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Small ubiquitin-related modifier 1 (SUMO-1) (GAP-modifying protein 1) (GMP1) (SMT3 homolog 3) (Sentrin) (Ubiquitin-homology domain protein PIC1) (Ubiquitin-like protein SMT3C) (Smt3C) (Ubiquitin-like protein UBL1)

 SUMO1_HUMAN             Reviewed;         101 AA.
P63165; A8MUS8; B2R4I5; P55856; Q6FGG0; Q6NZ62; Q93068;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
27-SEP-2004, sequence version 1.
25-OCT-2017, entry version 162.
RecName: Full=Small ubiquitin-related modifier 1;
Short=SUMO-1;
AltName: Full=GAP-modifying protein 1;
Short=GMP1;
AltName: Full=SMT3 homolog 3;
AltName: Full=Sentrin;
AltName: Full=Ubiquitin-homology domain protein PIC1;
AltName: Full=Ubiquitin-like protein SMT3C;
Short=Smt3C;
AltName: Full=Ubiquitin-like protein UBL1;
Flags: Precursor;
Name=SUMO1; Synonyms=SMT3C, SMT3H3, UBL1; ORFNames=OK/SW-cl.43;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9119407; DOI=10.1006/geno.1996.4556;
Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F.,
Brahe C.;
"SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to
chromosome 21qter and defines a novel gene family.";
Genomics 40:362-367(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain, and Placenta;
PubMed=8806687;
Boddy M.N., Howe K., Etkin L.D., Solomon E., Freemont P.S.;
"PIC 1, a novel ubiquitin-like protein which interacts with the PML
component of a multiprotein complex that is disrupted in acute
promyelocytic leukaemia.";
Oncogene 13:971-982(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8812453; DOI=10.1006/geno.1996.0462;
Shen Z., Pardington-Purtymun P.E., Comeaux J.C., Moyzis R.K.,
Chen D.J.;
"UBL1, a human ubiquitin-like protein associating with human
RAD51/RAD52 proteins.";
Genomics 36:271-279(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=9019411; DOI=10.1016/S0092-8674(00)81862-0;
Mahajan R., Delphin C., Guan T., Gerace L., Melchior F.;
"A small ubiquitin-related polypeptide involved in targeting RanGAP1
to nuclear pore complex protein RanBP2.";
Cell 88:97-107(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8978815; DOI=10.1083/jcb.135.6.1457;
Matunis M.J., Coutavas E., Blobel G.;
"A novel ubiquitin-like modification modulates the partitioning of the
Ran-GTPase-activating protein RanGAP1 between the cytosol and the
nuclear pore complex.";
J. Cell Biol. 135:1457-1470(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8906799;
Okura T., Gong L., Kamitani T., Wada T., Okura I., Wei C.F.,
Chang H.M., Yeh E.T.H.;
"Protection against Fas/APO-1- and tumor necrosis factor-mediated cell
death by a novel protein, sentrin.";
J. Immunol. 157:4277-4281(1996).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
PubMed=9162015; DOI=10.1074/jbc.272.22.14001;
Kamitani T., Nguyen H.P., Yeh E.T.H.;
"Preferential modification of nuclear proteins by a novel ubiquitin-
like molecule.";
J. Biol. Chem. 272:14001-14004(1997).
[15]
SUBCELLULAR LOCATION.
PubMed=10574707;
Everett R.D., Lomonte P., Sternsdorf T., van Driel R., Orr A.;
"Cell cycle regulation of PML modification and ND10 composition.";
J. Cell Sci. 112:4581-4588(1999).
[16]
INTERACTION WITH HIPK3; CHD3; PIAS1; EXOSC9 AND TDG.
PubMed=10961991; DOI=10.1074/jbc.M004293200;
Minty A., Dumont X., Kaghad M., Caput D.;
"Covalent modification of p73alpha by SUMO-1. Two-hybrid screening
with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1
interaction motif.";
J. Biol. Chem. 275:36316-36323(2000).
[17]
SUBCELLULAR LOCATION.
PubMed=12383504; DOI=10.1016/S0378-1119(02)00843-0;
Su H.-L., Li S.S.-L.;
"Molecular features of human ubiquitin-like SUMO genes and their
encoded proteins.";
Gene 296:65-73(2002).
[18]
INTERACTION WITH UBE2I.
