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Q99967 (CITE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cbp/p300-interacting transactivator 2
Alternative name(s):
MSG-related protein 1
Short name=MRG-1
P35srj
Gene names
Name:CITED2
Synonyms:MRG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8 Ref.9

Subunit structure

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. Ref.3 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus. Note: Colocalizes with EP300 in dot-like structures. Ref.1 Ref.3 Ref.8

Induction

By hypoxia and deferoxamine. Ref.3

Involvement in disease

Ventricular septal defect 2 (VSD2) [MIM:614431]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Atrial septal defect 8 (ASD8) [MIM:614433]: A congenital heart malformation characterized by incomplete closure of the wall between the atria resulting in blood flow from the left to the right atria.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Belongs to the CITED family.

Ontologies

Keywords
   Biological processDifferentiation
Stress response
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseAtrial septal defect
Disease mutation
   Molecular functionActivator
Developmental protein
Repressor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadrenal cortex formation

Inferred from sequence or structural similarity. Source: UniProtKB

bone morphogenesis

Inferred from electronic annotation. Source: Ensembl

cardiac neural crest cell development involved in heart development

Inferred from electronic annotation. Source: Ensembl

cell aging

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from direct assay Ref.9. Source: UniProtKB

central nervous system development

Inferred from electronic annotation. Source: Ensembl

cranial nerve morphogenesis

Inferred from electronic annotation. Source: Ensembl

decidualization

Inferred from electronic annotation. Source: Ensembl

determination of left/right symmetry

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic heart tube left/right pattern formation

Inferred from sequence or structural similarity. Source: BHF-UCL

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

embryonic process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

endocardial cushion development

Inferred from electronic annotation. Source: Ensembl

erythrocyte development

Inferred from electronic annotation. Source: Ensembl

granulocyte differentiation

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from mutant phenotype Ref.12. Source: UniProtKB

heart looping

Inferred from electronic annotation. Source: Ensembl

hematopoietic progenitor cell differentiation

Inferred from electronic annotation. Source: Ensembl

left/right axis specification

Inferred from sequence or structural similarity. Source: BHF-UCL

lens morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from sequence or structural similarity. Source: BHF-UCL

male gonad development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cell migration

Inferred from mutant phenotype PubMed 18054336. Source: BHF-UCL

negative regulation of gene expression

Inferred from direct assay Ref.9. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17906695. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter in response to hypoxia

Inferred from direct assay PubMed 22735262. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.9PubMed 99104162. Source: UniProtKB

neural tube closure

Inferred from electronic annotation. Source: Ensembl

nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry

Inferred from sequence or structural similarity. Source: BHF-UCL

outflow tract morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

peripheral nervous system development

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell-cell adhesion

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of gene expression

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of male gonad development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peroxisome proliferator activated receptor signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 22735262. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.9PubMed 9434189. Source: UniProtKB

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

pulmonary artery morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of RNA biosynthetic process

Inferred from direct assay Ref.8. Source: GOC

regulation of organ formation

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from direct assay Ref.6. Source: UniProtKB

response to fluid shear stress

Inferred from mutant phenotype PubMed 12960175. Source: BHF-UCL

response to hypoxia

Inferred from direct assay Ref.3. Source: UniProtKB

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

sex determination

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

spleen development

Inferred from sequence or structural similarity. Source: BHF-UCL

thymus development

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

trophectodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

ventricular septum morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from mutant phenotype Ref.8. Source: UniProtKB

nuclear chromatin

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 9434189Ref.3. Source: UniProtKB

   Molecular_functionLBD domain binding

Inferred from physical interaction Ref.9. Source: UniProtKB

RNA polymerase II transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription corepressor activity

Inferred from direct assay PubMed 22735262. Source: BHF-UCL

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyltransferase binding

Inferred from direct assay PubMed 22735262. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.6Ref.7Ref.9Ref.8. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99967-1)

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: Q99967-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Cbp/p300-interacting transactivator 2
PRO_0000144726

Regions

Compositional bias21 – 5737His-rich
Compositional bias162 – 19938Gly-rich
Compositional bias219 – 25840Asp/Glu-rich (acidic)

