SUMO3_HUMAN
ID SUMO3_HUMAN Reviewed; 103 AA.
AC P55854; B2R5X4; B4DUW4; Q53HI9; Q6FGD4; Q9BWR4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Small ubiquitin-related modifier 3 {ECO:0000305};
DE Short=SUMO-3 {ECO:0000305};
DE AltName: Full=SMT3 homolog 1 {ECO:0000312|HGNC:HGNC:11124};
DE AltName: Full=SUMO-2 {ECO:0000303|PubMed:10692421};
DE AltName: Full=Ubiquitin-like protein SMT3A {ECO:0000303|PubMed:9119407};
DE Short=Smt3A {ECO:0000303|PubMed:9119407};
DE Flags: Precursor;
GN Name=SUMO3 {ECO:0000312|HGNC:HGNC:11124};
GN Synonyms=SMT3A {ECO:0000303|PubMed:9119407},
GN SMT3H1 {ECO:0000312|HGNC:HGNC:11124};
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), AND VARIANT SER-38.
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 [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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, and Kidney;
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 [9]
RP IDENTIFICATION.
RX PubMed=10692421; DOI=10.1074/jbc.275.9.6252;
RA Saitoh H., Hinchey J.;
RT "Functional heterogeneity of small ubiquitin-related protein modifiers
RT SUMO-1 versus SUMO-2/3.";
RL J. Biol. Chem. 275:6252-6258(2000).
RN [10]
RP FUNCTION IN SUMOYLATION OF PML, POLYSUMOYLATION, INTERACTION WITH SAE1 AND
RP UBE2I, SUMOYLATION AT LYS-11, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF LYS-11.
RX PubMed=11451954; DOI=10.1074/jbc.m104214200;
RA Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H.,
RA Naismith J.H., Hay R.T.;
RT "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates
RT by SAE1/SAE2 and Ubc9.";
RL J. Biol. Chem. 276:35368-35374(2001).
RN [11]
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 [12]
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 [13]
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 [14]
RP CLEAVAGE, AND TISSUE SPECIFICITY.
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 [15]
RP CLEAVAGE.
RX PubMed=16608850; DOI=10.1074/jbc.m511658200;
RA Gong L., Yeh E.T.H.;
RT "Characterization of a family of nucleolar SUMO-specific proteases with
RT preference for SUMO-2 or SUMO-3.";
RL J. Biol. Chem. 281:15869-15877(2006).
RN [16]
RP FUNCTION IN SUMOYLATION OF USP25, INTERACTION WITH USP25, AND MUTAGENESIS
RP OF ILE-33 AND LYS-34.
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 [17]
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 [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [19]
RP FUNCTION IN SUMOYLATION OF SETX.
RX PubMed=24105744; DOI=10.1101/gad.224923.113;
RA Richard P., Feng S., Manley J.L.;
RT "A SUMO-dependent interaction between Senataxin and the exosome, disrupted
RT in the neurodegenerative disease AOA2, targets the exosome to sites of
RT transcription-induced DNA damage.";
RL Genes Dev. 27:2227-2232(2013).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-11, 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 [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-7 AND LYS-11, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [25]
RP STRUCTURE BY NMR OF 14-92.
RX PubMed=15723523; DOI=10.1021/bi0477586;
RA Ding H., Xu Y., Chen Q., Dai H., Tang Y., Wu J., Shi Y.;
RT "Solution structure of human SUMO-3 C47S and its binding surface for
RT Ubc9.";
RL Biochemistry 44:2790-2799(2005).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH SENP1, AND CLEAVAGE.
RX PubMed=16553580; DOI=10.1042/bj20052030;
RA Shen L.N., Dong C., Liu H., Naismith J.H., Hay R.T.;
RT "The structure of SENP1-SUMO-2 complex suggests a structural basis for
RT discrimination between SUMO paralogues during processing.";
RL Biochem. J. 397:279-288(2006).
CC -!- FUNCTION: Ubiquitin-like protein which can be covalently attached to
CC target lysines either as a monomer or as a lysine-linked polymer. Does
CC not seem to be involved in protein degradation and may function as an
CC antagonist of ubiquitin in the degradation process. Plays a role in a
CC number of cellular processes such as nuclear transport, DNA replication
CC and repair, mitosis and signal transduction. Covalent attachment to its
CC substrates requires prior activation by the E1 complex SAE1-SAE2 and
CC linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase
CC such as PIAS1-4, RANBP2 or CBX4 (PubMed:11451954, PubMed:18538659,
CC PubMed:21965678). Plays a role in the regulation of sumoylation status
CC of SETX (PubMed:24105744). {ECO:0000269|PubMed:11451954,
CC ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:21965678}.
