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Q92481

- AP2B_HUMAN

UniProt

Q92481 - AP2B_HUMAN

Protein

Transcription factor AP-2-beta

Gene

TFAP2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (10 Jul 2007)
      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. AP-2-beta appears to be required for normal face and limb development and for proper terminal differentiation and function of renal tubular epithelia.1 Publication

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. enhancer sequence-specific DNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein dimerization activity Source: UniProtKB
    7. protein heterodimerization activity Source: UniProtKB
    8. protein homodimerization activity Source: UniProtKB
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    10. RNA polymerase II core promoter sequence-specific DNA binding Source: UniProtKB
    11. RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity Source: UniProtKB
    12. RNA polymerase II transcription coactivator activity Source: UniProtKB
    13. RNA polymerase II transcription corepressor activity Source: UniProtKB
    14. sequence-specific DNA binding Source: UniProtKB
    15. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    16. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    17. transcription coactivator activity Source: UniProtKB
    18. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. aorta morphogenesis Source: UniProtKB
    2. calcium ion homeostasis Source: UniProtKB
    3. cellular ammonia homeostasis Source: UniProtKB
    4. cellular creatinine homeostasis Source: UniProtKB
    5. cellular urea homeostasis Source: UniProtKB
    6. collecting duct development Source: UniProtKB
    7. distal tubule development Source: UniProtKB
    8. ductus arteriosus closure Source: UniProtKB
    9. fat cell differentiation Source: UniProtKB
    10. forelimb morphogenesis Source: UniProtKB
    11. glucose homeostasis Source: UniProtKB
    12. glucose metabolic process Source: UniProtKB
    13. hindlimb morphogenesis Source: UniProtKB
    14. kidney development Source: UniProtKB
    15. magnesium ion homeostasis Source: UniProtKB
    16. metanephric nephron development Source: Ensembl
    17. negative regulation of apoptotic process Source: UniProtKB
    18. negative regulation of cell proliferation Source: UniProtKB
    19. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    20. negative regulation of neuron apoptotic process Source: Ensembl
    21. negative regulation of transcription, DNA-templated Source: UniProtKB
    22. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    23. phosphate ion homeostasis Source: UniProtKB
    24. positive regulation of cell proliferation Source: UniProtKB
    25. positive regulation of neuron apoptotic process Source: UniProtKB
    26. positive regulation of transcription, DNA-templated Source: UniProtKB
    27. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    28. positive regulation of urine volume Source: UniProtKB
    29. potassium ion homeostasis Source: UniProtKB
    30. regulation of BMP signaling pathway Source: UniProtKB
    31. regulation of cell differentiation Source: UniProtKB
    32. regulation of insulin secretion Source: UniProtKB
    33. regulation of transcription, DNA-templated Source: HGNC
    34. renal water homeostasis Source: UniProtKB
    35. response to drug Source: Ensembl
    36. response to lithium ion Source: Ensembl
    37. retina layer formation Source: UniProtKB
    38. skin development Source: Ensembl
    39. sodium ion homeostasis Source: UniProtKB
    40. sympathetic nervous system development Source: UniProtKB

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor AP-2-beta
    Short name:
    AP2-beta
    Alternative name(s):
    Activating enhancer-binding protein 2-beta
    Gene namesi
    Name:TFAP2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:11743. TFAP2B.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Char syndrome (CHAR) [MIM:169100]: An autosomal dominant disorder characterized by patent ductus arteriosus (PDA), facial dysmorphism and hand anomalies.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti73 – 731P → R in CHAR. 1 Publication
    VAR_016977
    Natural varianti236 – 2361R → C in CHAR. 1 Publication
    VAR_016978
    Natural varianti236 – 2361R → S in CHAR. 1 Publication
    VAR_016979
    Natural varianti275 – 2751A → D in CHAR. 1 Publication
    VAR_011318
    Natural varianti285 – 2851R → Q in CHAR. 1 Publication
    VAR_016980
    Natural varianti300 – 3001R → C in CHAR. 1 Publication
    VAR_011319

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi169100. phenotype.
    Orphaneti46627. Char syndrome.
    PharmGKBiPA36460.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 460460Transcription factor AP-2-betaPRO_0000184801Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki21 – 21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Modified residuei258 – 2581Phosphoserine; by PKABy similarity

    Post-translational modificationi

    Sumoylated on Lys-21; which inhibits transcriptional activity.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ92481.
    PaxDbiQ92481.
    PRIDEiQ92481.

    PTM databases

    PhosphoSiteiQ92481.

    Expressioni

    Gene expression databases

    ArrayExpressiQ92481.
    BgeeiQ92481.
    CleanExiHS_TFAP2B.
    GenevestigatoriQ92481.

    Organism-specific databases

    HPAiCAB010426.
    HPA034683.

    Interactioni

    Subunit structurei

    Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. 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.5 Publications

    Protein-protein interaction databases

    BioGridi112879. 11 interactions.
    IntActiQ92481. 4 interactions.
    MINTiMINT-1424146.
    STRINGi9606.ENSP00000377265.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92481.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi41 – 13191Gln/Pro-rich (transactivation domain)Add
    BLAST

    Sequence similaritiesi

    Belongs to the AP-2 family.Curated

    Phylogenomic databases

    eggNOGiNOG300693.
    HOVERGENiHBG002455.
    InParanoidiQ92481.
    KOiK09176.
    OMAiIGHPGME.
    OrthoDBiEOG7HHWS1.
    PhylomeDBiQ92481.
    TreeFamiTF313718.

    Family and domain databases

    InterProiIPR004979. TF_AP2.
    IPR008122. TF_AP2_beta.
    IPR013854. TF_AP2_C.
    [Graphical view]
    PANTHERiPTHR10812. PTHR10812. 1 hit.
    PfamiPF03299. TF_AP-2. 1 hit.
    [Graphical view]
    PRINTSiPR01750. AP2BTNSCPFCT.
    PR01748. AP2TNSCPFCT.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92481-1) [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

    MHSPPRDQAA IMLWKLVENV KYEDIYEDRH DGVPSHSSRL SQLGSVSQGP    50
    YSSAPPLSHT PSSDFQPPYF PPPYQPLPYH QSQDPYSHVN DPYSLNPLHQ 100
    PQQHPWGQRQ RQEVGSEAGS LLPQPRAALP QLSGLDPRRD YHSVRRPDVL 150
    LHSAHHGLDA GMGDSLSLHG LGHPGMEDVQ SVEDANNSGM NLLDQSVIKK 200
    VPVPPKSVTS LMMNKDGFLG GMSVNTGEVF CSVPGRLSLL SSTSKYKVTV 250
    GEVQRRLSPP ECLNASLLGG VLRRAKSKNG GRSLRERLEK IGLNLPAGRR 300
    KAANVTLLTS LVEGEAVHLA RDFGYICETE FPAKAVSEYL NRQHTDPSDL 350
    HSRKNMLLAT KQLCKEFTDL LAQDRTPIGN SRPSPILEPG IQSCLTHFSL 400
    ITHGFGAPAI CAALTALQNY LTEALKGMDK MFLNNTTTNR HTSGEGPGSK 450
    TGDKEEKHRK 460
    Length:460
    Mass (Da):50,474
    Last modified:July 10, 2007 - v2
    Checksum:iA6420EA0C265DDA2
    GO
    Isoform 2 (identifier: Q92481-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         27-27: E → EMLVHTYSSM

    Note: No experimental confirmation available.

    Show »
    Length:469
    Mass (Da):51,524
    Checksum:iC4E0DCC428DBF0F8
    GO

    Sequence cautioni

    The sequence CAA64990.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA71047.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB41305.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAC01130.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti258 – 2581S → A in CAA71047. (PubMed:9271117)Curated
    Sequence conflicti362 – 46099QLCKE…EKHRK → GNFVKNLRIYWRRTGHR in CAA71047. (PubMed:9271117)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti73 – 731P → R in CHAR. 1 Publication
    VAR_016977
    Natural varianti236 – 2361R → C in CHAR. 1 Publication
    VAR_016978
    Natural varianti236 – 2361R → S in CHAR. 1 Publication
    VAR_016979
    Natural varianti275 – 2751A → D in CHAR. 1 Publication
    VAR_011318
    Natural varianti285 – 2851R → Q in CHAR. 1 Publication
    VAR_016980
    Natural varianti300 – 3001R → C in CHAR. 1 Publication
    VAR_011319

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei27 – 271E → EMLVHTYSSM in isoform 2. CuratedVSP_006408

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09912 Genomic DNA. Translation: CAA71047.1. Different initiation.
    AL031224 Genomic DNA. Translation: CAB41305.1. Different initiation.
    AL031224, AL049693 Genomic DNA. Translation: CAI20235.2.
    AL049693 Genomic DNA. Translation: CAB89563.3.
    BC037225 mRNA. Translation: AAH37225.2.
    AJ278356 Genomic DNA. Translation: CAC01130.1. Different initiation.
    X95694 mRNA. Translation: CAA64990.1. Different initiation.
    CCDSiCCDS4934.2. [Q92481-1]
    RefSeqiNP_003212.2. NM_003221.3. [Q92481-1]
    UniGeneiHs.33102.

    Genome annotation databases

    EnsembliENST00000393655; ENSP00000377265; ENSG00000008196. [Q92481-1]
    GeneIDi7021.
    KEGGihsa:7021.
    UCSCiuc003pag.3. human. [Q92481-1]

    Polymorphism databases

    DMDMi152031557.

    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
    Y09912 Genomic DNA. Translation: CAA71047.1 . Different initiation.
    AL031224 Genomic DNA. Translation: CAB41305.1 . Different initiation.
    AL031224 , AL049693 Genomic DNA. Translation: CAI20235.2 .
    AL049693 Genomic DNA. Translation: CAB89563.3 .
    BC037225 mRNA. Translation: AAH37225.2 .
    AJ278356 Genomic DNA. Translation: CAC01130.1 . Different initiation.
    X95694 mRNA. Translation: CAA64990.1 . Different initiation.
    CCDSi CCDS4934.2. [Q92481-1 ]
    RefSeqi NP_003212.2. NM_003221.3. [Q92481-1 ]
    UniGenei Hs.33102.

    3D structure databases

    ProteinModelPortali Q92481.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112879. 11 interactions.
    IntActi Q92481. 4 interactions.
    MINTi MINT-1424146.
    STRINGi 9606.ENSP00000377265.

    PTM databases

    PhosphoSitei Q92481.

    Polymorphism databases

    DMDMi 152031557.

    Proteomic databases

    MaxQBi Q92481.
    PaxDbi Q92481.
    PRIDEi Q92481.

    Protocols and materials databases

    DNASUi 7021.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393655 ; ENSP00000377265 ; ENSG00000008196 . [Q92481-1 ]
    GeneIDi 7021.
    KEGGi hsa:7021.
    UCSCi uc003pag.3. human. [Q92481-1 ]

    Organism-specific databases

    CTDi 7021.
    GeneCardsi GC06P050833.
    GeneReviewsi TFAP2B.
    HGNCi HGNC:11743. TFAP2B.
    HPAi CAB010426.
    HPA034683.
    MIMi 169100. phenotype.
    601601. gene.
    neXtProti NX_Q92481.
    Orphaneti 46627. Char syndrome.
    PharmGKBi PA36460.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300693.
    HOVERGENi HBG002455.
    InParanoidi Q92481.
    KOi K09176.
    OMAi IGHPGME.
    OrthoDBi EOG7HHWS1.
    PhylomeDBi Q92481.
    TreeFami TF313718.

    Miscellaneous databases

    GeneWikii TFAP2B.
    GenomeRNAii 7021.
    NextBioi 27431.
    PROi Q92481.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92481.
    Bgeei Q92481.
    CleanExi HS_TFAP2B.
    Genevestigatori Q92481.

    Family and domain databases

    InterProi IPR004979. TF_AP2.
    IPR008122. TF_AP2_beta.
    IPR013854. TF_AP2_C.
    [Graphical view ]
    PANTHERi PTHR10812. PTHR10812. 1 hit.
    Pfami PF03299. TF_AP-2. 1 hit.
    [Graphical view ]
    PRINTSi PR01750. AP2BTNSCPFCT.
    PR01748. AP2TNSCPFCT.
    ProtoNeti Search...

    Publicationsi

    1. "Enhanced apoptotic cell death of renal epithelial cells in mice lacking transcription factor AP-2beta."
      Moser M., Buettner R.
      Genes Dev. 11:1938-1948(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Skin.
    4. "Characterisation of the human AP-2beta and AP-2gamma genes."
      Hasleton M.D., Skinner A., Hurst H.C.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
    5. "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] OF 2-460 (ISOFORM 1).
      Tissue: Mammary tumor.
    6. "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.
    7. "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.
    8. "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-21.
    9. "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.
    10. "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.
    11. "Mutations in TFAP2B cause Char syndrome, a familial form of patent ductus arteriosus."
      Satoda M., Zhao F., Diaz G.A., Burn J., Goodship J., Davidson H.R., Pierpont M.E.M., Gelb B.D.
      Nat. Genet. 25:42-46(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CHAR ASP-275 AND CYS-300.
    12. "Novel TFAP2B mutations that cause Char syndrome provide a genotype-phenotype correlation."
      Zhao F., Weismann C.G., Satoda M., Pierpont M.E.M., Sweeney E., Thompson E.M., Gelb B.D.
      Am. J. Hum. Genet. 69:695-703(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CHAR ARG-73; CYS-236; SER-236 AND GLN-285.

    Entry informationi

    Entry nameiAP2B_HUMAN
    AccessioniPrimary (citable) accession number: Q92481
    Secondary accession number(s): Q5JYX6
    , Q9NQ63, Q9NU99, Q9UJI7, Q9Y214, Q9Y3K3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 138 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, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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