Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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).1 Publication

GO - Molecular functioni

  • histone acetyltransferase binding Source: UniProtKB
  • protein heterodimerization activity Source: ParkinsonsUK-UCL
  • 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

BioCyciZFISH:ENSG00000178913-MONOMER.
ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
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:
TAFII553 Publications
Gene namesi
Name:TAF7
Synonyms:TAF2F, TAFII55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:11541. TAF7.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

  • Golgi apparatus Source: HPA
  • MLL1 complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • transcription factor complex Source: ParkinsonsUK-UCL
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi5K → R: Abolishes methylation in vitro. 1 Publication1
Mutagenesisi264S → A: Reduced H3 acetylation and transcription at target promoters. 1 Publication1
Mutagenesisi264S → D: 50% reduction in TAF1-binding, reduced incorporation of TAF7 into TFIID complexes. 1 Publication1

Organism-specific databases

DisGeNETi6879.
OpenTargetsiENSG00000178913.
PharmGKBiPA36316.

Polymorphism and mutation databases

BioMutaiTAF7.
DMDMi3024690.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001188811 – 349Transcription initiation factor TFIID subunit 7Add BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei171PhosphoserineCombined sources1
Modified residuei200PhosphoserineCombined sources1
Modified residuei201PhosphoserineCombined sources1
Modified residuei213PhosphoserineCombined sources1
Modified residuei264PhosphoserineCombined sources1 Publication1

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

EPDiQ15545.
MaxQBiQ15545.
PaxDbiQ15545.
PeptideAtlasiQ15545.
PRIDEiQ15545.

PTM databases

iPTMnetiQ15545.
PhosphoSitePlusiQ15545.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000178913.
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) (PubMed:27007846, PubMed:10438527). Part of a TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846). Interacts with TAF1; the interaction is direct (PubMed:25412659). Interacts with TAFII250, TAFII100, TAFII28, TAFII20, and TAFII18, but not with TAFII30 or TBP (PubMed:8702684, PubMed:10438527). 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 (PubMed:15960975). Binds to CIITA and TAF1 and inhibits their acetyltransferase activity, thereby repressing activated transcription and behaving as a repressor at these promoters.6 Publications

GO - Molecular functioni

  • histone acetyltransferase binding Source: UniProtKB
  • protein heterodimerization activity Source: ParkinsonsUK-UCL
  • thyroid hormone receptor binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • vitamin D receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112742. 42 interactors.
DIPiDIP-29047N.
IntActiQ15545. 14 interactors.
MINTiMINT-3031780.
STRINGi9606.ENSP00000312709.

Structurei

Secondary structure

1349
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 19Combined sources6
Helixi22 – 34Combined sources13
Helixi39 – 42Combined sources4
Beta strandi43 – 47Combined sources5
Beta strandi51 – 58Combined sources8
Beta strandi61 – 101Combined sources41
Helixi138 – 140Combined sources3
Helixi143 – 146Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RGWX-ray2.30B1-349[»]
5FURelectron microscopy8.50H1-349[»]
ProteinModelPortaliQ15545.
SMRiQ15545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili244 – 349Sequence analysisAdd BLAST106

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3 – 5[KR]-[STA]-K motif3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi227 – 230Poly-Ser4

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

eggNOGiKOG4011. Eukaryota.
COG5414. LUCA.
GeneTreeiENSGT00390000010815.
HOGENOMiHOG000035121.
HOVERGENiHBG013606.
InParanoidiQ15545.
KOiK03132.
OMAiQMLVCTL.
OrthoDBiEOG091G0S3N.
PhylomeDBiQ15545.
TreeFamiTF313044.

Family and domain databases

CDDicd08047. TAF7. 1 hit.
InterProiIPR006751. TAFII55_prot_cons_reg.
[Graphical view]
PfamiPF04658. TAFII55_N. 1 hit.
[Graphical view]
SMARTiSM01370. 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)DescriptionActionsGraphical viewLength
Sequence conflicti283K → N in AAB60347 (PubMed:7824954).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005629178S → R.1

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.4. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RGWX-ray2.30B1-349[»]
5FURelectron microscopy8.50H1-349[»]
ProteinModelPortaliQ15545.
SMRiQ15545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112742. 42 interactors.
DIPiDIP-29047N.
IntActiQ15545. 14 interactors.
MINTiMINT-3031780.
STRINGi9606.ENSP00000312709.

PTM databases

iPTMnetiQ15545.
PhosphoSitePlusiQ15545.

Polymorphism and mutation databases

BioMutaiTAF7.
DMDMi3024690.

Proteomic databases

EPDiQ15545.
MaxQBiQ15545.
PaxDbiQ15545.
PeptideAtlasiQ15545.
PRIDEiQ15545.

Protocols and materials databases

DNASUi6879.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313368; ENSP00000312709; ENSG00000178913.
GeneIDi6879.
KEGGihsa:6879.
UCSCiuc003ljg.4. human.

Organism-specific databases

CTDi6879.
DisGeNETi6879.
GeneCardsiTAF7.
HGNCiHGNC:11541. TAF7.
HPAiHPA006429.
MIMi600573. gene.
neXtProtiNX_Q15545.
OpenTargetsiENSG00000178913.
PharmGKBiPA36316.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4011. Eukaryota.
COG5414. LUCA.
GeneTreeiENSGT00390000010815.
HOGENOMiHOG000035121.
HOVERGENiHBG013606.
InParanoidiQ15545.
KOiK03132.
OMAiQMLVCTL.
OrthoDBiEOG091G0S3N.
PhylomeDBiQ15545.
TreeFamiTF313044.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000178913-MONOMER.
ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
SignaLinkiQ15545.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000178913.
CleanExiHS_TAF7.
ExpressionAtlasiQ15545. baseline and differential.
GenevisibleiQ15545. HS.

Family and domain databases

CDDicd08047. TAF7. 1 hit.
InterProiIPR006751. TAFII55_prot_cons_reg.
[Graphical view]
PfamiPF04658. TAFII55_N. 1 hit.
[Graphical view]
SMARTiSM01370. TAFII55_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 149 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

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 one 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.