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Protein

Cbp/p300-interacting transactivator 2

Gene

CITED2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional coactivator of the p300/CBP-mediated trancription complex. Acts as a bridge, linking TFAP2 transcription factors and the p300/CBP transcriptional coactivator complex in order to stimulate TFAP2-mediated transcriptional activation. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates the peroxisome proliferator-activated receptors PPARA transcriptional activity. Enhances estrogen-dependent transactivation mediated by estrogen receptors. Acts also as a transcriptional corepressor; interferes with the binding of the transcription factors HIF1A or STAT2 and the p300/CBP transcriptional coactivator complex. Participates in sex determination and early gonad development by stimulating transcription activation of SRY. Plays a role in controlling left-right patterning during embryogenesis; potentiates transcriptional activation of NODAL-mediated gene transcription in the left lateral plate mesoderm (LPM). Plays an essential role in differentiation of the adrenal cortex from the adrenogonadal primordium (AGP); stimulates WT1-mediated transcription activation thereby up-regulating the nuclear hormone receptor NR5A1 promoter activity. Associates with chromatin to the PITX2 P1 promoter region.3 Publications

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. histone acetyltransferase binding Source: BHF-UCL
  3. LBD domain binding Source: UniProtKB
  4. RNA polymerase II transcription corepressor activity Source: BHF-UCL
  5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  6. transcription coactivator activity Source: UniProtKB
  7. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. adrenal cortex formation Source: UniProtKB
  2. cell differentiation Source: UniProtKB-KW
  3. cell proliferation Source: UniProtKB
  4. determination of left/right symmetry Source: UniProtKB
  5. embryonic heart tube left/right pattern formation Source: BHF-UCL
  6. heart development Source: UniProtKB
  7. left/right axis specification Source: BHF-UCL
  8. liver development Source: BHF-UCL
  9. negative regulation of apoptotic process Source: BHF-UCL
  10. negative regulation of cell migration Source: BHF-UCL
  11. negative regulation of gene expression Source: UniProtKB
  12. negative regulation of transcription, DNA-templated Source: UniProtKB
  13. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  14. negative regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: BHF-UCL
  15. nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry Source: BHF-UCL
  16. outflow tract morphogenesis Source: BHF-UCL
  17. positive regulation of cell-cell adhesion Source: BHF-UCL
  18. positive regulation of cell cycle Source: UniProtKB
  19. positive regulation of gene expression Source: UniProtKB
  20. positive regulation of male gonad development Source: UniProtKB
  21. positive regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
  22. positive regulation of transcription, DNA-templated Source: UniProtKB
  23. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  24. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  25. regulation of nucleic acid-templated transcription Source: GOC
  26. regulation of organ formation Source: UniProtKB
  27. response to estrogen Source: UniProtKB
  28. response to fluid shear stress Source: BHF-UCL
  29. response to hypoxia Source: UniProtKB
  30. sex determination Source: UniProtKB
  31. spleen development Source: BHF-UCL
  32. ventricular septum morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Repressor

Keywords - Biological processi

Differentiation, Stress response, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Cbp/p300-interacting transactivator 2
Alternative name(s):
MSG-related protein 1
Short name:
MRG-1
P35srj
Gene namesi
Name:CITED2
Synonyms:MRG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:1987. CITED2.

Subcellular locationi

  1. Nucleus 3 Publications

  2. Note: Colocalizes with EP300 in dot-like structures.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nuclear chromatin Source: BHF-UCL
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Ventricular septal defect 2 (VSD2)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA common form of congenital cardiovascular anomaly that may occur alone or in combination with other cardiac malformations. It can affect any portion of the ventricular septum, resulting in abnormal communications between the two lower chambers of the heart. Classification is based on location of the communication, such as perimembranous, inlet, outlet (infundibular), central muscular, marginal muscular, or apical muscular defect. Large defects that go unrepaired may give rise to cardiac enlargement, congestive heart failure, pulmonary hypertension, Eisenmenger's syndrome, delayed fetal brain development, arrhythmias, and even sudden cardiac death.

See also OMIM:614431
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1789Missing in VSD2; reduces coactivation of the TFAP2C gene to 50% of that obtained with wild-type and represses HIF1A with about 60% efficiency compared to wild-type. 1 Publication
VAR_067583
Atrial septal defect 8 (ASD8)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria.

See also OMIM:614433
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti179 – 1791S → GGSSTPGGS in ASD8; demonstrates only about 75% of the repressive activity of wild-type.
VAR_067584
Natural varianti198 – 1992Missing in ASD8; demonstrates only about 75% of the repressive activity of wild-type. 1 Publication
VAR_067585

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi243 – 2464Missing : Inhibits transactivation activity. 1 Publication
Mutagenesisi243 – 2431L → E: Inhibits transactivation activity; when associated with E-246. 1 Publication
Mutagenesisi246 – 2461L → E: Inhibits transactivation activity; when associated with E-243. 1 Publication

Keywords - Diseasei

Atrial septal defect, Disease mutation

Organism-specific databases

MIMi614431. phenotype.
614433. phenotype.
Orphaneti99103. Atrial septal defect, ostium secundum type.
99105. Atrial septal defect, sinus venosus type.
99097. Single ventricular septal defect.
101063. Situs inversus totalis.
3303. Tetralogy of Fallot.
PharmGKBiPA26524.

Polymorphism and mutation databases

BioMutaiCITED2.
DMDMi21542403.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Cbp/p300-interacting transactivator 2PRO_0000144726Add
BLAST

Proteomic databases

PaxDbiQ99967.
PRIDEiQ99967.

Expressioni

Inductioni

By hypoxia and deferoxamine.1 Publication

Gene expression databases

BgeeiQ99967.
CleanExiHS_CITED2.
ExpressionAtlasiQ99967. baseline and differential.
GenevestigatoriQ99967.

Organism-specific databases

HPAiCAB016157.

Interactioni

Subunit structurei

Interacts (via C-terminus) with SMAD2. Interacts (via C-terminus) with SMAD3 (via MH2 domain). Interacts with LHX2 (via LIM domains). Interacts with WT1 (By similarity). Interacts (via C-terminus) with EP300 (via CH1 domain); the interaction is stimulated in response to hypoxia. Interacts with PPARA. Interacts (via C-terminus) with TFAP2A, TFAP2B and TFAP2C.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EP300Q094723EBI-937732,EBI-447295
HNF4AP412353EBI-937732,EBI-1049011
TFAP2CQ927542EBI-937732,EBI-937309

Protein-protein interaction databases

BioGridi115649. 12 interactions.
IntActiQ99967. 7 interactions.
MINTiMINT-112487.
STRINGi9606.ENSP00000356623.

Structurei

Secondary structure

1
270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi221 – 2233Combined sources
Helixi227 – 2359Combined sources
Beta strandi237 – 2393Combined sources
Helixi251 – 2533Combined sources
Helixi254 – 2563Combined sources
Helixi266 – 2683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P4QNMR-A216-259[»]
1R8UNMR-A220-269[»]
DisProtiDP00356.
ProteinModelPortaliQ99967.
SMRiQ99967. Positions 220-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99967.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi21 – 5737His-richAdd
BLAST
Compositional biasi162 – 19938Gly-richAdd
BLAST
Compositional biasi219 – 25840Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the CITED family.Curated

Phylogenomic databases

eggNOGiNOG44915.
GeneTreeiENSGT00530000063624.
HOGENOMiHOG000231079.
HOVERGENiHBG075182.
InParanoidiQ99967.
OMAiDHIHYGA.
OrthoDBiEOG72NRRB.
PhylomeDBiQ99967.
TreeFamiTF331915.

Family and domain databases

InterProiIPR007576. CITED.
[Graphical view]
PANTHERiPTHR17045. PTHR17045. 1 hit.
PfamiPF04487. CITED. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99967-1) [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
MADHMMAMNH GRFPDGTNGL HHHPAHRMGM GQFPSPHHHQ QQQPQHAFNA
60 70 80 90 100
LMGEHIHYGA GNMNATSGIR HAMGPGTVNG GHPPSALAPA ARFNNSQFMG
110 120 130 140 150
PPVASQGGSL PASMQLQKLN NQYFNHHPYP HNHYMPDLHP AAGHQMNGTN
160 170 180 190 200
QHFRDCNPKH SGGSSTPGGS GGSSTPGGSG SSSGGGAGSS NSGGGSGSGN
210 220 230 240 250
MPASVAHVPA AMLPPNVIDT DFIDEEVLMS LVIEMGLDRI KELPELWLGQ
260 270
NEFDFMTDFV CKQQPSRVSC
Length:270
Mass (Da):28,497
Last modified:June 20, 2002 - v2
Checksum:i45DDE3A9E2B4C472
GO
Isoform 2 (identifier: Q99967-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     159-215: Missing.

Show »
Length:213
Mass (Da):23,732
Checksum:iC91FAABA3D2A9AD1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1789Missing in VSD2; reduces coactivation of the TFAP2C gene to 50% of that obtained with wild-type and represses HIF1A with about 60% efficiency compared to wild-type. 1 Publication
VAR_067583
Natural varianti179 – 1791S → GGSSTPGGS in ASD8; demonstrates only about 75% of the repressive activity of wild-type.
VAR_067584
Natural varianti198 – 1992Missing in ASD8; demonstrates only about 75% of the repressive activity of wild-type. 1 Publication
VAR_067585

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei159 – 21557Missing in isoform 2. 1 PublicationVSP_001089Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65093 mRNA. Translation: AAC51114.1.
AF129290 Genomic DNA. Translation: AAF01263.1.
AF129290 Genomic DNA. Translation: AAF01264.1.
AF109161 mRNA. Translation: AAD10055.1.
AL592429 Genomic DNA. Translation: CAH70354.1.
BC004377 mRNA. Translation: AAH04377.1.
CCDSiCCDS5195.1. [Q99967-1]
RefSeqiNP_001161860.1. NM_001168388.2. [Q99967-1]
NP_001161861.2. NM_001168389.2.
NP_006070.2. NM_006079.4. [Q99967-1]
UniGeneiHs.82071.

Genome annotation databases

EnsembliENST00000367651; ENSP00000356623; ENSG00000164442. [Q99967-1]
ENST00000536159; ENSP00000442831; ENSG00000164442. [Q99967-1]
ENST00000618718; ENSP00000479918; ENSG00000164442. [Q99967-2]
GeneIDi10370.
KEGGihsa:10370.
UCSCiuc003qip.2. human. [Q99967-1]

Polymorphism and mutation databases

BioMutaiCITED2.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65093 mRNA. Translation: AAC51114.1.
AF129290 Genomic DNA. Translation: AAF01263.1.
AF129290 Genomic DNA. Translation: AAF01264.1.
AF109161 mRNA. Translation: AAD10055.1.
AL592429 Genomic DNA. Translation: CAH70354.1.
BC004377 mRNA. Translation: AAH04377.1.
CCDSiCCDS5195.1. [Q99967-1]
RefSeqiNP_001161860.1. NM_001168388.2. [Q99967-1]
NP_001161861.2. NM_001168389.2.
NP_006070.2. NM_006079.4. [Q99967-1]
UniGeneiHs.82071.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P4QNMR-A216-259[»]
1R8UNMR-A220-269[»]
DisProtiDP00356.
ProteinModelPortaliQ99967.
SMRiQ99967. Positions 220-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115649. 12 interactions.
IntActiQ99967. 7 interactions.
MINTiMINT-112487.
STRINGi9606.ENSP00000356623.

Polymorphism and mutation databases

BioMutaiCITED2.
DMDMi21542403.

Proteomic databases

PaxDbiQ99967.
PRIDEiQ99967.

