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Q99967

- CITE2_HUMAN

UniProt

Q99967 - CITE2_HUMAN

Protein

Cbp/p300-interacting transactivator 2

Gene

CITED2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (20 Jun 2002)
      Previous versions | rss
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    Functioni

    Transcriptional coactivator of the p300/CBP-mediated trancription complex. Acts as a bridge, linking TFAP2 transcription factors and the p300/CBP transcriptional coactivator complex in order to stimulate TFAP2-mediated transcriptional activation. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates the peroxisome proliferator-activated receptors PPARA transcriptional activity. Enhances estrogen-dependent transactivation mediated by estrogen receptors. Acts also as a transcriptional corepressor; interferes with the binding of the transcription factors HIF1A or STAT2 and the p300/CBP transcriptional coactivator complex. Participates in sex determination and early gonad development by stimulating transcription activation of SRY. Plays a role in controlling left-right patterning during embryogenesis; potentiates transcriptional activation of NODAL-mediated gene transcription in the left lateral plate mesoderm (LPM). Plays an essential role in differentiation of the adrenal cortex from the adrenogonadal primordium (AGP); stimulates WT1-mediated transcription activation thereby up-regulating the nuclear hormone receptor NR5A1 promoter activity. Associates with chromatin to the PITX2 P1 promoter region.3 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. histone acetyltransferase binding Source: BHF-UCL
    3. LBD domain binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. RNA polymerase II transcription coactivator activity Source: Ensembl
    6. RNA polymerase II transcription corepressor activity Source: BHF-UCL
    7. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    8. transcription coactivator activity Source: UniProtKB
    9. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. adrenal cortex formation Source: UniProtKB
    2. bone morphogenesis Source: Ensembl
    3. cardiac neural crest cell development involved in heart development Source: Ensembl
    4. cell aging Source: Ensembl
    5. cell proliferation Source: UniProtKB
    6. central nervous system development Source: Ensembl
    7. cranial nerve morphogenesis Source: Ensembl
    8. decidualization Source: Ensembl
    9. determination of left/right symmetry Source: UniProtKB
    10. embryonic camera-type eye morphogenesis Source: Ensembl
    11. embryonic heart tube left/right pattern formation Source: BHF-UCL
    12. embryonic placenta development Source: Ensembl
    13. embryonic process involved in female pregnancy Source: Ensembl
    14. endocardial cushion development Source: Ensembl
    15. erythrocyte development Source: Ensembl
    16. granulocyte differentiation Source: Ensembl
    17. heart development Source: UniProtKB
    18. heart looping Source: Ensembl
    19. hematopoietic progenitor cell differentiation Source: Ensembl
    20. left/right axis specification Source: BHF-UCL
    21. lens morphogenesis in camera-type eye Source: Ensembl
    22. liver development Source: BHF-UCL
    23. male gonad development Source: Ensembl
    24. negative regulation of apoptotic process Source: BHF-UCL
    25. negative regulation of cell migration Source: BHF-UCL
    26. negative regulation of gene expression Source: UniProtKB
    27. negative regulation of transcription, DNA-templated Source: UniProtKB
    28. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    29. negative regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: BHF-UCL
    30. neural tube closure Source: Ensembl
    31. nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry Source: BHF-UCL
    32. outflow tract morphogenesis Source: BHF-UCL
    33. peripheral nervous system development Source: Ensembl
    34. positive regulation of cell-cell adhesion Source: BHF-UCL
    35. positive regulation of cell cycle Source: UniProtKB
    36. positive regulation of gene expression Source: UniProtKB
    37. positive regulation of male gonad development Source: UniProtKB
    38. positive regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
    39. positive regulation of transcription, DNA-templated Source: UniProtKB
    40. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    41. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    42. pulmonary artery morphogenesis Source: Ensembl
    43. regulation of organ formation Source: UniProtKB
    44. regulation of RNA biosynthetic process Source: GOC
    45. response to estrogen Source: UniProtKB
    46. response to fluid shear stress Source: BHF-UCL
    47. response to hypoxia Source: UniProtKB
    48. response to mechanical stimulus Source: Ensembl
    49. sex determination Source: UniProtKB
    50. skeletal muscle cell differentiation Source: Ensembl
    51. spleen development Source: BHF-UCL
    52. thymus development Source: Ensembl
    53. transforming growth factor beta receptor signaling pathway Source: Ensembl
    54. trophectodermal cell differentiation Source: Ensembl
    55. vasculogenesis Source: Ensembl
    56. ventricular septum morphogenesis Source: BHF-UCL

    Keywords - Molecular functioni

    Activator, Developmental protein, Repressor

    Keywords - Biological processi

    Differentiation, Stress response, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cbp/p300-interacting transactivator 2
    Alternative name(s):
    MSG-related protein 1
    Short name:
    MRG-1
    P35srj
    Gene namesi
    Name:CITED2
    Synonyms:MRG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:1987. CITED2.

    Subcellular locationi

    Nucleus 3 Publications
    Note: Colocalizes with EP300 in dot-like structures.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nuclear chromatin Source: BHF-UCL
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Ventricular septal defect 2 (VSD2) [MIM:614431]: A common form of congenital cardiovascular anomaly that may occur alone or in combination with other cardiac malformations. It can affect any portion of the ventricular septum, resulting in abnormal communications between the two lower chambers of the heart. Classification is based on location of the communication, such as perimembranous, inlet, outlet (infundibular), central muscular, marginal muscular, or apical muscular defect. Large defects that go unrepaired may give rise to cardiac enlargement, congestive heart failure, pulmonary hypertension, Eisenmenger's syndrome, delayed fetal brain development, arrhythmias, and even sudden cardiac death.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti170 – 1789Missing in VSD2; reduces coactivation of the TFAP2C gene to 50% of that obtained with wild-type and represses HIF1A with about 60% efficiency compared to wild-type. 1 Publication
    VAR_067583
    Atrial septal defect 8 (ASD8) [MIM:614433]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791S → GGSSTPGGS in ASD8; demonstrates only about 75% of the repressive activity of wild-type.
    VAR_067584
    Natural varianti198 – 1992Missing in ASD8; demonstrates only about 75% of the repressive activity of wild-type. 1 Publication
    VAR_067585

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi243 – 2464Missing: Inhibits transactivation activity. 1 Publication
    Mutagenesisi243 – 2431L → E: Inhibits transactivation activity; when associated with E-246. 1 Publication
    Mutagenesisi246 – 2461L → E: Inhibits transactivation activity; when associated with E-243. 1 Publication

    Keywords - Diseasei

    Atrial septal defect, Disease mutation

    Organism-specific databases

    MIMi614431. phenotype.
    614433. phenotype.
    Orphaneti99103. Atrial septal defect, ostium secundum type.
    99105. Atrial septal defect, sinus venosus type.
    99097. Single ventricular septal defect.
    101063. Situs inversus totalis.
    3303. Tetralogy of Fallot.
    PharmGKBiPA26524.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 270270Cbp/p300-interacting transactivator 2PRO_0000144726Add
    BLAST

    Proteomic databases

    PaxDbiQ99967.
    PRIDEiQ99967.

    Expressioni

    Inductioni

    By hypoxia and deferoxamine.1 Publication

    Gene expression databases

    ArrayExpressiQ99967.
    BgeeiQ99967.
    CleanExiHS_CITED2.
    GenevestigatoriQ99967.

    Organism-specific databases

    HPAiCAB016157.

    Interactioni

    Subunit structurei

    Interacts (via C-terminus) with SMAD2. Interacts (via C-terminus) with SMAD3 (via MH2 domain). Interacts with LHX2 (via LIM domains). Interacts with WT1 By similarity. Interacts (via C-terminus) with EP300 (via CH1 domain); the interaction is stimulated in response to hypoxia. Interacts with PPARA. Interacts (via C-terminus) with TFAP2A, TFAP2B and TFAP2C.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EP300Q094723EBI-937732,EBI-447295
    HNF4AP412353EBI-937732,EBI-1049011
    TFAP2CQ927542EBI-937732,EBI-937309

    Protein-protein interaction databases

    BioGridi115649. 11 interactions.
    IntActiQ99967. 7 interactions.
    MINTiMINT-112487.
    STRINGi9606.ENSP00000356623.

    Structurei

    Secondary structure

    1
    270
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi221 – 2233
    Helixi227 – 2359
    Beta strandi237 – 2393
    Helixi251 – 2533
    Helixi254 – 2563
    Helixi266 – 2683

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P4QNMR-A216-259[»]
    1R8UNMR-A220-269[»]
    DisProtiDP00356.
    ProteinModelPortaliQ99967.
    SMRiQ99967. Positions 220-269.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99967.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi21 – 5737His-richAdd
    BLAST
    Compositional biasi162 – 19938Gly-richAdd
    BLAST
    Compositional biasi219 – 25840Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the CITED family.Curated

    Phylogenomic databases

    eggNOGiNOG44915.
    HOGENOMiHOG000231079.
    HOVERGENiHBG075182.
    InParanoidiQ99967.
    OMAiDHIHYGA.
    OrthoDBiEOG72NRRB.
    PhylomeDBiQ99967.
    TreeFamiTF331915.