CC -!- SUBUNIT: Covalently attached to a number of proteins. Interacts with
CC ARNTL/BMAL1 (By similarity). Interacts with USP25 (via ts SIM domain);
CC the interaction sumoylates USP25 and inhibits its ubiquitin hydrolyzing
CC activity. Interacts with SAE2 and UBE2I. {ECO:0000250,
CC ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:12924945,
CC ECO:0000269|PubMed:16553580, ECO:0000269|PubMed:18538659}.
CC -!- INTERACTION:
CC P55854; P54253: ATXN1; NbExp=6; IntAct=EBI-474067, EBI-930964;
CC P55854; Q99700-5: ATXN2; NbExp=3; IntAct=EBI-474067, EBI-25891409;
CC P55854; A4D161: FAM221A; NbExp=3; IntAct=EBI-474067, EBI-11960181;
CC P55854; P42858: HTT; NbExp=9; IntAct=EBI-474067, EBI-466029;
CC P55854; O43290: SART1; NbExp=2; IntAct=EBI-474067, EBI-607761;
CC P55854; Q9HC62: SENP2; NbExp=6; IntAct=EBI-474067, EBI-714881;
CC P55854; P23497: SP100; NbExp=2; IntAct=EBI-474067, EBI-751145;
CC P55854; Q5W0Q7: USPL1; NbExp=16; IntAct=EBI-474067, EBI-2513899;
CC P55854; Q86T24: ZBTB33; NbExp=3; IntAct=EBI-474067, EBI-2515625;
CC P55854; O15060: ZBTB39; NbExp=3; IntAct=EBI-474067, EBI-9995672;
CC P55854; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-474067, EBI-748373;
CC P55854; Q96IT1: ZNF496; NbExp=3; IntAct=EBI-474067, EBI-743906;
CC P55854; P62990: UBC; Xeno; NbExp=2; IntAct=EBI-474067, EBI-413053;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55854-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55854-2; Sequence=VSP_054693;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in liver.
CC {ECO:0000269|PubMed:15487983}.
CC -!- PTM: Polymeric chains can be formed through Lys-11 cross-linking.
CC -!- PTM: Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary
CC for function. {ECO:0000269|PubMed:15487983,
CC ECO:0000269|PubMed:16608850}.
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; X99584; CAA67896.1; -; mRNA.
DR EMBL; BT007008; AAP35654.1; -; mRNA.
DR EMBL; CR542173; CAG46970.1; -; mRNA.
DR EMBL; CR542188; CAG46985.1; -; mRNA.
DR EMBL; AK222591; BAD96311.1; -; mRNA.
DR EMBL; AK300822; BAG62476.1; -; mRNA.
DR EMBL; AK312350; BAG35271.1; -; mRNA.
DR EMBL; AL773603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09392.1; -; Genomic_DNA.
DR EMBL; BC000036; AAH00036.1; -; mRNA.
DR EMBL; BC008420; AAH08420.1; -; mRNA.
DR CCDS; CCDS33587.1; -. [P55854-1]
DR CCDS; CCDS68220.1; -. [P55854-2]
DR RefSeq; NP_001273345.1; NM_001286416.1. [P55854-2]
DR RefSeq; NP_008867.2; NM_006936.2. [P55854-1]
DR PDB; 1U4A; NMR; -; A=14-92.
DR PDB; 2IO1; X-ray; 2.60 A; B/D/F=14-103.
DR PDB; 2MP2; NMR; -; A=12-92, B=2-90.
DR PDB; 6K5R; NMR; -; A=15-91.
DR PDB; 6NNQ; X-ray; 2.62 A; B=15-92.
DR PDBsum; 1U4A; -.
DR PDBsum; 2IO1; -.
DR PDBsum; 2MP2; -.
DR PDBsum; 6K5R; -.
DR PDBsum; 6NNQ; -.
DR AlphaFoldDB; P55854; -.
DR BMRB; P55854; -.
DR SMR; P55854; -.
DR BioGRID; 112496; 99.
DR DIP; DIP-29255N; -.
DR ELM; P55854; -.
DR IntAct; P55854; 69.
DR MINT; P55854; -.
DR ChEMBL; CHEMBL3885639; -.
DR iPTMnet; P55854; -.
DR PhosphoSitePlus; P55854; -.
DR SwissPalm; P55854; -.
DR BioMuta; SUMO3; -.
