CITE2_HUMAN
ID CITE2_HUMAN Reviewed; 270 AA.
AC Q99967; O95426; Q5VTF4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Cbp/p300-interacting transactivator 2;
DE AltName: Full=MSG-related protein 1;
DE Short=MRG-1;
DE AltName: Full=P35srj;
GN Name=CITED2; Synonyms=MRG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=8901575; DOI=10.1073/pnas.93.22.12298;
RA Shioda T., Fenner M.H., Isselbacher K.J.;
RT "msg1, a novel melanocyte-specific gene, encodes a nuclear protein and is
RT associated with pigmentation.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12298-12303(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10552932; DOI=10.1006/geno.1999.5970;
RA Leung M.K., Jones T., Michels C.L., Livingston D.M., Bhattacharya S.;
RT "Molecular cloning and chromosomal localization of the human CITED2 gene
RT encoding p35srj/Mrg1.";
RL Genomics 61:307-313(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EP300, INDUCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9887100; DOI=10.1101/gad.13.1.64;
RA Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L.,
RA Livingston D.M.;
RT "Functional role of p35srj, a novel p300/CBP binding protein, during
RT transactivation by HIF-1.";
RL Genes Dev. 13:64-75(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
RX PubMed=11581164; DOI=10.1101/gad.906301;
RA Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S.,
RA Isselbacher K.J., Brown M., Shioda T.;
RT "Selective coactivation of estrogen-dependent transcription by CITED1
RT CBP/p300-binding protein.";
RL Genes Dev. 15:2598-2612(2001).
RN [7]
RP INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C.
RX PubMed=11694877; DOI=10.1038/ng768;
RA Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I.,
RA Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.;
RT "Cardiac malformations, adrenal agenesis, neural crest defects and
RT exencephaly in mice lacking Cited2, a new Tfap2 co-activator.";
RL Nat. Genet. 29:469-474(2001).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EP300; TFAP2A; TFAP2B
RP AND TFAP2C.
RX PubMed=12586840; DOI=10.1074/jbc.m208144200;
RA Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C.,
RA Bhattacharya S.;
RT "Physical and functional interactions among AP-2 transcription factors,
RT p300/CREB-binding protein, and CITED2.";
RL J. Biol. Chem. 278:16021-16029(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH PPARA.
RX PubMed=15051727; DOI=10.1074/jbc.m401489200;
RA Tien E.S., Davis J.W., Vanden Heuvel J.P.;
RT "Identification of the CREB-binding protein/p300-interacting protein CITED2
RT as a peroxisome proliferator-activated receptor alpha coregulator.";
RL J. Biol. Chem. 279:24053-24063(2004).
RN [10]
RP STRUCTURE BY NMR OF 216-259 IN COMPLEX WITH 323-423 OF EP300 AND ZINC IONS,
RP INTERACTION WITH EP300, AND MUTAGENESIS OF 243-LEU--LEU-246; LEU-243 AND
RP LEU-246.
RX PubMed=12778114; DOI=10.1038/nsb936;
RA Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J.;
RT "Structural basis for negative regulation of hypoxia-inducible factor-
RT 1alpha by CITED2.";
RL Nat. Struct. Biol. 10:504-512(2003).
RN [11]
RP STRUCTURE BY NMR OF 220-269 IN COMPLEX WITH 340-439 OF CREBBP AND ZINC
RP IONS.
RX PubMed=14594809; DOI=10.1074/jbc.m310348200;
RA De Guzman R.N., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
RT "Interaction of the TAZ1 domain of the CREB-binding protein with the
RT activation domain of CITED2: regulation by competition between
RT intrinsically unstructured ligands for non-identical binding sites.";
RL J. Biol. Chem. 279:3042-3049(2004).
RN [12]
RP VARIANT VSD2 170-SER--GLY-178 DEL, VARIANTS ASD8
RP GLY-GLY-SER-SER-THR-PRO-GLY-GLY-SER-179 INS AND 198-SER-GLY-199 DEL,
RP CHARACTERIZATION OF VARIANT VSD2 170-SER--GLY-178 DEL, AND CHARACTERIZATION
RP OF VARIANTS ASD8 GLY-GLY-SER-SER-THR-PRO-GLY-GLY-SER-179 INS AND
RP 198-SER-GLY-199 DEL.
RX PubMed=16287139; DOI=10.1002/humu.20262;
RA Sperling S., Grimm C.H., Dunkel I., Mebus S., Sperling H.P., Ebner A.,
RA Galli R., Lehrach H., Fusch C., Berger F., Hammer S.;
RT "Identification and functional analysis of CITED2 mutations in patients
RT with congenital heart defects.";
RL Hum. Mutat. 26:575-582(2005).
CC -!- FUNCTION: Transcriptional coactivator of the p300/CBP-mediated
CC transcription complex. Acts as a bridge, linking TFAP2 transcription
CC factors and the p300/CBP transcriptional coactivator complex in order
CC to stimulate TFAP2-mediated transcriptional activation. Positively
CC regulates TGF-beta signaling through its association with the
CC SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates
CC the peroxisome proliferator-activated receptors PPARA transcriptional
CC activity. Enhances estrogen-dependent transactivation mediated by
CC estrogen receptors. Acts also as a transcriptional corepressor;
CC interferes with the binding of the transcription factors HIF1A or STAT2
CC and the p300/CBP transcriptional coactivator complex. Participates in
CC sex determination and early gonad development by stimulating
CC transcription activation of SRY. Plays a role in controlling left-right
CC patterning during embryogenesis; potentiates transcriptional activation
CC of NODAL-mediated gene transcription in the left lateral plate mesoderm
CC (LPM). Plays an essential role in differentiation of the adrenal cortex
CC from the adrenogonadal primordium (AGP); stimulates WT1-mediated
CC transcription activation thereby up-regulating the nuclear hormone
CC receptor NR5A1 promoter activity. Associates with chromatin to the
CC PITX2 P1 promoter region. {ECO:0000269|PubMed:11581164,
CC ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:15051727}.
CC -!- SUBUNIT: Interacts (via C-terminus) with SMAD2. Interacts (via C-
CC terminus) with SMAD3 (via MH2 domain). Interacts with LHX2 (via LIM
CC domains). Interacts with WT1 (By similarity). Interacts (via C-
CC terminus) with EP300 (via CH1 domain); the interaction is stimulated in
CC response to hypoxia. Interacts with PPARA. Interacts (via C-terminus)
CC with TFAP2A, TFAP2B and TFAP2C. {ECO:0000250,
CC ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:12586840,
CC ECO:0000269|PubMed:12778114, ECO:0000269|PubMed:14594809,
CC ECO:0000269|PubMed:15051727, ECO:0000269|PubMed:9887100}.
CC -!- INTERACTION:
CC Q99967; Q09472: EP300; NbExp=3; IntAct=EBI-937732, EBI-447295;
CC Q99967; P28799: GRN; NbExp=3; IntAct=EBI-937732, EBI-747754;
CC Q99967; P41235: HNF4A; NbExp=3; IntAct=EBI-937732, EBI-1049011;
CC Q99967; P60891: PRPS1; NbExp=3; IntAct=EBI-937732, EBI-749195;
CC Q99967; Q92754: TFAP2C; NbExp=2; IntAct=EBI-937732, EBI-937309;
CC Q99967; O76024: WFS1; NbExp=3; IntAct=EBI-937732, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12586840,
CC ECO:0000269|PubMed:8901575, ECO:0000269|PubMed:9887100}.
CC Note=Colocalizes with EP300 in dot-like structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99967-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99967-2; Sequence=VSP_001089;
CC -!- INDUCTION: By hypoxia and deferoxamine. {ECO:0000269|PubMed:9887100}.
CC -!- DISEASE: Ventricular septal defect 2 (VSD2) [MIM:614431]: A common form
CC of congenital cardiovascular anomaly that may occur alone or in
CC combination with other cardiac malformations. It can affect any portion
CC of the ventricular septum, resulting in abnormal communications between
CC the two lower chambers of the heart. Classification is based on
CC location of the communication, such as perimembranous, inlet, outlet
CC (infundibular), central muscular, marginal muscular, or apical muscular
CC defect. Large defects that go unrepaired may give rise to cardiac
CC enlargement, congestive heart failure, pulmonary hypertension,
CC Eisenmenger's syndrome, delayed fetal brain development, arrhythmias,
CC and even sudden cardiac death. {ECO:0000269|PubMed:16287139}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Atrial septal defect 8 (ASD8) [MIM:614433]: A congenital heart
CC malformation characterized by incomplete closure of the wall between
CC the atria resulting in blood flow from the left to the right atria.
