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Q92754

- AP2C_HUMAN

UniProt

Q92754 - AP2C_HUMAN

Protein

Transcription factor AP-2 gamma

Gene

TFAP2C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.2 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein dimerization activity Source: UniProtKB
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: UniProtKB
    5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
    6. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
    7. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. cell-cell signaling Source: ProtInc
    2. cerebral cortex development Source: Ensembl
    3. dichotomous subdivision of terminal units involved in mammary gland duct morphogenesis Source: Ensembl
    4. epithelial cell proliferation involved in mammary gland duct elongation Source: Ensembl
    5. forebrain neuron fate commitment Source: Ensembl
    6. germ-line stem cell maintenance Source: Ensembl
    7. hair follicle development Source: Ensembl
    8. keratinocyte development Source: Ensembl
    9. male gonad development Source: UniProtKB
    10. negative regulation of transcription from RNA polymerase II promoter Source: GOC
    11. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    12. regulation of epidermis development Source: Ensembl
    13. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    14. sebaceous gland development Source: Ensembl
    15. somatic stem cell maintenance Source: Ensembl
    16. trophectodermal cell differentiation Source: Ensembl

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiQ92754.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor AP-2 gamma
    Short name:
    AP2-gamma
    Alternative name(s):
    Activating enhancer-binding protein 2 gamma
    Transcription factor ERF-1
    Gene namesi
    Name:TFAP2C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11744. TFAP2C.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591Y → A: Loss of interaction with WWOX; when associated with A-64. 1 Publication
    Mutagenesisi64 – 641Y → A: Loss of interaction with WWOX; when associated with A-59. 1 Publication

    Organism-specific databases

    PharmGKBiPA36461.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Transcription factor AP-2 gammaPRO_0000184803Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki10 – 10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei252 – 2521Phosphoserine; by PKABy similarity
    Modified residuei434 – 4341Phosphoserine2 Publications

    Post-translational modificationi

    Sumoylated on Lys-10; which inhibits transcriptional activity.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ92754.
    PaxDbiQ92754.
    PRIDEiQ92754.

    PTM databases

    PhosphoSiteiQ92754.

    Expressioni

    Inductioni

    During retinoic acid-mediated differentiation.

    Gene expression databases

    ArrayExpressiQ92754.
    BgeeiQ92754.
    CleanExiHS_TFAP2C.
    GenevestigatoriQ92754.

    Organism-specific databases

    HPAiCAB016061.
    CAB016079.

    Interactioni

    Subunit structurei

    Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members By similarity. Interacts with WWOX. Interacts with CITED4. Interacts with UBE2I. Interacts with KCTD1; this interaction represses transcription activation. Interacts with CITED2 (via C-terminus); the interaction stimulates TFAP2B-transcriptional activity. Interacts with MTA1.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CITED2Q999672EBI-937309,EBI-937732
    UBE2IP632793EBI-937309,EBI-80168

    Protein-protein interaction databases

    BioGridi112880. 18 interactions.
    IntActiQ92754. 7 interactions.
    STRINGi9606.ENSP00000201031.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92754.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni293 – 424132H-S-H (helix-span-helix), dimerizationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi59 – 646WW-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi30 – 11990Gln/Pro-rich (transactivation domain)Add
    BLAST

    Domaini

    The WW-binding motif mediates interaction with WWOX.1 Publication

    Sequence similaritiesi

    Belongs to the AP-2 family.Curated

    Phylogenomic databases

    eggNOGiNOG300693.
    HOGENOMiHOG000231737.
    HOVERGENiHBG002455.
    InParanoidiQ92754.
    KOiK09177.
    OMAiEEVQNVD.
    OrthoDBiEOG7HHWS1.
    PhylomeDBiQ92754.
    TreeFamiTF313718.

