SCX_HUMAN
ID SCX_HUMAN Reviewed; 201 AA.
AC Q7RTU7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Basic helix-loop-helix transcription factor scleraxis;
DE AltName: Full=Class A basic helix-loop-helix protein 41;
DE Short=bHLHa41;
DE AltName: Full=Class A basic helix-loop-helix protein 48;
DE Short=bHLHa48;
GN Name=SCX; Synonyms=BHLHA41, BHLHA48, SCXA, SCXB;
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 [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 [2]
RP IDENTIFICATION.
RX PubMed=12617822; DOI=10.1016/s0925-4773(02)00390-8;
RA McLellan A.S., Langlands K., Kealey T.;
RT "Exhaustive identification of human class II basic helix-loop-helix
RT proteins by virtual library screening.";
RL Gene Expr. Patterns 2:329-335(2002).
CC -!- FUNCTION: Plays an early essential role in mesoderm formation, as well
CC as a later role in formation of somite-derived chondrogenic lineages.
CC {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Dimerizes and binds the E-box consensus sequence with E12 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q7RTU7; P13349: MYF5; NbExp=3; IntAct=EBI-17492262, EBI-17491620;
CC Q7RTU7; O43639: NCK2; NbExp=3; IntAct=EBI-17492262, EBI-713635;
CC Q7RTU7; P15884-3: TCF4; NbExp=3; IntAct=EBI-17492262, EBI-13636688;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR EMBL; AC145291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK000280; DAA00239.1; -; Genomic_DNA.
DR CCDS; CCDS43779.1; -.
DR RefSeq; NP_001073983.1; NM_001080514.2.
DR RefSeq; XP_006716679.1; XM_006716616.2.
DR AlphaFoldDB; Q7RTU7; -.
DR SMR; Q7RTU7; -.
DR BioGRID; 568157; 6.
DR IntAct; Q7RTU7; 3.
DR STRING; 9606.ENSP00000476384; -.
DR iPTMnet; Q7RTU7; -.
DR PhosphoSitePlus; Q7RTU7; -.
DR BioMuta; SCX; -.
DR DMDM; 74749943; -.
DR MassIVE; Q7RTU7; -.
DR PaxDb; Q7RTU7; -.
DR PeptideAtlas; Q7RTU7; -.
DR PRIDE; Q7RTU7; -.
DR ProteomicsDB; 68909; -.
DR Antibodypedia; 72507; 88 antibodies from 19 providers.
DR DNASU; 642658; -.
DR Ensembl; ENST00000567180.3; ENSP00000476384.1; ENSG00000260428.3.
DR GeneID; 642658; -.
DR KEGG; hsa:642658; -.
DR MANE-Select; ENST00000567180.3; ENSP00000476384.1; NM_001080514.3; NP_001073983.1.
DR UCSC; uc003zbn.4; human.
DR CTD; 642658; -.
DR GeneCards; SCX; -.
DR HGNC; HGNC:32322; SCX.
DR HPA; ENSG00000260428; Tissue enhanced (pituitary gland, thyroid gland).
DR MIM; 609067; gene.
DR neXtProt; NX_Q7RTU7; -.
DR OpenTargets; ENSG00000260428; -.
DR PharmGKB; PA142670943; -.
DR VEuPathDB; HostDB:ENSG00000260428; -.
DR eggNOG; KOG4029; Eukaryota.
DR GeneTree; ENSGT00940000161897; -.
DR HOGENOM; CLU_115077_0_0_1; -.
DR InParanoid; Q7RTU7; -.
DR OMA; PPKEYRQ; -.
DR OrthoDB; 1511100at2759; -.
DR PhylomeDB; Q7RTU7; -.
DR TreeFam; TF315153; -.
DR PathwayCommons; Q7RTU7; -.
DR SignaLink; Q7RTU7; -.
DR SIGNOR; Q7RTU7; -.
DR BioGRID-ORCS; 642658; 12 hits in 678 CRISPR screens.
DR GeneWiki; LOC642658; -.
DR GenomeRNAi; 642658; -.
DR Pharos; Q7RTU7; Tbio.
DR PRO; PR:Q7RTU7; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q7RTU7; protein.
DR Bgee; ENSG00000260428; Expressed in thymus and 92 other tissues.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0070888; F:E-box binding; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
DR GO; GO:0035993; P:deltoid tuberosity development; ISS:UniProtKB.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; ISS:UniProtKB.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0003188; P:heart valve formation; ISS:UniProtKB.
DR GO; GO:0003179; P:heart valve morphogenesis; ISS:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0061036; P:positive regulation of cartilage development; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:UniProtKB.
DR GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0061035; P:regulation of cartilage development; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061056; P:sclerotome development; IEA:Ensembl.
DR GO; GO:0060008; P:Sertoli cell differentiation; ISS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0035990; P:tendon cell differentiation; ISS:UniProtKB.
DR GO; GO:0035989; P:tendon development; ISS:UniProtKB.
DR GO; GO:0035992; P:tendon formation; ISS:UniProtKB.
DR GO; GO:0001894; P:tissue homeostasis; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..201
FT /note="Basic helix-loop-helix transcription factor
FT scleraxis"
FT /id="PRO_0000273317"
FT DOMAIN 75..127
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..170
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 21596 MW; 4FDF2D23F977032A CRC64;
MSFATLRPAP PGRYLYPEVS PLSEDEDRGS DSSGSDEKPC RVHAARCGLQ GARRRAGGRR
AGGGGPGGRP GREPRQRHTA NARERDRTNS VNTAFTALRT LIPTEPADRK LSKIETLRLA
SSYISHLGNV LLAGEACGDG QPCHSGPAFF HAARAGSPPP PPPPPPARDG ENTQPKQICT
FCLSNQRKLS KDRDRKTAIR S
