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Q99966 (CITE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cbp/p300-interacting transactivator 1
Alternative name(s):
Melanocyte-specific protein 1
Gene names
Name:CITED1
Synonyms:MSG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.13

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Subcellular location

Nucleus. Cytoplasm. Note: Shuttles between the nucleus and the cytoplasm by a nuclear export signal and (NES) in a CRM1-dependent manner. Ref.11

Tissue specificity

Expressed only in melanocytes and testis.

Induction

Up-regulated by GPR39 in neuronal cells. Ref.13

Post-translational modification

Phosphorylated. Phosphorylation changes in a cell cycle-dependent manner and reduces its transcriptional coactivator activity. Ref.11

Sequence similarities

Belongs to the CITED family.

Sequence caution

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

Ontologies

Keywords
   Biological processApoptosis
Differentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionActivator
Developmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSMAD protein signal transduction

Inferred from direct assay Ref.7. Source: BHF-UCL

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

brain development

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cell proliferation

Traceable author statement PubMed 17336183. Source: BHF-UCL

embryonic axis specification

Inferred from electronic annotation. Source: Ensembl

labyrinthine layer development

Inferred from electronic annotation. Source: Ensembl

melanin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

melanocyte differentiation

Inferred from mutant phenotype Ref.1. Source: UniProtKB

mesenchymal to epithelial transition

Traceable author statement PubMed 17336183. Source: BHF-UCL

metanephros development

Traceable author statement PubMed 17336183. Source: BHF-UCL

negative regulation of Wnt signaling pathway

Traceable author statement PubMed 17336183. Source: BHF-UCL

negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of osteoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.9. Source: UniProtKB

nucleocytoplasmic transport

Inferred from direct assay Ref.11. Source: UniProtKB

pigmentation

Inferred from mutant phenotype Ref.1. Source: UniProtKB

placenta development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 9434189Ref.7. Source: UniProtKB

positive regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement PubMed 17336183. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 9434189. Source: ProtInc

response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

response to cytokine

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from direct assay Ref.9. Source: UniProtKB

response to insulin

Inferred from sequence or structural similarity. Source: UniProtKB

response to interferon-gamma

Inferred from sequence or structural similarity. Source: UniProtKB

response to interleukin-1

Inferred from sequence or structural similarity. Source: UniProtKB

response to interleukin-11

Inferred from sequence or structural similarity. Source: UniProtKB

response to interleukin-2

Inferred from sequence or structural similarity. Source: UniProtKB

response to interleukin-4

Inferred from sequence or structural similarity. Source: UniProtKB

response to interleukin-6

Inferred from sequence or structural similarity. Source: UniProtKB

response to interleukin-9

Inferred from sequence or structural similarity. Source: UniProtKB

response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: UniProtKB

response to parathyroid hormone

Inferred from sequence or structural similarity. Source: UniProtKB

response to transforming growth factor beta

Inferred from direct assay Ref.7. Source: UniProtKB

spongiotrophoblast layer development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.7. Source: BHF-UCL

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11PubMed 17710162. Source: UniProtKB

cytosol

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay Ref.11Ref.1PubMed 9434189. Source: UniProtKB

   Molecular_functionLBD domain binding

Inferred from direct assay Ref.9. Source: UniProtKB

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

co-SMAD binding

Inferred from physical interaction Ref.7. Source: BHF-UCL

protein C-terminus binding

Inferred from physical interaction PubMed 15843474. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.9PubMed 15843474Ref.11Ref.13Ref.7. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.13. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.1. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.9Ref.11Ref.7. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99966-1)

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.
Isoform 2 (identifier: Q99966-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPSAQQLQLAASLPANLSNFCQGSEM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Cbp/p300-interacting transactivator 1
PRO_0000144724

Regions

Motif158 – 16710Nuclear export signal
Compositional bias149 – 18840Asp/Glu-rich (acidic)

Natural variations

Alternative sequence11M → MEPSAQQLQLAASLPANLSN FCQGSEM in isoform 2.
VSP_039897
Natural variant961H → Q. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs3012627 [ dbSNP | Ensembl ].
VAR_053038