    Family and domain databases

    InterProiIPR004979. TF_AP2.
    IPR013854. TF_AP2_C.
    IPR008123. TF_AP2_gamma.
    [Graphical view]
    PANTHERiPTHR10812. PTHR10812. 1 hit.
    PfamiPF03299. TF_AP-2. 1 hit.
    [Graphical view]
    PRINTSiPR01751. AP2CTNSCPFCT.
    PR01748. AP2TNSCPFCT.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92754-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLWKITDNVK YEEDCEDRHD GSSNGNPRVP HLSSAGQHLY SPAPPLSHTG    50
    VAEYQPPPYF PPPYQQLAYS QSADPYSHLG EAYAAAINPL HQPAPTGSQQ 100
    QAWPGRQSQE GAGLPSHHGR PAGLLPHLSG LEAGAVSARR DAYRRSDLLL 150
    PHAHALDAAG LAENLGLHDM PHQMDEVQNV DDQHLLLHDQ TVIRKGPISM 200
    TKNPLNLPCQ KELVGAVMNP TEVFCSVPGR LSLLSSTSKY KVTVAEVQRR 250
    LSPPECLNAS LLGGVLRRAK SKNGGRSLRE KLDKIGLNLP AGRRKAAHVT 300
    LLTSLVEGEA VHLARDFAYV CEAEFPSKPV AEYLTRPHLG GRNEMAARKN 350
    MLLAAQQLCK EFTELLSQDR TPHGTSRLAP VLETNIQNCL SHFSLITHGF 400
    GSQAICAAVS ALQNYIKEAL IVIDKSYMNP GDQSPADSNK TLEKMEKHRK 450
    Length:450
    Mass (Da):49,177
    Last modified:February 1, 1997 - v1
    Checksum:i2D4F5FBC269A34A8
    GO
    Isoform 2 (identifier: Q92754-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-169: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:281
    Mass (Da):31,010
    Checksum:iA5A874EDB6D7B2BC
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 169169Missing in isoform 2. 1 PublicationVSP_056501Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95693 mRNA. Translation: CAA64989.1.
    U85658 mRNA. Translation: AAC51305.1.
    AJ315934 Genomic DNA. Translation: CAC86997.1.
    AK301572 mRNA. Translation: BAG63065.1.
    AL121920 Genomic DNA. Translation: CAC10334.1.
    BC035664 mRNA. Translation: AAH35664.2.
    BC051829 mRNA. Translation: AAH51829.2.
    AB041717 Genomic DNA. Translation: BAC11805.1.
    CCDSiCCDS13454.1.
    RefSeqiNP_003213.1. NM_003222.3.
    UniGeneiHs.473152.

    Genome annotation databases

    EnsembliENST00000201031; ENSP00000201031; ENSG00000087510.
    ENST00000544508; ENSP00000442274; ENSG00000087510.
    GeneIDi7022.
    KEGGihsa:7022.
    UCSCiuc002xya.3. human.

    Polymorphism databases

    DMDMi12643310.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Activatin protein 2 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95693 mRNA. Translation: CAA64989.1 .
    U85658 mRNA. Translation: AAC51305.1 .
    AJ315934 Genomic DNA. Translation: CAC86997.1 .
    AK301572 mRNA. Translation: BAG63065.1 .
    AL121920 Genomic DNA. Translation: CAC10334.1 .
    BC035664 mRNA. Translation: AAH35664.2 .
    BC051829 mRNA. Translation: AAH51829.2 .
    AB041717 Genomic DNA. Translation: BAC11805.1 .
    CCDSi CCDS13454.1.
    RefSeqi NP_003213.1. NM_003222.3.
    UniGenei Hs.473152.

    3D structure databases

    ProteinModelPortali Q92754.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112880. 18 interactions.
    IntActi Q92754. 7 interactions.
    STRINGi 9606.ENSP00000201031.

    PTM databases

    PhosphoSitei Q92754.

    Polymorphism databases

    DMDMi 12643310.

    Proteomic databases

    MaxQBi Q92754.
    PaxDbi Q92754.
    PRIDEi Q92754.

    Protocols and materials databases

    DNASUi 7022.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000201031 ; ENSP00000201031 ; ENSG00000087510 .
    ENST00000544508 ; ENSP00000442274 ; ENSG00000087510 .
    GeneIDi 7022.
    KEGGi hsa:7022.
    UCSCi uc002xya.3. human.

