Q99966 (CITE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cbp/p300-interacting transactivator 1

Alternative name(s):
Melanocyte-specific protein 1

Gene names

Name:	CITED1
Synonyms:	MSG1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	193 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Apoptosis Differentiation Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Activator Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SMAD 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: Compara 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: Compara labyrinthine layer development Inferred from electronic annotation. Source: Compara 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 receptor 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: Compara 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-dependent Inferred from direct assay Ref.9. Source: UniProtKB nucleocytoplasmic transport Inferred from direct assay Ref.11. Source: UniProtKB placenta development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent 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 estrogen stimulus Inferred from direct assay Ref.9. Source: UniProtKB response to insulin stimulus 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 stimulus Inferred from sequence or structural similarity. Source: UniProtKB spongiotrophoblast layer development Inferred from electronic annotation. Source: Compara transcription, DNA-dependent 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: Compara
Cellular_component	cytosol Inferred from direct assay Ref.11. Source: UniProtKB nucleus Inferred from direct assay Ref.11Ref.1PubMed 9434189. Source: UniProtKB
Molecular_function	LBD domain binding Inferred from direct assay Ref.9. Source: UniProtKB chromatin binding Inferred from sequence or structural similarity. 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

With	Entry	#Exp.	IntAct	Notes
ESR1	P03372	3	EBI-2624951,EBI-78473

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 193	193	Cbp/p300-interacting transactivator 1		PRO_0000144724
Regions
	Motif	158 – 167	10	Nuclear export signal
	Compositional bias	149 – 188	40	Asp/Glu-rich (acidic)
Natural variations
	Alternative sequence	1	1	M → MEPSAQQLQLAASLPANLSN FCQGSEM in isoform 2.		VSP_039897
	Natural variant	96	1	H → Q. Ref.1 Ref.2 Ref.4 Ref.5 Corresponds to variant rs3012627 [ dbSNP | Ensembl ].		VAR_053038
Experimental info
	Mutagenesis	16	1	S → 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
	Mutagenesis	63	1	S → 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
	Mutagenesis	67	1	S → 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
	Mutagenesis	71	1	S → 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
	Mutagenesis	91	1	L → A: Does not change subcellular localization; when associated with A-95.
	Mutagenesis	95	1	M → A: Does not change subcellular localization; when associated with A-91.
	Mutagenesis	137	1	S → A: Reduces strongly phosphorylation; when associated with A-16; A-63; A-67 and A-71. Ref.11
	Mutagenesis	155 – 156	2	EE → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
	Mutagenesis	157 – 158	2	VL → AA: Inhibits interaction with ESR1 and ER-coactivation activity.
	Mutagenesis	159 – 160	2	MS → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
	Mutagenesis	161 – 162	2	LV → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
	Mutagenesis	163 – 164	2	VE → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity.
	Mutagenesis	165	1	L → A: Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-167. Ref.9
	Mutagenesis	166 – 167	2	GL → AA: Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-165.
	Mutagenesis	176	1	L → A: Does not change subcellular localization; when associated with A-178.
	Mutagenesis	178	1	L → A: Does not change subcellular localization; when associated with A-176.

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 9B0CF50CA639ECCB	FASTA	193	19,896
	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
	Isoform 2 [UniParc]. Checksum: CB89284B2F0B952B	FASTA	219	22,613
	10 20 30 40 50 60 MEPSAQQLQL AASLPANLSN FCQGSEMPTT SRPALDVKGG TSPAKEDANQ EMSSVAYSNL 70 80 90 100 110 120 AVKDRKAVAI LHYPGVASNG TKASGAPTSS SGSPIGSPTT TPPTKPPSFN LHPAPHLLAS 130 140 150 160 170 180 MHLQKLNSQY QGMAAATPGQ PGEAGPLQNW DFGAQAGGAE SLSPSAGAQS PAIIDSDPVD 190 200 210 EEVLMSLVVE LGLDRANELP ELWLGQNEFD FTADFPSSC

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. , 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.
IPI	IPI00019174. IPI00920996.
PIR	JC6114.
RefSeq	NP_001138357.1. NM_001144885.1. NP_001138358.1. NM_001144886.1. NP_001138359.1. NM_001144887.1. NP_004134.2. NM_004143.3.
UniGene	Hs.40403.
3D structure databases
ProteinModelPortal	Q99966.
SMR	Q99966. Positions 150-189.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99966. 3 interactions.
MINT	MINT-223965.
STRING	9606.ENSP00000388548.
PTM databases
PhosphoSite	Q99966.
Polymorphism databases
DMDM	296434447.
Proteomic databases
PaxDb	Q99966.
PRIDE	Q99966.
Protocols and materials databases
DNASU	4435.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000246139; ENSP00000246139; ENSG00000125931. ENST00000373619; ENSP00000362721; ENSG00000125931. ENST00000431381; ENSP00000388548; ENSG00000125931. ENST00000445983; ENSP00000403274; ENSG00000125931. ENST00000453707; ENSP00000401764; ENSG00000125931.
GeneID	4435.
KEGG	hsa:4435.
UCSC	uc004eas.3. human. uc011mqc.2. human.
Organism-specific databases
CTD	4435.
GeneCards	GC0XM071521.
H-InvDB	HIX0016869.
HGNC	HGNC:1986. CITED1.
MIM	300149. gene.
neXtProt	NX_Q99966.
PharmGKB	PA26523.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG41708.
HOGENOM	HOG000072675.
HOVERGEN	HBG075182.
InParanoid	Q99966.
OMA	AKEDANQ.
OrthoDB	EOG4X97JC.
PhylomeDB	Q99966.
Enzyme and pathway databases
Pathway_Interaction_DB	smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
Gene expression databases
ArrayExpress	Q99966.
Bgee	Q99966.
CleanEx	HS_CITED1.
Genevestigator	Q99966.
GermOnline	ENSG00000125931. Homo sapiens.
Family and domain databases
InterPro	IPR007576. CITED. [Graphical view]
PANTHER	PTHR17045. PTHR17045. 1 hit.
Pfam	PF04487. CITED. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CITED1. human.
GenomeRNAi	4435.
NextBio	17285.
SOURCE	Search...

Entry information

Entry name

CITE1_HUMAN

Accession

Primary (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:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.