SOX5_HUMAN
ID SOX5_HUMAN Reviewed; 763 AA.
AC P35711; B7Z8V0; F5H5B0; Q86UK8; Q8J017; Q8J018; Q8J019; Q8J020; Q8N1D9;
AC Q8N7E0; Q8TEA4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Transcription factor SOX-5 {ECO:0000305};
GN Name=SOX5 {ECO:0000303|PubMed:12406576, ECO:0000312|HGNC:HGNC:11201};
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] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RX PubMed=12406576; DOI=10.1016/s0378-1119(02)00927-7;
RA Ikeda T., Zhang J., Chano T., Mabuchi A., Fukuda A., Kawaguchi H.,
RA Nakamura K., Ikegawa S.;
RT "Identification and characterization of the human long form of Sox5 (L-
RT SOX5) gene.";
RL Gene 298:59-68(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5).
RC TISSUE=Liver, Testis, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 388-763 (ISOFORM 3).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 389-763.
RC TISSUE=Testis;
RX PubMed=8812465; DOI=10.1006/geno.1996.0474;
RA Wunderle V.M., Critcher R., Ashworth A., Goodfellow P.N.;
RT "Cloning and characterization of SOX5, a new member of the human SOX gene
RT family.";
RL Genomics 36:354-358(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 567-620.
RC TISSUE=Fetal heart, and Heart;
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 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 INVOLVEMENT IN LAMSHF.
RX PubMed=22290657; DOI=10.1002/humu.22037;
RA Lamb A.N., Rosenfeld J.A., Neill N.J., Talkowski M.E., Blumenthal I.,
RA Girirajan S., Keelean-Fuller D., Fan Z., Pouncey J., Stevens C.,
RA Mackay-Loder L., Terespolsky D., Bader P.I., Rosenbaum K., Vallee S.E.,
RA Moeschler J.B., Ladda R., Sell S., Martin J., Ryan S., Jones M.C.,
RA Moran R., Shealy A., Madan-Khetarpal S., McConnell J., Surti U.,
RA Delahaye A., Heron-Longe B., Pipiras E., Benzacken B., Passemard S.,
RA Verloes A., Isidor B., Le Caignec C., Glew G.M., Opheim K.E., Descartes M.,
RA Eichler E.E., Morton C.C., Gusella J.F., Schultz R.A., Ballif B.C.,
RA Shaffer L.G.;
RT "Haploinsufficiency of SOX5 at 12p12.1 is associated with developmental
RT delays with prominent language delay, behavior problems, and mild
RT dysmorphic features.";
RL Hum. Mutat. 33:728-740(2012).
RN [9]
RP INVOLVEMENT IN LAMSHF.
RX PubMed=23220431; DOI=10.1016/j.ejmg.2012.11.001;
RA Schanze I., Schanze D., Bacino C.A., Douzgou S., Kerr B., Zenker M.;
RT "Haploinsufficiency of SOX5, a member of the SOX (SRY-related HMG-box)
RT family of transcription factors is a cause of intellectual disability.";
RL Eur. J. Med. Genet. 56:108-113(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-411; SER-414 AND
RP SER-439, AND 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 [11]
RP INVOLVEMENT IN LAMSHF.
RX PubMed=23498568; DOI=10.1016/j.pediatrneurol.2012.12.013;
RA Lee R.W., Bodurtha J., Cohen J., Fatemi A., Batista D.;
RT "Deletion 12p12 involving SOX5 in two children with developmental delay and
RT dysmorphic features.";
RL Pediatr. Neurol. 48:317-320(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-131; SER-370;
RP THR-372; SER-414 AND SER-439, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP INVOLVEMENT IN LAMSHF.
RX PubMed=26111154; DOI=10.1002/ajmg.a.37221;
RA Nesbitt A., Bhoj E.J., McDonald Gibson K., Yu Z., Denenberg E., Sarmady M.,
RA Tischler T., Cao K., Dubbs H., Zackai E.H., Santani A.;
RT "Exome sequencing expands the mechanism of SOX5-associated intellectual
RT disability: A case presentation with review of sox-related disorders.";
RL Am. J. Med. Genet. A 167A:2548-2554(2015).
RN [14]
RP VARIANT PRO-362.
RX PubMed=21220648; DOI=10.1001/archneurol.2010.351;
RA Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D.,
RA Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A.,
RA Rouleau G.A.;
RT "Resequencing of 29 candidate genes in patients with familial and sporadic
RT amyotrophic lateral sclerosis.";
RL Arch. Neurol. 68:587-593(2011).