CC {ECO:0000269|PubMed:16287139}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CITED family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CITED2ID40087ch6q24.html";
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DR EMBL; U65093; AAC51114.1; -; mRNA.
DR EMBL; AF129290; AAF01263.1; -; Genomic_DNA.
DR EMBL; AF129290; AAF01264.1; -; Genomic_DNA.
DR EMBL; AF109161; AAD10055.1; -; mRNA.
DR EMBL; AL592429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004377; AAH04377.1; -; mRNA.
DR CCDS; CCDS5195.1; -. [Q99967-1]
DR RefSeq; NP_001161860.1; NM_001168388.2. [Q99967-1]
DR RefSeq; NP_001161861.2; NM_001168389.2.
DR RefSeq; NP_006070.2; NM_006079.4. [Q99967-1]
DR PDB; 1P4Q; NMR; -; A=216-259.
DR PDB; 1R8U; NMR; -; A=220-269.
DR PDB; 7LVS; X-ray; 2.02 A; F=216-246.
DR PDBsum; 1P4Q; -.
DR PDBsum; 1R8U; -.
DR PDBsum; 7LVS; -.
DR AlphaFoldDB; Q99967; -.
DR SMR; Q99967; -.
DR BioGRID; 115649; 16.
DR IntAct; Q99967; 10.
DR MINT; Q99967; -.
DR STRING; 9606.ENSP00000444198; -.
DR iPTMnet; Q99967; -.
DR PhosphoSitePlus; Q99967; -.
DR BioMuta; CITED2; -.
DR DMDM; 21542403; -.
DR MassIVE; Q99967; -.
DR PaxDb; Q99967; -.
DR PeptideAtlas; Q99967; -.
DR PRIDE; Q99967; -.
DR ProteomicsDB; 78555; -. [Q99967-1]
DR ProteomicsDB; 78556; -. [Q99967-2]
DR Antibodypedia; 4252; 272 antibodies from 34 providers.
DR DNASU; 10370; -.
DR Ensembl; ENST00000367651.4; ENSP00000356623.2; ENSG00000164442.10. [Q99967-1]
DR Ensembl; ENST00000536159.2; ENSP00000442831.1; ENSG00000164442.10. [Q99967-1]
DR Ensembl; ENST00000618718.1; ENSP00000479918.1; ENSG00000164442.10. [Q99967-2]
DR GeneID; 10370; -.
DR KEGG; hsa:10370; -.
DR MANE-Select; ENST00000367651.4; ENSP00000356623.2; NM_006079.5; NP_006070.2.
DR UCSC; uc003qip.3; human. [Q99967-1]
DR CTD; 10370; -.
DR DisGeNET; 10370; -.
DR GeneCards; CITED2; -.
DR HGNC; HGNC:1987; CITED2.
DR HPA; ENSG00000164442; Low tissue specificity.
DR MalaCards; CITED2; -.
DR MIM; 602937; gene.
DR MIM; 614431; phenotype.
DR MIM; 614433; phenotype.
DR neXtProt; NX_Q99967; -.
DR OpenTargets; ENSG00000164442; -.
DR Orphanet; 99103; Atrial septal defect, ostium secundum type.
DR Orphanet; 99105; Atrial septal defect, sinus venosus type.
DR Orphanet; 1480; NON RARE IN EUROPE: Ventricular septal defect.
DR Orphanet; 101063; Situs inversus totalis.
DR Orphanet; 3303; Tetralogy of Fallot.
DR PharmGKB; PA26524; -.
DR VEuPathDB; HostDB:ENSG00000164442; -.
DR eggNOG; ENOG502QSRC; Eukaryota.
DR GeneTree; ENSGT00530000063624; -.
DR HOGENOM; CLU_090678_0_0_1; -.
DR InParanoid; Q99967; -.
DR OMA; HAMGPGN; -.
DR OrthoDB; 1378769at2759; -.
DR PhylomeDB; Q99967; -.
DR TreeFam; TF331915; -.
DR PathwayCommons; Q99967; -.
DR Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-HSA-8866906; TFAP2 (AP-2) family regulates transcription of other transcription factors.
DR Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes.
DR SignaLink; Q99967; -.
DR SIGNOR; Q99967; -.
DR BioGRID-ORCS; 10370; 66 hits in 1077 CRISPR screens.
