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 02-SEP-2026, entry version 217. 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}, SMT3H1 GN {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 BMAL1 (By similarity). Interacts with USP25 (via ts SIM domain); the CC 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; Q86X55: CARM1; NbExp=2; IntAct=EBI-474067, EBI-2339854; 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=7; IntAct=EBI-474067, EBI-714881; CC P55854; P23497: SP100; NbExp=2; IntAct=EBI-474067, EBI-751145; CC P55854; Q5W0Q7: USPL1; NbExp=17; 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=4; 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001286416.2. [P55854-2] DR RefSeq; NP_008867.2; NM_006936.3. [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 PDB; 7R2E; X-ray; 1.74 A; C/D=16-91. DR PDB; 7ZJU; X-ray; 2.17 A; B/D=2-91. DR PDB; 9GNN; X-ray; 2.36 A; C/D=14-91. DR AlphaFoldDB; P55854; -. DR BMRB; P55854; -. DR SMR; P55854; -. DR BioGRID; 112496; 123. DR CORUM; P55854; -. DR DIP; DIP-29255N; -. DR ELM; P55854; -. DR FunCoup; P55854; 2911. DR IntAct; P55854; 87. DR MINT; P55854; -. DR NDEx; IQUERY-CP-SUMO3; 1 NDEx IQuery Curated Pathway. DR ChEMBL; CHEMBL3885639; -. DR GlyGen; P55854; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P55854; -. DR PhosphoSitePlus; P55854; -. DR SwissPalm; P55854; -. DR BioMuta; SUMO3; -. DR DMDM; 23503102; -. DR jPOST; P55854; -. DR MassIVE; P55854; -. DR PeptideAtlas; P55854; -. DR ProteomicsDB; 5226; -. DR ProteomicsDB; 56874; -. [P55854-1] DR Pumba; P55854; -. DR TopDownProteomics; P55854-1; -. [P55854-1] DR Antibodypedia; 24332; 479 antibodies from 42 providers. DR DNASU; 6612; -. DR Ensembl; ENST00000332859.11; ENSP00000330343.7; ENSG00000184900.17. [P55854-1] DR Ensembl; ENST00000411651.6; ENSP00000409666.2; ENSG00000184900.17. [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 AGR; HGNC:11124; -. DR ClinPGx; PA35973; -. 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 OpenTargets; ENSG00000184900; -. DR VEuPathDB; HostDB:ENSG00000184900; -. DR GeneTree; ENSGT00950000182895; -. DR HOGENOM; CLU_148322_2_1_1; -. DR InParanoid; P55854; -. DR OMA; CHRPCIC; -. DR PAN-GO; P55854; 4 GO annotations based on evolutionary models. DR PhylomeDB; P55854; -. 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 Agora; ENSG00000184900; -. DR BioGRID-ORCS; 6612; 11 hits in 1161 CRISPR screens. DR CD-CODE; B5B9A610; PML body. DR CD-CODE; E0298522; Synthetic Condensate 000165. 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 215 other cell types or tissues. DR ExpressionAtlas; P55854; baseline and differential. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0000776; C:kinetochore; TAS:ProtInc. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; IDA:UniProtKB. DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl. DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl. DR GO; GO:0031386; F:protein tag activity; IDA:UniProtKB. DR GO; GO:0019789; F:SUMO transferase activity; IEA:Ensembl. DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central. DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB. DR GO; GO:1900180; P:regulation of protein localization to nucleus; IDA:UniProtKB. DR CDD; cd16115; Ubl_SUMO2_3_4; 1. DR FunFam; 3.10.20.90:FF:000022; Small ubiquitin-related modifier; 1. DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1. DR IDEAL; IID00350; -. DR InterPro; IPR022617; Rad60/SUMO-like_dom. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10562; SMALL UBIQUITIN-RELATED MODIFIER; 1. DR Pfam; PF11976; Rad60-SLD; 1. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. DR PDBsum; 1U4A; -. DR PDBsum; 2IO1; -. DR PDBsum; 2MP2; -. DR PDBsum; 6K5R; -. DR PDBsum; 6NNQ; -. DR PDBsum; 7R2E; -. DR PDBsum; 7ZJU; -. DR PDBsum; 9GNN; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus; KW Proteomics identification; Reference proteome; Ubl conjugation; KW 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 17..22 FT /evidence="ECO:0007829|PDB:7R2E" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:1U4A" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:1U4A" FT HELIX 40..49 FT /evidence="ECO:0007829|PDB:7R2E" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:7R2E" FT TURN 72..76 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:7R2E" 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 //