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Protein

Transcription factor AP-4

Gene

TFAP4

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

Functioni

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. E-box binding Source: UniProtKB
  3. histone deacetylase binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  7. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  8. sequence-specific DNA binding Source: UniProtKB
  9. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. cellular response to dexamethasone stimulus Source: Ensembl
  2. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
  3. negative regulation by host of viral transcription Source: UniProtKB
  4. negative regulation of cell cycle arrest Source: UniProtKB
  5. negative regulation of cell proliferation Source: UniProtKB
  6. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  7. negative regulation of DNA binding Source: UniProtKB
  8. negative regulation of transcription, DNA-templated Source: UniProtKB
  9. positive regulation by host of viral transcription Source: UniProtKB
  10. positive regulation of apoptotic process Source: UniProtKB
  11. positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: Ensembl
  12. positive regulation of transcription, DNA-templated Source: UniProtKB
  13. protein complex assembly Source: UniProtKB
  14. regulation of transcription from RNA polymerase II promoter Source: GO_Central
  15. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TFAP4
Synonyms:BHLHC41
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:11745. TFAP4.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. transcriptional repressor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Transcription factor AP-4PRO_0000127458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei123 – 1231Phosphoserine1 Publication
Modified residuei124 – 1241Phosphoserine3 Publications
Modified residuei139 – 1391Phosphoserine3 Publications
Modified residuei282 – 2821Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ01664.
PaxDbiQ01664.
PRIDEiQ01664.

PTM databases

PhosphoSiteiQ01664.

Expressioni

Gene expression databases

BgeeiQ01664.
CleanExiHS_TFAP4.
ExpressionAtlasiQ01664. baseline and differential.
GenevestigatoriQ01664.

Organism-specific databases

HPAiHPA001912.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi112881. 90 interactions.
IntActiQ01664. 1 interaction.
STRINGi9606.ENSP00000204517.

Structurei

3D structure databases

ProteinModelPortaliQ01664.
SMRiQ01664. Positions 46-102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 9952bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 12021Leucine-zipper 1Add
BLAST
Regioni151 – 17929Leucine-zipper 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi193 – 22230Gln-richAdd
BLAST
Compositional biasi225 – 24420Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270566.
GeneTreeiENSGT00390000015189.
HOGENOMiHOG000294087.
HOVERGENiHBG061473.
InParanoidiQ01664.
KOiK09108.
OMAiPTHHATV.
OrthoDBiEOG7BP83C.
PhylomeDBiQ01664.
TreeFamiTF316489.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01664-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEYFMVPTQK VPSLQHFRKT EKEVIGGLCS LANIPLTPET QRDQERRIRR
60 70 80 90 100
EIANSNERRR MQSINAGFQS LKTLIPHTDG EKLSKAAILQ QTAEYIFSLE
110 120 130 140 150
QEKTRLLQQN TQLKRFIQEL SGSSPKRRRA EDKDEGIGSP DIWEDEKAED
160 170 180 190 200
LRREMIELRQ QLDKERSVRM MLEEQVRSLE AHMYPEKLKV IAQQVQLQQQ
210 220 230 240 250
QEQVRLLHQE KLEREQQQLR TQLLPPPAPT HHPTVIVPAP PPPPSHHINV
260 270 280 290 300
VTMGPSSVIN SVSTSRQNLD TIVQAIQHIE GTQEKQELEE EQRRAVIVKP
310 320 330
VRSCPEAPTS DTASDSEASD SDAMDQSREE PSGDGELP
Length:338
Mass (Da):38,726
Last modified:October 1, 1996 - v2
Checksum:i540C008658596B83
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti218 – 2181Q → H.1 Publication
Corresponds to variant rs251732 [ dbSNP | Ensembl ].
VAR_059346

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73885 mRNA. Translation: AAB32235.1.
AC004653 Genomic DNA. Translation: AAC17116.1.
BC010576 mRNA. Translation: AAH10576.1.
X57435 mRNA. Translation: CAA40683.1.
CCDSiCCDS10510.1.
PIRiI56893.
RefSeqiNP_003214.1. NM_003223.2.
UniGeneiHs.513305.

Genome annotation databases

EnsembliENST00000204517; ENSP00000204517; ENSG00000090447.
GeneIDi7023.
KEGGihsa:7023.
UCSCiuc010uxg.2. human.

Polymorphism databases

DMDMi1729833.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73885 mRNA. Translation: AAB32235.1.
AC004653 Genomic DNA. Translation: AAC17116.1.
BC010576 mRNA. Translation: AAH10576.1.
X57435 mRNA. Translation: CAA40683.1.
CCDSiCCDS10510.1.
PIRiI56893.
RefSeqiNP_003214.1. NM_003223.2.
UniGeneiHs.513305.

3D structure databases

ProteinModelPortaliQ01664.
SMRiQ01664. Positions 46-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112881. 90 interactions.
IntActiQ01664. 1 interaction.
STRINGi9606.ENSP00000204517.

PTM databases

PhosphoSiteiQ01664.

Polymorphism databases

DMDMi1729833.

Proteomic databases

MaxQBiQ01664.
PaxDbiQ01664.
PRIDEiQ01664.

Protocols and materials databases

DNASUi7023.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000204517; ENSP00000204517; ENSG00000090447.
GeneIDi7023.
KEGGihsa:7023.
UCSCiuc010uxg.2. human.

Organism-specific databases

CTDi7023.
GeneCardsiGC16M004307.
HGNCiHGNC:11745. TFAP4.
HPAiHPA001912.
MIMi600743. gene.
neXtProtiNX_Q01664.
PharmGKBiPA36462.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG270566.
GeneTreeiENSGT00390000015189.
HOGENOMiHOG000294087.
HOVERGENiHBG061473.
InParanoidiQ01664.
KOiK09108.
OMAiPTHHATV.
OrthoDBiEOG7BP83C.
PhylomeDBiQ01664.
TreeFamiTF316489.

Miscellaneous databases

GeneWikiiTFAP4.
GenomeRNAii7023.
NextBioi27439.
PROiQ01664.
SOURCEiSearch...

Gene expression databases

BgeeiQ01664.
CleanExiHS_TFAP4.
ExpressionAtlasiQ01664. baseline and differential.
GenevestigatoriQ01664.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. 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].

Entry informationi

Entry nameiTFAP4_HUMAN
AccessioniPrimary (citable) accession number: Q01664
Secondary accession number(s): O60409
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 143 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. 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.