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Q01664 (TFAP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor AP-4
Alternative name(s):
Activating enhancer-binding protein 4
Class C basic helix-loop-helix protein 41
Short name=bHLHc41
Gene names
Name:TFAP4
Synonyms:BHLHC41
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that activates both viral and cellular genes by binding to the symmetrical DNA sequence 5'-CAGCTG-3'.

Subunit structure

Efficient DNA binding requires dimerization with another bHLH protein. Homodimer.

Subcellular location

Nucleus.

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from direct assay PubMed 18818310. Source: UniProtKB

cellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation by host of viral transcription

Inferred from direct assay PubMed 14645924PubMed 16540471. Source: UniProtKB

negative regulation of DNA binding

Inferred from direct assay PubMed 16540471Ref.1. Source: UniProtKB

negative regulation of cell cycle arrest

Inferred from mutant phenotype PubMed 18818310. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 18818310. Source: UniProtKB

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 18818310. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16924111PubMed 19505873PubMed 9931457. Source: UniProtKB

positive regulation by host of viral transcription

Inferred from direct assay PubMed 2833704. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 18818310. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 12663744. Source: UniProtKB

protein complex assembly

Inferred from direct assay PubMed 19505873. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 2833704. Source: GOC

   Cellular_componentnucleus

Inferred from direct assay PubMed 11171123PubMed 12663744PubMed 19505873Ref.1PubMed 9931457. Source: UniProtKB

transcriptional repressor complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 9931457. Source: UniProtKB

E-box binding

Inferred from direct assay PubMed 11171123PubMed 12663744PubMed 18818310PubMed 19505873Ref.1. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 2833704. Source: UniProtKB

histone deacetylase binding

Inferred from physical interaction PubMed 16540471PubMed 16924111. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.4. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay Ref.4. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 14645924PubMed 16540471. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Transcription factor AP-4
PRO_0000127458

Regions

Domain48 – 9952bHLH
Region100 – 12021Leucine-zipper 1
Region151 – 17929Leucine-zipper 2
Compositional bias193 – 22230Gln-rich
Compositional bias225 – 24420Pro-rich

Amino acid modifications

Modified residue1231Phosphoserine Ref.9
Modified residue1241Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue1391Phosphoserine Ref.5 Ref.8 Ref.9
Modified residue2821Phosphothreonine Ref.9

Natural variations

Natural variant2181Q → H. Ref.2
Corresponds to variant rs251732 [ dbSNP | Ensembl ].
VAR_059346

Sequences

Sequence LengthMass (Da)Tools
Q01664 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 540C008658596B83

FASTA33838,726
        10         20         30         40         50         60 
MEYFMVPTQK VPSLQHFRKT EKEVIGGLCS LANIPLTPET QRDQERRIRR EIANSNERRR 

        70         80         90        100        110        120 
MQSINAGFQS LKTLIPHTDG EKLSKAAILQ QTAEYIFSLE QEKTRLLQQN TQLKRFIQEL 

       130        140        150        160        170        180 
SGSSPKRRRA EDKDEGIGSP DIWEDEKAED LRREMIELRQ QLDKERSVRM MLEEQVRSLE 

       190        200        210        220        230        240 
AHMYPEKLKV IAQQVQLQQQ QEQVRLLHQE KLEREQQQLR TQLLPPPAPT HHPTVIVPAP 

       250        260        270        280        290        300 
PPPPSHHINV VTMGPSSVIN SVSTSRQNLD TIVQAIQHIE GTQEKQELEE EQRRAVIVKP 

       310        320        330 
VRSCPEAPTS DTASDSEASD SDAMDQSREE PSGDGELP 

« Hide

References

« Hide 'large scale' references
[1]"Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function."
Ou S.H., Garcia-Martinez L.F., Paulssen E.J., Gaynor R.B.
J. Virol. 68:7188-7199(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-218.
[3]"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: Brain.
[4]"Transcription factor AP-4 contains multiple dimerization domains that regulate dimer specificity."
Hu Y.-F., Luescher B., Admon A., Mermod N., Tjian R.
Genes Dev. 4:1741-1752(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-338, PARTIAL PROTEIN SEQUENCE.
[5]"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-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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-124 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-123; SER-124; SER-139 AND THR-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S73885 mRNA. Translation: AAB32235.1.
AC004653 Genomic DNA. Translation: AAC17116.1.
BC010576 mRNA. Translation: AAH10576.1.
X57435 mRNA. Translation: CAA40683.1.
PIRI56893.
RefSeqNP_003214.1. NM_003223.2.
UniGeneHs.513305.

3D structure databases

ProteinModelPortalQ01664.
SMRQ01664. Positions 46-102.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112881. 83 interactions.
IntActQ01664. 1 interaction.
STRING9606.ENSP00000204517.

PTM databases

PhosphoSiteQ01664.

Polymorphism databases

DMDM1729833.

Proteomic databases

PaxDbQ01664.
PRIDEQ01664.

Protocols and materials databases

DNASU7023.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000204517; ENSP00000204517; ENSG00000090447.
GeneID7023.
KEGGhsa:7023.
UCSCuc010uxg.2. human.

Organism-specific databases

CTD7023.
GeneCardsGC16M004307.
HGNCHGNC:11745. TFAP4.
HPAHPA001912.
MIM600743. gene.
neXtProtNX_Q01664.
PharmGKBPA36462.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270566.
HOGENOMHOG000294087.
HOVERGENHBG061473.
InParanoidQ01664.
KOK09108.
OMAPTHHATV.
OrthoDBEOG7BP83C.
PhylomeDBQ01664.
TreeFamTF316489.

Gene expression databases

ArrayExpressQ01664.
BgeeQ01664.
CleanExHS_TFAP4.
GenevestigatorQ01664.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTFAP4.
GenomeRNAi7023.
NextBio27439.
PROQ01664.
SOURCESearch...

Entry information

Entry nameTFAP4_HUMAN
AccessionPrimary (citable) accession number: Q01664
Secondary accession number(s): O60409
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 136 of the entry and version 2 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 16

Human chromosome 16: entries, gene names and cross-references to MIM