SP130_HUMAN
ID SP130_HUMAN Reviewed; 1048 AA.
AC Q9H0E3; B7ZLM3; C9K0X9; Q4ZFV4; Q53T46; Q8WVW4; Q9H9G8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Histone deacetylase complex subunit SAP130;
DE AltName: Full=130 kDa Sin3-associated polypeptide;
DE AltName: Full=Sin3-associated polypeptide p130;
GN Name=SAP130;
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), FUNCTION, TISSUE SPECIFICITY,
RP ACETYLATION, AND IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A;
RP SAP130; SUDS3; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [6]
RP SUMOYLATION WITH SUMO1, AND SUBCELLULAR LOCATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-355; SER-442 AND SER-875, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 THR-355; SER-442; SER-855 AND
RP THR-856, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-856, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442; SER-465; SER-855 AND
RP THR-856, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [11]
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 [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-232, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-785 AND LYS-869, AND
RP IDENTIFICATION BY MASS 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-869, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-785; LYS-864 AND LYS-869, 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: Acts as a transcriptional repressor. May function in the
CC assembly and/or enzymatic activity of the mSin3A corepressor complex or
CC in mediating interactions between the complex and other regulatory
CC complexes. {ECO:0000269|PubMed:12724404}.
CC -!- SUBUNIT: Component of a mSin3A corepressor complex that contains SIN3A,
CC SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts
CC (released by dead or dying cells) with CLEC4E (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15561718}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H0E3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0E3-2; Sequence=VSP_024355, VSP_024356;
CC Name=3;
CC IsoId=Q9H0E3-3; Sequence=VSP_024356;
CC -!- TISSUE SPECIFICITY: Expressed in various cancer cell ines.
CC {ECO:0000269|PubMed:12724404}.
CC -!- DOMAIN: The N-terminus may interact with a transcriptional coactivator.
CC -!- DOMAIN: The C-terminus may interact with HDAC-dependent and HDAC-
CC independent corepressors.
CC -!- PTM: Acetylated. {ECO:0000305|PubMed:12724404}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:15561718}.
CC -!- SIMILARITY: Belongs to the SAP130 family. {ECO:0000305}.
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DR EMBL; AY220791; AAO63591.1; -; mRNA.
DR EMBL; AL136833; CAB66767.1; -; mRNA.
DR EMBL; AK022823; BAB14261.1; -; mRNA.
DR EMBL; AC118060; AAX88975.1; -; Genomic_DNA.
DR EMBL; AC012306; AAY14878.1; -; Genomic_DNA.
DR EMBL; BC017453; AAH17453.2; -; mRNA.
DR EMBL; BC117255; AAI17256.1; -; mRNA.
DR EMBL; BC143898; AAI43899.1; -; mRNA.
DR CCDS; CCDS2153.1; -. [Q9H0E3-1]
DR CCDS; CCDS54397.1; -. [Q9H0E3-3]
DR RefSeq; NP_001139400.1; NM_001145928.1. [Q9H0E3-3]
DR RefSeq; NP_001317228.1; NM_001330299.1.
DR RefSeq; NP_078821.2; NM_024545.3. [Q9H0E3-1]
DR AlphaFoldDB; Q9H0E3; -.
DR SMR; Q9H0E3; -.
DR BioGRID; 122735; 141.
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; Q9H0E3; -.
DR IntAct; Q9H0E3; 52.
DR MINT; Q9H0E3; -.
DR STRING; 9606.ENSP00000350333; -.
DR ChEMBL; CHEMBL1229012; -.
DR GlyGen; Q9H0E3; 23 sites, 2 O-linked glycans (23 sites).
DR iPTMnet; Q9H0E3; -.
DR MetOSite; Q9H0E3; -.
DR PhosphoSitePlus; Q9H0E3; -.
DR BioMuta; SAP130; -.
DR DMDM; 74717977; -.
DR EPD; Q9H0E3; -.
DR jPOST; Q9H0E3; -.
DR MassIVE; Q9H0E3; -.
DR MaxQB; Q9H0E3; -.
DR PaxDb; Q9H0E3; -.
DR PeptideAtlas; Q9H0E3; -.
DR PRIDE; Q9H0E3; -.
DR ProteomicsDB; 80261; -. [Q9H0E3-1]
DR ProteomicsDB; 80262; -. [Q9H0E3-2]
DR ProteomicsDB; 80263; -. [Q9H0E3-3]
DR Antibodypedia; 33473; 163 antibodies from 25 providers.
DR DNASU; 79595; -.
DR Ensembl; ENST00000259235.7; ENSP00000259235.3; ENSG00000136715.19. [Q9H0E3-1]
DR Ensembl; ENST00000357702.9; ENSP00000350333.5; ENSG00000136715.19. [Q9H0E3-3]
DR GeneID; 79595; -.
DR KEGG; hsa:79595; -.
