ID SUMO1_HUMAN Reviewed; 101 AA.
AC P63165; B2R4I5; P55856; Q6FGG0; Q6NZ62; Q93068;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 01-MAY-2013, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
RX PubMed=8812453; DOI=10.1006/geno.1996.0462;
RA Shen Z., Pardington-Purtymun P.E., Comeaux J.C., Moyzis R.K.,
RA Chen D.J.;
RT "UBL1, a human ubiquitin-like protein associating with human
RT RAD51/RAD52 proteins.";
RL Genomics 36:271-279(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], 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
RT to nuclear pore complex protein RanBP2.";
RL Cell 88:97-107(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT Ran-GTPase-activating protein RanGAP1 between the cytosol and the
RT nuclear pore complex.";
RL J. Cell Biol. 135:1457-1470(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8906799;
RA Okura T., Gong L., Kamitani T., Wada T., Okura I., Wei C.F.,
RA Chang H.M., 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].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive 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].
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: 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-
RT like molecule.";
RL J. Biol. Chem. 272:14001-14004(1997).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=10574707;
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
RT with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1
RT interaction 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
RT encoded 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.,
RA Rodriguez M.S., 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.,
RA Everett R.D.;
RT "The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through
RT both 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 CLEAVAGE.
RX PubMed=15487983; DOI=10.1042/BJ20041210;
RA Xu Z., Au S.W.N.;
RT "Mapping residues of SUMO precursors essential in differential
RT maturation by SUMO-specific protease, SENP1.";
RL Biochem. J. 386:325-330(2005).
RN [21]
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
RT mechanism for SUMO paralog selection.";
RL Nat. Struct. Mol. Biol. 12:67-74(2005).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [23]
RP INTERACTION WITH PARK2.
RX PubMed=16955485; DOI=10.1002/jnr.21041;
RA Um J.W., Chung K.C.;
RT "Functional modulation of parkin through physical interaction with
RT SUMO-1.";
RL J. Neurosci. Res. 84:1543-1554(2006).
RN [24]
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.,
RA Maas R.L.;
RT "SUMO1 haploinsufficiency leads to cleft lip and palate.";
RL Science 313:1751-1751(2006).
RN [25]
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 [26]
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
RT ubiquitin-specific protease 25.";
RL Mol. Cell 30:610-619(2008).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [28]
RP FUNCTION.
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
RT arsenic-induced PML degradation.";
RL Nat. Cell Biol. 10:538-546(2008).
RN [29]
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 [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2 AND SER-9, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [31]
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.,
RA Buerckstuemmer T., 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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [33]
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 [34]
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 [35]
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-
RT 1.";
RL J. Mol. Biol. 280:275-286(1998).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-97 IN COMPLEX WITH SENP2,
RP AND 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
RT Senp2 and a Senp2-SUMO complex.";
RL Structure 12:1519-1531(2004).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-97 IN COMPLEX WITH SAE1;
RP SAE2 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 [38]
RP STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH PIAS2, AND MUTAGENESIS OF
RP 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
RT motif: a reversal of the bound orientation.";
RL J. Biol. Chem. 280:40122-40129(2005).
RN [39]
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-
RT Nup358 complex.";
RL Nature 435:687-692(2005).
RN [40]
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 [41]
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 [42]
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 [43]
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) IN COMPLEX WITH RANGAP1 AND
RP 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
RT bond.";
RL Nat. Struct. Mol. Biol. 13:1069-1077(2006).
CC -!- FUNCTION: Ubiquitin-like protein that can be covalently attached
CC to proteins as a monomer or a lysine-linked polymer. Covalent
CC attachment via an isopeptide bond to its substrates requires prior
CC activation by the E1 complex SAE1-SAE2 and linkage to the E2
CC enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4,
CC RANBP2 or CBX4. This post-translational modification on lysine
CC residues of proteins plays a crucial role in a number of cellular
CC processes such as nuclear transport, DNA replication and repair,
CC mitosis and signal transduction. Involved for instance in
CC targeting RANGAP1 to the nuclear pore complex protein RANBP2.
CC Polymeric SUMO1 chains are also susceptible to polyubiquitination
CC which functions as a signal for proteasomal degradation of
CC modified proteins. May also regulate a network of genes involved
CC in palate development.
CC -!- SUBUNIT: Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2.
CC Interacts with PARK2. Covalently attached to a number of proteins
CC such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2,
CC JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3,
CC CHD3, EXOSC9, RAD51 and RAD52. Interacts with USP25 (via ts SIM
CC domain); the interaction weakly sumoylates USP25. Interacts with
CC SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains).
CC -!- INTERACTION:
CC P10275:AR; NbExp=7; IntAct=EBI-80140, EBI-608057;
CC Q9UER7:DAXX; NbExp=5; IntAct=EBI-80140, EBI-77321;
CC Q9UBC3:DNMT3B; NbExp=4; IntAct=EBI-80140, EBI-80125;
CC Q16665:HIF1A; NbExp=2; IntAct=EBI-80140, EBI-447269;
CC P10242:MYB; NbExp=3; IntAct=EBI-80140, EBI-298355;
CC P29590:PML; NbExp=2; IntAct=EBI-80140, EBI-295890;
CC P46060:RANGAP1; NbExp=3; IntAct=EBI-80140, EBI-396091;
CC Q9Y3V2:RWDD3; NbExp=2; IntAct=EBI-80140, EBI-1549885;
CC O43290:SART1; NbExp=2; IntAct=EBI-80140, EBI-607761;
CC Q01826:SATB1; NbExp=2; IntAct=EBI-80140, EBI-743747;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane. Nucleus speckle.
