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Q99966

- CITE1_HUMAN

UniProt

Q99966 - CITE1_HUMAN

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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

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 C-terminus binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  7. transcription coactivator activity Source: UniProtKB
  8. 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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi157 – 1582VL → AA: Inhibits interaction with ESR1 and ER-coactivation activity. 1 Publication
Mutagenesisi159 – 1602MS → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity. 1 Publication
Mutagenesisi161 – 1622LV → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity. 1 Publication
Mutagenesisi163 – 1642VE → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity. 1 Publication
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. 1 Publication
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

BgeeiQ99966.
CleanExiHS_CITED1.
ExpressionAtlasiQ99966. baseline and differential.
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.
GeneTreeiENSGT00530000063624.
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

        10         20         30         40         50
MPTTSRPALD VKGGTSPAKE DANQEMSSVA YSNLAVKDRK AVAILHYPGV
60 70 80 90 100
ASNGTKASGA PTSSSGSPIG SPTTTPPTKP PSFNLHPAPH LLASMHLQKL
110 120 130 140 150
NSQYQGMAAA TPGQPGEAGP LQNWDFGAQA GGAESLSPSA GAQSPAIIDS
160 170 180 190
DPVDEEVLMS LVVELGLDRA NELPELWLGQ NEFDFTADFP SSC
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00530000063624.
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

Bgeei Q99966.
CleanExi HS_CITED1.
ExpressionAtlasi Q99966. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 119 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