Experimental info

Mutagenesis161S → 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. Ref.11
Mutagenesis631S → 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. Ref.11
Mutagenesis671S → 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. Ref.11
Mutagenesis711S → 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. Ref.11
Mutagenesis911L → A: Does not change subcellular localization; when associated with A-95.
Mutagenesis951M → A: Does not change subcellular localization; when associated with A-91.
Mutagenesis1371S → A: Reduces strongly phosphorylation; when associated with A-16; A-63; A-67 and A-71. Ref.11
Mutagenesis155 – 1562EE → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
Mutagenesis157 – 1582VL → AA: Inhibits interaction with ESR1 and ER-coactivation activity.
Mutagenesis159 – 1602MS → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
Mutagenesis161 – 1622LV → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
Mutagenesis163 – 1642VE → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
Mutagenesis1651L → A: Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-167. Ref.9
Mutagenesis166 – 1672GL → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-165.
Mutagenesis1761L → A: Does not change subcellular localization; when associated with A-178.
Mutagenesis1781L → A: Does not change subcellular localization; when associated with A-176.

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 9B0CF50CA639ECCB

FASTA19319,896
        10         20         30         40         50         60 
MPTTSRPALD VKGGTSPAKE DANQEMSSVA YSNLAVKDRK AVAILHYPGV ASNGTKASGA 

        70         80         90        100        110        120 
PTSSSGSPIG SPTTTPPTKP PSFNLHPAPH LLASMHLQKL NSQYQGMAAA TPGQPGEAGP 

       130        140        150        160        170        180 
LQNWDFGAQA GGAESLSPSA GAQSPAIIDS DPVDEEVLMS LVVELGLDRA NELPELWLGQ 

       190 
NEFDFTADFP SSC 

« Hide

Isoform 2 [UniParc].

Checksum: CB89284B2F0B952B
Show »

FASTA21922,613

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"WashU-NCI human EST project."
Hillier L., Allen M., Bowles L., Dubuque T., Geisel G., Jost S., Krizman D., Kucaba T., Lacy M., Le N., Lennon G., Marra M., Martin J., Moore B., Schellenberg K., Steptoe M., Tan F., Theising B. expand/collapse author list , White Y., Wylie T., Waterston R., Wilson R.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14419.1. [Q99966-1]
CCDS48136.1. [Q99966-2]
PIRJC6114.
RefSeqNP_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]
UniGeneHs.40403.

3D structure databases

ProteinModelPortalQ99966.
SMRQ99966. Positions 150-189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110572. 7 interactions.
IntActQ99966. 7 interactions.
MINTMINT-223965.
STRING9606.ENSP00000388548.

PTM databases

PhosphoSiteQ99966.

Polymorphism databases

DMDM296434447.

Proteomic databases

PaxDbQ99966.
PRIDEQ99966.

Protocols and materials databases

DNASU4435.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246139; ENSP00000246139; ENSG00000125931. [Q99966-1]
ENST00000373619; ENSP00000362721; ENSG00000125931. [Q99966-1]
ENST00000431381; ENSP00000388548; ENSG00000125931. [Q99966-2]
ENST00000445983; ENSP00000403274; ENSG00000125931. [Q99966-1]
ENST00000453707; ENSP00000401764; ENSG00000125931. [Q99966-2]
GeneID4435.
KEGGhsa:4435.
UCSCuc004eas.3. human. [Q99966-1]
uc011mqc.2. human. [Q99966-2]

Organism-specific databases

CTD4435.
GeneCardsGC0XM071521.
H-InvDBHIX0016869.
HGNCHGNC:1986. CITED1.
MIM300149. gene.
neXtProtNX_Q99966.
PharmGKBPA26523.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41708.
HOGENOMHOG000072675.
HOVERGENHBG075182.
InParanoidQ99966.
OMAQYHGMAA.
OrthoDBEOG7TJ3K5.
PhylomeDBQ99966.
TreeFamTF331915.

Gene expression databases

ArrayExpressQ99966.
BgeeQ99966.
CleanExHS_CITED1.
GenevestigatorQ99966.

Family and domain databases

InterProIPR007576. CITED.
[Graphical view]
PANTHERPTHR17045. PTHR17045. 1 hit.
PfamPF04487. CITED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCITED1. human.
GeneWikiCITED1.
GenomeRNAi4435.
NextBio17285.
PROQ99966.
SOURCESearch...

Entry information

Entry nameCITE1_HUMAN
AccessionPrimary (citable) accession number: Q99966
Secondary accession number(s): B5BU50, B5BUI2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM