SDS3_HUMAN
ID SDS3_HUMAN Reviewed; 328 AA.
AC Q9H7L9; Q4KMQ5; Q8N6H0; Q9H8D2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Sin3 histone deacetylase corepressor complex component SDS3;
DE AltName: Full=45 kDa Sin3-associated polypeptide;
DE AltName: Full=Suppressor of defective silencing 3 protein homolog;
GN Name=SUDS3; Synonyms=SAP45, SDS3;
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 [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen.";
RL DNA Res. 7:357-366(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3;
RP ARID4B; HDAC1 AND HDAC2.
RX PubMed=12724404; DOI=10.1128/mcb.23.10.3456-3467.2003;
RA Fleischer T.C., Yun U.J., Ayer D.E.;
RT "Identification and characterization of three new components of the mSin3A
RT corepressor complex.";
RL Mol. Cell. Biol. 23:3456-3467(2003).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH30252.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000312|EMBL:AAH30252.1}, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000312|EMBL:BAB15750.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-328.
RC TISSUE=Placenta {ECO:0000312|EMBL:BAB14685.1}, and
RC Spleen {ECO:0000312|EMBL:BAB15750.1};
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] {ECO:0000305}
RP INTERACTION WITH HCFC1.
RX PubMed=12670868; DOI=10.1101/gad.252103;
RA Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
RT "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
RT methyltransferase are tethered together selectively by the cell-
RT proliferation factor HCF-1.";
RL Genes Dev. 17:896-911(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-49, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49; SER-53; SER-234
RP AND THR-244, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-49, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49 AND SER-234, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP FUNCTION, INTERACTION WITH USP17L2, SUBCELLULAR LOCATION, UBIQUITINATION,
RP AND DEUBIQUITINATION BY USP17L2.
RX PubMed=21239494; DOI=10.1074/jbc.m110.162321;
RA Ramakrishna S., Suresh B., Lee E.J., Lee H.J., Ahn W.S., Baek K.H.;
RT "Lys-63-specific deubiquitination of SDS3 by USP17 regulates HDAC
RT activity.";
RL J. Biol. Chem. 286:10505-10514(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-32; SER-45; SER-228 AND SER-234, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49 AND SER-234, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-69, 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 [16]
RP INTERACTION WITH FOXK2.
RX PubMed=25805136; DOI=10.1016/j.devcel.2015.01.031;
RA Wang W., Li X., Lee M., Jun S., Aziz K.E., Feng L., Tran M.K., Li N.,
RA McCrea P.D., Park J.I., Chen J.;
RT "FOXKs promote Wnt/beta-catenin signaling by translocating DVL into the
RT nucleus.";
RL Dev. Cell 32:707-718(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, AND IDENTIFICATION BY MASS
RP 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-178 AND LYS-201, 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).
CC -!- FUNCTION: Regulatory protein which represses transcription and augments
CC histone deacetylase activity of HDAC1. May have a potential role in
CC tumor suppressor pathways through regulation of apoptosis. May function
CC in the assembly and/or enzymatic activity of the mSin3A corepressor
CC complex or in mediating interactions between the complex and other
CC regulatory complexes. {ECO:0000269|PubMed:12724404,
CC ECO:0000269|PubMed:21239494}.
CC -!- SUBUNIT: Homodimer. Component of the SIN3 histone deacetylase (HDAC)
CC corepressor complex. Interacts with SIN3A. Interaction with SIN3B
CC enhances the interaction between SIN3B and HDAC1 to form a complex (By
CC similarity). Interacts with HCFC1. Component of a mSin3A corepressor
CC complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1
CC and HDAC2. Interacts with USP17L2; the interaction is direct. Interacts
CC with FOXK2 (PubMed:25805136). {ECO:0000250,
CC ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:12724404,
CC ECO:0000269|PubMed:21239494, ECO:0000269|PubMed:25805136}.
CC -!- INTERACTION:
CC Q9H7L9; Q9HCU9: BRMS1; NbExp=2; IntAct=EBI-540496, EBI-714781;
CC Q9H7L9; Q08379: GOLGA2; NbExp=3; IntAct=EBI-540496, EBI-618309;
CC Q9H7L9; P51610: HCFC1; NbExp=2; IntAct=EBI-540496, EBI-396176;
CC Q9H7L9; O95751: LDOC1; NbExp=3; IntAct=EBI-540496, EBI-740738;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21239494}.
CC -!- TISSUE SPECIFICITY: Expressed in various cancer cell ines.
CC {ECO:0000269|PubMed:12724404}.
CC -!- DOMAIN: The C-terminus is involved in transcriptional repression by
CC HDAC-independent mechanisms.
CC -!- PTM: Polyubiquitinated. 'Lys-63'-polyubiquitinated SUDS3 positively
CC regulates histone deacetylation. Regulated through deubiquitination by
CC USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains.
CC {ECO:0000269|PubMed:21239494}.
CC -!- SIMILARITY: Belongs to the SDS3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14685.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15750.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK024460; BAB15750.1; ALT_INIT; mRNA.