PubMed=12924945; DOI=10.1021/bi0345283;
Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J.,
Rodriguez M.S., Hay R.T., Chen Y.;
"Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and
conjugation.";
Biochemistry 42:9959-9969(2003).
[19]
INTERACTION WITH HIPK2.
PubMed=12565818; DOI=10.1016/S0014-4827(02)00025-3;
Engelhardt O.G., Boutell C., Orr A., Ullrich E., Haller O.,
Everett R.D.;
"The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through
both its kinase domain and a SUMO-1 interaction motif and alters the
posttranslational modification of PML.";
Exp. Cell Res. 283:36-50(2003).
[20]
CLEAVAGE.
PubMed=15487983; DOI=10.1042/BJ20041210;
Xu Z., Au S.W.N.;
"Mapping residues of SUMO precursors essential in differential
maturation by SUMO-specific protease, SENP1.";
Biochem. J. 386:325-330(2005).
[21]
INTERACTION WITH RANBP2.
PubMed=15608651; DOI=10.1038/nsmb878;
Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.;
"Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a
mechanism for SUMO paralog selection.";
Nat. Struct. Mol. Biol. 12:67-74(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[23]
INTERACTION WITH PRKN.
PubMed=16955485; DOI=10.1002/jnr.21041;
Um J.W., Chung K.C.;
"Functional modulation of parkin through physical interaction with
SUMO-1.";
J. Neurosci. Res. 84:1543-1554(2006).
[24]
CHROMOSOMAL TRANSLOCATION, AND INVOLVEMENT IN OFC10.
PubMed=16990542; DOI=10.1126/science.1128406;
Alkuraya F.S., Saadi I., Lund J.J., Turbe-Doan A., Morton C.C.,
Maas R.L.;
"SUMO1 haploinsufficiency leads to cleft lip and palate.";
Science 313:1751-1751(2006).
[25]
INTERACTION WITH UBE2I AND RWDD3.
PubMed=17956732; DOI=10.1016/j.cell.2007.07.044;
Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M.,
Silberstein S., Stalla G.K., Holsboer F., Arzt E.;
"RSUME, a small RWD-containing protein, enhances SUMO conjugation and
stabilizes HIF-1alpha during hypoxia.";
Cell 131:309-323(2007).
[26]
PHOSPHORYLATION AT SER-2.
PubMed=18707152; DOI=10.1021/pr800368m;
Matic I., Macek B., Hilger M., Walther T.C., Mann M.;
"Phosphorylation of SUMO-1 occurs in vivo and is conserved through
evolution.";
J. Proteome Res. 7:4050-4057(2008).
[27]
FUNCTION IN SUMOYLATION OF USP25, AND INTERACTION WITH USP25.
PubMed=18538659; DOI=10.1016/j.molcel.2008.03.021;
Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.;
"Mechanism and consequences for paralog-specific sumoylation of
ubiquitin-specific protease 25.";
Mol. Cell 30:610-619(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[29]
FUNCTION.
PubMed=18408734; DOI=10.1038/ncb1716;
Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N.,
Jaffray E.G., Palvimo J.J., Hay R.T.;
"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for
arsenic-induced PML degradation.";
Nat. Cell Biol. 10:538-546(2008).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[31]
FUNCTION IN KCNB1 SUMOYLATION, INTERACTION WITH KCNB1, AND SUBCELLULAR
LOCATION.
PubMed=19223394; DOI=10.1242/jcs.036632;
Dai X.Q., Kolic J., Marchi P., Sipione S., Macdonald P.E.;
"SUMOylation regulates Kv2.1 and modulates pancreatic beta-cell
excitability.";
J. Cell Sci. 122:775-779(2009).
[32]
SUMOYLATION AT LYS-7 AND LYS-25, AND ACETYLATION AT SER-2.
TISSUE=Cervix carcinoma;
PubMed=20388717; DOI=10.1074/jbc.M110.106955;
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
Eriksson J.E., Sistonen L.;
"In vivo identification of sumoylation sites by a signature tag and
cysteine-targeted affinity purification.";
J. Biol. Chem. 285:19324-19329(2010).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2 AND SER-9, CLEAVAGE OF INITIATOR METHIONINE
[LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[35]
FUNCTION, AND INTERACTION WITH MTA1.