CC -!- FUNCTION: Transcription factor involved in chondrocytes differentiation
CC and cartilage formation. Specifically binds the 5'-AACAAT-3' DNA motif
CC present in enhancers and super-enhancers and promotes expression of
CC genes important for chondrogenesis, including cartilage matrix protein-
CC coding genes, such as COL2A1 and AGC1. Required for overt
CC chondrogenesis when condensed prechondrocytes differentiate into early
CC 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 SOX6, 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 {ECO:0000250|UniProtKB:P35710}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with SOX6.
CC {ECO:0000250|UniProtKB:P35710}.
CC -!- INTERACTION:
CC P35711; Q9HC52: CBX8; NbExp=3; IntAct=EBI-3505701, EBI-712912;
CC P35711; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-3505701, EBI-396137;
CC P35711; O43186: CRX; NbExp=4; IntAct=EBI-3505701, EBI-748171;
CC P35711; Q92993: KAT5; NbExp=3; IntAct=EBI-3505701, EBI-399080;
CC P35711; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-3505701, EBI-2125614;
CC P35711; P25800: LMO1; NbExp=3; IntAct=EBI-3505701, EBI-8639312;
CC P35711; P25791: LMO2; NbExp=3; IntAct=EBI-3505701, EBI-739696;
CC P35711; Q6PF18: MORN3; NbExp=3; IntAct=EBI-3505701, EBI-9675802;
CC P35711; P86479: PRR20C; NbExp=3; IntAct=EBI-3505701, EBI-10172814;
CC P35711; O15266: SHOX; NbExp=2; IntAct=EBI-3505701, EBI-3505698;
CC P35711; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-3505701, EBI-10175576;
CC P35711; Q96A09: TENT5B; NbExp=3; IntAct=EBI-3505701, EBI-752030;
CC P35711; Q08117: TLE5; NbExp=4; IntAct=EBI-3505701, EBI-717810;
CC P35711; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-3505701, EBI-745520;
CC P35711; P03410: tax; Xeno; NbExp=3; IntAct=EBI-3505701, EBI-9676218;
CC P35711-4; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-11954419, EBI-517623;
CC P35711-4; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-11954419, EBI-1383687;
CC P35711-4; O43186: CRX; NbExp=3; IntAct=EBI-11954419, EBI-748171;
CC P35711-4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-11954419, EBI-14069005;
CC P35711-4; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-11954419, EBI-716006;
CC P35711-4; P35548: MSX2; NbExp=3; IntAct=EBI-11954419, EBI-6447480;
CC P35711-4; O75928-2: PIAS2; NbExp=3; IntAct=EBI-11954419, EBI-348567;
CC P35711-4; P78317: RNF4; NbExp=3; IntAct=EBI-11954419, EBI-2340927;
CC P35711-4; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-11954419, EBI-11523345;
CC P35711-4; Q08117-2: TLE5; NbExp=3; IntAct=EBI-11954419, EBI-11741437;
CC P35711-4; Q12933: TRAF2; NbExp=3; IntAct=EBI-11954419, EBI-355744;
CC P35711-4; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-11954419, EBI-10180829;
CC P35711-4; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-11954419, EBI-3918996;
CC P35711-5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25930989, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35710}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=L-SOX5A {ECO:0000303|PubMed:12406576};
CC IsoId=P35711-1; Sequence=Displayed;
CC Name=2; Synonyms=L-SOX5B {ECO:0000303|PubMed:12406576};
CC IsoId=P35711-2; Sequence=VSP_007261;
CC Name=3;
CC IsoId=P35711-3; Sequence=VSP_007262, VSP_007263;
CC Name=4;
CC IsoId=P35711-4; Sequence=VSP_007261, VSP_007264;
CC Name=5;
CC IsoId=P35711-5; Sequence=VSP_045997;
CC -!- DISEASE: Lamb-Shaffer syndrome (LAMSHF) [MIM:616803]: An autosomal
CC dominant, neurodevelopmental disorder characterized by global
CC developmental delay, intellectual disability, language and motor
CC impairment, and distinct facial features. Additional variable skeletal
CC abnormalities may also be present. {ECO:0000269|PubMed:22290657,
CC ECO:0000269|PubMed:23220431, ECO:0000269|PubMed:23498568,
CC ECO:0000269|PubMed:26111154}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB49537.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB081588; BAC16233.1; -; mRNA.
