SOX13_HUMAN
ID SOX13_HUMAN Reviewed; 622 AA.
AC Q9UN79; B4E2B0; O95275; O95826; Q3KQV7; Q5SXX1; Q9UHW7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Transcription factor SOX-13;
DE AltName: Full=Islet cell antigen 12;
DE AltName: Full=SRY (Sex determining region Y)-box 13;
DE AltName: Full=Type 1 diabetes autoantigen ICA12;
GN Name=SOX13;
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].
RC TISSUE=Kidney;
RX PubMed=9421502; DOI=10.1093/nar/26.2.469;
RA Roose J., Korver W., Oving E., Wilson A., Wagenaar G., Markman M.,
RA Lamers W., Clevers H.;
RT "High expression of the HMG box factor sox-13 in arterial walls during
RT embryonic development.";
RL Nucleic Acids Res. 26:469-476(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreatic islet;
RA LaGasse J.M., Gleason S., Rabin D.U., Michaels D., Kletter G., Pihoker K.,
RA Mahoney P., Valle T., Nguyen C., Hagopian W.A.;
RT "ICA12: a novel autoantigen in type I diabetes.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas, and Placenta;
RA Kasimiotis H., Myers M.A., Mertin S., Argentaro A., Fida S., Ferro T.,
RA Olsson J.E., Rowley M.J., Harley V.R.;
RT "SOX13 encodes an autoimmune antigen in type 1 diabetes.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Argentaro A., Olsson J., Critcher R., McDowall S.G., Harley V.R.;
RT "Genomic structure and precise chromosomal localization of human SOX13.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INVOLVEMENT IN TYPE 1 DIABETES.
RX PubMed=10871192; DOI=10.2337/diabetes.49.4.555;
RA Kasimiotis H., Myers M.A., Argentaro A., Mertin S., Fida S., Ferraro T.,
RA Olsson J., Rowley M.J., Harley V.R.;
RT "Sex-determining region Y-related protein SOX13 is a diabetes autoantigen
RT expressed in pancreatic islets.";
RL Diabetes 49:555-561(2000).
RN [10]
RP INTERACTION WITH TCF7.
RX PubMed=17218525; DOI=10.1126/science.1135344;
RA Melichar H.J., Narayan K., Der S.D., Hiraoka Y., Gardiol N., Jeannet G.,
RA Held W., Chambers C.A., Kang J.;
RT "Regulation of gammadelta versus alphabeta T lymphocyte differentiation by
RT the transcription factor SOX13.";
RL Science 315:230-233(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-382, 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 [12]
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 [13]
RP FUNCTION, INTERACTION WITH HHEX AND TCF7, AND TISSUE SPECIFICITY.
RX PubMed=20028982; DOI=10.1074/jbc.m109.046649;
RA Marfil V., Moya M., Pierreux C.E., Castell J.V., Lemaigre F.P., Real F.X.,
RA Bort R.;
RT "Interaction between Hhex and SOX13 modulates Wnt/TCF activity.";
RL J. Biol. Chem. 285:5726-5737(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-613, AND
RP IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385 AND SER-386, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
CC -!- FUNCTION: Transcription factor that binds to DNA at the consensus
CC sequence 5'-AACAAT-3' (PubMed:10871192). Binds to the proximal promoter
CC region of the myelin protein MPZ gene, and may thereby be involved in
CC the differentiation of oligodendroglia in the developing spinal tube
CC (By similarity). Binds to the gene promoter of MBP and acts as a
CC transcriptional repressor (By similarity). Binds to and modifies the
CC activity of TCF7/TCF1, thereby inhibiting transcription and modulates
CC normal gamma-delta T-cell development and differentiation of IL17A
CC expressing gamma-delta T-cells (By similarity). Regulates expression of
CC BLK in the differentiation of IL17A expressing gamma-delta T-cells (By
CC similarity). Promotes brown adipocyte differentiation (By similarity).
CC Inhibitor of WNT signaling (PubMed:20028982).
CC {ECO:0000250|UniProtKB:Q04891, ECO:0000269|PubMed:10871192,
CC ECO:0000269|PubMed:20028982}.