PubMed=21965678; DOI=10.1074/jbc.M111.267237;
Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
"SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor
antigen 1 (MTA1) synergistically regulate its transcriptional
repressor function.";
J. Biol. Chem. 286:43793-43808(2011).
[36]
INTERACTION WITH BHLHE40/DEC1.
PubMed=21829689; DOI=10.1371/journal.pone.0023046;
Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X.,
Chang A.K., Wu H.;
"SUMOylation of DEC1 protein regulates its transcriptional activity
and enhances its stability.";
PLoS ONE 6:E23046-E23046(2011).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[38]
SUBCELLULAR LOCATION.
PubMed=22406621; DOI=10.1158/0008-5472.CAN-11-3159;
Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A.,
Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J.,
Scaglioni P.P.;
"The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its
oncogenic counterpart PML-RARA.";
Cancer Res. 72:2275-2284(2012).
[39]
IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, AND INTERACTION WITH
SIMC1; CASP8AP2; RNF111 AND SOBP.
PubMed=23086935; DOI=10.1074/jbc.M112.410985;
Sun H., Hunter T.;
"PolySUMO-binding proteins identified through a string search.";
J. Biol. Chem. 287:42071-42083(2012).
[40]
INTERACTION WITH EPSTEIN-BARR VIRUS BGLF4.
PubMed=22398289; DOI=10.1128/JVI.00314-12;
Li R., Wang L., Liao G., Guzzo C.M., Matunis M.J., Zhu H.,
Hayward S.D.;
"SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is
crucial for BGLF4 function.";
J. Virol. 86:5412-5421(2012).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-32, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[43]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-16 AND LYS-17, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[44]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24651376; DOI=10.1371/journal.pone.0092746;
Sun X., Li J., Dong F.N., Dong J.T.;
"Characterization of nuclear localization and SUMOylation of the ATBF1
transcription factor in epithelial cells.";
PLoS ONE 9:E92746-E92746(2014).
[45]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-17, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[46]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-37, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[47]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-16; LYS-17; LYS-23;
LYS-37; LYS-39; LYS-45 AND LYS-46, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[48]
STRUCTURE BY NMR.
PubMed=9654451; DOI=10.1006/jmbi.1998.1839;
Bayer P., Arndt A., Metzger S., Mahajan R., Melchior F., Jaenicke R.,
Becker J.;
"Structure determination of the small ubiquitin-related modifier SUMO-
1.";
J. Mol. Biol. 280:275-286(1998).
[49]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-97 IN COMPLEX WITH SENP2,
AND CLEAVAGE.
PubMed=15296745; DOI=10.1016/j.str.2004.05.023;
Reverter D., Lima C.D.;
"A basis for SUMO protease specificity provided by analysis of human
Senp2 and a Senp2-SUMO complex.";
Structure 12:1519-1531(2004).
[50]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-97 IN COMPLEX WITH SAE1;
SAE2 AND ATP.
PubMed=15660128; DOI=10.1038/sj.emboj.7600552;
Lois L.M., Lima C.D.;
"Structures of the SUMO E1 provide mechanistic insights into SUMO
activation and E2 recruitment to E1.";
EMBO J. 24:439-451(2005).
[51]
STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH PIAS2, AND MUTAGENESIS OF
PHE-36.
PubMed=16204249; DOI=10.1074/jbc.M507059200;
Song J., Zhang Z., Hu W., Chen Y.;
"Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding
motif: a reversal of the bound orientation.";
J. Biol. Chem. 280:40122-40129(2005).
[52]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 18-97 IN COMPLEX WITH UBE2I;
RANGAP1 AND RANBP2.
PubMed=15931224; DOI=10.1038/nature03588;
Reverter D., Lima C.D.;
"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-
Nup358 complex.";
Nature 435:687-692(2005).
[53]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-97 CONJUGATED TO TDG.
PubMed=15959518; DOI=10.1038/nature03634;
Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K.,
Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.;
"Crystal structure of thymine DNA glycosylase conjugated to SUMO-1.";
Nature 435:979-982(2005).
[54]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-97 CONJUGATED TO HIP2.
PubMed=15723079; DOI=10.1038/nsmb903;
Pichler A., Knipscheer P., Oberhofer E., van Dijk W.J., Koerner R.,
Olsen J.V., Jentsch S., Melchior F., Sixma T.K.;
"SUMO modification of the ubiquitin-conjugating enzyme E2-25K.";
Nat. Struct. Mol. Biol. 12:264-269(2005).
