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Q15561 (TEAD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional enhancer factor TEF-3
Alternative name(s):
TEA domain family member 4
Short name=TEAD-4
Transcription factor 13-like 1
Transcription factor RTEF-1
Gene names
Name:TEAD4
Synonyms:RTEF1, TCF13L1, TEF3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and non-cooperatively to the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription. Binds to the M-CAT motif. Ref.8 Ref.9

Subunit structure

Interacts with YAP1 and WWTR1/TAZ. Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus.

Tissue specificity

Preferentially expressed in skeletal muscle. Lower levels in pancreas, placenta, and heart.

Sequence similarities

Contains 1 TEA DNA-binding domain.

Sequence caution

The sequence CAA64212.2 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WWTR1Q9GZV52EBI-747736,EBI-747743

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15561-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q15561-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-129: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q15561-3)

The sequence of this isoform differs from the canonical sequence as follows:
     119-161: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Transcriptional enhancer factor TEF-3
PRO_0000205937

Regions

DNA binding38 – 10568TEA

Natural variations

Alternative sequence1 – 129129Missing in isoform 2.
VSP_043099
Alternative sequence119 – 16143Missing in isoform 3.
VSP_045657
Natural variant3231P → S.
Corresponds to variant rs11550887 [ dbSNP | Ensembl ].
VAR_052279

Experimental info

Mutagenesis2661D → A: Reduced transforming ability. Ref.10
Mutagenesis2971K → A: Important loss of interaction with YAP1 and complete loss of transforming ability. Ref.10
Mutagenesis2991W → A: Important loss of interaction with YAP1 and complete loss of transforming ability. Ref.10
Mutagenesis3371F → A: Reduced interaction with YAP1. Ref.10
Mutagenesis3731F → A: Reduced transforming ability. Ref.10
Mutagenesis3801L → A: Reduced transforming ability. Ref.10
Mutagenesis3911E → A: Reduced transforming ability. Ref.10
Mutagenesis3931F → A: Reduced transforming ability. Ref.10
Mutagenesis4271H → A: Reduced transforming ability. Ref.10
Mutagenesis4291Y → A or H: Loss of interaction with YAP1 and also activation by YAP1. Ref.8 Ref.10
Mutagenesis4291Y → A: Important loss of interaction with YAP1 and complete loss of transforming ability. Ref.8 Ref.10
Sequence conflict391A → G in AAC50763. Ref.1
Sequence conflict1491A → R in AAC50763. Ref.1
Sequence conflict1721G → E in AAC50763. Ref.1
Sequence conflict218 – 2203SVA → RRG in AAC50763. Ref.1
Sequence conflict258 – 2592SD → LR in AAC50763. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 544DDFD86E88D9A8

FASTA43448,329
        10         20         30         40         50         60 
MEGTAGTITS NEWSSPTSPE GSTASGGSQA LDKPIDNDAE GVWSPDIEQS FQEALAIYPP 

        70         80         90        100        110        120 
CGRRKIILSD EGKMYGRNEL IARYIKLRTG KTRTRKQVSS HIQVLARRKA REIQAKLKDQ 

       130        140        150        160        170        180 
AAKDKALQSM AAMSSAQIIS ATAFHSSMAL ARGPGRPAVS GFWQGALPGQ AGTSHDVKPF 

       190        200        210        220        230        240 
SQQTYAVQPP LPLPGFESPA GPAPSPSAPP APPWQGRSVA SSKLWMLEFS AFLEQQQDPD 

       250        260        270        280        290        300 
TYNKHLFVHI GQSSPSYSDP YLEAVDIRQI YDKFPEKKGG LKDLFERGPS NAFFLVKFWA 

       310        320        330        340        350        360 
DLNTNIEDEG SSFYGVSSQY ESPENMIITC STKVCSFGKQ VVEKVETEYA RYENGHYSYR 

       370        380        390        400        410        420 
IHRSPLCEYM INFIHKLKHL PEKYMMNSVL ENFTILQVVT NRDTQETLLC IAYVFEVSAS 

       430 
EHGAQHHIYR LVKE 

« Hide

Isoform 2 [UniParc].

Checksum: 6A3BDF596BCE7797
Show »

FASTA30534,158
Isoform 3 [UniParc].

Checksum: 68B36C4E607ADB1E
Show »

FASTA39144,058

References

« Hide 'large scale' references
[1]"Cloning of human RTEF-1, a transcriptional enhancer factor-1-related gene preferentially expressed in skeletal muscle: evidence for an ancient multigene family."
Stewart A.F.R., Richard C.W. III, Suzow J., Stephan D., Weremowicz S., Morton C.C., Adra C.N.
Genomics 37:68-76(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Heart.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterine endothelium.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[6]"A novel family of developmentally regulated mammalian transcription factors containing the TEA/ATTS DNA binding domain."
Jacquemin P., Hwang J.-J., Martial J.A., Dolle P., Davidson I.
J. Biol. Chem. 271:21775-21785(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-434 (ISOFORM 1).
[7]"Role of MCAT binding factors during muscle hypertrophy."
Tsika R.W., Karasseva N.G., Tsika G.L.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-391 (ISOFORM 3).
[8]"TEAD mediates YAP-dependent gene induction and growth control."
Zhao B., Ye X., Yu J., Li L., Li W., Li S., Yu J., Lin J.D., Wang C.Y., Chinnaiyan A.M., Lai Z.C., Guan K.L.
Genes Dev. 22:1962-1971(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH YAP1, MUTAGENESIS OF TYR-429.
[9]"TEAD transcription factors mediate the function of TAZ in cell growth and epithelial-mesenchymal transition."
Zhang H., Liu C.Y., Zha Z.Y., Zhao B., Yao J., Zhao S., Xiong Y., Lei Q.Y., Guan K.L.
J. Biol. Chem. 284:13355-13362(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH WWTR1.
[10]"Structural basis of YAP recognition by TEAD4 in the hippo pathway."
Chen L., Chan S.W., Zhang X., Walsh M., Lim C.J., Hong W., Song H.
Genes Dev. 24:290-300(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YAP1, MUTAGENESIS OF ASP-266; LYS-297; TRP-299; PHE-337; PHE-373; LEU-380; GLU-391; PHE-393; HIS-427 AND TYR-429.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U63824 mRNA. Translation: AAC50763.1.
BX640921 mRNA. Translation: CAE45959.1.
AC005911 Genomic DNA. No translation available.
AC125807 Genomic DNA. No translation available.
AC131234 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88872.1.
BC015497 mRNA. Translation: AAH15497.2.
X94438 mRNA. Translation: CAA64212.2. Sequence problems.
AY101179 mRNA. Translation: AAM89497.1.
CCDSCCDS31729.1. [Q15561-1]
CCDS31730.1. [Q15561-3]
CCDS41737.1. [Q15561-2]
RefSeqNP_003204.2. NM_003213.3. [Q15561-1]
NP_958849.1. NM_201441.2. [Q15561-3]
NP_958851.1. NM_201443.2. [Q15561-2]
UniGeneHs.94865.

3D structure databases

ProteinModelPortalQ15561.
SMRQ15561. Positions 35-113, 217-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112863. 5 interactions.
IntActQ15561. 3 interactions.
MINTMINT-1460562.
STRING9606.ENSP00000352926.

PTM databases

PhosphoSiteQ15561.

Proteomic databases

MaxQBQ15561.
PaxDbQ15561.
PRIDEQ15561.

Protocols and materials databases

DNASU7004.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397122; ENSP00000380311; ENSG00000197905. [Q15561-2]
GeneID7004.
KEGGhsa:7004.
UCSCuc001qln.3. human. [Q15561-1]

Organism-specific databases

CTD7004.
GeneCardsGC12P003068.
HGNCHGNC:11717. TEAD4.
HPAHPA056896.
MIM601714. gene.
neXtProtNX_Q15561.
PharmGKBPA36435.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246992.
HOGENOMHOG000253933.
HOVERGENHBG056905.
InParanoidQ15561.
KOK09448.
PhylomeDBQ15561.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ15561.
BgeeQ15561.
CleanExHS_TEAD4.
GenevestigatorQ15561.

Family and domain databases

InterProIPR000818. TEA/ATTS.
IPR016361. TEF.
IPR027255. TEF-3.
[Graphical view]
PANTHERPTHR11834. PTHR11834. 1 hit.
PfamPF01285. TEA. 1 hit.
[Graphical view]
PIRSFPIRSF002603. TEF. 1 hit.
PIRSF500722. TEF-3. 1 hit.
PRINTSPR00065. TEADOMAIN.
SMARTSM00426. TEA. 1 hit.
[Graphical view]
PROSITEPS00554. TEA_1. 1 hit.
PS51088. TEA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTEAD4.
GenomeRNAi7004.
NextBio27354.
PROQ15561.
SOURCESearch...

Entry information

Entry nameTEAD4_HUMAN
AccessionPrimary (citable) accession number: Q15561
Secondary accession number(s): H0Y308 expand/collapse secondary AC list , Q6MZR9, Q8NEV5, Q92883, Q96BK2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM