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TEAD1_MOUSE
ID   TEAD1_MOUSE             Reviewed;         426 AA.
AC   P30051;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   25-MAY-2022, entry version 174.
DE   RecName: Full=Transcriptional enhancer factor TEF-1;
DE   AltName: Full=NTEF-1;
DE   AltName: Full=Protein GT-IIC;
DE   AltName: Full=TEA domain family member 1;
DE            Short=TEAD-1;
DE   AltName: Full=Transcription factor 13;
DE            Short=TCF-13;
GN   Name=Tead1; Synonyms=Tcf13, Tef-1, Tef1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8441689; DOI=10.1093/nar/21.3.747;
RA   Blatt C., Depamphilis M.L.;
RT   "Striking homology between mouse and human transcription enhancer factor-1
RT   (TEF-1).";
RL   Nucleic Acids Res. 21:747-748(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Heart;
RX   PubMed=8396764; DOI=10.1093/nar/21.17.4103;
RA   Shimizu N.N., Smith G., Izumo S.;
RT   "Both a ubiquitous factor mTEF-1 and a distinct muscle-specific factor bind
RT   to the M-CAT motif of the myosin heavy chain beta gene.";
RL   Nucleic Acids Res. 21:4103-4110(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7958896; DOI=10.1101/gad.8.19.2293;
RA   Chen Z., Friedrich G.A., Soriano P.;
RT   "Transcriptional enhancer factor 1 disruption by a retroviral gene trap
RT   leads to heart defects and embryonic lethality in mice.";
RL   Genes Dev. 8:2293-2301(1994).
CC   -!- FUNCTION: Transcription factor which plays a key role in the Hippo
CC       signaling pathway, a pathway involved in organ size control and tumor
CC       suppression by restricting proliferation and promoting apoptosis. The
CC       core of this pathway is composed of a kinase cascade wherein MST1/MST2,
CC       in complex with its regulatory protein SAV1, phosphorylates and
CC       activates LATS1/2 in complex with its regulatory protein MOB1, which in
CC       turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ.
CC       Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby
CC       regulating cell proliferation, migration and epithelial mesenchymal
CC       transition (EMT) induction. Binds specifically and cooperatively to the
CC       SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates
CC       transcription in vivo in a cell-specific manner. The activation
CC       function appears to be mediated by a limiting cell-specific
CC       transcriptional intermediary factor (TIF). Involved in cardiac
CC       development. Binds to the M-CAT motif (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with YAP1 and WWTR1/TAZ. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P30051; P46938: Yap1; NbExp=4; IntAct=EBI-3953905, EBI-1211949;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: In developing skeletal muscle and myocardium, in
CC       mitotic neuroblasts both in the brain and spinal cord. At later stages
CC       of embryogenesis expressed in several developing structures such as the
CC       olfactory system, the intestine, and the kidney.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA40410.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATT isoleucine codon.; Evidence={ECO:0000305};
CC       Sequence=AAA40411.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATT isoleucine codon.; Evidence={ECO:0000305};
CC       Sequence=AAB32420.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATT isoleucine codon.; Evidence={ECO:0000305};
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DR   EMBL; L06865; AAA40410.1; ALT_SEQ; mRNA.
DR   EMBL; L13853; AAA40411.1; ALT_SEQ; mRNA.
DR   EMBL; S74227; AAB32420.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS52367.1; -.
DR   PIR; A54882; A54882.
DR   PIR; S40779; S40779.
DR   PIR; S41767; S41767.
DR   AlphaFoldDB; P30051; -.
DR   SMR; P30051; -.
DR   BioGRID; 204098; 16.
DR   ComplexPortal; CPX-394; YAP1-TEAD1 complex.
DR   CORUM; P30051; -.
DR   DIP; DIP-41748N; -.
DR   IntAct; P30051; 2.
DR   MINT; P30051; -.
DR   STRING; 10090.ENSMUSP00000060671; -.
DR   iPTMnet; P30051; -.
DR   PhosphoSitePlus; P30051; -.
DR   SwissPalm; P30051; -.
DR   MaxQB; P30051; -.
DR   PRIDE; P30051; -.
DR   ProteomicsDB; 263267; -.
DR   DNASU; 21676; -.
DR   UCSC; uc009jgz.2; mouse.
DR   MGI; MGI:101876; Tead1.
DR   eggNOG; KOG3841; Eukaryota.
DR   InParanoid; P30051; -.
DR   PhylomeDB; P30051; -.
DR   Reactome; R-MMU-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR   Reactome; R-MMU-8951671; RUNX3 regulates YAP1-mediated transcription.
DR   BioGRID-ORCS; 21676; 6 hits in 74 CRISPR screens.
DR   ChiTaRS; Tead1; mouse.
DR   PRO; PR:P30051; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P30051; protein.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR   GO; GO:0140552; C:TEAD-YAP complex; IPI:ComplexPortal.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IDA:MGI.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; IGI:MGI.
DR   GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0035329; P:hippo signaling; IGI:MGI.
DR   GO; GO:0048368; P:lateral mesoderm development; IGI:MGI.
DR   GO; GO:0030903; P:notochord development; IGI:MGI.
DR   GO; GO:0048339; P:paraxial mesoderm development; IGI:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:1902459; P:positive regulation of stem cell population maintenance; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
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; IDA:MGI.
DR   GO; GO:0014883; P:transition between fast and slow fiber; IDA:MGI.
DR   Gene3D; 6.10.20.40; -; 1.
DR   InterPro; IPR000818; TEA/ATTS_dom.
DR   InterPro; IPR038096; TEA/ATTS_sf.
DR   InterPro; IPR016361; TEF_metazoa.
DR   InterPro; IPR041086; YBD.
DR   Pfam; PF01285; TEA; 1.
DR   Pfam; PF17725; YBD; 1.
DR   PIRSF; PIRSF002603; TEF; 1.
DR   PRINTS; PR00065; TEADOMAIN.
DR   SMART; SM00426; TEA; 1.
DR   PROSITE; PS00554; TEA_1; 1.
DR   PROSITE; PS51088; TEA_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..426
FT                   /note="Transcriptional enhancer factor TEF-1"
FT                   /id="PRO_0000205931"
FT   DNA_BIND        28..104
FT                   /note="TEA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..426
FT                   /note="Transcriptional activation"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P28347"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28347"
FT   CONFLICT        9..10
FT                   /note="SE -> RR (in Ref. 3; AAB32420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="K -> KVTSM (in Ref. 2; AAA40411)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  47948 MW;  AEC83DAD2DDAF07A CRC64;
     MEPSSWSGSE SPAENMERMS DSADKPIDND AEGVWSPDIE QSFQEALAIY PPCGRRKIIL
     SDEGKMYGRN ELIARYIKLR TGKTRTRKQV SSHIQVLARR KSRDFHSKLK DQTAKDKALQ
     HMAAMSSAQI VSATAIHNKL GLPGIPRPTF PGGPGFWPGM IQTGQPGSSQ DVKPFVQQAY
     PIQPAVTAPI PGFEPTSAPA PSVPAWQGRS IGTTKLRLVE FSAFLEQQRD PDSYNKHLFV
     HIGHANHSYS DPLLESVDIR QIYDKFPEKK GGLKELFGKG PQNAFFLVKF WADLNCNIQD
     DAGAFYGVSS QYESSENMTV TCSTKVCSFG KQVVEKVETE YARFENGRFV YRINRSPMCE
     YMINFIHKLK HLPEKYMMNS VLENFTILLV VTNRDTQETL LCMACVFEVS NSEHGAQHHI
     YRLVKD
 
 
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