TEAD1

TEA domain family member 1 (SV40 transcriptional enhancer factor)

PDB rendering based on 2hzd.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2HZD, 3KYS

Identifiers

Symbols

TEAD1 ; AA; NTEF-1; REF1; TCF-13; TCF13; TEAD-1; TEF-1

External IDs

OMIM: 189967 MGI: 101876 HomoloGene: 2418 GeneCards: TEAD1 Gene

Gene ontology
Molecular function	• DNA binding • sequence-specific DNA binding transcription factor activity • protein binding
Cellular component	• nucleus • nucleoplasm • nucleolus • cytoplasm • Golgi apparatus
Biological process	• regulation of transcription, DNA-templated • transcription initiation from RNA polymerase II promoter • gene expression • hippo signaling
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
12.7 – 12.97 Mb

Chr 7:
112.68 – 112.91 Mb

PubMed search

Transcriptional enhancer factor TEF-1 is a protein that in humans is encoded by the TEAD1 gene.^[1]^[2]^[3]^[4]

Interactions

TEAD1 has been shown to interact with MEF2C,^[5] Serum response factor^[6] and MAX.^[7]

References

↑ Xiao JH, Davidson I, Matthes H, Garnier JM, Chambon P (June 1991). "Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1". Cell 65 (4): 551–68. doi:10.1016/0092-8674(91)90088-G. PMID 1851669.
↑ Jacquemin P, Depetris D, Mattei MG, Martial JA, Davidson I (March 1999). "Localization of human transcription factor TEF-4 and TEF-5 (TEAD2, TEAD3) genes to chromosomes 19q13.3 and 6p21.2 using fluorescence in situ hybridization and radiation hybrid analysis". Genomics 55 (1): 127–9. doi:10.1006/geno.1998.5628. PMID 9889009.
↑ Fossdal R, Jonasson F, Kristjansdottir GT, Kong A, Stefansson H, Gosh S, Gulcher JR, Stefansson K (April 2004). "A novel TEAD1 mutation is the causative allele in Sveinsson's chorioretinal atrophy (helicoid peripapillary chorioretinal degeneration)". Hum Mol Genet 13 (9): 975–81. doi:10.1093/hmg/ddh106. PMID 15016762.
↑ "Entrez Gene: TEAD1 TEA domain family member 1 (SV40 transcriptional enhancer factor)".
↑ Maeda, Tomoji; Gupta Mahesh P; Stewart Alexandre F R (June 2002). "TEF-1 and MEF2 transcription factors interact to regulate muscle-specific promoters". Biochem. Biophys. Res. Commun. (United States) 294 (4): 791–7. doi:10.1016/S0006-291X(02)00556-9. ISSN 0006-291X. PMID 12061776.
↑ Gupta, M; Kogut P; Davis F J; Belaguli N S; Schwartz R J; Gupta M P (March 2001). "Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1". J. Biol. Chem. (United States) 276 (13): 10413–22. doi:10.1074/jbc.M008625200. ISSN 0021-9258. PMID 11136726.
↑ Gupta, M P; Amin C S; Gupta M; Hay N; Zak R (July 1997). "Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression". Mol. Cell. Biol. (UNITED STATES) 17 (7): 3924–36. ISSN 0270-7306. PMC 232245. PMID 9199327.

