SOX6_HUMAN
ID SOX6_HUMAN Reviewed; 828 AA.
AC P35712; Q86VX7; Q9BXQ3; Q9BXQ4; Q9BXQ5; Q9H0I8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Transcription factor SOX-6 {ECO:0000305};
GN Name=SOX6 {ECO:0000303|PubMed:11255018, ECO:0000312|HGNC:HGNC:16421};
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 [GENOMIC DNA / MRNA] (ISOFORM 3), ALTERNATIVE SPLICING,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Lymphocyte, and Myoblast;
RX PubMed=11255018; DOI=10.1016/s0378-1119(01)00346-8;
RA Cohen-Barak O., Hagiwara N., Arlt M.F., Horton J.P., Brilliant M.H.;
RT "Cloning, characterization and chromosome mapping of the human SOX6 gene.";
RL Gene 265:157-164(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 632-685 (ISOFORMS 1/2/3).
RX PubMed=1614875; DOI=10.1093/nar/20.11.2887;
RA Denny P., Swift S., Brand N., Dabhade N., Barton P., Ashworth A.;
RT "A conserved family of genes related to the testis determining gene, SRY.";
RL Nucleic Acids Res. 20:2887-2887(1992).
RN [7]
RP SUMOYLATION AT LYS-404 AND LYS-417, MUTAGENESIS OF LYS-404 AND LYS-417, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16442531; DOI=10.1016/j.febslet.2006.01.031;
RA Fernandez-Lloris R., Osses N., Jaffray E., Shen L.N., Vaughan O.A.,
RA Girwood D., Bartrons R., Rosa J.L., Hay R.T., Ventura F.;
RT "Repression of SOX6 transcriptional activity by SUMO modification.";
RL FEBS Lett. 580:1215-1221(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119; SER-399 AND SER-439, AND
RP IDENTIFICATION BY 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 [10]
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 [11]
RP INVOLVEMENT IN TOLCAS, VARIANTS TOLCAS 81-SER--ASN-828 DEL; 93-ARG--ASN-828
RP DEL; 98-SER--ASN-828 DEL; CYS-161; 240-GLN--ARN-828 DEL; THR-625; ARG-659
RP AND LEU-766, AND DEVELOPMENTAL STAGE.
RX PubMed=32442410; DOI=10.1016/j.ajhg.2020.04.015;
RG Genomics England Research Consortium;
RA Tolchin D., Yeager J.P., Prasad P., Dorrani N., Russi A.S.,
RA Martinez-Agosto J.A., Haseeb A., Angelozzi M., Santen G.W.E.,
RA Ruivenkamp C., Mercimek-Andrews S., Depienne C., Kuechler A., Mikat B.,
RA Ludecke H.J., Bilan F., Le Guyader G., Gilbert-Dussardier B., Keren B.,
RA Heide S., Haye D., Van Esch H., Keldermans L., Ortiz D., Lancaster E.,
RA Krantz I.D., Krock B.L., Pechter K.B., Arkader A., Medne L., DeChene E.T.,
RA Calpena E., Melistaccio G., Wilkie A.O.M., Suri M., Foulds N., Begtrup A.,
RA Henderson L.B., Forster C., Reed P., McDonald M.T., McConkie-Rosell A.,
RA Thevenon J., Le Tanno P., Coutton C., Tsai A.C.H., Stewart S., Maver A.,
RA Gorazd R., Pichon O., Nizon M., Cogne B., Isidor B., Martin-Coignard D.,
RA Stoeva R., Lefebvre V., Le Caignec C.;
RT "De Novo SOX6 Variants Cause a Neurodevelopmental Syndrome Associated with
RT ADHD, Craniosynostosis, and Osteochondromas.";
RL Am. J. Hum. Genet. 106:830-845(2020).
CC -!- FUNCTION: Transcription factor that plays a key role in several
CC developmental processes, including neurogenesis, chondrocytes
CC differentiation and cartilage formation (Probable). Specifically binds
CC the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and
CC promotes expression of genes important for chondrogenesis. Required for
CC overt chondrogenesis when condensed prechondrocytes differentiate into
CC early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on
CC active enhancers and super-enhancers associated with cartilage-specific
CC genes, and thereby potentiate SOX9's ability to transactivate. Not
CC involved in precartilaginous condensation, the first step in
CC chondrogenesis, during which skeletal progenitors differentiate into
CC prechondrocytes. Together with SOX5, required to form and maintain a
CC pool of highly proliferating chondroblasts between epiphyses and
CC metaphyses, to form columnar chondroblasts, delay chondrocyte
CC prehypertrophy but promote hypertrophy, and to delay terminal
CC differentiation of chondrocytes on contact with ossification fronts.
