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 27-MAR-2024, entry version 169. 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 Spleen RC {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}; 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; 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; 138. 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; 45. DR MINT; Q9H7L9; -. DR STRING; 9606.ENSP00000443988; -. DR GlyGen; Q9H7L9; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000443988; -. DR PeptideAtlas; Q9H7L9; -. DR ProteomicsDB; 81128; -. DR Pumba; Q9H7L9; -. DR Antibodypedia; 31389; 130 antibodies from 21 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 AGR; HGNC:29545; -. 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; 1382942at2759; -. 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; 413 hits in 1160 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 184 other cell types or tissues. 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:0070822; C:Sin3-type complex; ISS:UniProtKB. 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:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; NAS:ComplexPortal. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; NAS:ComplexPortal. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB. DR InterPro; IPR013907; Sds3. DR PANTHER; PTHR21964; BREAST CANCER METASTASIS-SUPPRESSOR 1; 1. DR PANTHER; PTHR21964:SF34; SIN3 HISTONE DEACETYLASE COREPRESSOR COMPLEX COMPONENT SDS3; 1. DR Pfam; PF08598; Sds3; 1. DR SMART; SM01401; Sds3; 1. DR Genevisible; Q9H7L9; HS. 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 //