Boam DS, Davidson I, Chambon P (1995). "A TATA-less promoter containing binding sites for ubiquitous transcription factors mediates cell type-specific regulation of the gene for transcription enhancer factor-1 (TEF-1)". J. Biol. Chem. 270 (33): 19487–94. doi:10.1074/jbc.270.33.19487. PMID 7642633.
Fossdal R, Magnússon L, Weber JL, Jensson O (1995). "Mapping the locus of atrophia areata, a helicoid peripapillary chorioretinal degeneration with autosomal dominant inheritance, to chromosome 11p15". Hum. Mol. Genet. 4 (3): 479–83. doi:10.1093/hmg/4.3.479. PMID 7795606.
Kariya K, Farrance IK, Simpson PC (1994). "Transcriptional enhancer factor-1 in cardiac myocytes interacts with an alpha 1-adrenergic- and beta-protein kinase C-inducible element in the rat beta-myosin heavy chain promoter". J. Biol. Chem. 268 (35): 26658–62. PMID 8253797.
Shimizu N, Smith G, Izumo S (1993). "Both a ubiquitous factor mTEF-1 and a distinct muscle-specific factor bind to the M-CAT motif of the myosin heavy chain beta gene". Nucleic Acids Res. 21 (17): 4103–10. doi:10.1093/nar/21.17.4103. PMC 310013. PMID 8396764.
Stewart AF; Richard CW; Suzow J et al. (1997). "Cloning of human RTEF-1, a transcriptional enhancer factor-1-related gene preferentially expressed in skeletal muscle: evidence for an ancient multigene family". Genomics 37 (1): 68–76. doi:10.1006/geno.1996.0522. PMID 8921372.
Gupta MP; Amin CS; Gupta M et al. (1997). "Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression". Mol. Cell. Biol. 17 (7): 3924–36. PMC 232245. PMID 9199327.
Simmonds AJ; Liu X; Soanes KH et al. (1999). "Molecular interactions between Vestigial and Scalloped promote wing formation in Drosophila". Genes Dev. 12 (24): 3815–20. doi:10.1101/gad.12.24.3815. PMC 317270. PMID 9869635.
Vaudin P; Delanoue R; Davidson I et al. (1999). "TONDU (TDU), a novel human protein related to the product of vestigial (vg) gene of Drosophila melanogaster interacts with vertebrate TEF factors and substitutes for Vg function in wing formation". Development 126 (21): 4807–16. PMID 10518497.
Gupta M; Kogut P; Davis FJ et al. (2001). "Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1". J. Biol. Chem. 276 (13): 10413–22. doi:10.1074/jbc.M008625200. PMID 11136726.
Vassilev A; Kaneko KJ; Shu H et al. (2001). "TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm". Genes Dev. 15 (10): 1229–41. doi:10.1101/gad.888601. PMC 313800. PMID 11358867.
Carlini LE, Getz MJ, Strauch AR, Kelm RJ (2002). "Cryptic MCAT enhancer regulation in fibroblasts and smooth muscle cells. Suppression of TEF-1 mediated activation by the single-stranded DNA-binding proteins, Pur alpha, Pur beta, and MSY1". J. Biol. Chem. 277 (10): 8682–92. doi:10.1074/jbc.M109754200. PMID 11751932.
Maeda T, Gupta MP, Stewart AF (2002). "TEF-1 and MEF2 transcription factors interact to regulate muscle-specific promoters". Biochem. Biophys. Res. Commun. 294 (4): 791–7. doi:10.1016/S0006-291X(02)00556-9. PMID 12061776.
Maeda T, Chapman DL, Stewart AF (2003). "Mammalian vestigial-like 2, a cofactor of TEF-1 and MEF2 transcription factors that promotes skeletal muscle differentiation". J. Biol. Chem. 277 (50): 48889–98. doi:10.1074/jbc.M206858200. PMID 12376544.
Strausberg RL; Feingold EA; Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Thompson M; Andrade VA; Andrade SJ et al. (2003). "Inhibition of the TEF/TEAD transcription factor activity by nuclear calcium and distinct kinase pathways". Biochem. Biophys. Res. Commun. 301 (2): 267–74. doi:10.1016/S0006-291X(02)03024-3. PMID 12565854.
Karasseva N; Tsika G; Ji J et al. (2003). "Transcription Enhancer Factor 1 Binds Multiple Muscle MEF2 and A/T-Rich Elements during Fast-to-Slow Skeletal Muscle Fiber Type Transitions". Mol. Cell. Biol. 23 (15): 5143–64. doi:10.1128/MCB.23.15.5143-5164.2003. PMC 165722. PMID 12861002.
Ota T; Suzuki Y; Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Günther S, Mielcarek M, Krüger M, Braun T (2004). "VITO-1 is an essential cofactor of TEF1-dependent muscle-specific gene regulation". Nucleic Acids Res. 32 (2): 791–802. doi:10.1093/nar/gkh248. PMC 373362. PMID 14762206.

PDB gallery

2hzd: NMR structure of the DNA-binding TEA domain and insights into TEF-1 function

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor AATF 1 2 3 4 5 6 7 AP-1 c-Fos FOSB FOSL1 FOSL2 JDP2 c-Jun JUNB JunD BACH 1 2 BATF BLZF1 C/EBP α β γ δ ε ζ CREB 1 3 L1 CREM DBP DDIT3 GABPA HLF MAF B F G K NFE 2 L1 L2 L3 NFIL3 NRL NRF 1 2 3 XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 AhR AHRR ARNT ASCL1 BHLH 2 3 9 ARNTL ARNTL ARNTL2 CLOCK EPAS1 FIGLA HAND 1 2 HES 5 6 HEY 1 2 L HES1 HIF 1A 3A ID 1 2 3 4 LYL1 MESP2 MXD4 MYCL1 MYCN Myogenic regulatory factors MyoD Myogenin MYF5 MYF6 Neurogenins 1 2 3 NeuroD 1 2 NPAS 1 2 3 OLIG 1 2 Pho4 Scleraxis SIM 1 2 TAL 1 2 Twist USF1

(1.3) bHLH-ZIP	AP-4 MAX MXD3 MITF MNT MLX MXI1 Myc SREBP 1 2

(1.4) NF-1	NFI A B C X SMAD R-SMAD 1 2 3 5 9 I-SMAD 6 7 4)

(1.5) RF-X	RFX 1 2 3 4 5 6 ANK

(1.6) Basic helix-span-helix (bHSH)	AP-2 α β γ δ ε

(2) Zinc finger DNA-binding domains

(2.1) Nuclear receptor (Cys₄)

subfamily 1	Thyroid hormone α β CAR FXR LXR α β PPAR α β/δ γ PXR RAR α β γ ROR α β γ Rev-ErbA α β VDR

subfamily 2	COUP-TF (I II Ear-2 HNF4 α γ PNR RXR α β γ Testicular receptor 2 4 TLX

subfamily 3	Steroid hormone Androgen Estrogen α β Glucocorticoid Mineralocorticoid Progesterone Estrogen related α β γ

subfamily 4	NUR NGFIB NOR1 NURR1

subfamily 5	LRH-1 SF1

subfamily 6	GCNF

subfamily 0	DAX1 SHP

(2.2) Other Cys₄

GATA
- 1
- 2
- 3
- 4
- 5
- 6
MTA
- 1
- 2
- 3
TRPS1

(2.3) Cys₂His₂

General transcription factors
- TFIIA
- TFIIB
- TFIID
- TFIIE
  - 1
  - 2
- TFIIF
- 1
- 2
  - TFIIH
  - 1
  - 2
  - 4
  - 2I
  - 3A
  - 3C1
  - 3C2

ATBF1
BCL
- 6
- 11A
- 11B
CTCF
E4F1
EGR
- 1
- 2
- 3
- 4
ERV3
GFI1
GLI-Krüppel family
- 1
- 2
- 3
- REST
- S1
- S2
- YY1
HIC
- 1
- 2
HIVEP
- 1
- 2
- 3
IKZF
- 1
- 2
- 3
ILF
- 2
- 3
KLF
- 1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15
- 17
MTF1
MYT1
OSR1
PRDM9
SALL
- 1
- 2
- 3
- 4
SP
- 1
- 2
- 4
- 7
- 8
TSHZ3
WT1
Zbtb7
- 7A
- 7B
ZBTB
- 11
- 16
- 17
- 20
- 32
- 33
- 40
zinc finger
- 3
- 7
- 9
- 10
- 19
- 22
- 24
- 33B
- 34
- 35
- 41
- 43
- 44
- 51
- 74
- 143
- 146
- 148
- 165
- 202
- 217
- 219
- 238
- 239
- 259
- 267
- 268
- 281
- 295
- 300
- 318
- 330
- 346
- 350
- 365
- 366
- 384
- 423
- 451
- 452
- 471
- 593
- 638
- 644
- 649
- 655

(2.4) Cys₆

HIVEP1

(2.5) Alternating composition

AIRE
DIDO1
GRLF1
ING
- 1
- 2
- 4
JARID
- 1A
- 1B
- 1C
- 1D
- 2
JMJD1B

(2.6) WRKY

WRKY

(3) Helix-turn-helix domains

(3.1) Homeodomain	ARX CDX 1 2 CRX CUTL1 DBX 1 2 DLX 3 4 5 EMX 1 2 EN 1 2 FHL 1 2 3 HESX1 HHEX HLX Homeobox A1 A2 A3 A4 A5 A7 A9 A10 A11 A13 B1 B2 B3 B4 B5 B6 B7 B8 B9 B13 C4 C5 C6 C8 C9 C10 C11 C12 C13 D1 D3 D4 D8 D9 D10 D11 D12 D13 HOPX IRX 1 2 3 4 5 6 MKX LMX 1A 1B MEIS 1 2 MEOX2 MNX1 MSX 1 2 NANOG NKX 2-1 2-2 2-3 2-5 3-1 3-2 6-1 6-2 NOBOX PBX 1 2 3 PHF 1 3 6 8 10 16 17 20 21A PHOX 2A 2B PITX 1 2 3 POU domain PIT-1 BRN-3: A B C Octamer transcription factor: 1 2 3/4 6 7 11 OTX 1 2 PDX1 SATB2 SHOX2 SIX 1 2 3 4 5 VAX1 ZEB 1 2

(3.2) Paired box	PAX 1 2 3 4 5 6 7 8 9 PRRX 1 2 RAX

(3.3) Fork head / winged helix	E2F 1 2 3 4 5 FOX proteins A1 A2 A3 C1 C2 D3 D4 E1 E3 F1 G1 H1 I1 J1 J2 K1 K2 L2 M1 N1 N3 O1 O3 O4 P1 P2 P3 P4

(3.4) Heat shock factors	HSF 1 2 4

(3.5) Tryptophan clusters	ELF 2 4 5 EGF ELK 1 3 4 ERF ETS 1 2 ERG SPIB ETV 1 4 5 6 FLI1 Interferon regulatory factors 1 2 3 4 5 6 7 8 MYB MYBL2

(3.6) TEA domain	transcriptional enhancer factor 1 2 3 4

(4) β-Scaffold factors with minor groove contacts

(4.1) Rel homology region	NF-κB NFKB1 NFKB2 REL RELA RELB NFAT C1 C2 C3 C4 5

(4.2) STAT	STAT 1 2 3 4 5 6

(4.3) p53	p53 TBX 1 2 3 5 19 21 22 TBR1 TBR2 TFT MYRF TP63

(4.4) MADS box	Mef2 A B C D SRF

(4.6) TATA-binding proteins	TBP TBPL1

(4.7) High-mobility group	BBX HMGB 1 2 3 4 HMGN 1 2 3 4 HNF 1A 1B LEF1 SOX 1 2 3 4 5 6 8 9 10 11 12 13 14 15 18 21 SRY SSRP1 TCF 3 4 TOX 1 2 3 4

(4.9) Grainyhead	TFCP2

(4.10) Cold-shock domain	CSDA YBX1

(4.11) Runt	CBF CBFA2T2 CBFA2T3 RUNX1 RUNX2 RUNX3 RUNX1T1

(0) Other transcription factors

(0.2) HMGI(Y)	HMGA 1 2 HBP1

(0.3) Pocket domain	Rb RBL1 RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 EREBP B3

(0.6) Miscellaneous	ARID 1A 1B 2 3A 3B 4A CAP IFI 16 35 MLL 2 3 T1 MNDA NFY A B C Rho/Sigma

see also transcription factor/coregulator deficiencies

Index of genetics

Description	Gene expression DNA replication cycle recombination repair binding proteins Transcription factors regulators nucleic acids RNA RNA binding proteins ribonucleoproteins repeated sequence modification Translation ribosome modification nexins Proteins domains Structure primary secondary tertiary quaternary

Disease	Replication and repair Transcription factor Transcription Translation

TEAD1

Interactions

References

Further reading