DR UCSC; uc002tpp.3; human. [Q9H0E3-1]
DR CTD; 79595; -.
DR DisGeNET; 79595; -.
DR GeneCards; SAP130; -.
DR HGNC; HGNC:29813; SAP130.
DR HPA; ENSG00000136715; Tissue enhanced (testis).
DR MIM; 609697; gene.
DR neXtProt; NX_Q9H0E3; -.
DR OpenTargets; ENSG00000136715; -.
DR PharmGKB; PA143485608; -.
DR VEuPathDB; HostDB:ENSG00000136715; -.
DR eggNOG; ENOG502QQ6P; Eukaryota.
DR GeneTree; ENSGT00440000037733; -.
DR InParanoid; Q9H0E3; -.
DR OMA; IHQPIQA; -.
DR OrthoDB; 242848at2759; -.
DR PhylomeDB; Q9H0E3; -.
DR TreeFam; TF332685; -.
DR PathwayCommons; Q9H0E3; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR SignaLink; Q9H0E3; -.
DR BioGRID-ORCS; 79595; 269 hits in 1085 CRISPR screens.
DR ChiTaRS; SAP130; human.
DR GeneWiki; SAP130; -.
DR GenomeRNAi; 79595; -.
DR Pharos; Q9H0E3; Tdark.
DR PRO; PR:Q9H0E3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H0E3; protein.
DR Bgee; ENSG00000136715; Expressed in sperm and 176 other tissues.
DR ExpressionAtlas; Q9H0E3; baseline and differential.
DR Genevisible; Q9H0E3; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
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:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR InterPro; IPR024137; His_deAcase_cplx_SAP130.
DR InterPro; IPR031963; SAP130_C.
DR PANTHER; PTHR13497; PTHR13497; 1.
DR Pfam; PF16014; SAP130_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1048
FT /note="Histone deacetylase complex subunit SAP130"
FT /id="PRO_0000283736"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..1047
FT /note="Interactions with SIN3A and HDAC1"
FT COMPBIAS 24..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 355
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 856
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 785
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 864
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 869
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..470
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024355"
FT VAR_SEQ 678
FT /note="D -> DGMAVRKTLIPPQPPDVASPRVESSMRSTSGSPRPA (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_024356"
SQ SEQUENCE 1048 AA; 110324 MW; EB4E74E35BA07AEE CRC64;
MGPPRHPQAG EIEAGGAGGG RRLQVEMSSQ QFPRLGAPST GLSQAPSQIA NSGSAGLINP
AATVNDESGR DSEVSAREHM SSSSSLQSRE EKQEPVVVRP YPQVQMLSTH HAVASATPVA
VTAPPAHLTP AVPLSFSEGL MKPPPKPTMP SRPIAPAPPS TLSLPPKVPG QVTVTMESSI
PQASAIPVAT ISGQQGHPSN LHHIMTTNVQ MSIIRSNAPG PPLHIGASHL PRGAAAAAVM
SSSKVTTVLR PTSQLPNAAT AQPAVQHIIH QPIQSRPPVT TSNAIPPAVV ATVSATRAQS
PVITTTAAHA TDSALSRPTL SIQHPPSAAI SIQRPAQSRD VTTRITLPSH PALGTPKQQL
HTMAQKTIFS TGTPVAAATV APILATNTIP SATTAGSVSH TQAPTSTIVT MTVPSHSSHA
TAVTTSNIPV AKVVPQQITH TSPRIQPDYP AERSSLIPIS GHRASPNPVA METRSDNRPS
VPVQFQYFLP TYPPSAYPLA AHTYTPITSS VSTIRQYPVS AQAPNSAITA QTGVGVASTV
HLNPMQLMTV DASHARHIQG IQPAPISTQG IQPAPIGTPG IQPAPLGTQG IHSATPINTQ
GLQPAPMGTQ QPQPEGKTSA VVLADGATIV ANPISNPFSA APAATTVVQT HSQSASTNAP
AQGSSPRPSI LRKKPATDGA KPKSEIHVSM ATPVTVSMET VSNQNNDQPT IAVPPTAQQP
PPTIPTMIAA ASPPSQPAVA LSTIPGAVPI TPPITTIAAA PPPSVTVGGS LSSVLGPPVP
EIKVKEEVEP MDIMRPVSAV PPLATNTVSP SLALLANNLS MPTSDLPPGA SPRKKPRKQQ
HVISTEEGDM METNSTDDEK STAKSLLVKA EKRKSPPKEY IDEEGVRYVP VRPRPPITLL
RHYRNPWKAA YHHFQRYSDV RVKEEKKAML QEIANQKGVS CRAQGWKVHL CAAQLLQLTN
LEHDVYERLT NLQEGIIPKK KAATDDDLHR INELIQGNMQ RCKLVMDQIS EARDSMLKVL
DHKDRVLKLL NKNGTVKKVS KLKRKEKV
