSG00000116030.17. [P63165-1]
DR Ensembl; ENST00000392246.7; ENSP00000376077.2; ENSG00000116030.17. [P63165-1]
DR GeneID; 7341; -.
DR KEGG; hsa:7341; -.
DR MANE-Select; ENST00000392246.7; ENSP00000376077.2; NM_003352.8; NP_003343.1.
DR UCSC; uc002uyz.2; human. [P63165-1]
DR CTD; 7341; -.
DR DisGeNET; 7341; -.
DR GeneCards; SUMO1; -.
DR HGNC; HGNC:12502; SUMO1.
DR HPA; ENSG00000116030; Low tissue specificity.
DR MalaCards; SUMO1; -.
DR MIM; 601912; gene.
DR MIM; 613705; phenotype.
DR neXtProt; NX_P63165; -.
DR OpenTargets; ENSG00000116030; -.
DR Orphanet; 99798; Oligodontia.
DR PharmGKB; PA37149; -.
DR VEuPathDB; HostDB:ENSG00000116030; -.
DR eggNOG; KOG1769; Eukaryota.
DR GeneTree; ENSGT00940000154319; -.
DR HOGENOM; CLU_148322_0_0_1; -.
DR InParanoid; P63165; -.
DR OMA; TIECHIE; -.
DR PhylomeDB; P63165; -.
DR TreeFam; TF315116; -.
DR BioCyc; MetaCyc:ENSG00000116030-MON; -.
DR PathwayCommons; P63165; -.
DR Reactome; R-HSA-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-HSA-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-HSA-3065679; SUMO is proteolytically processed.
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-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-877312; Regulation of IFNG signaling.
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; P63165; -.
DR SIGNOR; P63165; -.
DR BioGRID-ORCS; 7341; 46 hits in 1041 CRISPR screens.
DR ChiTaRS; SUMO1; human.
DR EvolutionaryTrace; P63165; -.
DR GeneWiki; Small_ubiquitin-related_modifier_1; -.
DR GenomeRNAi; 7341; -.
DR Pharos; P63165; Tbio.
DR PRO; PR:P63165; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P63165; protein.
DR Bgee; ENSG00000116030; Expressed in ganglionic eminence and 178 other tissues.
DR ExpressionAtlas; P63165; baseline and differential.
DR Genevisible; P63165; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0097165; C:nuclear stress granule; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0044388; F:small protein activating enzyme binding; IPI:CAFA.
DR GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0045759; P:negative regulation of action potential; IDA:UniProtKB.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:CAFA.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:GO_Central.
DR GO; GO:0030578; P:PML body organization; IEA:Ensembl.
DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0090204; P:protein localization to nuclear pore; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl.
DR GO; GO:0032880; P:regulation of protein localization; TAS:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR CDD; cd16114; Ubl_SUMO1; 1.
DR DisProt; DP02294; -.
DR IDEAL; IID00378; -.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR046332; SUMO1_Ubl.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Chromosomal rearrangement; Cytoplasm; Host-virus interaction;
KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20388717,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..97
FT /note="Small ubiquitin-related modifier 1"
FT /id="PRO_0000035939"
FT PROPEP 98..101
FT /evidence="ECO:0000269|PubMed:15487983"
FT /id="PRO_0000035940"
FT DOMAIN 20..97
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 16..25
FT /note="(Microbial infection) Interaction with Tula
FT hantavirus"
FT /evidence="ECO:0000269|PubMed:12606074"
FT REGION 37..40
FT /note="(Microbial infection) Interaction with Tula
FT hantavirus"
FT /evidence="ECO:0000269|PubMed:12606074"
FT SITE 36
FT /note="Interaction with PIAS2"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:20388717,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18707152,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 23
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT CROSSLNK 37
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 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000269|PubMed:27068747"
FT VAR_SEQ 4..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046756"
FT MUTAGEN 36
FT /note="F->A: Abolishes binding to PIAS2."
FT /evidence="ECO:0000269|PubMed:16204249"
FT MUTAGEN 97
FT /note="G->A: Abolishes sumoylation of ZBED1."
FT /evidence="ECO:0000269|PubMed:27068747"
FT CONFLICT 75
FT /note="H -> N (in Ref. 13; AAH66306)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:6WW3"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1A5R"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2KQS"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:6UYR"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1Z5S"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:6UYR"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2PE6"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:6XOG"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:6UYR"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6UYR"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6UYR"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5B7A"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:6UYR"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6UYR"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2N1A"
SQ SEQUENCE 101 AA; 11557 MW; 89BE97D2D054FB33 CRC64;
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V
