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Q01664

- TFAP4_HUMAN

UniProt

Q01664 - TFAP4_HUMAN

Protein

Transcription factor AP-4

Gene

TFAP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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 binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
    7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    8. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
    9. sequence-specific DNA binding Source: UniProtKB
    10. 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. transcription from RNA polymerase II promoter Source: GOC

    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

    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

    ArrayExpressiQ01664.
    BgeeiQ01664.
    CleanExiHS_TFAP4.
    GenevestigatoriQ01664.

    Organism-specific databases

    HPAiHPA001912.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi112881. 86 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.
    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

    MEYFMVPTQK VPSLQHFRKT EKEVIGGLCS LANIPLTPET QRDQERRIRR    50
    EIANSNERRR MQSINAGFQS LKTLIPHTDG EKLSKAAILQ QTAEYIFSLE 100
    QEKTRLLQQN TQLKRFIQEL SGSSPKRRRA EDKDEGIGSP DIWEDEKAED 150
    LRREMIELRQ QLDKERSVRM MLEEQVRSLE AHMYPEKLKV IAQQVQLQQQ 200
    QEQVRLLHQE KLEREQQQLR TQLLPPPAPT HHPTVIVPAP PPPPSHHINV 250
    VTMGPSSVIN SVSTSRQNLD TIVQAIQHIE GTQEKQELEE EQRRAVIVKP 300
    VRSCPEAPTS DTASDSEASD SDAMDQSREE PSGDGELP 338
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S73885 mRNA. Translation: AAB32235.1 .
    AC004653 Genomic DNA. Translation: AAC17116.1 .
    BC010576 mRNA. Translation: AAH10576.1 .
    X57435 mRNA. Translation: CAA40683.1 .
    CCDSi CCDS10510.1.
    PIRi I56893.
    RefSeqi NP_003214.1. NM_003223.2.
    UniGenei Hs.513305.

    3D structure databases

    ProteinModelPortali Q01664.
    SMRi Q01664. Positions 46-102.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112881. 86 interactions.
    IntActi Q01664. 1 interaction.
    STRINGi 9606.ENSP00000204517.

    PTM databases

    PhosphoSitei Q01664.

    Polymorphism databases

    DMDMi 1729833.

    Proteomic databases

    MaxQBi Q01664.
    PaxDbi Q01664.
    PRIDEi Q01664.

    Protocols and materials databases

    DNASUi 7023.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000204517 ; ENSP00000204517 ; ENSG00000090447 .
    GeneIDi 7023.
    KEGGi hsa:7023.
    UCSCi uc010uxg.2. human.

    Organism-specific databases

    CTDi 7023.
    GeneCardsi GC16M004307.
    HGNCi HGNC:11745. TFAP4.
    HPAi HPA001912.
    MIMi 600743. gene.
    neXtProti NX_Q01664.
    PharmGKBi PA36462.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270566.
    HOGENOMi HOG000294087.
    HOVERGENi HBG061473.
    InParanoidi Q01664.
    KOi K09108.
    OMAi PTHHATV.
    OrthoDBi EOG7BP83C.
    PhylomeDBi Q01664.
    TreeFami TF316489.

    Miscellaneous databases

    GeneWikii TFAP4.
    GenomeRNAii 7023.
    NextBioi 27439.
    PROi Q01664.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01664.
    Bgeei Q01664.
    CleanExi HS_TFAP4.
    Genevestigatori Q01664.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    InterProi IPR011598. bHLH_dom.
    [Graphical view ]
    Pfami PF00010. HLH. 1 hit.
    [Graphical view ]
    SMARTi SM00353. HLH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    PROSITEi PS50888. BHLH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 140 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