    Family and domain databases

    InterProiIPR007576. CITED.
    [Graphical view]
    PANTHERiPTHR17045. PTHR17045. 1 hit.
    PfamiPF04487. CITED. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99967-1) [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

    MADHMMAMNH GRFPDGTNGL HHHPAHRMGM GQFPSPHHHQ QQQPQHAFNA    50
    LMGEHIHYGA GNMNATSGIR HAMGPGTVNG GHPPSALAPA ARFNNSQFMG 100
    PPVASQGGSL PASMQLQKLN NQYFNHHPYP HNHYMPDLHP AAGHQMNGTN 150
    QHFRDCNPKH SGGSSTPGGS GGSSTPGGSG SSSGGGAGSS NSGGGSGSGN 200
    MPASVAHVPA AMLPPNVIDT DFIDEEVLMS LVIEMGLDRI KELPELWLGQ 250
    NEFDFMTDFV CKQQPSRVSC 270
    Length:270
    Mass (Da):28,497
    Last modified:June 20, 2002 - v2
    Checksum:i45DDE3A9E2B4C472
    GO
    Isoform 2 (identifier: Q99967-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         159-215: Missing.

    Show »
    Length:213
    Mass (Da):23,732
    Checksum:iC91FAABA3D2A9AD1
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti170 – 1789Missing in VSD2; reduces coactivation of the TFAP2C gene to 50% of that obtained with wild-type and represses HIF1A with about 60% efficiency compared to wild-type. 1 Publication
    VAR_067583
    Natural varianti179 – 1791S → GGSSTPGGS in ASD8; demonstrates only about 75% of the repressive activity of wild-type.
    VAR_067584
    Natural varianti198 – 1992Missing in ASD8; demonstrates only about 75% of the repressive activity of wild-type. 1 Publication
    VAR_067585

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei159 – 21557Missing in isoform 2. 1 PublicationVSP_001089Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65093 mRNA. Translation: AAC51114.1.
    AF129290 Genomic DNA. Translation: AAF01263.1.
    AF129290 Genomic DNA. Translation: AAF01264.1.
    AF109161 mRNA. Translation: AAD10055.1.
    AL592429 Genomic DNA. Translation: CAH70354.1.
    BC004377 mRNA. Translation: AAH04377.1.
    CCDSiCCDS5195.1. [Q99967-1]
    RefSeqiNP_001161860.1. NM_001168388.2. [Q99967-1]
    NP_001161861.2. NM_001168389.2.
    NP_006070.2. NM_006079.4. [Q99967-1]
    UniGeneiHs.82071.

    Genome annotation databases

    EnsembliENST00000367651; ENSP00000356623; ENSG00000164442. [Q99967-1]
    ENST00000536159; ENSP00000442831; ENSG00000164442. [Q99967-1]
    ENST00000537332; ENSP00000444198; ENSG00000164442. [Q99967-1]
    GeneIDi10370.
    KEGGihsa:10370.
    UCSCiuc003qip.2. human. [Q99967-1]

    Polymorphism databases

    DMDMi21542403.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65093 mRNA. Translation: AAC51114.1 .
    AF129290 Genomic DNA. Translation: AAF01263.1 .
    AF129290 Genomic DNA. Translation: AAF01264.1 .
    AF109161 mRNA. Translation: AAD10055.1 .
    AL592429 Genomic DNA. Translation: CAH70354.1 .
    BC004377 mRNA. Translation: AAH04377.1 .
    CCDSi CCDS5195.1. [Q99967-1 ]
    RefSeqi NP_001161860.1. NM_001168388.2. [Q99967-1 ]
    NP_001161861.2. NM_001168389.2.
    NP_006070.2. NM_006079.4. [Q99967-1 ]
    UniGenei Hs.82071.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P4Q NMR - A 216-259 [» ]
    1R8U NMR - A 220-269 [» ]
    DisProti DP00356.
    ProteinModelPortali Q99967.
    SMRi Q99967. Positions 220-269.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115649. 11 interactions.
    IntActi Q99967. 7 interactions.
    MINTi MINT-112487.
    STRINGi 9606.ENSP00000356623.

    Polymorphism databases

    DMDMi 21542403.

    Proteomic databases

    PaxDbi Q99967.
    PRIDEi Q99967.