[55]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SENP1.
PubMed=16712526; DOI=10.1042/BJ20060526;
Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N.;
"Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the
hydrolytic mechanism of SUMO-specific protease.";
Biochem. J. 398:345-352(2006).
[56]
X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) IN COMPLEX WITH RANGAP1 AND
SENP1.
PubMed=17099698; DOI=10.1038/nsmb1172;
Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.;
"SUMO protease SENP1 induces isomerization of the scissile peptide
bond.";
Nat. Struct. Mol. Biol. 13:1069-1077(2006).
-!- FUNCTION: Ubiquitin-like protein that can be covalently attached
to proteins as a monomer or a lysine-linked polymer. Covalent
attachment via an isopeptide bond to its substrates requires prior
activation by the E1 complex SAE1-SAE2 and linkage to the E2
enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4,
RANBP2 or CBX4. This post-translational modification on lysine
residues of proteins plays a crucial role in a number of cellular
processes such as nuclear transport, DNA replication and repair,
mitosis and signal transduction. Involved for instance in
targeting RANGAP1 to the nuclear pore complex protein RANBP2.
Covalently attached to the voltage-gated potassium channel KCNB1;
this modulates the gating characteristics of KCNB1
(PubMed:19223394). Polymeric SUMO1 chains are also susceptible to
polyubiquitination which functions as a signal for proteasomal
degradation of modified proteins. May also regulate a network of
genes involved in palate development. Covalently attached to ZFHX3
(PubMed:24651376). {ECO:0000269|PubMed:18408734,
ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:19223394,
ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24651376,
ECO:0000269|PubMed:9019411, ECO:0000269|PubMed:9162015}.
-!- SUBUNIT: Covalently attached to KCNB1; UBE2I increases cross-
linking with KCNB1 and PIAS1 decreases cross-links with KCNB1
(PubMed:19223394). Interacts with SAE2, RANBP2, PIAS1 and PIAS2.
Interacts with PRKN. Covalently attached to a number of proteins
such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2,
JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3,
CHD3, EXOSC9, RAD51 and RAD52. Interacts with USP25 (via ts SIM
domain); the interaction weakly sumoylates USP25. Interacts with
SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with
BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and
this interaction is enhanced in the presence of RWDD3. Interacts
with MTA1. Interacts with Epstein-barr virus BGLF4.
{ECO:0000269|PubMed:10961991, ECO:0000269|PubMed:12565818,
ECO:0000269|PubMed:12924945, ECO:0000269|PubMed:15296745,
ECO:0000269|PubMed:15608651, ECO:0000269|PubMed:15660128,
ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:16204249,
ECO:0000269|PubMed:16712526, ECO:0000269|PubMed:16955485,
ECO:0000269|PubMed:17099698, ECO:0000269|PubMed:17956732,
ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:19223394,
ECO:0000269|PubMed:21829689, ECO:0000269|PubMed:21965678,
ECO:0000269|PubMed:22398289, ECO:0000269|PubMed:23086935}.
-!- INTERACTION:
G2XKQ0:-; NbExp=3; IntAct=EBI-80140, EBI-10175576;
Q59GP6:-; NbExp=3; IntAct=EBI-80140, EBI-10243413;
P10275:AR; NbExp=7; IntAct=EBI-80140, EBI-608057;
Q5BIX2:ARKL1; NbExp=5; IntAct=EBI-80140, EBI-10243491;