DR ChiTaRS; CITED2; human.
DR EvolutionaryTrace; Q99967; -.
DR GeneWiki; CITED2; -.
DR GenomeRNAi; 10370; -.
DR Pharos; Q99967; Tbio.
DR PRO; PR:Q99967; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q99967; protein.
DR Bgee; ENSG00000164442; Expressed in stromal cell of endometrium and 204 other tissues.
DR ExpressionAtlas; Q99967; baseline and differential.
DR Genevisible; Q99967; HS.
DR GO; GO:0000785; C:chromatin; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IDA:BHF-UCL.
DR GO; GO:0050693; F:LBD domain binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0035802; P:adrenal cortex formation; ISS:UniProtKB.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0061308; P:cardiac neural crest cell development involved in heart development; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0021602; P:cranial nerve morphogenesis; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0007368; P:determination of left/right symmetry; ISS:UniProtKB.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0060971; P:embryonic heart tube left/right pattern formation; ISS:BHF-UCL.
DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0003197; P:endocardial cushion development; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0070986; P:left/right axis specification; ISS:BHF-UCL.
DR GO; GO:0060972; P:left/right pattern formation; IBA:GO_Central.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; ISS:BHF-UCL.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:1900164; P:nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry; ISS:BHF-UCL.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:2000020; P:positive regulation of male gonad development; ISS:UniProtKB.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; IEA:Ensembl.
DR GO; GO:0003156; P:regulation of animal organ formation; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR GO; GO:0034405; P:response to fluid shear stress; IMP:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0007530; P:sex determination; ISS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; ISS:BHF-UCL.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR DisProt; DP00356; -.
DR IDEAL; IID00179; -.
DR InterPro; IPR007576; CITED.
DR PANTHER; PTHR17045; PTHR17045; 1.
DR Pfam; PF04487; CITED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Atrial septal defect;
KW Developmental protein; Differentiation; Disease variant; Nucleus;
KW Reference proteome; Repressor; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..270
FT /note="Cbp/p300-interacting transactivator 2"
FT /id="PRO_0000144726"
FT REGION 138..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 159..215
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8901575"
FT /id="VSP_001089"
FT VARIANT 170..178
FT /note="Missing (in VSD2; reduces coactivation of the TFAP2C
FT gene to 50% of that obtained with wild-type and represses
FT HIF1A with about 60% efficiency compared to wild-type)"
FT /evidence="ECO:0000269|PubMed:16287139"
FT /id="VAR_067583"
FT VARIANT 179
FT /note="S -> GGSSTPGGS (in ASD8; demonstrates only about 75%
FT of the repressive activity of wild-type)"
FT /id="VAR_067584"
FT VARIANT 198..199
FT /note="Missing (in ASD8; demonstrates only about 75% of the
FT repressive activity of wild-type)"
FT /evidence="ECO:0000269|PubMed:16287139"
FT /id="VAR_067585"
FT MUTAGEN 243..246
FT /note="Missing: Inhibits transactivation activity."
FT /evidence="ECO:0000269|PubMed:12778114"
FT MUTAGEN 243
FT /note="L->E: Inhibits transactivation activity; when
FT associated with E-246."
FT /evidence="ECO:0000269|PubMed:12778114"
FT MUTAGEN 246
FT /note="L->E: Inhibits transactivation activity; when
FT associated with E-243."
FT /evidence="ECO:0000269|PubMed:12778114"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1P4Q"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:7LVS"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:7LVS"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1R8U"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1P4Q"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1R8U"
SQ SEQUENCE 270 AA; 28497 MW; 45DDE3A9E2B4C472 CRC64;
MADHMMAMNH GRFPDGTNGL HHHPAHRMGM GQFPSPHHHQ QQQPQHAFNA LMGEHIHYGA
GNMNATSGIR HAMGPGTVNG GHPPSALAPA ARFNNSQFMG PPVASQGGSL PASMQLQKLN
NQYFNHHPYP HNHYMPDLHP AAGHQMNGTN QHFRDCNPKH SGGSSTPGGS GGSSTPGGSG
SSSGGGAGSS NSGGGSGSGN MPASVAHVPA AMLPPNVIDT DFIDEEVLMS LVIEMGLDRI
KELPELWLGQ NEFDFMTDFV CKQQPSRVSC
