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 24-JAN-2024, entry version 200. 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}; 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; 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; 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. 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; 9606-ENSP00000398273; -. DR PeptideAtlas; 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 Pumba; P35711; -. DR TopDownProteomics; P35711-1; -. [P35711-1] DR Antibodypedia; 12481; 284 antibodies from 30 providers. DR DNASU; 6660; -. DR Ensembl; ENST00000396007.6; ENSP00000379328.2; ENSG00000134532.20. [P35711-3] DR Ensembl; ENST00000451604.7; ENSP00000398273.2; ENSG00000134532.20. [P35711-1] DR Ensembl; ENST00000545921.5; ENSP00000443520.1; ENSG00000134532.20. [P35711-5] DR Ensembl; ENST00000646273.1; ENSP00000493866.1; ENSG00000134532.20. [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 AGR; HGNC:11201; -. 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; 2902801at2759; -. DR PhylomeDB; P35711; -. DR TreeFam; TF320471; -. DR PathwayCommons; P35711; -. DR SignaLink; P35711; -. DR SIGNOR; P35711; -. DR BioGRID-ORCS; 6660; 17 hits in 1180 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 152 other cell types or tissues. DR ExpressionAtlas; P35711; baseline and differential. 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 CDD; cd22042; HMG-box_EGL13-like; 1. DR Gene3D; 1.10.30.10; High mobility group box domain; 1. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR PANTHER; PTHR45789; FI18025P1; 1. DR PANTHER; PTHR45789:SF3; TRANSCRIPTION FACTOR SOX-5; 1. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF47095; HMG-box; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. DR Genevisible; P35711; HS. 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 //