TEAD3_HUMAN
ID TEAD3_HUMAN Reviewed; 435 AA.
AC Q99594; O95910; Q5BJG7; Q8N6Y4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Transcriptional enhancer factor TEF-5;
DE AltName: Full=DTEF-1;
DE AltName: Full=TEA domain family member 3;
DE Short=TEAD-3;
GN Name=TEAD3; Synonyms=TEAD5, TEF5;
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].
RX PubMed=9148898; DOI=10.1074/jbc.272.20.12928;
RA Jacquemin P., Martial J.A., Davidson I.;
RT "Human TEF-5 is preferentially expressed in placenta and binds to multiple
RT functional elements of the human chorionic somatomammotropin-B gene
RT enhancer.";
RL J. Biol. Chem. 272:12928-12937(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and PNS;
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 [4]
RP FUNCTION, AND INTERACTION WITH YAP1.
RX PubMed=18579750; DOI=10.1101/gad.1664408;
RA Zhao B., Ye X., Yu J., Li L., Li W., Li S., Yu J., Lin J.D., Wang C.Y.,
RA Chinnaiyan A.M., Lai Z.C., Guan K.L.;
RT "TEAD mediates YAP-dependent gene induction and growth control.";
RL Genes Dev. 22:1962-1971(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH WWTR1.
RX PubMed=19324877; DOI=10.1074/jbc.m900843200;
RA Zhang H., Liu C.Y., Zha Z.Y., Zhao B., Yao J., Zhao S., Xiong Y., Lei Q.Y.,
RA Guan K.L.;
RT "TEAD transcription factors mediate the function of TAZ in cell growth and
RT epithelial-mesenchymal transition.";
RL J. Biol. Chem. 284:13355-13362(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
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 to multiple functional elements of
CC the human chorionic somatomammotropin-B gene enhancer.
CC {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}.
CC -!- SUBUNIT: Interacts with YAP1 and WWTR1/TAZ.
CC {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}.
CC -!- INTERACTION:
CC Q99594; Q99990: VGLL1; NbExp=4; IntAct=EBI-746720, EBI-11983165;
CC Q99594; Q8N8G2: VGLL2; NbExp=3; IntAct=EBI-746720, EBI-10267981;
CC Q99594; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-746720, EBI-11957216;
CC Q99594; Q14135: VGLL4; NbExp=3; IntAct=EBI-746720, EBI-5278589;
CC Q99594; Q9GZV5: WWTR1; NbExp=3; IntAct=EBI-746720, EBI-747743;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the placenta.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27877.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.; Evidence={ECO:0000305};
CC Sequence=AAH91488.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.; Evidence={ECO:0000305};
CC Sequence=CAA64213.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.; Evidence={ECO:0000305};
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DR EMBL; X94439; CAA64213.2; ALT_SEQ; mRNA.
DR EMBL; AL022721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027877; AAH27877.1; ALT_SEQ; mRNA.
DR EMBL; BC091488; AAH91488.2; ALT_SEQ; mRNA.
DR CCDS; CCDS47414.1; -.
DR RefSeq; NP_003205.2; NM_003214.3.
DR PDB; 5EMW; X-ray; 2.55 A; A/B/C/D=219-435.
DR PDB; 7CNL; X-ray; 2.60 A; A/B/C/D=216-435.
DR PDBsum; 5EMW; -.
DR PDBsum; 7CNL; -.
DR AlphaFoldDB; Q99594; -.
DR SMR; Q99594; -.
DR BioGRID; 112864; 30.
DR DIP; DIP-50657N; -.
DR IntAct; Q99594; 26.
DR MINT; Q99594; -.
DR STRING; 9606.ENSP00000345772; -.
DR BindingDB; Q99594; -.
DR ChEMBL; CHEMBL4523435; -.
DR GlyGen; Q99594; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99594; -.
DR PhosphoSitePlus; Q99594; -.
DR SwissPalm; Q99594; -.
DR BioMuta; TEAD3; -.
DR DMDM; 2501157; -.
DR EPD; Q99594; -.
DR jPOST; Q99594; -.
DR MassIVE; Q99594; -.
DR MaxQB; Q99594; -.
DR PaxDb; Q99594; -.
DR PeptideAtlas; Q99594; -.
DR PRIDE; Q99594; -.
DR ProteomicsDB; 78349; -.
DR Antibodypedia; 6662; 262 antibodies from 30 providers.
DR DNASU; 7005; -.
DR Ensembl; ENST00000338863.13; ENSP00000345772.8; ENSG00000007866.22.
DR GeneID; 7005; -.
DR KEGG; hsa:7005; -.
DR MANE-Select; ENST00000338863.13; ENSP00000345772.8; NM_003214.4; NP_003205.2.
DR UCSC; uc063obu.1; human.
DR CTD; 7005; -.
DR DisGeNET; 7005; -.
DR GeneCards; TEAD3; -.
DR HGNC; HGNC:11716; TEAD3.
DR HPA; ENSG00000007866; Low tissue specificity.
DR MIM; 603170; gene.
DR neXtProt; NX_Q99594; -.
DR OpenTargets; ENSG00000007866; -.
DR PharmGKB; PA36434; -.
DR VEuPathDB; HostDB:ENSG00000007866; -.
DR eggNOG; KOG3841; Eukaryota.
DR GeneTree; ENSGT00950000182956; -.
DR HOGENOM; CLU_012515_0_1_1; -.
DR InParanoid; Q99594; -.
DR OrthoDB; 823827at2759; -.
DR PhylomeDB; Q99594; -.
DR TreeFam; TF313443; -.
DR PathwayCommons; Q99594; -.
DR Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
DR SignaLink; Q99594; -.
DR SIGNOR; Q99594; -.
DR BioGRID-ORCS; 7005; 93 hits in 1104 CRISPR screens.
DR ChiTaRS; TEAD3; human.
DR GeneWiki; TEAD3; -.
DR GenomeRNAi; 7005; -.
DR Pharos; Q99594; Tbio.
DR PRO; PR:Q99594; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q99594; protein.
DR Bgee; ENSG00000007866; Expressed in muscle layer of sigmoid colon and 169 other tissues.
DR ExpressionAtlas; Q99594; baseline and differential.
DR Genevisible; Q99594; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IGI:UniProtKB.
DR GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
DR GO; GO:0035329; P:hippo signaling; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 6.10.20.40; -; 1.
DR InterPro; IPR000818; TEA/ATTS_dom.
DR InterPro; IPR038096; TEA/ATTS_sf.
DR InterPro; IPR027253; TEF-5.
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 PIRSF; PIRSF500720; TEF-5; 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 3D-structure; Acetylation; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..435
FT /note="Transcriptional enhancer factor TEF-5"
FT /id="PRO_0000205934"
FT DNA_BIND 28..104
FT /note="TEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..435
FT /note="Transcriptional activation"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 254
FT /note="T -> M (in dbSNP:rs35080860)"
FT /id="VAR_052278"
FT STRAND 226..239
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:7CNL"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:5EMW"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:5EMW"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5EMW"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:5EMW"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 314..325
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 328..337
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 340..350
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 357..366
FT /evidence="ECO:0007829|PDB:5EMW"
FT HELIX 370..379
FT /evidence="ECO:0007829|PDB:5EMW"
FT HELIX 384..391
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 394..402
FT /evidence="ECO:0007829|PDB:5EMW"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 408..418
FT /evidence="ECO:0007829|PDB:5EMW"
FT STRAND 426..433
FT /evidence="ECO:0007829|PDB:5EMW"
SQ SEQUENCE 435 AA; 48676 MW; 9F8E7900EB13D4DC CRC64;
MASNSWNASS SPGEAREDGP EGLDKGLDND AEGVWSPDIE QSFQEALAIY PPCGRRKIIL
SDEGKMYGRN ELIARYIKLR TGKTRTRKQV SSHIQVLARK KVREYQVGIK AMNLDQVSKD
KALQSMASMS SAQIVSASVL QNKFSPPSPL PQAVFSTSSR FWSSPPLLGQ QPGPSQDIKP
FAQPAYPIQP PLPPTLSSYE PLAPLPSAAA SVPVWQDRTI ASSRLRLLEY SAFMEVQRDP
DTYSKHLFVH IGQTNPAFSD PPLEAVDVRQ IYDKFPEKKG GLKELYEKGP PNAFFLVKFW
ADLNSTIQEG PGAFYGVSSQ YSSADSMTIS VSTKVCSFGK QVVEKVETEY ARLENGRFVY
RIHRSPMCEY MINFIHKLKH LPEKYMMNSV LENFTILQVV TSRDSQETLL VIAFVFEVST
SEHGAQHHVY KLVKD