DR DMDM; 23503102; -.
DR EPD; P55854; -.
DR jPOST; P55854; -.
DR MassIVE; P55854; -.
DR MaxQB; P55854; -.
DR PaxDb; P55854; -.
DR PeptideAtlas; P55854; -.
DR PRIDE; P55854; -.
DR ProteomicsDB; 5226; -.
DR ProteomicsDB; 56874; -. [P55854-1]
DR TopDownProteomics; P55854-1; -. [P55854-1]
DR Antibodypedia; 24332; 495 antibodies from 40 providers.
DR DNASU; 6612; -.
DR Ensembl; ENST00000332859.11; ENSP00000330343.7; ENSG00000184900.16. [P55854-1]
DR Ensembl; ENST00000411651.6; ENSP00000409666.2; ENSG00000184900.16. [P55854-2]
DR GeneID; 6612; -.
DR KEGG; hsa:6612; -.
DR MANE-Select; ENST00000332859.11; ENSP00000330343.7; NM_006936.3; NP_008867.2.
DR UCSC; uc002zfz.1; human. [P55854-1]
DR CTD; 6612; -.
DR DisGeNET; 6612; -.
DR GeneCards; SUMO3; -.
DR HGNC; HGNC:11124; SUMO3.
DR HPA; ENSG00000184900; Low tissue specificity.
DR MIM; 602231; gene.
DR neXtProt; NX_P55854; -.
DR OpenTargets; ENSG00000184900; -.
DR PharmGKB; PA35973; -.
DR VEuPathDB; HostDB:ENSG00000184900; -.
DR GeneTree; ENSGT00950000182895; -.
DR HOGENOM; CLU_148322_2_1_1; -.
DR InParanoid; P55854; -.
DR OMA; MICKEDG; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; P55854; -.
DR TreeFam; TF315116; -.
DR PathwayCommons; P55854; -.
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-3232118; SUMOylation of transcription factors.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-4755510; SUMOylation of immune response proteins.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR SignaLink; P55854; -.
DR BioGRID-ORCS; 6612; 10 hits in 1083 CRISPR screens.
DR ChiTaRS; SUMO3; human.
DR EvolutionaryTrace; P55854; -.
DR GeneWiki; SUMO3; -.
DR GenomeRNAi; 6612; -.
DR Pharos; P55854; Tbio.
DR PRO; PR:P55854; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P55854; protein.
DR Bgee; ENSG00000184900; Expressed in endothelial cell and 213 other tissues.
DR ExpressionAtlas; P55854; baseline and differential.
DR Genevisible; P55854; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:CAFA.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IDA:UniProtKB.
DR IDEAL; IID00350; -.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
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; Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..92
FT /note="Small ubiquitin-related modifier 3"
FT /id="PRO_0000035957"
FT PROPEP 93..103
FT /evidence="ECO:0000269|PubMed:15487983,
FT ECO:0000269|PubMed:16608850"
FT /id="PRO_0000035958"
FT DOMAIN 15..92
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 7
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 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT VAR_SEQ 50
FT /note="Q -> QVRHLAPPQSLPVCALVLCVPGIPRARASRGWTQMQLPE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054693"
FT VARIANT 38
FT /note="P -> S (in dbSNP:rs1051311)"
FT /evidence="ECO:0000269|PubMed:9119407"
FT /id="VAR_052692"
FT MUTAGEN 11
FT /note="K->R: Abolishes the formation of poly(SUMO) chains."
FT /evidence="ECO:0000269|PubMed:11451954"
FT MUTAGEN 33
FT /note="I->A: Impaired interaction with USP25; when
FT associated with A-34."
FT /evidence="ECO:0000269|PubMed:18538659"
FT MUTAGEN 34
FT /note="K->A: Impaired interaction with USP25; when
FT associated with A-33."
FT /evidence="ECO:0000269|PubMed:18538659"
FT CONFLICT 32
FT /note="K -> E (in Ref. 5; BAD96311)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="E -> R (in Ref. 1; CAA67896)"
FT /evidence="ECO:0000305"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2MP2"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:2IO1"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1U4A"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:2IO1"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1U4A"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:2IO1"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2IO1"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:2IO1"
FT TURN 72..76
FT /evidence="ECO:0007829|PDB:2IO1"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2IO1"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2IO1"
SQ SEQUENCE 103 AA; 11637 MW; E337E34CB5B3B187 CRC64;
MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR
FDGQPINETD TPAQLEMEDE DTIDVFQQQT GGVPESSLAG HSF