CC Binds to the proximal promoter region of the myelin protein MPZ gene,
CC and is thereby involved in the differentiation of oligodendroglia in
CC the developing spinal tube. Binds to the gene promoter of MBP and acts
CC as a transcriptional repressor (By similarity).
CC {ECO:0000250|UniProtKB:P40645, ECO:0000305|PubMed:32442410}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with DAZAP2 (By
CC similarity). May interact with CENPK (By similarity).
CC {ECO:0000250|UniProtKB:P40645}.
CC -!- INTERACTION:
CC P35712; O15266: SHOX; NbExp=3; IntAct=EBI-3505706, EBI-3505698;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:16442531}. Cytoplasm {ECO:0000250|UniProtKB:P40645}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P35712-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35712-2; Sequence=VSP_039693, VSP_039694, VSP_039695;
CC Name=3;
CC IsoId=P35712-3; Sequence=VSP_039696;
CC Name=4;
CC IsoId=P35712-4; Sequence=VSP_039694, VSP_039695;
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues, most
CC abundantly in skeletal musclen. {ECO:0000269|PubMed:11255018}.
CC -!- DEVELOPMENTAL STAGE: Expressed in many prospective brain structures of
CC fetuses (at protein level). Highly expressed in the developing brain
CC with higher expression in the ganglionic eminence, the amygdaloid
CC complex, and the hippocampus. The expression declines in all brain
CC structures in the final stages of gestation and in the neonatal period,
CC such that it is already as low in infants as in adults.
CC {ECO:0000269|PubMed:32442410}.
CC -!- PTM: Sumoylation inhibits the transcriptional activity.
CC {ECO:0000269|PubMed:16442531}.
CC -!- DISEASE: Tolchin-Le Caignec syndrome (TOLCAS) [MIM:618971]: An
CC autosomal dominant disorder characterized by mildly to moderately
CC impaired intellectual development and behavioral problems, such as
CC autism, attention deficit and hyperactivity disorder, and aggressive
CC episodes. Highly variable, additional features include osteochondroma,
CC craniosynostosis, dysmorphic facies, arachnodactyly, and large head
CC circumference. {ECO:0000269|PubMed:32442410}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC037866; Type=Frameshift; 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; AF309034; AAK26115.1; -; mRNA.
DR EMBL; AF309476; AAK26243.1; -; Genomic_DNA.
DR EMBL; AF309471; AAK26243.1; JOINED; Genomic_DNA.
DR EMBL; AF309472; AAK26243.1; JOINED; Genomic_DNA.
DR EMBL; AF309473; AAK26243.1; JOINED; Genomic_DNA.
DR EMBL; AF309474; AAK26243.1; JOINED; Genomic_DNA.
DR EMBL; AF309475; AAK26243.1; JOINED; Genomic_DNA.
DR EMBL; AF309476; AAK26244.1; -; Genomic_DNA.
DR EMBL; AF309471; AAK26244.1; JOINED; Genomic_DNA.
DR EMBL; AF309472; AAK26244.1; JOINED; Genomic_DNA.
DR EMBL; AF309473; AAK26244.1; JOINED; Genomic_DNA.
DR EMBL; AF309474; AAK26244.1; JOINED; Genomic_DNA.
DR EMBL; AF309475; AAK26244.1; JOINED; Genomic_DNA.
DR EMBL; AL136780; CAB66714.1; -; mRNA.
DR EMBL; AC009869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68458.1; -; Genomic_DNA.
DR EMBL; BC037866; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC047064; AAH47064.2; -; mRNA.
DR EMBL; X65663; CAA46614.1; -; mRNA.
DR CCDS; CCDS53604.1; -. [P35712-4]
DR CCDS; CCDS53605.1; -. [P35712-4]
DR CCDS; CCDS7821.1; -. [P35712-3]
DR RefSeq; NP_001139283.1; NM_001145811.1. [P35712-4]
DR RefSeq; NP_001139291.1; NM_001145819.1. [P35712-1]
DR RefSeq; NP_059978.1; NM_017508.2. [P35712-4]
DR RefSeq; NP_201583.2; NM_033326.3. [P35712-3]
DR AlphaFoldDB; P35712; -.