P15336:ATF2; NbExp=5; IntAct=EBI-80140, EBI-1170906;
P38398:BRCA1; NbExp=3; IntAct=EBI-80140, EBI-349905;
Q9H257:CARD9; NbExp=3; IntAct=EBI-80140, EBI-751319;
Q9UER7:DAXX; NbExp=7; IntAct=EBI-80140, EBI-77321;
Q05D60:DEUP1; NbExp=3; IntAct=EBI-80140, EBI-748597;
Q9UBC3:DNMT3B; NbExp=4; IntAct=EBI-80140, EBI-80125;
Q86UW9:DTX2; NbExp=3; IntAct=EBI-80140, EBI-740376;
Q8WWZ3:EDARADD; NbExp=5; IntAct=EBI-80140, EBI-2949647;
P06730:EIF4E; NbExp=5; IntAct=EBI-80140, EBI-73440;
P19419:ELK1; NbExp=5; IntAct=EBI-80140, EBI-726632;
P19419-1:ELK1; NbExp=2; IntAct=EBI-80140, EBI-15799641;
Q9BPY3:FAM118B; NbExp=3; IntAct=EBI-80140, EBI-726822;
Q8TES7-6:FBF1; NbExp=3; IntAct=EBI-80140, EBI-10244131;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-80140, EBI-10172181;
O95073:FSBP; NbExp=3; IntAct=EBI-80140, EBI-1059030;
O14964:HGS; NbExp=3; IntAct=EBI-80140, EBI-740220;
Q16665:HIF1A; NbExp=4; IntAct=EBI-80140, EBI-447269;
P07910:HNRNPC; NbExp=5; IntAct=EBI-80140, EBI-357966;
Q00613:HSF1; NbExp=2; IntAct=EBI-80140, EBI-719620;
Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-80140, EBI-81279;
P10914:IRF1; NbExp=2; IntAct=EBI-80140, EBI-1055781;
O00180:KCNK1; NbExp=3; IntAct=EBI-80140, EBI-3914675;
Q8NDC0:MAPK1IP1L; NbExp=3; IntAct=EBI-80140, EBI-741424;
Q9UIS9:MBD1; NbExp=3; IntAct=EBI-80140, EBI-867196;
Q02078-1:MEF2A; NbExp=3; IntAct=EBI-80140, EBI-15799584;
P10242:MYB; NbExp=3; IntAct=EBI-80140, EBI-298355;
Q00653:NFKB2; NbExp=2; IntAct=EBI-80140, EBI-307326;
P06748-1:NPM1; NbExp=3; IntAct=EBI-80140, EBI-354150;
P09874:PARP1; NbExp=2; IntAct=EBI-80140, EBI-355676;
O75928:PIAS2; NbExp=6; IntAct=EBI-80140, EBI-348555;
P29590:PML; NbExp=6; IntAct=EBI-80140, EBI-295890;
P29590-9:PML; NbExp=2; IntAct=EBI-80140, EBI-6861318;
O75626-2:PRDM1; NbExp=2; IntAct=EBI-80140, EBI-7839538;
Q60636:Prdm1 (xeno); NbExp=3; IntAct=EBI-80140, EBI-7000804;
O75475:PSIP1; NbExp=4; IntAct=EBI-80140, EBI-1801773;
Q9Y4B4:RAD54L2; NbExp=5; IntAct=EBI-80140, EBI-948156;
P46060:RANGAP1; NbExp=13; IntAct=EBI-80140, EBI-396091;
P10276:RARA; NbExp=5; IntAct=EBI-80140, EBI-413374;
Q9BQY4:RHOXF2; NbExp=3; IntAct=EBI-80140, EBI-372094;
Q9Y3V2:RWDD3; NbExp=2; IntAct=EBI-80140, EBI-1549885;
O43290:SART1; NbExp=2; IntAct=EBI-80140, EBI-607761;
Q01826:SATB1; NbExp=2; IntAct=EBI-80140, EBI-743747;
Q9P0U3:SENP1; NbExp=8; IntAct=EBI-80140, EBI-2822935;
Q9HC62:SENP2; NbExp=2; IntAct=EBI-80140, EBI-714881;
P56693:SOX10; NbExp=2; IntAct=EBI-80140, EBI-1167533;
P48431:SOX2; NbExp=3; IntAct=EBI-80140, EBI-6124081;
P23497:SP100; NbExp=6; IntAct=EBI-80140, EBI-751145;
Q92844:TANK; NbExp=8; IntAct=EBI-80140, EBI-356349;
Q12800:TFCP2; NbExp=3; IntAct=EBI-80140, EBI-717422;
P04637:TP53; NbExp=3; IntAct=EBI-80140, EBI-366083;
Q12888-1:TP53BP1; NbExp=2; IntAct=EBI-80140, EBI-8022649;
Q9BUZ4:TRAF4; NbExp=3; IntAct=EBI-80140, EBI-3650647;
Q9UBT2:UBA2; NbExp=7; IntAct=EBI-80140, EBI-718569;
P63279:UBE2I; NbExp=9; IntAct=EBI-80140, EBI-80168;
Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-80140, EBI-10180829;
Q5W0Q7:USPL1; NbExp=5; IntAct=EBI-80140, EBI-2513899;
Q9HCK0:ZBTB26; NbExp=7; IntAct=EBI-80140, EBI-3918996;
Q15916:ZBTB6; NbExp=3; IntAct=EBI-80140, EBI-7227791;
Q6PEW1:ZCCHC12; NbExp=6; IntAct=EBI-80140, EBI-748373;
Q96MM3:ZFP42; NbExp=4; IntAct=EBI-80140, EBI-12151755;
Q9UJ78:ZMYM5; NbExp=3; IntAct=EBI-80140, EBI-7228860;
-!- SUBCELLULAR LOCATION: Nucleus membrane. Nucleus speckle.
Cytoplasm. Nucleus, PML body. Cell membrane
{ECO:0000269|PubMed:19223394}. Nucleus
{ECO:0000269|PubMed:24651376}. Note=Recruited by BCL11A into the
nuclear body. In the presence of ZFHX3, sequesterd to nuclear body
(NB)-like dots in the nucleus some of which overlap or closely
associate with PML body. {ECO:0000250|UniProtKB:P63166,
ECO:0000269|PubMed:24651376}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P63165-1; Sequence=Displayed;
Name=2;
IsoId=P63165-2; Sequence=VSP_046756;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for
function.
-!- PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4.
-!- DISEASE: Non-syndromic orofacial cleft 10 (OFC10) [MIM:613705]: A
birth defect consisting of cleft lips with or without cleft
palate. Cleft lips are associated with cleft palate in two-third
of cases. A cleft lip can occur on one or both sides and range in
severity from a simple notch in the upper lip to a complete
opening in the lip extending into the floor of the nostril and
involving the upper gum. {ECO:0000269|PubMed:16990542}. Note=The
disease is caused by mutations affecting the gene represented in
this entry. A chromosomal aberration involving SUMO1 is the cause
of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint
occurred in the SUMO1 gene and resulted in haploinsufficiency
confirmed by protein assays.
-!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=SUMO protein entry;
URL="https://en.wikipedia.org/wiki/SUMO_protein";
-----------------------------------------------------------------------
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EMBL; X99586; CAA67898.1; -; mRNA.
EMBL; U61397; AAB40388.1; -; mRNA.
EMBL; U38784; AAC50733.1; -; mRNA.
EMBL; U67122; AAC50996.1; -; mRNA.
EMBL; U72722; AAB40390.1; -; mRNA.
EMBL; U83117; AAB39999.1; -; mRNA.
EMBL; AB062294; BAB93477.1; -; mRNA.
EMBL; BT006632; AAP35278.1; -; mRNA.
EMBL; CR542147; CAG46944.1; -; mRNA.
EMBL; CR542156; CAG46953.1; -; mRNA.
EMBL; AK311840; BAG34782.1; -; mRNA.
EMBL; AC079354; AAY24035.1; -; Genomic_DNA.
EMBL; CH471063; EAW70304.1; -; Genomic_DNA.
EMBL; CH471063; EAW70307.1; -; Genomic_DNA.
EMBL; BC006462; AAH06462.1; -; mRNA.
EMBL; BC053528; AAH53528.1; -; mRNA.
EMBL; BC066306; AAH66306.1; -; mRNA.
CCDS; CCDS2352.1; -. [P63165-1]
CCDS; CCDS46493.1; -. [P63165-2]
RefSeq; NP_001005781.1; NM_001005781.1. [P63165-1]
RefSeq; NP_001005782.1; NM_001005782.1. [P63165-2]
RefSeq; NP_003343.1; NM_003352.4. [P63165-1]
UniGene; Hs.81424; -.
PDB; 1A5R; NMR; -; A=1-101.
PDB; 1TGZ; X-ray; 2.80 A; B=18-97.
PDB; 1WYW; X-ray; 2.10 A; B=1-97.
PDB; 1Y8R; X-ray; 2.75 A; C/F=1-97.
PDB; 1Z5S; X-ray; 3.01 A; B=18-97.
PDB; 2ASQ; NMR; -; A=1-97.
PDB; 2BF8; X-ray; 2.30 A; B=21-97.
PDB; 2G4D; X-ray; 2.80 A; B/D=20-97.
PDB; 2IO2; X-ray; 2.90 A; B=18-97.
PDB; 2IY0; X-ray; 2.77 A; B=20-101.
PDB; 2IY1; X-ray; 2.46 A; B/D=20-101.
PDB; 2KQS; NMR; -; A=1-97.
PDB; 2LAS; NMR; -; A=1-101.
PDB; 2MW5; NMR; -; A=1-97.
PDB; 2N1A; NMR; -; A=1-101.
PDB; 2N1V; NMR; -; A=1-97.
PDB; 2PE6; X-ray; 2.40 A; B=1-97.
PDB; 2UYZ; X-ray; 1.40 A; B=20-97.
PDB; 2VRR; X-ray; 2.22 A; B=20-97.
PDB; 3KYC; X-ray; 2.45 A; D=1-97.
PDB; 3KYD; X-ray; 2.61 A; D=1-94.
PDB; 3RZW; X-ray; 2.15 A; C/D=1-97.
PDB; 3UIP; X-ray; 2.29 A; B=18-97.
PDB; 4WJN; X-ray; 1.50 A; A=17-97.
PDB; 4WJO; X-ray; 1.46 A; A=17-97.
PDB; 4WJP; X-ray; 1.70 A; A/C=17-97.
PDB; 4WJQ; X-ray; 1.35 A; A/C=17-97.
PDB; 5AEK; X-ray; 3.00 A; B/D/F/H/J/L/N/P/R/T/V/X=20-97.
PDB; 5B7A; NMR; -; A=1-97.
PDB; 5ELJ; X-ray; 1.98 A; B=18-97.
PDB; 5GHD; NMR; -; A=1-97.
PDBsum; 1A5R; -.
PDBsum; 1TGZ; -.
PDBsum; 1WYW; -.
PDBsum; 1Y8R; -.
PDBsum; 1Z5S; -.
PDBsum; 2ASQ; -.
PDBsum; 2BF8; -.
PDBsum; 2G4D; -.
PDBsum; 2IO2; -.
PDBsum; 2IY0; -.
PDBsum; 2IY1; -.
PDBsum; 2KQS; -.
PDBsum; 2LAS; -.
PDBsum; 2MW5; -.
PDBsum; 2N1A; -.
PDBsum; 2N1V; -.
PDBsum; 2PE6; -.
PDBsum; 2UYZ; -.
PDBsum; 2VRR; -.
PDBsum; 3KYC; -.
PDBsum; 3KYD; -.
PDBsum; 3RZW; -.
PDBsum; 3UIP; -.
PDBsum; 4WJN; -.
PDBsum; 4WJO; -.
PDBsum; 4WJP; -.
PDBsum; 4WJQ; -.
PDBsum; 5AEK; -.
PDBsum; 5B7A; -.
PDBsum; 5ELJ; -.
PDBsum; 5GHD; -.
ProteinModelPortal; P63165; -.
SMR; P63165; -.
BioGrid; 113188; 168.
CORUM; P63165; -.
DIP; DIP-29080N; -.
IntAct; P63165; 156.
MINT; MINT-137859; -.
STRING; 9606.ENSP00000376076; -.
ChEMBL; CHEMBL2146296; -.
iPTMnet; P63165; -.
PhosphoSitePlus; P63165; -.
BioMuta; SUMO1; -.
DMDM; 52783799; -.
EPD; P63165; -.
MaxQB; P63165; -.
PaxDb; P63165; -.
PeptideAtlas; P63165; -.
PRIDE; P63165; -.
TopDownProteomics; P63165-1; -. [P63165-1]
DNASU; 7341; -.
Ensembl; ENST00000392244; ENSP00000376075; ENSG00000116030. [P63165-2]
Ensembl; ENST00000392245; ENSP00000376076; ENSG00000116030. [P63165-1]
Ensembl; ENST00000392246; ENSP00000376077; ENSG00000116030. [P63165-1]
GeneID; 7341; -.
KEGG; hsa:7341; -.
UCSC; uc002uyz.2; human. [P63165-1]
CTD; 7341; -.
DisGeNET; 7341; -.
EuPathDB; HostDB:ENSG00000116030.16; -.
GeneCards; SUMO1; -.
HGNC; HGNC:12502; SUMO1.
HPA; CAB004269; -.
HPA; HPA056956; -.
MalaCards; SUMO1; -.
MIM; 601912; gene.
MIM; 613705; phenotype.
neXtProt; NX_P63165; -.
OpenTargets; ENSG00000116030; -.
Orphanet; 1991; Cleft lip with or without cleft palate.
PharmGKB; PA37149; -.
eggNOG; KOG1769; Eukaryota.
eggNOG; COG5227; LUCA.
