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Protein

Transcription initiation factor TFIID subunit 7

Gene

TAF7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a component of the DNA-binding general transcription factor complex TFIID, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively).

GO - Molecular functioni

  • histone acetyltransferase binding Source: UniProtKB
  • thyroid hormone receptor binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB
  • vitamin D receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

SignaLinkiQ15545.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 7
Alternative name(s):
RNA polymerase II TBP-associated factor subunit F
Transcription initiation factor TFIID 55 kDa subunit
Short name:
TAF(II)55
Short name:
TAFII-55
Short name:
TAFII55
Gene namesi
Name:TAF7
Synonyms:TAF2F, TAFII55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:11541. TAF7.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: HPA
  • MLL1 complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • transcription factor TFIID complex Source: UniProtKB
  • transcription factor TFTC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51K → R: Abolishes methylation in vitro. 1 Publication
Mutagenesisi264 – 2641S → A: Reduced H3 acetylation and transcription at target promoters. 1 Publication
Mutagenesisi264 – 2641S → D: 50% reduction in TAF1-binding, reduced incorporation of TAF7 into TFIID complexes. 1 Publication

Organism-specific databases

PharmGKBiPA36316.

Polymorphism and mutation databases

BioMutaiTAF7.
DMDMi3024690.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Transcription initiation factor TFIID subunit 7PRO_0000118881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711Phosphoserine2 Publications
Modified residuei213 – 2131Phosphoserine1 Publication
Modified residuei264 – 2641Phosphoserine6 Publications

Post-translational modificationi

Phosphorylated by CIITA. Phosphorylation at Ser-264 by TAF1 in early G1 phase disrupts binding to TAF1.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15545.
PaxDbiQ15545.
PRIDEiQ15545.

PTM databases

PhosphoSiteiQ15545.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ15545.
CleanExiHS_TAF7.
ExpressionAtlasiQ15545. baseline and differential.
GenevisibleiQ15545. HS.

Organism-specific databases

HPAiHPA006429.

Interactioni

Subunit structurei

TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Interacts with TAFII250, TAFII100, TAFII28, TAFII20, and TAFII18, but not with TAFII30 or TBP. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Binds to CIITA and TAF1 and inhibits their acetyltransferase activity, thereby repressing activated transcription and behaving as a repressor at these promoters.2 Publications

Protein-protein interaction databases

BioGridi112742. 34 interactions.
DIPiDIP-29047N.
IntActiQ15545. 8 interactions.
MINTiMINT-3031780.
STRINGi9606.ENSP00000312709.

Structurei

Secondary structure

1
349
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196Combined sources
Helixi22 – 3413Combined sources
Helixi39 – 424Combined sources
Beta strandi43 – 475Combined sources
Beta strandi51 – 588Combined sources
Beta strandi61 – 10141Combined sources
Helixi138 – 1403Combined sources
Helixi143 – 1464Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RGWX-ray2.30B1-349[»]
ProteinModelPortaliQ15545.
SMRiQ15545. Positions 11-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili244 – 349106Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3 – 53[KR]-[STA]-K motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi227 – 2304Poly-Ser

Domaini

The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase, which methylates Lys-5 in vitro.By similarity

Sequence similaritiesi

Belongs to the TAF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5414.
GeneTreeiENSGT00390000010815.
HOGENOMiHOG000035121.
HOVERGENiHBG013606.
InParanoidiQ15545.
KOiK03132.
OMAiQMLVCTL.
OrthoDBiEOG7GJ6FT.
PhylomeDBiQ15545.
TreeFamiTF313044.

Family and domain databases

InterProiIPR006751. TAFII55_prot_cons_reg.
[Graphical view]
PfamiPF04658. TAFII55_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15545-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSKDDAPH ELESQFILRL PPEYASTVRR AVQSGHVNLK DRLTIELHPD
60 70 80 90 100
GRHGIVRVDR VPLASKLVDL PCVMESLKTI DKKTFYKTAD ICQMLVSTVD
110 120 130 140 150
GDLYPPVEEP VASTDPKASK KKDKDKEKKF IWNHGITLPL KNVRKRRFRK
160 170 180 190 200
TAKKKYIESP DVEKEVKRLL STDAEAVSTR WEIIAEDETK EAENQGLDIS
210 220 230 240 250
SPGMSGHRQG HDSLEHDELR EIFNDLSSSS EDEDETQHQD EEDINIIDTE
260 270 280 290 300
EDLERQLQDK LNESDEQHQE NEGTNQLVMG IQKQIDNMKG KLQETQDRAK
310 320 330 340
RQEDLIMKVE NLALKNRFQA VLDELKQKED REKEQLSSLQ EELESLLEK
Length:349
Mass (Da):40,259
Last modified:November 1, 1996 - v1
Checksum:i0AAFD3E33E3CCD6E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti283 – 2831K → N in AAB60347 (PubMed:7824954).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti178 – 1781S → R.
VAR_005629

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97999 mRNA. Translation: CAA66636.1.
U18062 mRNA. Translation: AAB60347.1.
AF349038 Genomic DNA. Translation: AAK30585.1.
AK314837 mRNA. Translation: BAG37356.1.
CH471062 Genomic DNA. Translation: EAW61966.1.
BC032737 mRNA. Translation: AAH32737.1.
CCDSiCCDS4259.1.
PIRiI38904.
RefSeqiNP_005633.2. NM_005642.2.
UniGeneiHs.438838.

Genome annotation databases

EnsembliENST00000313368; ENSP00000312709; ENSG00000178913.
GeneIDi6879.
KEGGihsa:6879.
UCSCiuc003ljg.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97999 mRNA. Translation: CAA66636.1.
U18062 mRNA. Translation: AAB60347.1.
AF349038 Genomic DNA. Translation: AAK30585.1.
AK314837 mRNA. Translation: BAG37356.1.
CH471062 Genomic DNA. Translation: EAW61966.1.
BC032737 mRNA. Translation: AAH32737.1.
CCDSiCCDS4259.1.
PIRiI38904.
RefSeqiNP_005633.2. NM_005642.2.
UniGeneiHs.438838.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RGWX-ray2.30B1-349[»]
ProteinModelPortaliQ15545.
SMRiQ15545. Positions 11-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112742. 34 interactions.
DIPiDIP-29047N.
IntActiQ15545. 8 interactions.
MINTiMINT-3031780.
STRINGi9606.ENSP00000312709.

PTM databases

PhosphoSiteiQ15545.

Polymorphism and mutation databases

BioMutaiTAF7.
DMDMi3024690.

Proteomic databases

MaxQBiQ15545.
PaxDbiQ15545.
PRIDEiQ15545.

Protocols and materials databases

DNASUi6879.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313368; ENSP00000312709; ENSG00000178913.
GeneIDi6879.
KEGGihsa:6879.
UCSCiuc003ljg.3. human.

Organism-specific databases

CTDi6879.
GeneCardsiGC05M140678.
HGNCiHGNC:11541. TAF7.
HPAiHPA006429.
MIMi600573. gene.
neXtProtiNX_Q15545.
PharmGKBiPA36316.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5414.
GeneTreeiENSGT00390000010815.
HOGENOMiHOG000035121.
HOVERGENiHBG013606.
InParanoidiQ15545.
KOiK03132.
OMAiQMLVCTL.
OrthoDBiEOG7GJ6FT.
PhylomeDBiQ15545.
TreeFamiTF313044.

Enzyme and pathway databases

SignaLinkiQ15545.

Miscellaneous databases

ChiTaRSiTAF7. human.
GeneWikiiTAF7.
GenomeRNAii6879.
NextBioi26869.
PROiQ15545.
SOURCEiSearch...

Gene expression databases

BgeeiQ15545.
CleanExiHS_TAF7.
ExpressionAtlasiQ15545. baseline and differential.
GenevisibleiQ15545. HS.

Family and domain databases

InterProiIPR006751. TAFII55_prot_cons_reg.
[Graphical view]
PfamiPF04658. TAFII55_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple interactions between hTAFII55 and other TFIID subunits. Requirements for the formation of stable ternary complexes between hTAFII55 and the TATA-binding protein."
    Lavigne A.C., Mengus G., May M., Dubrowskaya V., Tora L., Davidson I.
    J. Biol. Chem. 271:19774-19780(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators."
    Chiang C.-M., Roeder R.G.
    Science 267:531-536(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The intronless and TATA-less human TAFII55 gene contains a functional initiator and a downstream promoter element."
    Zhou T., Chiang C.-M.
    J. Biol. Chem. 276:25503-25511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Skin.
  7. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Structural basis for the methylation site specificity of SET7/9."
    Couture J.-F., Collazo E., Hauk G., Trievel R.C.
    Nat. Struct. Mol. Biol. 13:140-146(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MOTIF, MUTAGENESIS OF LYS-5.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Phosphorylation-dependent regulation of cyclin D1 and cyclin A gene transcription by TFIID subunits TAF1 and TAF7."
    Kloet S.L., Whiting J.L., Gafken P., Ranish J., Wang E.H.
    Mol. Cell. Biol. 32:3358-3369(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF1, MISCELLANEOUS, PHOSPHORYLATION AT SER-264, MUTAGENESIS OF SER-264.
  16. "Transcriptional coactivator CIITA, a functional homolog of TAF1, has kinase activity."
    Soe K.C., Devaiah B.N., Singer D.S.
    Biochim. Biophys. Acta 1829:1184-1190(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CIITA.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTAF7_HUMAN
AccessioniPrimary (citable) accession number: Q15545
Secondary accession number(s): B2RBV9, Q13036
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Overexpression of TAF7 in HeLa cells inhibits cyclin D1 and cyclin A gene transcription and causes the cells to accumulate in early S phase. In contrast, depletion of TAF7 from TFIID complexes by siRNAs increases histone H3 acetylation at both cyclin promoters and stimulates cyclins CCND1 and CCNA gene transcription.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.