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Q99966

- CITE1_HUMAN

UniProt

Q99966 - CITE1_HUMAN

Protein

Cbp/p300-interacting transactivator 1

Gene

CITED1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Transcriptional coactivator of the p300/CBP-mediated trancription complex. Enhances SMAD-mediated transcription by strengthening the functional link between the DNA-binding SMAD transcription factors and the p300/CBP transcription coactivator complex. Stimulates estrogen-dependent transactivation activity mediated by estrogen receptors signaling; stabilizes the interaction of estrogen receptor ESR1 and histone acetyltransferase EP300. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Induces transcription from estrogen-responsive promoters and protection against cell death. Potentiates EGR2-mediated transcriptional activation activity from the ERBB2 promoter. Acts as an inhibitor of osteoblastic mineralization through a cAMP-dependent parathyroid hormone receptor signaling. May play a role in pigmentation of melanocytes. Associates with chromatin to the estrogen-responsive TGF-alpha promoter region in a estrogen-dependent manner.3 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. co-SMAD binding Source: BHF-UCL
    3. LBD domain binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    8. transcription coactivator activity Source: UniProtKB
    9. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. brain development Source: Ensembl
    3. branching involved in ureteric bud morphogenesis Source: UniProtKB
    4. cell proliferation Source: BHF-UCL
    5. embryonic axis specification Source: Ensembl
    6. labyrinthine layer development Source: Ensembl
    7. melanin biosynthetic process Source: UniProtKB
    8. melanocyte differentiation Source: UniProtKB
    9. mesenchymal to epithelial transition Source: BHF-UCL
    10. metanephros development Source: BHF-UCL
    11. negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis Source: Ensembl
    12. negative regulation of neuron apoptotic process Source: UniProtKB
    13. negative regulation of osteoblast differentiation Source: UniProtKB
    14. negative regulation of transcription, DNA-templated Source: UniProtKB
    15. negative regulation of Wnt signaling pathway Source: BHF-UCL
    16. nucleocytoplasmic transport Source: UniProtKB
    17. pigmentation Source: UniProtKB
    18. placenta development Source: UniProtKB
    19. positive regulation of gene expression Source: UniProtKB
    20. positive regulation of transcription, DNA-templated Source: UniProtKB
    21. positive regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    22. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    23. response to cAMP Source: UniProtKB
    24. response to cytokine Source: UniProtKB
    25. response to estrogen Source: UniProtKB
    26. response to insulin Source: UniProtKB
    27. response to interferon-gamma Source: UniProtKB
    28. response to interleukin-1 Source: UniProtKB
    29. response to interleukin-11 Source: UniProtKB
    30. response to interleukin-2 Source: UniProtKB
    31. response to interleukin-4 Source: UniProtKB
    32. response to interleukin-6 Source: UniProtKB
    33. response to interleukin-9 Source: UniProtKB
    34. response to lipopolysaccharide Source: UniProtKB
    35. response to parathyroid hormone Source: UniProtKB
    36. response to transforming growth factor beta Source: UniProtKB
    37. SMAD protein signal transduction Source: BHF-UCL
    38. spongiotrophoblast layer development Source: Ensembl
    39. transcription, DNA-templated Source: UniProtKB-KW
    40. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    41. vasculogenesis Source: Ensembl

    Keywords - Molecular functioni

    Activator, Developmental protein

    Keywords - Biological processi

    Apoptosis, Differentiation, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cbp/p300-interacting transactivator 1
    Alternative name(s):
    Melanocyte-specific protein 1
    Gene namesi
    Name:CITED1
    Synonyms:MSG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:1986. CITED1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Shuttles between the nucleus and the cytoplasm by a nuclear export signal and (NES) in a CRM1-dependent manner.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161S → A: Reduces strongly phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-63; A-67; A-71 and A-137. 1 Publication
    Mutagenesisi63 – 631S → A: Reduces strongly phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-16; A-67; A-71 and A-137. 1 Publication
    Mutagenesisi67 – 671S → A: Reduces strongly phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-16; A-63; A-71 and A-137. 1 Publication
    Mutagenesisi71 – 711S → A: Reduces strongly phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-16; A-63; A-67 and A-137. 1 Publication
    Mutagenesisi91 – 911L → A: Does not change subcellular localization; when associated with A-95.
    Mutagenesisi95 – 951M → A: Does not change subcellular localization; when associated with A-91.
    Mutagenesisi137 – 1371S → A: Reduces strongly phosphorylation; when associated with A-16; A-63; A-67 and A-71. 1 Publication
    Mutagenesisi155 – 1562EE → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
    Mutagenesisi157 – 1582VL → AA: Inhibits interaction with ESR1 and ER-coactivation activity.
    Mutagenesisi159 – 1602MS → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
    Mutagenesisi161 – 1622LV → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
    Mutagenesisi163 – 1642VE → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
    Mutagenesisi165 – 1651L → A: Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-167. 1 Publication
    Mutagenesisi166 – 1672GL → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-165.
    Mutagenesisi176 – 1761L → A: Does not change subcellular localization; when associated with A-178.
    Mutagenesisi178 – 1781L → A: Does not change subcellular localization; when associated with A-176.

    Organism-specific databases

    PharmGKBiPA26523.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 193193Cbp/p300-interacting transactivator 1PRO_0000144724Add
    BLAST

    Post-translational modificationi

    Phosphorylated. Phosphorylation changes in a cell cycle-dependent manner and reduces its transcriptional coactivator activity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ99966.
    PRIDEiQ99966.

    PTM databases

    PhosphoSiteiQ99966.

    Expressioni

    Tissue specificityi

    Expressed only in melanocytes and testis.

    Inductioni

    Up-regulated by GPR39 in neuronal cells.1 Publication

    Gene expression databases

    ArrayExpressiQ99966.
    BgeeiQ99966.
    CleanExiHS_CITED1.
    GenevestigatoriQ99966.

    Interactioni

    Subunit structurei

    Interacts (via C-terminus) with CREBBP. Interacts with EGR2 By similarity. Homodimer. Binds to RBM14. Interacts (via N-terminus) with HSPA8; the interaction suppresses the association of CITED1 with p300/CBP and SMAD-mediated transcription transactivation. Interacts (via C-terminus) with TOX3 (via HGM box); the interaction increases estrogen-response element (ERE)-dependent transcription and protection against cell death. Interacts with ESR1; the interaction occurs in a estrogen-dependent manner By similarity. Interacts (unphosphorylated form preferentially and via C-terminus) with EP300.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATF2P153362EBI-2624951,EBI-1170906
    ESR1P033723EBI-2624951,EBI-78473
    JUNP054122EBI-2624951,EBI-852823

    Protein-protein interaction databases

    BioGridi110572. 7 interactions.
    IntActiQ99966. 7 interactions.
    MINTiMINT-223965.
    STRINGi9606.ENSP00000388548.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99966.
    SMRiQ99966. Positions 150-189.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi158 – 16710Nuclear export signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi149 – 18840Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the CITED family.Curated

    Phylogenomic databases

    eggNOGiNOG41708.
    HOGENOMiHOG000072675.
    HOVERGENiHBG075182.
    InParanoidiQ99966.
    OMAiQYHGMAA.
    OrthoDBiEOG7TJ3K5.
    PhylomeDBiQ99966.
    TreeFamiTF331915.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99966-1) [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

    MPTTSRPALD VKGGTSPAKE DANQEMSSVA YSNLAVKDRK AVAILHYPGV    50
    ASNGTKASGA PTSSSGSPIG SPTTTPPTKP PSFNLHPAPH LLASMHLQKL 100
    NSQYQGMAAA TPGQPGEAGP LQNWDFGAQA GGAESLSPSA GAQSPAIIDS 150
    DPVDEEVLMS LVVELGLDRA NELPELWLGQ NEFDFTADFP SSC 193
    Length:193
    Mass (Da):19,896
    Last modified:May 18, 2010 - v2
    Checksum:i9B0CF50CA639ECCB
    GO
    Isoform 2 (identifier: Q99966-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEPSAQQLQLAASLPANLSNFCQGSEM

    Note: No experimental confirmation available.

    Show »
    Length:219
    Mass (Da):22,613
    Checksum:iCB89284B2F0B952B
    GO

    Sequence cautioni

    The sequence N30508 differs from that shown. Reason: Frameshift at position 67.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961H → Q.4 Publications
    Corresponds to variant rs3012627 [ dbSNP | Ensembl ].
    VAR_053038

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MEPSAQQLQLAASLPANLSN FCQGSEM in isoform 2. 1 PublicationVSP_039897

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65092 mRNA. Translation: AAC51113.1.
    AB451286 mRNA. Translation: BAG70100.1.
    AB451418 mRNA. Translation: BAG70232.1.
    AL135749 Genomic DNA. No translation available.
    CH471213 Genomic DNA. Translation: EAW71819.1.
    BC004240 mRNA. Translation: AAH04240.1.
    N30508 mRNA. No translation available.
    CCDSiCCDS14419.1. [Q99966-1]
    CCDS48136.1. [Q99966-2]
    PIRiJC6114.
    RefSeqiNP_001138357.1. NM_001144885.1. [Q99966-2]
    NP_001138358.1. NM_001144886.1. [Q99966-1]
    NP_001138359.1. NM_001144887.1. [Q99966-1]
    NP_004134.2. NM_004143.3. [Q99966-1]
    XP_005262323.1. XM_005262266.2. [Q99966-2]
    XP_005262324.1. XM_005262267.2. [Q99966-1]
    UniGeneiHs.40403.

    Genome annotation databases

    EnsembliENST00000246139; ENSP00000246139; ENSG00000125931. [Q99966-1]
    ENST00000373619; ENSP00000362721; ENSG00000125931. [Q99966-1]
    ENST00000431381; ENSP00000388548; ENSG00000125931. [Q99966-2]
    ENST00000445983; ENSP00000403274; ENSG00000125931. [Q99966-1]
    ENST00000453707; ENSP00000401764; ENSG00000125931. [Q99966-2]
    GeneIDi4435.
    KEGGihsa:4435.
    UCSCiuc004eas.3. human. [Q99966-1]
    uc011mqc.2. human. [Q99966-2]

    Polymorphism databases

    DMDMi296434447.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65092 mRNA. Translation: AAC51113.1 .
    AB451286 mRNA. Translation: BAG70100.1 .
    AB451418 mRNA. Translation: BAG70232.1 .
    AL135749 Genomic DNA. No translation available.
    CH471213 Genomic DNA. Translation: EAW71819.1 .
    BC004240 mRNA. Translation: AAH04240.1 .
    N30508 mRNA. No translation available.
    CCDSi CCDS14419.1. [Q99966-1 ]
    CCDS48136.1. [Q99966-2 ]
    PIRi JC6114.
    RefSeqi NP_001138357.1. NM_001144885.1. [Q99966-2 ]
    NP_001138358.1. NM_001144886.1. [Q99966-1 ]
    NP_001138359.1. NM_001144887.1. [Q99966-1 ]
    NP_004134.2. NM_004143.3. [Q99966-1 ]
    XP_005262323.1. XM_005262266.2. [Q99966-2 ]
    XP_005262324.1. XM_005262267.2. [Q99966-1 ]
    UniGenei Hs.40403.

    3D structure databases

    ProteinModelPortali Q99966.
    SMRi Q99966. Positions 150-189.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110572. 7 interactions.
    IntActi Q99966. 7 interactions.
    MINTi MINT-223965.
    STRINGi 9606.ENSP00000388548.

    PTM databases

    PhosphoSitei Q99966.

    Polymorphism databases

    DMDMi 296434447.

    Proteomic databases

    PaxDbi Q99966.
    PRIDEi Q99966.

    Protocols and materials databases

    DNASUi 4435.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246139 ; ENSP00000246139 ; ENSG00000125931 . [Q99966-1 ]
    ENST00000373619 ; ENSP00000362721 ; ENSG00000125931 . [Q99966-1 ]
    ENST00000431381 ; ENSP00000388548 ; ENSG00000125931 . [Q99966-2 ]
    ENST00000445983 ; ENSP00000403274 ; ENSG00000125931 . [Q99966-1 ]
    ENST00000453707 ; ENSP00000401764 ; ENSG00000125931 . [Q99966-2 ]
    GeneIDi 4435.
    KEGGi hsa:4435.
    UCSCi uc004eas.3. human. [Q99966-1 ]
    uc011mqc.2. human. [Q99966-2 ]

    Organism-specific databases

    CTDi 4435.
    GeneCardsi GC0XM071521.
    H-InvDB HIX0016869.
    HGNCi HGNC:1986. CITED1.
    MIMi 300149. gene.
    neXtProti NX_Q99966.
    PharmGKBi PA26523.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41708.
    HOGENOMi HOG000072675.
    HOVERGENi HBG075182.
    InParanoidi Q99966.
    OMAi QYHGMAA.
    OrthoDBi EOG7TJ3K5.
    PhylomeDBi Q99966.
    TreeFami TF331915.

    Miscellaneous databases

    ChiTaRSi CITED1. human.
    GeneWikii CITED1.
    GenomeRNAii 4435.
    NextBioi 17285.
    PROi Q99966.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99966.
    Bgeei Q99966.
    CleanExi HS_CITED1.
    Genevestigatori Q99966.

    Family and domain databases

    InterProi IPR007576. CITED.
    [Graphical view ]
    PANTHERi PTHR17045. PTHR17045. 1 hit.
    Pfami PF04487. CITED. 1 hit.
    [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 1), VARIANT GLN-96.
    2. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-96.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-96.
    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], VARIANT GLN-96.
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-86 (ISOFORM 2).
      Tissue: Melanocyte.
    7. "Transcriptional activating activity of Smad4: roles of SMAD hetero-oligomerization and enhancement by an associating transactivator."
      Shioda T., Lechleider R.J., Dunwoodie S.L., Li H., Yahata T., de Caestecker M.P., Fenner M.H., Roberts A.B., Isselbacher K.J.
      Proc. Natl. Acad. Sci. U.S.A. 95:9785-9790(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMAD4.
    8. "The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
      Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
      J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CREBBP; EP300 AND HSPA8.
    9. "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, INTERACTION WITH ESR1, ASSOCIATION WITH CHROMATIN, MUTAGENESIS OF 155-GLU-GLU-156; 157-VAL-LEU-158; 159-MET-SER-160; 161-LEU-VAL-162; 163-VAL-GLU-164; LEU-165 AND 166-GLY-LEU-167.
    10. "Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)."
      Iwasaki T., Chin W.W., Ko L.
      J. Biol. Chem. 276:33375-33383(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM14.
    11. "The transcriptional activity of CITED1 is regulated by phosphorylation in a cell cycle-dependent manner."
      Shi G., Boyle S.C., Sparrow D.B., Dunwoodie S.L., Shioda T., de Caestecker M.P.
      J. Biol. Chem. 281:27426-27435(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH EP300, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-16; SER-63; SER-67; SER-71 AND SER-137.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "TOX3 is a neuronal survival factor that induces transcription depending on the presence of CITED1 or phosphorylated CREB in the transcriptionally active complex."
      Dittmer S., Kovacs Z., Yuan S.H., Siszler G., Kogl M., Summer H., Geerts A., Golz S., Shioda T., Methner A.
      J. Cell Sci. 124:252-260(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, INDUCTION, INTERACTION WITH TOX3.

    Entry informationi

    Entry nameiCITE1_HUMAN
    AccessioniPrimary (citable) accession number: Q99966
    Secondary accession number(s): B5BU50, B5BUI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 118 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 X
      Human chromosome X: 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