DR EMBL; AB081589; BAC16234.1; -; mRNA.
DR EMBL; AB081590; BAC16235.1; -; Genomic_DNA.
DR EMBL; AB081591; BAC16236.1; -; Genomic_DNA.
DR EMBL; AK074317; BAB85048.1; -; mRNA.
DR EMBL; AK098610; BAC05353.1; -; mRNA.
DR EMBL; AK303970; BAH14086.1; -; mRNA.
DR EMBL; AC087244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029220; AAH29220.2; -; mRNA.
DR EMBL; BC035227; AAH35227.1; -; mRNA.
DR EMBL; BC047665; AAH47665.2; -; mRNA.
DR EMBL; BC060773; AAH60773.1; -; mRNA.
DR EMBL; S83308; AAB49537.1; ALT_INIT; mRNA.
DR EMBL; X65662; CAA46613.1; -; mRNA.
DR CCDS; CCDS41761.1; -. [P35711-3]
DR CCDS; CCDS44844.1; -. [P35711-2]
DR CCDS; CCDS58216.1; -. [P35711-4]
DR CCDS; CCDS58217.1; -. [P35711-5]
DR CCDS; CCDS8699.1; -. [P35711-1]
DR PIR; S22939; S22939.
DR RefSeq; NP_001248343.1; NM_001261414.2. [P35711-4]
DR RefSeq; NP_001248344.1; NM_001261415.2. [P35711-5]
DR RefSeq; NP_001317714.1; NM_001330785.1.
DR RefSeq; NP_008871.3; NM_006940.5. [P35711-1]
DR RefSeq; NP_694534.1; NM_152989.4. [P35711-2]
DR RefSeq; NP_821078.1; NM_178010.3. [P35711-3]
DR RefSeq; XP_016875385.1; XM_017019896.1. [P35711-2]
DR AlphaFoldDB; P35711; -.
DR BMRB; P35711; -.
DR SMR; P35711; -.
DR BioGRID; 112543; 158.
DR IntAct; P35711; 147.
DR MINT; P35711; -.
DR STRING; 9606.ENSP00000398273; -.
DR GlyGen; P35711; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35711; -.
DR PhosphoSitePlus; P35711; -.
DR BioMuta; SOX5; -.
DR DMDM; 30179883; -.
DR EPD; P35711; -.
DR jPOST; P35711; -.
DR MassIVE; P35711; -.
DR MaxQB; P35711; -.
DR PaxDb; P35711; -.
DR PeptideAtlas; P35711; -.
DR PRIDE; P35711; -.
DR ProteomicsDB; 26824; -.
DR ProteomicsDB; 55137; -. [P35711-1]
DR ProteomicsDB; 55138; -. [P35711-2]
DR ProteomicsDB; 55139; -. [P35711-3]
DR ProteomicsDB; 55140; -. [P35711-4]
DR TopDownProteomics; P35711-1; -. [P35711-1]
DR Antibodypedia; 12481; 248 antibodies from 30 providers.
DR DNASU; 6660; -.
DR Ensembl; ENST00000381381.6; ENSP00000370788.2; ENSG00000134532.19. [P35711-4]
DR Ensembl; ENST00000396007.6; ENSP00000379328.2; ENSG00000134532.19. [P35711-3]
DR Ensembl; ENST00000451604.7; ENSP00000398273.2; ENSG00000134532.19. [P35711-1]
DR Ensembl; ENST00000545921.5; ENSP00000443520.1; ENSG00000134532.19. [P35711-5]
DR Ensembl; ENST00000646273.1; ENSP00000493866.1; ENSG00000134532.19. [P35711-4]
DR GeneID; 6660; -.
DR KEGG; hsa:6660; -.
DR MANE-Select; ENST00000451604.7; ENSP00000398273.2; NM_006940.6; NP_008871.3.
DR UCSC; uc001rfv.5; human. [P35711-1]
DR CTD; 6660; -.
DR DisGeNET; 6660; -.
DR GeneCards; SOX5; -.
DR HGNC; HGNC:11201; SOX5.
DR HPA; ENSG00000134532; Tissue enhanced (testis).
DR MalaCards; SOX5; -.
DR MIM; 604975; gene.
DR MIM; 616803; phenotype.
DR neXtProt; NX_P35711; -.
DR OpenTargets; ENSG00000134532; -.
DR Orphanet; 313884; 12p12.1 microdeletion syndrome.
