STAG1_HUMAN
ID STAG1_HUMAN Reviewed; 1258 AA.
AC Q8WVM7; O00539; Q6P275;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cohesin subunit SA-1;
DE AltName: Full=SCC3 homolog 1;
DE AltName: Full=Stromal antigen 1;
GN Name=STAG1; Synonyms=SA1, SCC3 {ECO:0000303|PubMed:22628566};
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).
RC TISSUE=Thymus;
RX PubMed=9305759; DOI=10.1016/s0378-1119(97)00121-2;
RA Carramolino L., Lee B.C., Zaballos A., Peled A., Barthelemy I.,
RA Shav-Tal Y., Prieto I., Carmi P., Gothelf Y., Gonzalez de Buitrago G.,
RA Aracil M., Marquez G., Barbero J.L., Zipori D.;
RT "SA-1, a nuclear protein encoded by one member of a novel gene family:
RT molecular cloning and detection in hemopoietic organs.";
RL Gene 195:151-159(1997).
RN [2]
RP ERRATUM OF PUBMED:9305759.
RA Carramolino L., Lee B.C., Zaballos A., Peled A., Barthelemy I.,
RA Shav-Tal Y., Prieto I., Carmi P., Gothelf Y., Gonzalez de Buitrago G.,
RA Aracil M., Marquez G., Barbero J.L., Zipori D.;
RL Gene 206:283-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 787-1258 (ISOFORM 1).
RC TISSUE=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 [5]
RP IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A AND SMC3.
RX PubMed=11076961; DOI=10.1083/jcb.151.4.749;
RA Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M.;
RT "Characterization of vertebrate cohesin complexes and their regulation in
RT prophase.";
RL J. Cell Biol. 151:749-762(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1062, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, 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 [8]
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 [9]
RP IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A; SMC3 AND RAD21.
RX PubMed=22628566; DOI=10.1073/pnas.1206840109;
RA Bermudez V.P., Farina A., Higashi T.L., Du F., Tappin I., Takahashi T.S.,
RA Hurwitz J.;
RT "In vitro loading of human cohesin on DNA by the human Scc2-Scc4 loader
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:9366-9371(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-756 AND SER-1093, AND
RP 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 INVOLVEMENT IN MRD47, AND VARIANTS MRD47 ARG-214; GLY-216; ARG-220;
RP GLN-333; TRP-351; GLN-373; PRO-478 AND ARG-979.
RX PubMed=28119487; DOI=10.1136/jmedgenet-2016-104468;
RA Lehalle D., Mosca-Boidron A.L., Begtrup A., Boute-Benejean O., Charles P.,
RA Cho M.T., Clarkson A., Devinsky O., Duffourd Y., Duplomb-Jego L.,
RA Gerard B., Jacquette A., Kuentz P., Masurel-Paulet A., McDougall C.,
RA Moutton S., Olivie H., Park S.M., Rauch A., Revencu N., Riviere J.B.,
RA Rubin K., Simonic I., Shears D.J., Smol T., Taylor Tavares A.L., Terhal P.,
RA Thevenon J., Van Gassen K., Vincent-Delorme C., Willemsen M.H.,
RA Wilson G.N., Zackai E., Zweier C., Callier P., Thauvin-Robinet C.,
RA Faivre L.;
RT "STAG1 mutations cause a novel cohesinopathy characterised by unspecific
RT syndromic intellectual disability.";
RL J. Med. Genet. 54:479-488(2017).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1161, AND IDENTIFICATION BY MASS
RP 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 [13]
RP VARIANTS ILE-85 AND CYS-377.
RX PubMed=30158690; DOI=10.1038/s41436-018-0085-6;
RG DDD Study;
RA Yuan B., Neira J., Pehlivan D., Santiago-Sim T., Song X., Rosenfeld J.,
RA Posey J.E., Patel V., Jin W., Adam M.P., Baple E.L., Dean J., Fong C.T.,
RA Hickey S.E., Hudgins L., Leon E., Madan-Khetarpal S., Rawlins L.,
RA Rustad C.F., Stray-Pedersen A., Tveten K., Wenger O., Diaz J., Jenkins L.,
RA Martin L., McGuire M., Pietryga M., Ramsdell L., Slattery L., Abid F.,
RA Bertuch A.A., Grange D., Immken L., Schaaf C.P., Van Esch H., Bi W.,
RA Cheung S.W., Breman A.M., Smith J.L., Shaw C., Crosby A.H., Eng C.,
RA Yang Y., Lupski J.R., Xiao R., Liu P.;
RT "Clinical exome sequencing reveals locus heterogeneity and phenotypic
RT variability of cohesinopathies.";
RL Genet. Med. 21:663-675(2019).
CC -!- FUNCTION: Component of cohesin complex, a complex required for the
CC cohesion of sister chromatids after DNA replication. The cohesin
CC complex apparently forms a large proteinaceous ring within which sister
CC chromatids can be trapped. At anaphase, the complex is cleaved and
CC dissociates from chromatin, allowing sister chromatids to segregate.
CC The cohesin complex may also play a role in spindle pole assembly
CC during mitosis.
CC -!- SUBUNIT: Cohesin complexes are composed of a heterodimer between a SMC1
CC protein (SMC1A or SMC1B) and SMC3, which are attached via their hinge
CC domain, and RAD21 which link them at their heads, and one STAG protein
CC (STAG1, STAG2 or STAG3). In cohesin complexes, STAG1 is mutually
CC exclusive with STAG2 and STAG3 (PubMed:11076961). Interacts directly
CC with RAD21 in cohesin complex (By similarity). Found in a cohesin
CC complex with SMC1A, SMC3 and RAD21 (PubMed:22628566).
CC {ECO:0000250|UniProtKB:Q9DGN1, ECO:0000269|PubMed:11076961,
CC ECO:0000269|PubMed:22628566}.
CC -!- INTERACTION:
CC Q8WVM7; Q29RF7: PDS5A; NbExp=3; IntAct=EBI-1175097, EBI-1175454;
CC Q8WVM7; Q9NTI5: PDS5B; NbExp=4; IntAct=EBI-1175097, EBI-1175604;
CC Q8WVM7; Q9UQE7: SMC3; NbExp=13; IntAct=EBI-1175097, EBI-80718;
CC Q8WVM7; Q8N3U4: STAG2; NbExp=5; IntAct=EBI-1175097, EBI-1057252;
CC Q8WVM7; P54274: TERF1; NbExp=4; IntAct=EBI-1175097, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
CC Note=Associates with chromatin. Before prophase it is scattered along
CC chromosome arms. During prophase, most of cohesin complexes dissociate
CC from chromatin probably because of phosphorylation by PLK1, except at
CC centromeres, where cohesin complexes remain. At anaphase, the RAD21
CC subunit of cohesin is cleaved, leading to the dissociation of the
CC complex from chromosomes, allowing chromosome separation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WVM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WVM7-2; Sequence=VSP_054496;
CC -!- PTM: Phosphorylated by PLK1. The large dissociation of cohesin from
CC chromosome arms during prophase is partly due to its phosphorylation
CC (By similarity). {ECO:0000250}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 47
CC (MRD47) [MIM:617635]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD47
CC patients manifest developmental delay and mild to moderate intellectual
CC disability, usually with delayed speech. {ECO:0000269|PubMed:28119487}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
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DR EMBL; Z75330; CAA99731.1; -; mRNA.
DR EMBL; AC069514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017735; AAH17735.1; -; mRNA.
DR EMBL; BC064699; AAH64699.1; -; mRNA.
DR CCDS; CCDS3090.1; -. [Q8WVM7-1]
DR RefSeq; NP_005853.2; NM_005862.2. [Q8WVM7-1]
DR PDB; 5QSM; X-ray; 2.74 A; A/B=459-915.
DR PDB; 5QSN; X-ray; 2.66 A; A/B=459-915.
DR PDB; 5QSO; X-ray; 2.70 A; A/B=457-900.
DR PDB; 5QSP; X-ray; 2.89 A; A/B=457-900.
DR PDB; 5QSQ; X-ray; 2.48 A; A/B=459-915.
DR PDB; 5QSR; X-ray; 3.28 A; A/B=459-915.
DR PDB; 5QSS; X-ray; 3.08 A; A/B=459-915.
DR PDB; 5QST; X-ray; 2.58 A; A/B/C/D=86-420.
DR PDB; 5QSU; X-ray; 2.73 A; A/B/C/D=86-420.
DR PDB; 5QSV; X-ray; 2.76 A; A/B/C/D=86-420.
DR PDB; 5QSW; X-ray; 3.03 A; A/B/C/D=86-420.
DR PDB; 5QSX; X-ray; 2.34 A; A/B/C/D=86-420.
DR PDB; 5QSY; X-ray; 2.40 A; A/B=459-915.
DR PDB; 5QSZ; X-ray; 3.08 A; A/B=459-915.
DR PDB; 6QB5; X-ray; 2.02 A; A/B/C/D=86-420.
DR PDB; 6R7O; X-ray; 2.31 A; A/B=459-915.
DR PDB; 6RRC; X-ray; 2.37 A; A/C=86-420.
DR PDB; 6RRK; X-ray; 3.17 A; A/B=459-915.
DR PDB; 6WG3; EM; 5.30 A; D=1-1258.
DR PDBsum; 5QSM; -.
DR PDBsum; 5QSN; -.
DR PDBsum; 5QSO; -.
DR PDBsum; 5QSP; -.
DR PDBsum; 5QSQ; -.
DR PDBsum; 5QSR; -.
DR PDBsum; 5QSS; -.
DR PDBsum; 5QST; -.
DR PDBsum; 5QSU; -.
DR PDBsum; 5QSV; -.
DR PDBsum; 5QSW; -.
DR PDBsum; 5QSX; -.
DR PDBsum; 5QSY; -.
DR PDBsum; 5QSZ; -.
DR PDBsum; 6QB5; -.
DR PDBsum; 6R7O; -.
DR PDBsum; 6RRC; -.
DR PDBsum; 6RRK; -.
DR PDBsum; 6WG3; -.
DR AlphaFoldDB; Q8WVM7; -.
DR SMR; Q8WVM7; -.
DR BioGRID; 115564; 91.
DR ComplexPortal; CPX-5989; Nuclear meiotic cohesin complex, STAG1 variant.
DR CORUM; Q8WVM7; -.
DR DIP; DIP-35421N; -.
DR IntAct; Q8WVM7; 34.
DR MINT; Q8WVM7; -.
DR STRING; 9606.ENSP00000372689; -.
DR GlyGen; Q8WVM7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WVM7; -.
DR PhosphoSitePlus; Q8WVM7; -.
DR BioMuta; STAG1; -.
DR DMDM; 209572720; -.
DR EPD; Q8WVM7; -.
DR jPOST; Q8WVM7; -.
DR MassIVE; Q8WVM7; -.
DR MaxQB; Q8WVM7; -.
DR PaxDb; Q8WVM7; -.
DR PeptideAtlas; Q8WVM7; -.
DR PRIDE; Q8WVM7; -.
DR ProteomicsDB; 66881; -.
DR ProteomicsDB; 74804; -. [Q8WVM7-1]
DR Antibodypedia; 17829; 271 antibodies from 28 providers.
DR DNASU; 10274; -.
DR Ensembl; ENST00000236698.9; ENSP00000236698.5; ENSG00000118007.13. [Q8WVM7-2]
DR Ensembl; ENST00000383202.7; ENSP00000372689.2; ENSG00000118007.13. [Q8WVM7-1]
DR GeneID; 10274; -.
DR KEGG; hsa:10274; -.
DR MANE-Select; ENST00000383202.7; ENSP00000372689.2; NM_005862.3; NP_005853.2.
DR UCSC; uc003era.2; human. [Q8WVM7-1]
DR CTD; 10274; -.
DR DisGeNET; 10274; -.
DR GeneCards; STAG1; -.
DR HGNC; HGNC:11354; STAG1.
DR HPA; ENSG00000118007; Low tissue specificity.
DR MalaCards; STAG1; -.
DR MIM; 604358; gene.
DR MIM; 617635; phenotype.
DR neXtProt; NX_Q8WVM7; -.
DR OpenTargets; ENSG00000118007; -.
DR Orphanet; 502434; STAG1-related intellectual disability-facial dysmorphism-gastroesophageal reflux syndrome.
DR PharmGKB; PA36176; -.
DR VEuPathDB; HostDB:ENSG00000118007; -.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR HOGENOM; CLU_005067_1_0_1; -.
DR InParanoid; Q8WVM7; -.
DR OMA; XIVVQAL; -.
DR PhylomeDB; Q8WVM7; -.
DR TreeFam; TF314604; -.
DR PathwayCommons; Q8WVM7; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; Q8WVM7; -.
DR SIGNOR; Q8WVM7; -.
DR BioGRID-ORCS; 10274; 56 hits in 1082 CRISPR screens.
DR ChiTaRS; STAG1; human.
DR GeneWiki; STAG1; -.
DR GenomeRNAi; 10274; -.
DR Pharos; Q8WVM7; Tbio.
DR PRO; PR:Q8WVM7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8WVM7; protein.
DR Bgee; ENSG00000118007; Expressed in calcaneal tendon and 213 other tissues.
DR ExpressionAtlas; Q8WVM7; baseline and differential.
DR Genevisible; Q8WVM7; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; TAS:Reactome.
DR GO; GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
DR GO; GO:0008278; C:cohesin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; IC:ComplexPortal.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199; PTHR11199; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51425; SCD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Chromosome partition; Disease variant; Intellectual disability;
KW Isopeptide bond; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1258
FT /note="Cohesin subunit SA-1"
FT /id="PRO_0000120182"
FT DOMAIN 296..381
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3E6"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 1161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1150..1186
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054496"
FT VARIANT 85
FT /note="V -> I (found in a patient with cohesinopathy;
FT unknown pathological significance; dbSNP:rs1559904167)"
FT /evidence="ECO:0000269|PubMed:30158690"
FT /id="VAR_082291"
FT VARIANT 214
FT /note="Q -> R (in MRD47; dbSNP:rs1553738694)"
FT /evidence="ECO:0000269|PubMed:28119487"
FT /id="VAR_079487"
FT VARIANT 216
FT /note="R -> G (in MRD47; dbSNP:rs1553738686)"
FT /evidence="ECO:0000269|PubMed:28119487"
FT /id="VAR_079488"
FT VARIANT 220
FT /note="H -> R (in MRD47; dbSNP:rs1057519153)"
FT /evidence="ECO:0000269|PubMed:28119487"
FT /id="VAR_079489"
FT VARIANT 333
FT /note="K -> Q (in MRD47; dbSNP:rs1553728634)"
FT /evidence="ECO:0000269|PubMed:28119487"
FT /id="VAR_079490"
FT VARIANT 351
FT /note="L -> W (in MRD47; dbSNP:rs1553727865)"
FT /evidence="ECO:0000269|PubMed:28119487"
FT /id="VAR_079491"
FT VARIANT 373
FT /note="R -> Q (in MRD47; dbSNP:rs1376334317)"
FT /evidence="ECO:0000269|PubMed:28119487"
FT /id="VAR_079492"
FT VARIANT 377
FT /note="R -> C (found in a patient with cohesinopathy;
FT dbSNP:rs1559824939)"
FT /evidence="ECO:0000269|PubMed:30158690"
FT /id="VAR_082292"
FT VARIANT 478
FT /note="H -> P (in MRD47; dbSNP:rs1553722309)"
FT /evidence="ECO:0000269|PubMed:28119487"
FT /id="VAR_079493"
FT VARIANT 979
FT /note="K -> R (in MRD47; dbSNP:rs1471479119)"
FT /evidence="ECO:0000269|PubMed:28119487"
FT /id="VAR_079494"
FT VARIANT 1132
FT /note="Q -> H (in dbSNP:rs34149860)"
FT /id="VAR_046968"
FT CONFLICT 645
FT /note="S -> N (in Ref. 1; CAA99731)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="H -> Q (in Ref. 1; CAA99731)"
FT /evidence="ECO:0000305"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:6QB5"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6RRC"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6QB5"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 174..189
FT /evidence="ECO:0007829|PDB:6QB5"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6QB5"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 216..255
FT /evidence="ECO:0007829|PDB:6QB5"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 265..294
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:6QB5"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6RRC"
FT HELIX 305..321
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 344..358
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 368..380
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 387..403
FT /evidence="ECO:0007829|PDB:6QB5"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:6RRC"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:6RRC"
FT HELIX 460..474
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:6RRK"
FT HELIX 481..496
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 499..507
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 519..538
FT /evidence="ECO:0007829|PDB:6R7O"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:5QSR"
FT HELIX 554..581
FT /evidence="ECO:0007829|PDB:6R7O"
FT TURN 582..584
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 586..592
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 603..606
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 610..626
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 630..643
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 648..677
FT /evidence="ECO:0007829|PDB:6R7O"
FT TURN 680..682
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 685..701
FT /evidence="ECO:0007829|PDB:6R7O"
FT TURN 702..704
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 707..709
FT /evidence="ECO:0007829|PDB:5QSS"
FT HELIX 712..725
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 731..754
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 759..779
FT /evidence="ECO:0007829|PDB:6R7O"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:5QSQ"
FT HELIX 785..801
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 804..807
FT /evidence="ECO:0007829|PDB:6R7O"
FT TURN 808..810
FT /evidence="ECO:0007829|PDB:6RRK"
FT HELIX 812..817
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 823..836
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 856..877
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 883..893
FT /evidence="ECO:0007829|PDB:6R7O"
FT HELIX 895..909
FT /evidence="ECO:0007829|PDB:6R7O"
SQ SEQUENCE 1258 AA; 144427 MW; FAF911998EC52179 CRC64;
MITSELPVLQ DSTNETTAHS DAGSELEETE VKGKRKRGRP GRPPSTNKKP RKSPGEKSRI
EAGIRGAGRG RANGHPQQNG EGEPVTLFEV VKLGKSAMQS VVDDWIESYK QDRDIALLDL
INFFIQCSGC RGTVRIEMFR NMQNAEIIRK MTEEFDEDSG DYPLTMPGPQ WKKFRSNFCE
FIGVLIRQCQ YSIIYDEYMM DTVISLLTGL SDSQVRAFRH TSTLAAMKLM TALVNVALNL
SIHQDNTQRQ YEAERNKMIG KRANERLELL LQKRKELQEN QDEIENMMNS IFKGIFVHRY
RDAIAEIRAI CIEEIGVWMK MYSDAFLNDS YLKYVGWTLH DRQGEVRLKC LKALQSLYTN
RELFPKLELF TNRFKDRIVS MTLDKEYDVA VEAIRLVTLI LHGSEEALSN EDCENVYHLV
YSAHRPVAVA AGEFLHKKLF SRHDPQAEEA LAKRRGRNSP NGNLIRMLVL FFLESELHEH
AAYLVDSLWE SSQELLKDWE CMTELLLEEP VQGEEAMSDR QESALIELMV CTIRQAAEAH
PPVGRGTGKR VLTAKERKTQ IDDRNKLTEH FIITLPMLLS KYSADAEKVA NLLQIPQYFD
LEIYSTGRME KHLDALLKQI KFVVEKHVES DVLEACSKTY SILCSEEYTI QNRVDIARSQ
LIDEFVDRFN HSVEDLLQEG EEADDDDIYN VLSTLKRLTS FHNAHDLTKW DLFGNCYRLL
KTGIEHGAMP EQIVVQALQC SHYSILWQLV KITDGSPSKE DLLVLRKTVK SFLAVCQQCL
SNVNTPVKEQ AFMLLCDLLM IFSHQLMTGG REGLQPLVFN PDTGLQSELL SFVMDHVFID
QDEENQSMEG DEEDEANKIE ALHKRRNLLA AFSKLIIYDI VDMHAAADIF KHYMKYYNDY
GDIIKETLSK TRQIDKIQCA KTLILSLQQL FNELVQEQGP NLDRTSAHVS GIKELARRFA
LTFGLDQIKT REAVATLHKD GIEFAFKYQN QKGQEYPPPN LAFLEVLSEF SSKLLRQDKK
TVHSYLEKFL TEQMMERRED VWLPLISYRN SLVTGGEDDR MSVNSGSSSS KTSSVRNKKG
RPPLHKKRVE DESLDNTWLN RTDTMIQTPG PLPAPQLTST VLRENSRPMG DQIQEPESEH
GSEPDFLHNP QMQISWLGQP KLEDLNRKDR TGMNYMKVRT GVRHAVRGLM EEDAEPIFED
VMMSSRSQLE DMNEEFEDTM VIDLPPSRNR RERAELRPDF FDSAAIIEDD SGFGMPMF
