SOX7_HUMAN
ID SOX7_HUMAN Reviewed; 388 AA.
AC Q9BT81; B4DKV0; Q53YD0;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Transcription factor SOX-7;
GN Name=SOX7;
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), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Fetal thymus;
RX PubMed=11691915; DOI=10.1093/nar/29.21.4274;
RA Takash W., Canizares J., Bonneaud N., Poulat F., Mattei M.-G., Jay P.,
RA Berta P.;
RT "SOX7 transcription factor: sequence, chromosomal localisation, expression,
RT transactivation and interference with Wnt signalling.";
RL Nucleic Acids Res. 29:4274-4283(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 FUNCTION, INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18819930; DOI=10.1158/1541-7786.mcr-07-2175;
RA Guo L., Zhong D., Lau S., Liu X., Dong X.Y., Sun X., Yang V.W.,
RA Vertino P.M., Moreno C.S., Varma V., Dong J.T., Zhou W.;
RT "Sox7 Is an independent checkpoint for beta-catenin function in prostate
RT and colon epithelial cells.";
RL Mol. Cancer Res. 6:1421-1430(2008).
CC -!- FUNCTION: Binds to and activates the CDH5 promoter, hence plays a role
CC in the transcriptional regulation of genes expressed in the hemogenic
CC endothelium and blocks further differentiation into blood precursors
CC (By similarity). May be required for the survival of both hematopoietic
CC and endothelial precursors during specification (By similarity).
CC Competes with GATA4 for binding and activation of the FGF3 promoter (By
CC similarity). Represses Wnt/beta-catenin-stimulated transcription,
CC probably by targeting CTNNB1 to proteasomal degradation. Binds the DNA
CC sequence 5'-AACAAT-3'. {ECO:0000250, ECO:0000269|PubMed:18819930}.
CC -!- SUBUNIT: Interacts with CTNNB1/beta-catenin; this interaction may lead
CC to the proteasomal degradation of active CTNNB1 and thus inhibition of
CC Wnt/beta-catenin-stimulated transcription.
CC {ECO:0000269|PubMed:18819930}.
CC -!- INTERACTION:
CC Q9BT81; Q92870-2: APBB2; NbExp=3; IntAct=EBI-7239117, EBI-21535880;
CC Q9BT81; O76003: GLRX3; NbExp=3; IntAct=EBI-7239117, EBI-374781;
CC Q9BT81; P42858: HTT; NbExp=15; IntAct=EBI-7239117, EBI-466029;
CC Q9BT81; Q8N9R8: SCAI; NbExp=3; IntAct=EBI-7239117, EBI-4395514;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC Cytoplasm {ECO:0000269|PubMed:18819930}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BT81-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BT81-2; Sequence=VSP_056667;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues.
CC Present both in mesenchymal and epithelial cells in some adult tissues,
CC including colon. Tends to be down-regulated in prostate adenocarcinomas
CC and colorectal tumors due to promoter hypermethylation.
CC {ECO:0000269|PubMed:11691915, ECO:0000269|PubMed:18819930}.
CC -!- DEVELOPMENTAL STAGE: In 8 week-old embryo, expressed in brain, tongue,
CC heart, liver, lung and vertebrae. {ECO:0000269|PubMed:11691915}.
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DR EMBL; AJ409320; CAC84226.1; -; mRNA.
DR EMBL; BT006693; AAP35339.1; -; mRNA.
DR EMBL; AK055556; BAB70955.1; -; mRNA.
DR EMBL; AK296724; BAG59312.1; -; mRNA.
DR EMBL; AC011008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC071947; AAH71947.1; -; mRNA.
DR CCDS; CCDS5977.1; -. [Q9BT81-1]
DR RefSeq; NP_113627.1; NM_031439.3. [Q9BT81-1]
DR AlphaFoldDB; Q9BT81; -.
DR SMR; Q9BT81; -.
DR BioGRID; 123691; 7.
DR IntAct; Q9BT81; 80.
DR MINT; Q9BT81; -.
DR STRING; 9606.ENSP00000301921; -.
DR iPTMnet; Q9BT81; -.
DR PhosphoSitePlus; Q9BT81; -.
DR BioMuta; SOX7; -.
DR DMDM; 20532272; -.
DR EPD; Q9BT81; -.
DR jPOST; Q9BT81; -.
DR MassIVE; Q9BT81; -.
DR MaxQB; Q9BT81; -.
DR PaxDb; Q9BT81; -.
DR PeptideAtlas; Q9BT81; -.
DR PRIDE; Q9BT81; -.
DR ProteomicsDB; 4490; -.
DR ProteomicsDB; 78959; -. [Q9BT81-1]
DR Antibodypedia; 1821; 223 antibodies from 30 providers.
DR DNASU; 83595; -.
DR Ensembl; ENST00000304501.2; ENSP00000301921.1; ENSG00000171056.8. [Q9BT81-1]
DR Ensembl; ENST00000646538.2; ENSP00000495029.1; ENSG00000285438.2. [Q9BT81-1]
DR GeneID; 83595; -.
DR KEGG; hsa:83595; -.
DR MANE-Select; ENST00000304501.2; ENSP00000301921.1; NM_031439.4; NP_113627.1.
DR UCSC; uc003wtf.5; human. [Q9BT81-1]
DR CTD; 83595; -.
DR DisGeNET; 83595; -.
DR GeneCards; SOX7; -.
DR HGNC; HGNC:18196; SOX7.
DR HPA; ENSG00000171056; Tissue enhanced (vagina).
DR MIM; 612202; gene.
DR neXtProt; NX_Q9BT81; -.
DR OpenTargets; ENSG00000171056; -.
DR OpenTargets; ENSG00000258724; -.
DR PharmGKB; PA38307; -.
DR VEuPathDB; HostDB:ENSG00000171056; -.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000161092; -.
DR HOGENOM; CLU_044994_0_0_1; -.
DR InParanoid; Q9BT81; -.
DR OMA; ESFECPG; -.
DR OrthoDB; 1042753at2759; -.
DR PhylomeDB; Q9BT81; -.
DR TreeFam; TF321918; -.
DR PathwayCommons; Q9BT81; -.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR SignaLink; Q9BT81; -.
DR SIGNOR; Q9BT81; -.
DR BioGRID-ORCS; 83595; 17 hits in 1087 CRISPR screens.
DR ChiTaRS; SOX7; human.
DR GenomeRNAi; 83595; -.
DR Pharos; Q9BT81; Tbio.
DR PRO; PR:Q9BT81; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9BT81; protein.
DR Bgee; ENSG00000171056; Expressed in lower esophagus mucosa and 97 other tissues.
DR Genevisible; Q9BT81; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001706; P:endoderm formation; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR033392; Sox7/17/18_central.
DR InterPro; IPR021934; Sox_C.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF12067; Sox17_18_mid; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS51516; SOX_C; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..388
FT /note="Transcription factor SOX-7"
FT /id="PRO_0000048731"
FT DOMAIN 268..388
FT /note="Sox C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00849"
FT DNA_BIND 45..113
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 20..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..79
FT /note="MASLLGAYPWPEGLECPALDAELSDGQSPPAVPRPPGDKGSESRIRRPMNAF
FT MVWAKDERKRLAVQNPDLHNAELSKML -> MSMLAERRRKQKWAVDPQNTAWSNDDSK
FT FGQRMLEKMGWSKGKGLGAQEQGATDHIKVQVKNNHLGLGATINNEDNWIAHQDDFNQL
FT LAELNTCHGQETTDSSDKKEKKSFSLEEKSKISKNRVHYMKFTK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056667"
SQ SEQUENCE 388 AA; 42197 MW; DBA0EFE440DC2A74 CRC64;
MASLLGAYPW PEGLECPALD AELSDGQSPP AVPRPPGDKG SESRIRRPMN AFMVWAKDER
KRLAVQNPDL HNAELSKMLG KSWKALTLSQ KRPYVDEAER LRLQHMQDYP NYKYRPRRKK
QAKRLCKRVD PGFLLSSLSR DQNALPEKRS GSRGALGEKE DRGEYSPGTA LPSLRGCYHE
GPAGGGGGGT PSSVDTYPYG LPTPPEMSPL DVLEPEQTFF SSPCQEEHGH PRRIPHLPGH
PYSPEYAPSP LHCSHPLGSL ALGQSPGVSM MSPVPGCPPS PAYYSPATYH PLHSNLQAHL
GQLSPPPEHP GFDALDQLSQ VELLGDMDRN EFDQYLNTPG HPDSATGAMA LSGHVPVSQV
TPTGPTETSL ISVLADATAT YYNSYSVS