DR Orphanet; 313892; Developmental and speech delay due to SOX5 deficiency.
DR PharmGKB; PA36038; -.
DR VEuPathDB; HostDB:ENSG00000134532; -.
DR eggNOG; KOG0528; Eukaryota.
DR GeneTree; ENSGT00940000156122; -.
DR HOGENOM; CLU_018522_0_0_1; -.
DR InParanoid; P35711; -.
DR OMA; PPPKSKX; -.
DR OrthoDB; 465521at2759; -.
DR PhylomeDB; P35711; -.
DR TreeFam; TF320471; -.
DR PathwayCommons; P35711; -.
DR SignaLink; P35711; -.
DR SIGNOR; P35711; -.
DR BioGRID-ORCS; 6660; 17 hits in 1102 CRISPR screens.
DR ChiTaRS; SOX5; human.
DR GeneWiki; SOX5; -.
DR GenomeRNAi; 6660; -.
DR Pharos; P35711; Tbio.
DR PRO; PR:P35711; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P35711; protein.
DR Bgee; ENSG00000134532; Expressed in cortical plate and 150 other tissues.
DR ExpressionAtlas; P35711; baseline and differential.
DR Genevisible; P35711; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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:0055059; P:asymmetric neuroblast division; IGI: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:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
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:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
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; Coiled coil; Differentiation; DNA-binding;
KW Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..763
FT /note="Transcription factor SOX-5"
FT /id="PRO_0000048726"
FT DNA_BIND 556..624
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 193..274
FT /evidence="ECO:0000255"
FT COILED 448..515
FT /evidence="ECO:0000255"
FT COMPBIAS 77..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..750
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..386
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007262"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12406576,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007261"
FT VAR_SEQ 1..13
FT /note="MLTDPDLPQEFER -> MSV (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045997"
FT VAR_SEQ 387..388
FT /note="SK -> MH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007263"
FT VAR_SEQ 388..495
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007264"
FT VARIANT 362
FT /note="Q -> P (in a patient with amyotrophic lateral
FT sclerosis; dbSNP:rs144670919)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065754"
FT CONFLICT 276
FT /note="P -> L (in Ref. 2; BAH14086)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="Q -> H (in Ref. 2; BAB85048)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="N -> S (in Ref. 2; BAB85048)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="E -> Q (in Ref. 5; AAB49537)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="E -> G (in Ref. 2; BAB85048)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="S -> N (in Ref. 2; BAC05353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 763 AA; 84026 MW; 02B5B13429A59CAA CRC64;
MLTDPDLPQE FERMSSKRPA SPYGEADGEV AMVTSRQKVE EEESDGLPAF HLPLHVSFPN
KPHSEEFQPV SLLTQETCGH RTPTSQHNTM EVDGNKVMSS FAPHNSSTSP QKAEEGGRQS
GESLSSTALG TPERRKGSLA DVVDTLKQRK MEELIKNEPE ETPSIEKLLS KDWKDKLLAM
GSGNFGEIKG TPESLAEKER QLMGMINQLT SLREQLLAAH DEQKKLAASQ IEKQRQQMEL
AKQQQEQIAR QQQQLLQQQH KINLLQQQIQ VQGQLPPLMI PVFPPDQRTL AAAAQQGFLL
PPGFSYKAGC SDPYPVQLIP TTMAAAAAAT PGLGPLQLQQ LYAAQLAAMQ VSPGGKLPGI
PQGNLGAAVS PTSIHTDKST NSPPPKSKDE VAQPLNLSAK PKTSDGKSPT SPTSPHMPAL
RINSGAGPLK ASVPAALASP SARVSTIGYL NDHDAVTKAI QEARQMKEQL RREQQVLDGK
VAVVNSLGLN NCRTEKEKTT LESLTQQLAV KQNEEGKFSH AMMDFNLSGD SDGSAGVSES
RIYRESRGRG SNEPHIKRPM NAFMVWAKDE RRKILQAFPD MHNSNISKIL GSRWKAMTNL
EKQPYYEEQA RLSKQHLEKY PDYKYKPRPK RTCLVDGKKL RIGEYKAIMR NRRQEMRQYF
NVGQQAQIPI ATAGVVYPGA IAMAGMPSPH LPSEHSSVSS SPEPGMPVIQ STYGVKGEEP
HIKEEIQAED INGEIYDEYD EEEDDPDVDY GSDSENHIAG QAN