GeneTree; ENSGT00390000018808; -.
HOGENOM; HOG000207495; -.
HOVERGEN; HBG053025; -.
InParanoid; P63165; -.
KO; K12160; -.
PhylomeDB; P63165; -.
TreeFam; TF315116; -.
BioCyc; MetaCyc:ENSG00000116030-MONOMER; -.
Reactome; R-HSA-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
Reactome; R-HSA-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
Reactome; R-HSA-3065679; SUMO is proteolytically processed.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3232118; SUMOylation of transcription factors.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-877312; Regulation of IFNG signaling.
Reactome; R-HSA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
SignaLink; P63165; -.
SIGNOR; P63165; -.
EvolutionaryTrace; P63165; -.
GeneWiki; Small_ubiquitin-related_modifier_1; -.
GenomeRNAi; 7341; -.
PMAP-CutDB; P63165; -.
PRO; PR:P63165; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000116030; -.
CleanEx; HS_SUMO1; -.
ExpressionAtlas; P63165; baseline and differential.
Genevisible; P63165; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0097165; C:nuclear stress granule; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0031510; C:SUMO activating enzyme complex; IDA:CAFA.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0001741; C:XY body; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:CAFA.
GO; GO:0035259; F:glucocorticoid receptor binding; IPI:CAFA.
GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
GO; GO:0030674; F:protein binding, bridging; IMP:CAFA.
GO; GO:0008022; F:protein C-terminus binding; IDA:CAFA.
GO; GO:0031386; F:protein tag; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0044388; F:small protein activating enzyme binding; IPI:CAFA.
GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
GO; GO:0001222; F:transcription corepressor binding; IPI:CAFA.
GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0071276; P:cellular response to cadmium ion; IDA:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0045759; P:negative regulation of action potential; IDA:UniProtKB.
GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:CAFA.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0060021; P:palate development; ISS:UniProtKB.
GO; GO:0030578; P:PML body organization; IEA:Ensembl.
GO; GO:1901896; P:positive regulation of calcium-transporting ATPase activity; IEA:Ensembl.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
GO; GO:0090204; P:protein localization to nuclear pore; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0032880; P:regulation of protein localization; TAS:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd01763; Sumo; 1.
InterPro; IPR022617; Rad60/SUMO-like_dom.
InterPro; IPR033950; Sumo.
InterPro; IPR029071; Ubiquitin-rel_dom.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF11976; Rad60-SLD; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Host-virus interaction; Isopeptide bond; Membrane; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:20388717}.
CHAIN 2 97 Small ubiquitin-related modifier 1.
/FTId=PRO_0000035939.
PROPEP 98 101
/FTId=PRO_0000035940.
DOMAIN 20 97 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
SITE 36 36 Interaction with PIAS2.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:20388717}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18707152}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 17 17 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 23 23 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 25 25 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
CROSSLNK 37 37 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 39 39 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 45 45 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 46 46 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 97 97 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
proteins).
VAR_SEQ 4 28 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_046756.
MUTAGEN 36 36 F->A: Abolishes binding to PIAS2.
{ECO:0000269|PubMed:16204249}.
CONFLICT 75 75 H -> N (in Ref. 13; AAH66306).
{ECO:0000305}.
STRAND 2 6 {ECO:0000244|PDB:1A5R}.
TURN 9 11 {ECO:0000244|PDB:1A5R}.
TURN 16 18 {ECO:0000244|PDB:2KQS}.
STRAND 22 27 {ECO:0000244|PDB:4WJQ}.
STRAND 29 31 {ECO:0000244|PDB:1Z5S}.
STRAND 33 38 {ECO:0000244|PDB:4WJQ}.
STRAND 40 42 {ECO:0000244|PDB:2PE6}.
HELIX 45 55 {ECO:0000244|PDB:4WJQ}.
HELIX 59 61 {ECO:0000244|PDB:4WJQ}.
STRAND 62 66 {ECO:0000244|PDB:4WJQ}.
HELIX 77 80 {ECO:0000244|PDB:4WJQ}.
STRAND 87 92 {ECO:0000244|PDB:4WJQ}.
STRAND 96 99 {ECO:0000244|PDB:2N1A}.
SEQUENCE 101 AA; 11557 MW; 89BE97D2D054FB33 CRC64;
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V


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