DR SMR; P35712; -.
DR BioGRID; 120714; 148.
DR ELM; P35712; -.
DR IntAct; P35712; 141.
DR MINT; P35712; -.
DR STRING; 9606.ENSP00000379644; -.
DR iPTMnet; P35712; -.
DR PhosphoSitePlus; P35712; -.
DR BioMuta; SOX6; -.
DR DMDM; 215274178; -.
DR EPD; P35712; -.
DR jPOST; P35712; -.
DR MassIVE; P35712; -.
DR MaxQB; P35712; -.
DR PaxDb; P35712; -.
DR PeptideAtlas; P35712; -.
DR PRIDE; P35712; -.
DR ProteomicsDB; 55141; -. [P35712-1]
DR ProteomicsDB; 55142; -. [P35712-2]
DR ProteomicsDB; 55143; -. [P35712-3]
DR ProteomicsDB; 55144; -. [P35712-4]
DR Antibodypedia; 1097; 299 antibodies from 33 providers.
DR DNASU; 55553; -.
DR Ensembl; ENST00000316399.10; ENSP00000324948.6; ENSG00000110693.19. [P35712-3]
DR Ensembl; ENST00000396356.7; ENSP00000379644.3; ENSG00000110693.19. [P35712-3]
DR Ensembl; ENST00000527619.6; ENSP00000434455.2; ENSG00000110693.19. [P35712-4]
DR Ensembl; ENST00000528252.5; ENSP00000432134.1; ENSG00000110693.19. [P35712-4]
DR Ensembl; ENST00000528429.5; ENSP00000433233.1; ENSG00000110693.19. [P35712-1]
DR Ensembl; ENST00000655819.1; ENSP00000499737.1; ENSG00000110693.19. [P35712-2]
DR Ensembl; ENST00000683767.1; ENSP00000507545.1; ENSG00000110693.19. [P35712-1]
DR GeneID; 55553; -.
DR KEGG; hsa:55553; -.
DR MANE-Select; ENST00000683767.1; ENSP00000507545.1; NM_001367873.1; NP_001354802.1.
DR UCSC; uc001mmd.4; human. [P35712-1]
DR CTD; 55553; -.
DR DisGeNET; 55553; -.
DR GeneCards; SOX6; -.
DR HGNC; HGNC:16421; SOX6.
DR HPA; ENSG00000110693; Tissue enhanced (bone).
DR MalaCards; SOX6; -.
DR MIM; 607257; gene.
DR MIM; 618971; phenotype.
DR neXtProt; NX_P35712; -.
DR OpenTargets; ENSG00000110693; -.
DR PharmGKB; PA38137; -.
DR VEuPathDB; HostDB:ENSG00000110693; -.
DR eggNOG; KOG0528; Eukaryota.
DR GeneTree; ENSGT00940000156433; -.
DR HOGENOM; CLU_018522_0_1_1; -.
DR InParanoid; P35712; -.
DR OMA; GDKAMNG; -.
DR OrthoDB; 465521at2759; -.
DR PhylomeDB; P35712; -.
DR TreeFam; TF320471; -.
DR PathwayCommons; P35712; -.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR SignaLink; P35712; -.
DR SIGNOR; P35712; -.
DR BioGRID-ORCS; 55553; 18 hits in 1099 CRISPR screens.
DR ChiTaRS; SOX6; human.
DR GeneWiki; SOX6; -.
DR GenomeRNAi; 55553; -.
DR Pharos; P35712; Tbio.
DR PRO; PR:P35712; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P35712; protein.
DR Bgee; ENSG00000110693; Expressed in epithelial cell of pancreas and 166 other tissues.
DR ExpressionAtlas; P35712; baseline and differential.
DR Genevisible; P35712; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IMP:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0001502; P:cartilage condensation; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; NAS:UniProtKB.
DR GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IMP:BHF-UCL.
DR GO; GO:0061036; P:positive regulation of cartilage development; IDA:UniProtKB.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IDA:UniProtKB.
DR GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0021529; P:spinal cord oligodendrocyte cell differentiation; ISS:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR027153; SOX-6.