CC Cytoplasm. Nucleus, PML body. Note=Recruited by BCL11A into the
CC nuclear body (By similarity).
CC -!- PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for
CC function.
CC -!- PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4.
CC -!- DISEASE: Non-syndromic orofacial cleft 10 (OFC10) [MIM:613705]: A
CC birth defect consisting of cleft lips with or without cleft
CC palate. Cleft lips are associated with cleft palate in two-third
CC of cases. A cleft lip can occur on one or both sides and range in
CC severity from a simple notch in the upper lip to a complete
CC opening in the lip extending into the floor of the nostril and
CC involving the upper gum. Note=The disease is caused by mutations
CC affecting the gene represented in this entry. A chromosomal
CC aberation 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 -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=SUMO protein entry;
CC URL="http://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; BC006462; AAH06462.1; -; mRNA.
DR EMBL; BC053528; AAH53528.1; -; mRNA.
DR EMBL; BC066306; AAH66306.1; -; mRNA.
DR IPI; IPI00303105; -.
DR RefSeq; NP_001005781.1; NM_001005781.1.
DR RefSeq; NP_003343.1; NM_003352.4.
DR UniGene; Hs.81424; -.
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=20-97.
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 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; 2PE6; -.
DR PDBsum; 2UYZ; -.
DR PDBsum; 2VRR; -.
DR PDBsum; 3KYC; -.
DR PDBsum; 3KYD; -.
DR PDBsum; 3RZW; -.
DR PDBsum; 3UIP; -.
DR ProteinModelPortal; P63165; -.
DR DIP; DIP-29080N; -.
DR IntAct; P63165; 59.
DR MINT; MINT-137859; -.
DR STRING; 9606.ENSP00000376076; -.
DR PhosphoSite; P63165; -.
DR DMDM; 52783799; -.
DR PaxDb; P63165; -.
DR PRIDE; P63165; -.
DR DNASU; 7341; -.
DR Ensembl; ENST00000392245; ENSP00000376076; ENSG00000116030.
DR Ensembl; ENST00000392246; ENSP00000376077; ENSG00000116030.
DR GeneID; 7341; -.
DR KEGG; hsa:7341; -.
DR UCSC; uc002uyz.1; human.
DR CTD; 7341; -.
DR GeneCards; GC02M203070; -.
DR HGNC; HGNC:12502; SUMO1.
DR HPA; CAB004269; -.
DR MIM; 601912; gene.
DR MIM; 613705; phenotype.
DR neXtProt; NX_P63165; -.
DR Orphanet; 1991; Cleft lip with or without cleft palate.
DR PharmGKB; PA37149; -.
DR eggNOG; COG5227; -.
DR HOGENOM; HOG000207495; -.
DR HOVERGEN; HBG053025; -.
DR KO; K12160; -.
DR OrthoDB; EOG42JNSX; -.
DR PhylomeDB; P63165; -.
DR Pathway_Interaction_DB; hdac_classi_pathway; Signaling events mediated by HDAC Class I.
DR Pathway_Interaction_DB; hdac_classii_pathway; Signaling events mediated by HDAC Class II.
DR Pathway_Interaction_DB; ranbp2pathway; Sumoylation by RanBP2 regulates transcriptional repression.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; P63165; -.
DR GenomeRNAi; 7341; -.
DR NextBio; 28734; -.
DR PMAP-CutDB; P63165; -.
DR ArrayExpress; P63165; -.
DR Bgee; P63165; -.
DR CleanEx; HS_SUMO1; -.
DR Genevestigator; P63165; -.
DR GermOnline; ENSG00000116030; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:Compara.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Compara.
DR GO; GO:0019789; F:SUMO ligase activity; IEA:Compara.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0043392; P:negative regulation of DNA binding; IMP:UniProtKB.
DR GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0060021; P:palate development; ISS:UniProtKB.
DR GO; GO:0030578; P:PML body organization; IEA:Compara.
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 complex assembly; IDA:BHF-UCL.
DR GO; GO:0090204; P:protein localization to nuclear pore; IEA:Compara.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0032880; P:regulation of protein localization; TAS:UniProtKB.
DR InterPro; IPR000626; Ubiquitin.
DR InterPro; IPR019955; Ubiquitin_supergroup.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosomal rearrangement;
KW Complete proteome; Cytoplasm; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 97 Small ubiquitin-related modifier 1.
FT /FTId=PRO_0000035939.
FT PROPEP 98 101
FT /FTId=PRO_0000035940.
FT DOMAIN 20 97 Ubiquitin-like.
FT SITE 36 36 Interaction with PIAS2.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 9 9 Phosphoserine.
FT CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO-1).
FT CROSSLNK 25 25 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO-1).
FT CROSSLNK 97 97 Glycyl lysine isopeptide (Gly-Lys)
FT (interchain with K-? in acceptor
FT proteins).
FT MUTAGEN 36 36 F->A: Abolishes binding to PIAS2.
FT CONFLICT 75 75 H -> N (in Ref. 13; AAH66306).
FT STRAND 2 6
FT TURN 9 11
FT TURN 16 18
FT STRAND 21 27
FT STRAND 29 31
FT STRAND 33 39
FT STRAND 40 42
FT HELIX 45 55
FT HELIX 59 61
FT STRAND 62 66
FT HELIX 77 80
FT STRAND 86 92
SQ SEQUENCE 101 AA; 11557 MW; 89BE97D2D054FB33 CRC64;
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V
//