Protocols and materials databases

DNASUi10370.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367651; ENSP00000356623; ENSG00000164442. [Q99967-1]
ENST00000536159; ENSP00000442831; ENSG00000164442. [Q99967-1]
ENST00000618718; ENSP00000479918; ENSG00000164442. [Q99967-2]
GeneIDi10370.
KEGGihsa:10370.
UCSCiuc003qip.2. human. [Q99967-1]

Organism-specific databases

CTDi10370.
GeneCardsiGC06M139735.
H-InvDBHIX0006261.
HGNCiHGNC:1987. CITED2.
HPAiCAB016157.
MIMi602937. gene.
614431. phenotype.
614433. phenotype.
neXtProtiNX_Q99967.
Orphaneti99103. Atrial septal defect, ostium secundum type.
99105. Atrial septal defect, sinus venosus type.
99097. Single ventricular septal defect.
101063. Situs inversus totalis.
3303. Tetralogy of Fallot.
PharmGKBiPA26524.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44915.
GeneTreeiENSGT00530000063624.
HOGENOMiHOG000231079.
HOVERGENiHBG075182.
InParanoidiQ99967.
OMAiDHIHYGA.
OrthoDBiEOG72NRRB.
PhylomeDBiQ99967.
TreeFamiTF331915.

Miscellaneous databases

ChiTaRSiCITED2. human.
EvolutionaryTraceiQ99967.
GeneWikiiCITED2.
GenomeRNAii10370.
NextBioi39307.
PROiQ99967.
SOURCEiSearch...

Gene expression databases

BgeeiQ99967.
CleanExiHS_CITED2.
ExpressionAtlasiQ99967. baseline and differential.
GenevestigatoriQ99967.

Family and domain databases

InterProiIPR007576. CITED.
[Graphical view]
PANTHERiPTHR17045. PTHR17045. 1 hit.
PfamiPF04487. CITED. 2 hits.
[Graphical view]
ProtoNetiSearch...

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 2), SUBCELLULAR LOCATION.
  2. "Molecular cloning and chromosomal localization of the human CITED2 gene encoding p35srj/Mrg1."
    Leung M.K., Jones T., Michels C.L., Livingston D.M., Bhattacharya S.
    Genomics 61:307-313(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1."
    Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L., Livingston D.M.
    Genes Dev. 13:64-75(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EP300, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Pancreas.
  6. "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.
  7. "Cardiac malformations, adrenal agenesis, neural crest defects and exencephaly in mice lacking Cited2, a new Tfap2 co-activator."
    Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I., Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.
    Nat. Genet. 29:469-474(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C.
  8. "Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2."
    Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C., Bhattacharya S.
    J. Biol. Chem. 278:16021-16029(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EP300; TFAP2A; TFAP2B AND TFAP2C.
  9. "Identification of the CREB-binding protein/p300-interacting protein CITED2 as a peroxisome proliferator-activated receptor alpha coregulator."
    Tien E.S., Davis J.W., Vanden Heuvel J.P.
    J. Biol. Chem. 279:24053-24063(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPARA.
  10. "Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2."
    Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J.
    Nat. Struct. Biol. 10:504-512(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 216-259 IN COMPLEX WITH 323-423 OF EP300 AND ZINC IONS, INTERACTION WITH EP300, MUTAGENESIS OF 243-LEU--LEU-246; LEU-243 AND LEU-246.
  11. "Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites."
    De Guzman R.N., Martinez-Yamout M.A., Dyson H.J., Wright P.E.
    J. Biol. Chem. 279:3042-3049(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 220-269 IN COMPLEX WITH 340-439 OF CREBBP AND ZINC IONS.
  12. "Identification and functional analysis of CITED2 mutations in patients with congenital heart defects."
    Sperling S., Grimm C.H., Dunkel I., Mebus S., Sperling H.P., Ebner A., Galli R., Lehrach H., Fusch C., Berger F., Hammer S.
    Hum. Mutat. 26:575-582(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VSD2 170-SER--GLY-178 DEL, VARIANTS ASD8 GLY-GLY-SER-SER-THR-PRO-GLY-GLY-SER-179 INS AND 198-SER-GLY-199 DEL, CHARACTERIZATION OF VARIANT VSD2 170-SER--GLY-178 DEL, CHARACTERIZATION OF VARIANTS ASD8 GLY-GLY-SER-SER-THR-PRO-GLY-GLY-SER-179 INS AND 198-SER-GLY-199 DEL.

Entry informationi

Entry nameiCITE2_HUMAN
AccessioniPrimary (citable) accession number: Q99967
Secondary accession number(s): O95426, Q5VTF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 20, 2002
Last modified: April 29, 2015
This is version 143 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.