DR PANTHER; PTHR45789:SF1; PTHR45789:SF1; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Autism spectrum disorder; Coiled coil;
KW Cytoplasm; Developmental protein; Differentiation; Disease variant;
KW DNA-binding; Intellectual disability; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..828
FT /note="Transcription factor SOX-6"
FT /id="PRO_0000048729"
FT DNA_BIND 621..689
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..262
FT /evidence="ECO:0000255"
FT COMPBIAS 21..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..813
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40645"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40645"
FT CROSSLNK 404
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT VAR_SEQ 1
FT /note="M -> MGRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_039693"
FT VAR_SEQ 327..367
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039694"
FT VAR_SEQ 477
FT /note="S -> SLGKWKSQHQEETYE (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039695"
FT VAR_SEQ 578..597
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11255018"
FT /id="VSP_039696"
FT VARIANT 81..828
FT /note="Missing (in TOLCAS)"
FT /evidence="ECO:0000269|PubMed:32442410"
FT /id="VAR_084739"
FT VARIANT 93..828
FT /note="Missing (in TOLCAS)"
FT /evidence="ECO:0000269|PubMed:32442410"
FT /id="VAR_084740"
FT VARIANT 98..828
FT /note="Missing (in TOLCAS)"
FT /evidence="ECO:0000269|PubMed:32442410"
FT /id="VAR_084741"
FT VARIANT 161
FT /note="W -> C (in TOLCAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32442410"
FT /id="VAR_084742"
FT VARIANT 240..828
FT /note="Missing (in TOLCAS)"
FT /evidence="ECO:0000269|PubMed:32442410"
FT /id="VAR_084743"
FT VARIANT 625
FT /note="M -> T (in TOLCAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32442410"
FT /id="VAR_084744"
FT VARIANT 659
FT /note="W -> R (in TOLCAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32442410"
FT /id="VAR_084745"
FT VARIANT 766
FT /note="S -> L (in TOLCAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32442410"
FT /id="VAR_084746"
FT MUTAGEN 404
FT /note="K->R: Partial loss of sumoylation. Complete loss of
FT sumoylation; when associated with R-417."
FT /evidence="ECO:0000269|PubMed:16442531"
FT MUTAGEN 417
FT /note="K->R: Partial loss of sumoylation. Complete loss of
FT sumoylation; when associated with R-404."
FT /evidence="ECO:0000269|PubMed:16442531"
FT CONFLICT 330
FT /note="V -> A (in Ref. 1; AAK26115)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="K -> R (in Ref. 6; CAA46614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 828 AA; 91921 MW; 38CA781528C839CF CRC64;
MSSKQATSPF ACAADGEDAM TQDLTSREKE EGSDQHVASH LPLHPIMHNK PHSEELPTLV
STIQQDADWD SVLSSQQRME SENNKLCSLY SFRNTSTSPH KPDEGSRDRE IMTSVTFGTP
ERRKGSLADV VDTLKQKKLE EMTRTEQEDS SCMEKLLSKD WKEKMERLNT SELLGEIKGT
PESLAEKERQ LSTMITQLIS LREQLLAAHD EQKKLAASQI EKQRQQMDLA RQQQEQIARQ
QQQLLQQQHK INLLQQQIQV QGHMPPLMIP IFPHDQRTLA AAAAAQQGFL FPPGITYKPG
DNYPVQFIPS TMAAAAASGL SPLQLQKGHV SHPQINQRLK GLSDRFGRNL DTFEHGGGHS
YNHKQIEQLY AAQLASMQVS PGAKMPSTPQ PPNTAGTVSP TGIKNEKRGT SPVTQVKDEA
AAQPLNLSSR PKTAEPVKSP TSPTQNLFPA SKTSPVNLPN KSSIPSPIGG SLGRGSSLDI
LSSLNSPALF GDQDTVMKAI QEARKMREQI QREQQQQQPH GVDGKLSSIN NMGLNSCRNE
KERTRFENLG PQLTGKSNED GKLGPGVIDL TRPEDAEGSK AMNGSAAKLQ QYYCWPTGGA
TVAEARVYRD ARGRASSEPH IKRPMNAFMV WAKDERRKIL QAFPDMHNSN ISKILGSRWK
SMSNQEKQPY YEEQARLSKI HLEKYPNYKY KPRPKRTCIV DGKKLRIGEY KQLMRSRRQE
MRQFFTVGQQ PQIPITTGTG VVYPGAITMA TTTPSPQMTS DCSSTSASPE PSLPVIQSTY
GMKTDGGSLA GNEMINGEDE MEMYDDYEDD PKSDYSSENE APEAVSAN