    Organism-specific databases

    CTDi 7022.
    GeneCardsi GC20P055204.
    HGNCi HGNC:11744. TFAP2C.
    HPAi CAB016061.
    CAB016079.
    MIMi 601602. gene.
    neXtProti NX_Q92754.
    PharmGKBi PA36461.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300693.
    HOGENOMi HOG000231737.
    HOVERGENi HBG002455.
    InParanoidi Q92754.
    KOi K09177.
    OMAi EEVQNVD.
    OrthoDBi EOG7HHWS1.
    PhylomeDBi Q92754.
    TreeFami TF313718.

    Enzyme and pathway databases

    SignaLinki Q92754.

    Miscellaneous databases

    GeneWikii TFAP2C.
    GenomeRNAii 7022.
    NextBioi 27435.
    PROi Q92754.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92754.
    Bgeei Q92754.
    CleanExi HS_TFAP2C.
    Genevestigatori Q92754.

    Family and domain databases

    InterProi IPR004979. TF_AP2.
    IPR013854. TF_AP2_C.
    IPR008123. TF_AP2_gamma.
    [Graphical view ]
    PANTHERi PTHR10812. PTHR10812. 1 hit.
    Pfami PF03299. TF_AP-2. 1 hit.
    [Graphical view ]
    PRINTSi PR01751. AP2CTNSCPFCT.
    PR01748. AP2TNSCPFCT.
    ProtoNeti Search...

    Publicationsi

    1. "Chromosomal mapping of the human and mouse homologues of two new members of the AP-2 family of transcription factors."
      Williamson J.A., Bosher J.M., Skinner A., Sheer D., Williams T., Hurst H.C.
      Genomics 35:262-264(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Mammary tumor.
    2. "Identification of ERF-1 as a member of the AP2 transcription factor family."
      McPherson L.A., Baichwal V.R., Weigel R.J.
      Proc. Natl. Acad. Sci. U.S.A. 94:4342-4347(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 203-211 AND 361-370.
      Tissue: Mammary tumor.
    3. "Characterisation of the human AP-2gamma and AP-2beta genes."
      Haselton M.D., Ibbitt C.J., Hurst H.C.
      Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
      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] (ISOFORM 2).
      Tissue: Mammary gland.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Ovary and Skin.
    7. "Structure of human AP-2gamma gene."
      Nishizawa M., Ito S.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-450.
      Tissue: Liver.
    8. "Cardiac malformations, adrenal agenesis, neural crest defects and exencephaly in mice lacking Cited2, a new Tfap2 co-activator."
      Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I., Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.
      Nat. Genet. 29:469-474(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CITED2.
    9. "Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2."
      Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J., Hurst H.C., Shioda T., Bhattacharya S.
      J. Biol. Chem. 277:8559-8565(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CITED4.
    10. "Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo."
      Eloranta J.J., Hurst H.C.
      J. Biol. Chem. 277:30798-30804(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2I, SUMOYLATION AT LYS-10.
    11. "Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2."
      Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C., Bhattacharya S.
      J. Biol. Chem. 278:16021-16029(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CITED2.
    12. "Physical and functional interactions between the Wwox tumor suppressor protein and the AP-2gamma transcription factor."
      Aqeilan R.I., Palamarchuk A., Weigel R.J., Herrero J.J., Pekarsky Y., Croce C.M.
      Cancer Res. 64:8256-8261(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WWOX, DOMAIN, MUTAGENESIS OF TYR-59 AND TYR-64.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "The interaction of KCTD1 with transcription factor AP-2alpha inhibits its transactivation."
      Ding X., Luo C., Zhou J., Zhong Y., Hu X., Zhou F., Ren K., Gan L., He A., Zhu J., Gao X., Zhang J.
      J. Cell. Biochem. 106:285-295(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCTD1.
    16. "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-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Differential regulation of estrogen receptor alpha expression in breast cancer cells by metastasis-associated protein 1."
      Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y., Kim Y.N., Seong J.K., Lee M.O.
      Cancer Res. 74:1484-1494(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MTA1, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiAP2C_HUMAN
    AccessioniPrimary (citable) accession number: Q92754
    Secondary accession number(s): B4DWK3
    , O00685, O00730, Q86V30, Q8IVB6, Q9P1X2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 139 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3