DR EMBL; BC030252; AAH30252.1; -; mRNA.
DR EMBL; BC098404; AAH98404.1; -; mRNA.
DR EMBL; AK023801; BAB14685.1; ALT_INIT; mRNA.
DR CCDS; CCDS44993.1; -.
DR RefSeq; NP_071936.2; NM_022491.2.
DR AlphaFoldDB; Q9H7L9; -.
DR SMR; Q9H7L9; -.
DR BioGRID; 122174; 113.
DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR CORUM; Q9H7L9; -.
DR IntAct; Q9H7L9; 44.
DR MINT; Q9H7L9; -.
DR STRING; 9606.ENSP00000443988; -.
DR iPTMnet; Q9H7L9; -.
DR PhosphoSitePlus; Q9H7L9; -.
DR BioMuta; SUDS3; -.
DR DMDM; 68053233; -.
DR EPD; Q9H7L9; -.
DR jPOST; Q9H7L9; -.
DR MassIVE; Q9H7L9; -.
DR MaxQB; Q9H7L9; -.
DR PaxDb; Q9H7L9; -.
DR PeptideAtlas; Q9H7L9; -.
DR PRIDE; Q9H7L9; -.
DR ProteomicsDB; 81128; -.
DR Antibodypedia; 31389; 110 antibodies from 20 providers.
DR DNASU; 64426; -.
DR Ensembl; ENST00000543473.2; ENSP00000443988.1; ENSG00000111707.12.
DR GeneID; 64426; -.
DR KEGG; hsa:64426; -.
DR MANE-Select; ENST00000543473.2; ENSP00000443988.1; NM_022491.3; NP_071936.2.
DR UCSC; uc001twz.4; human.
DR CTD; 64426; -.
DR DisGeNET; 64426; -.
DR GeneCards; SUDS3; -.
DR HGNC; HGNC:29545; SUDS3.
DR HPA; ENSG00000111707; Low tissue specificity.
DR MIM; 608250; gene.
DR neXtProt; NX_Q9H7L9; -.
DR OpenTargets; ENSG00000111707; -.
DR PharmGKB; PA143485626; -.
DR VEuPathDB; HostDB:ENSG00000111707; -.
DR eggNOG; KOG4466; Eukaryota.
DR GeneTree; ENSGT00910000144281; -.
DR HOGENOM; CLU_050862_0_1_1; -.
DR InParanoid; Q9H7L9; -.
DR OMA; IGTEAIW; -.
DR OrthoDB; 1456563at2759; -.
DR PhylomeDB; Q9H7L9; -.
DR TreeFam; TF323740; -.
DR PathwayCommons; Q9H7L9; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; Q9H7L9; -.
DR SIGNOR; Q9H7L9; -.
DR BioGRID-ORCS; 64426; 389 hits in 1083 CRISPR screens.
DR ChiTaRS; SUDS3; human.
DR GeneWiki; SUDS3; -.
DR GenomeRNAi; 64426; -.
DR Pharos; Q9H7L9; Tbio.
DR PRO; PR:Q9H7L9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H7L9; protein.
DR Bgee; ENSG00000111707; Expressed in oviduct epithelium and 182 other tissues.
DR Genevisible; Q9H7L9; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; ISS:UniProtKB.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR InterPro; IPR013907; Sds3.
DR PANTHER; PTHR21964; PTHR21964; 1.
DR Pfam; PF08598; Sds3; 1.
DR SMART; SM01401; Sds3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Chromatin regulator; Coiled coil; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..328
FT /note="Sin3 histone deacetylase corepressor complex
FT component SDS3"
FT /id="PRO_0000097652"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..170
FT /note="Mediates interaction with USP17L2"
FT /evidence="ECO:0000269|PubMed:21239494"
FT REGION 188..226
FT /note="Sin3 interaction domain (SID)"
FT /evidence="ECO:0000250|UniProtKB:Q8BR65"
FT REGION 226..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..171
FT /evidence="ECO:0000255"
FT COMPBIAS 35..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 178
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 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 164..171
FT /note="EKLTMELT -> HASAHASA (in Ref. 2; AAH30252)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="S -> R (in Ref. 3; BAB14685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 38136 MW; 10A7393B607117EB CRC64;
MSAAGLLAPA PAQAGAPPAP EYYPEEDEEL ESAEDDERSC RGRESDEDTE DASETDLAKH
DEEDYVEMKE QMYQDKLASL KRQLQQLQEG TLQEYQKRMK KLDQQYKERI RNAELFLQLE
TEQVERNYIK EKKAAVKEFE DKKVELKENL IAELEEKKKM IENEKLTMEL TGDSMEVKPI
MTRKLRRRPN DPVPIPDKRR KPAPAQLNYL LTDEQIMEDL RTLNKLKSPK RPASPSSPEH
LPATPAESPA QRFEARIEDG KLYYDKRWYH KSQAIYLESK DNQKLSCVIS SVGANEIWVR
KTSDSTKMRI YLGQLQRGLF VIRRRSAA