CC -!- SUBUNIT: Homodimer; homodimerization reduces DNA binding efficiency
CC (PubMed:10871192). Interacts with TCF7/TCF1 long isoform (via N-
CC terminus); inhibits WNT-mediated transcriptional activity
CC (PubMed:17218525, PubMed:20028982). Interacts with HHEX (via N-
CC terminus); abolishes the SOX13-mediated inhibition of WNT-mediated
CC transcriptional activity via competitive inhibition of the SOX13-TCF7
CC complex (PubMed:20028982). {ECO:0000269|PubMed:10871192,
CC ECO:0000269|PubMed:17218525, ECO:0000269|PubMed:20028982}.
CC -!- INTERACTION:
CC Q9UN79; P56545: CTBP2; NbExp=2; IntAct=EBI-3928516, EBI-741533;
CC Q9UN79; P56545-3: CTBP2; NbExp=3; IntAct=EBI-3928516, EBI-10171902;
CC Q9UN79; Q9C086: INO80B; NbExp=3; IntAct=EBI-3928516, EBI-715611;
CC Q9UN79; Q12933: TRAF2; NbExp=3; IntAct=EBI-3928516, EBI-355744;
CC Q9UN79; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-3928516, EBI-6116822;
CC Q9UN79; Q14119: VEZF1; NbExp=3; IntAct=EBI-3928516, EBI-11980193;
CC Q9UN79; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-3928516, EBI-6427977;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC Cytoplasm {ECO:0000269|PubMed:10871192}.
CC -!- TISSUE SPECIFICITY: Expressed in exocrine cells and islets of
CC Langerhans in the pancreas (at protein level) (PubMed:10871192).
CC Expressed in the pancreas, placenta, kidney, brain, heart, lung, and
CC liver (PubMed:10871192, PubMed:20028982). Expressed in adipose tissue,
CC cervix, colon, esophagus, ovary, prostate, small intestine, spleen,
CC testicle, thymus and thyroid (PubMed:20028982).
CC {ECO:0000269|PubMed:10871192, ECO:0000269|PubMed:20028982}.
CC -!- DISEASE: Note=Autoantibodies against SOX13 are present in sera from
CC patients with type 1 diabetes. {ECO:0000269|PubMed:10871192}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC83687.1; Type=Miscellaneous discrepancy; Note=Several frameshifts.; Evidence={ECO:0000305};
CC Sequence=AAF23875.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG65072.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF083105; AAC83687.1; ALT_SEQ; mRNA.
DR EMBL; AF098915; AAD16237.1; -; mRNA.
DR EMBL; AF116571; AAF23875.1; ALT_INIT; mRNA.
DR EMBL; AK304192; BAG65072.1; ALT_INIT; mRNA.
DR EMBL; AF149301; AAD50120.1; -; Genomic_DNA.
DR EMBL; AL592146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91500.1; -; Genomic_DNA.
DR EMBL; BC106038; AAI06039.1; -; mRNA.
DR CCDS; CCDS44299.1; -.
DR RefSeq; NP_005677.2; NM_005686.2.
DR AlphaFoldDB; Q9UN79; -.
DR SMR; Q9UN79; -.
DR BioGRID; 114948; 29.
DR IntAct; Q9UN79; 16.
DR MINT; Q9UN79; -.
DR STRING; 9606.ENSP00000356172; -.
DR GlyGen; Q9UN79; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UN79; -.
DR PhosphoSitePlus; Q9UN79; -.
DR BioMuta; SOX13; -.
DR DMDM; 288558840; -.
DR EPD; Q9UN79; -.
DR jPOST; Q9UN79; -.
DR MassIVE; Q9UN79; -.
DR MaxQB; Q9UN79; -.
DR PaxDb; Q9UN79; -.
DR PeptideAtlas; Q9UN79; -.
DR PRIDE; Q9UN79; -.
DR ProteomicsDB; 85269; -.
DR Antibodypedia; 11334; 189 antibodies from 30 providers.
DR DNASU; 9580; -.
DR Ensembl; ENST00000367204.6; ENSP00000356172.1; ENSG00000143842.15.
DR Ensembl; ENST00000618875.4; ENSP00000478239.1; ENSG00000143842.15.
DR GeneID; 9580; -.
DR KEGG; hsa:9580; -.
DR MANE-Select; ENST00000367204.6; ENSP00000356172.1; NM_005686.3; NP_005677.2.
DR UCSC; uc001ham.4; human.
DR CTD; 9580; -.
DR DisGeNET; 9580; -.
DR GeneCards; SOX13; -.
DR HGNC; HGNC:11192; SOX13.
DR HPA; ENSG00000143842; Low tissue specificity.
DR MIM; 604748; gene.
DR neXtProt; NX_Q9UN79; -.
DR OpenTargets; ENSG00000143842; -.
DR PharmGKB; PA36029; -.
DR VEuPathDB; HostDB:ENSG00000143842; -.
DR eggNOG; KOG0528; Eukaryota.
DR GeneTree; ENSGT00940000158759; -.
DR HOGENOM; CLU_018522_1_1_1; -.
DR InParanoid; Q9UN79; -.
DR OMA; KMSNCGP; -.
DR OrthoDB; 465521at2759; -.
DR PhylomeDB; Q9UN79; -.
DR TreeFam; TF320471; -.
DR PathwayCommons; Q9UN79; -.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR SignaLink; Q9UN79; -.
DR BioGRID-ORCS; 9580; 10 hits in 1091 CRISPR screens.
DR ChiTaRS; SOX13; human.
DR GeneWiki; SOX13; -.
DR GenomeRNAi; 9580; -.
DR Pharos; Q9UN79; Tbio.
DR PRO; PR:Q9UN79; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UN79; protein.
DR Bgee; ENSG00000143842; Expressed in sural nerve and 181 other tissues.
DR ExpressionAtlas; Q9UN79; baseline and differential.
DR Genevisible; Q9UN79; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0042492; P:gamma-delta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IEA:Ensembl.
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; ISS: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; IPR029547; SOX-13.
DR PANTHER; PTHR45789:SF4; PTHR45789:SF4; 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 Cytoplasm; Differentiation; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..622
FT /note="Transcription factor SOX-13"
FT /id="PRO_0000048756"
FT DNA_BIND 424..492
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 27..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..344
FT /note="Required for homodimerization"
FT /evidence="ECO:0000269|PubMed:10871192"
FT REGION 274..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VARIANT 532
FT /note="P -> S (in dbSNP:rs34758764)"
FT /id="VAR_062671"
FT CONFLICT 91
FT /note="V -> A (in Ref. 2; AAD16237)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="V -> G (in Ref. 4; AAD50120)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="P -> L (in Ref. 4; AAD50120)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="Y -> C (in Ref. 4; AAD50120)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="A -> G (in Ref. 4; AAD50120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 69228 MW; F8C102AF63128C06 CRC64;
MSMRSPISAQ LALDGVGTMV NCTIKSEEKK EPCHEAPQGS ATAAEPQPGD PARASQDSAD
PQAPAQGNFR GSWDCSSPEG NGSPEPKRPG VSEAASGSQE KLDFNRNLKE VVPAIEKLLS
SDWKERFLGR NSMEAKDVKG TQESLAEKEL QLLVMIHQLS TLRDQLLTAH SEQKNMAAML
FEKQQQQMEL ARQQQEQIAK QQQQLIQQQH KINLLQQQIQ QVNMPYVMIP AFPPSHQPLP
VTPDSQLALP IQPIPCKPVE YPLQLLHSPP APVVKRPGAM ATHHPLQEPS QPLNLTAKPK
APELPNTSSS PSLKMSSCVP RPPSHGGPTR DLQSSPPSLP LGFLGEGDAV TKAIQDARQL
LHSHSGALDG SPNTPFRKDL ISLDSSPAKE RLEDGCVHPL EEAMLSCDMD GSRHFPESRN
SSHIKRPMNA FMVWAKDERR KILQAFPDMH NSSISKILGS RWKSMTNQEK QPYYEEQARL
SRQHLEKYPD YKYKPRPKRT CIVEGKRLRV GEYKALMRTR RQDARQSYVI PPQAGQVQMS
SSDVLYPRAA GMPLAQPLVE HYVPRSLDPN MPVIVNTCSL REEGEGTDDR HSVADGEMYR
YSEDEDSEGE EKSDGELVVL TD