    Protocols and materials databases

    DNASUi 10370.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367651 ; ENSP00000356623 ; ENSG00000164442 . [Q99967-1 ]
    ENST00000536159 ; ENSP00000442831 ; ENSG00000164442 . [Q99967-1 ]
    ENST00000537332 ; ENSP00000444198 ; ENSG00000164442 . [Q99967-1 ]
    GeneIDi 10370.
    KEGGi hsa:10370.
    UCSCi uc003qip.2. human. [Q99967-1 ]

    Organism-specific databases

    CTDi 10370.
    GeneCardsi GC06M139735.
    H-InvDB HIX0006261.
    HGNCi HGNC:1987. CITED2.
    HPAi CAB016157.
    MIMi 602937. gene.
    614431. phenotype.
    614433. phenotype.
    neXtProti NX_Q99967.
    Orphaneti 99103. Atrial septal defect, ostium secundum type.
    99105. Atrial septal defect, sinus venosus type.
    99097. Single ventricular septal defect.
    101063. Situs inversus totalis.
    3303. Tetralogy of Fallot.
    PharmGKBi PA26524.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44915.
    HOGENOMi HOG000231079.
    HOVERGENi HBG075182.
    InParanoidi Q99967.
    OMAi DHIHYGA.
    OrthoDBi EOG72NRRB.
    PhylomeDBi Q99967.
    TreeFami TF331915.

    Miscellaneous databases

    ChiTaRSi CITED2. human.
    EvolutionaryTracei Q99967.
    GeneWikii CITED2.
    GenomeRNAii 10370.
    NextBioi 39307.
    PROi Q99967.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99967.
    Bgeei Q99967.
    CleanExi HS_CITED2.
    Genevestigatori Q99967.

    Family and domain databases

    InterProi IPR007576. CITED.
    [Graphical view ]
    PANTHERi PTHR17045. PTHR17045. 1 hit.
    Pfami PF04487. CITED. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "msg1, a novel melanocyte-specific gene, encodes a nuclear protein and is associated with pigmentation."
      Shioda T., Fenner M.H., Isselbacher K.J.
      Proc. Natl. Acad. Sci. U.S.A. 93:12298-12303(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
    2. "Molecular cloning and chromosomal localization of the human CITED2 gene encoding p35srj/Mrg1."
      Leung M.K., Jones T., Michels C.L., Livingston D.M., Bhattacharya S.
      Genomics 61:307-313(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1."
      Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L., Livingston D.M.
      Genes Dev. 13:64-75(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EP300, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "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].
    5. "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: Pancreas.
    6. "Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein."
      Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S., Isselbacher K.J., Brown M., Shioda T.
      Genes Dev. 15:2598-2612(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "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: INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C.
    8. "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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EP300; TFAP2A; TFAP2B AND TFAP2C.
    9. "Identification of the CREB-binding protein/p300-interacting protein CITED2 as a peroxisome proliferator-activated receptor alpha coregulator."
      Tien E.S., Davis J.W., Vanden Heuvel J.P.
      J. Biol. Chem. 279:24053-24063(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPARA.
    10. "Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2."
      Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J.
      Nat. Struct. Biol. 10:504-512(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 216-259 IN COMPLEX WITH 323-423 OF EP300 AND ZINC IONS, INTERACTION WITH EP300, MUTAGENESIS OF 243-LEU--LEU-246; LEU-243 AND LEU-246.
    11. "Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites."
      De Guzman R.N., Martinez-Yamout M.A., Dyson H.J., Wright P.E.
      J. Biol. Chem. 279:3042-3049(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 220-269 IN COMPLEX WITH 340-439 OF CREBBP AND ZINC IONS.
    12. "Identification and functional analysis of CITED2 mutations in patients with congenital heart defects."
      Sperling S., Grimm C.H., Dunkel I., Mebus S., Sperling H.P., Ebner A., Galli R., Lehrach H., Fusch C., Berger F., Hammer S.
      Hum. Mutat. 26:575-582(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VSD2 170-SER--GLY-178 DEL, VARIANTS ASD8 GLY-GLY-SER-SER-THR-PRO-GLY-GLY-SER-179 INS AND 198-SER-GLY-199 DEL, CHARACTERIZATION OF VARIANT VSD2 170-SER--GLY-178 DEL, CHARACTERIZATION OF VARIANTS ASD8 GLY-GLY-SER-SER-THR-PRO-GLY-GLY-SER-179 INS AND 198-SER-GLY-199 DEL.

    Entry informationi

    Entry nameiCITE2_HUMAN
    AccessioniPrimary (citable) accession number: Q99967
    Secondary accession number(s): O95426, Q5VTF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 20, 2002
    Last modified: October 1, 2014
    This is version 137 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

    3D-structure, 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3