Natural variations

Alternative sequence159 – 21557Missing in isoform 2.
VSP_001089
Natural variant170 – 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.
VAR_067583
Natural variant1791S → GGSSTPGGS in ASD8; demonstrates only about 75% of the repressive activity of wild-type.
VAR_067584
Natural variant198 – 1992Missing in ASD8; demonstrates only about 75% of the repressive activity of wild-type.
VAR_067585

Experimental info

Mutagenesis243 – 2464Missing: Inhibits transactivation activity. Ref.10
Mutagenesis2431L → E: Inhibits transactivation activity; when associated with E-246. Ref.10
Mutagenesis2461L → E: Inhibits transactivation activity; when associated with E-243. Ref.10

Secondary structure

............ 270
Helix Strand Turn

Details...

Sequences

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

Last modified June 20, 2002. Version 2.
Checksum: 45DDE3A9E2B4C472

FASTA27028,497
        10         20         30         40         50         60 
MADHMMAMNH GRFPDGTNGL HHHPAHRMGM GQFPSPHHHQ QQQPQHAFNA LMGEHIHYGA 

        70         80         90        100        110        120 
GNMNATSGIR HAMGPGTVNG GHPPSALAPA ARFNNSQFMG PPVASQGGSL PASMQLQKLN 

       130        140        150        160        170        180 
NQYFNHHPYP HNHYMPDLHP AAGHQMNGTN QHFRDCNPKH SGGSSTPGGS GGSSTPGGSG 

       190        200        210        220        230        240 
SSSGGGAGSS NSGGGSGSGN MPASVAHVPA AMLPPNVIDT DFIDEEVLMS LVIEMGLDRI 

       250        260        270 
KELPELWLGQ NEFDFMTDFV CKQQPSRVSC 

« Hide

Isoform 2 [UniParc].

Checksum: C91FAABA3D2A9AD1
Show »

FASTA21323,732

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 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001161860.1. NM_001168388.2.
NP_001161861.2. NM_001168389.2.
NP_006070.2. NM_006079.4.
UniGeneHs.82071.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P4QNMR-A216-259[»]
1R8UNMR-A220-269[»]
DisProtDP00356.
ProteinModelPortalQ99967.
SMRQ99967. Positions 220-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115649. 11 interactions.
IntActQ99967. 7 interactions.
MINTMINT-112487.
STRING9606.ENSP00000356623.

Polymorphism databases

DMDM21542403.

Proteomic databases

PaxDbQ99967.
PRIDEQ99967.

Protocols and materials databases

DNASU10370.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367651; ENSP00000356623; ENSG00000164442. [Q99967-1]
ENST00000536159; ENSP00000442831; ENSG00000164442. [Q99967-1]
ENST00000537332; ENSP00000444198; ENSG00000164442. [Q99967-1]
GeneID10370.
KEGGhsa:10370.
UCSCuc003qip.2. human. [Q99967-1]

Organism-specific databases

CTD10370.
GeneCardsGC06M139735.
H-InvDBHIX0006261.
HGNCHGNC:1987. CITED2.
HPACAB016157.
MIM602937. gene.
614431. phenotype.
614433. phenotype.
neXtProtNX_Q99967.
Orphanet99103. 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.
1480. Ventricular septal defect.
PharmGKBPA26524.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44915.
HOGENOMHOG000231079.
HOVERGENHBG075182.
InParanoidQ99967.
OMADHIHYGA.
OrthoDBEOG72NRRB.
PhylomeDBQ99967.
TreeFamTF331915.

Gene expression databases

ArrayExpressQ99967.
BgeeQ99967.
CleanExHS_CITED2.
GenevestigatorQ99967.

Family and domain databases

InterProIPR007576. CITED.
[Graphical view]
PANTHERPTHR17045. PTHR17045. 1 hit.
PfamPF04487. CITED. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCITED2. human.
EvolutionaryTraceQ99967.
GeneWikiCITED2.
GenomeRNAi10370.
NextBio39307.
PROQ99967.
SOURCESearch...

Entry information

Entry nameCITE2_HUMAN
AccessionPrimary (citable) accession number: Q99967
Secondary accession number(s): O95426, Q5VTF4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 20, 2002
Last modified: April 16, 2014
This is version 133 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM