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Q8N726 (CD2A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Cyclin-dependent kinase inhibitor 2A, isoform 4
Alternative name(s):
p14ARF
p19ARF
Gene names
Name:CDKN2A
Synonyms:CDKN2, MLM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length132 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development. Isoform 6 may be involved in regulation of autophagy and caspase-independent cell death; the short-lived mitochondrial isoform isstabilized by C1QBP. Ref.9 Ref.10 Ref.11 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.24 UniProtKB Q64364

Subunit structure

Does not interact with cyclins, CDK1, CDK2, CDK4, CDK5 or CDK6. Binds to BCL6, E2F1, HUWE1, MDM2, MYC, NPM1/B23, TOP1/TOPOI and UBE2I/UBC9. Interacts with TBRG1 and COMMD1. Interacts with CDKN2AIP and E4F1. Isoform 6 interacts with C1QBP. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24

Subcellular location

Nucleusnucleolus. Nucleusnucleoplasm Ref.21 Ref.24.

Isoform 6: Mitochondrion Ref.21 Ref.24.

Post-translational modification

Ubiquitinated in normal cells by TRIP12 via the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination at the N-terminus, regardeless of the absence of lysine residues. Ubiquitination leads to its degradation. In cancer cells, however, TRIP12 is located in a different cell compartment, preventing ubiquitination and degradation. Ref.25

Sequence caution

The sequence AAB01737.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAC60649.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH15960.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH21998.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAM77919.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAH70601.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence EAW58600.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence EAW58601.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
rRNA processing
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentMitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   LigandDNA-binding
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 12082630. Source: BHF-UCL

apoptotic mitochondrial changes

Inferred from mutant phenotype PubMed 12082630. Source: BHF-UCL

cell cycle arrest

Inferred from mutant phenotype PubMed 15582998. Source: BHF-UCL

cellular senescence

Inferred from mutant phenotype PubMed 14966292. Source: BHF-UCL

negative regulation of B cell proliferation

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

negative regulation of cell proliferation

Inferred from direct assay PubMed 17569660. Source: UniProtKB

negative regulation of immature T cell proliferation in thymus

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

negative regulation of protein kinase activity

Inferred from mutant phenotype PubMed 15582998. Source: BHF-UCL

negative regulation of ubiquitin-protein ligase activity

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

positive regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from direct assay PubMed 9529249. Source: BHF-UCL

positive regulation of cell cycle arrest

Inferred from direct assay PubMed 9529249. Source: BHF-UCL

positive regulation of protein sumoylation

Inferred from mutant phenotype PubMed 19057511. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17569660. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 17569660. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from direct assay Ref.24. Source: UniProtKB

protein destabilization

Inferred from direct assay PubMed 9529249PubMed 9529249. Source: BHF-UCL

protein polyubiquitination

Inferred from direct assay Ref.24. Source: UniProtKB

protein stabilization

Inferred from direct assay PubMed 10360174PubMed 9529249. Source: BHF-UCL

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 15582998. Source: BHF-UCL

regulation of apoptotic DNA fragmentation

Inferred from mutant phenotype PubMed 12082630. Source: BHF-UCL

regulation of protein export from nucleus

Inferred from mutant phenotype PubMed 10360174. Source: BHF-UCL

regulation of protein stability

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

somatic stem cell division

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

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay PubMed 10360174. Source: BHF-UCL

nucleoplasm

Inferred from direct assay PubMed 10360174. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 11800646. Source: BHF-UCL

protein complex

Inferred from direct assay PubMed 9529249. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

MDM2/MDM4 family protein binding

Inferred from physical interaction PubMed 9529249. Source: BHF-UCL

p53 binding

Inferred from physical interaction PubMed 9529249. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction PubMed 19057511. Source: BHF-UCL

ubiquitin-protein ligase inhibitor activity

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

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoform 1 and isoform 4 arise due to the use of two alternative first exons joined to a common exon 2 at the same acceptor site but in different reading frames, resulting in two completely different isoforms.
Isoform 4 Ref.1 (identifier: Q8N726-1)

Also known as: p14ARF; p19ARF; ARF;

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 1 Ref.20 (identifier: P42771-1)

Also known as: p16INK4a;

The sequence of this isoform can be found in the external entry P42771.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform 2 Ref.20 (identifier: P42771-2)

The sequence of this isoform can be found in the external entry P42771.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform 3 Ref.20 (identifier: P42771-3)

Also known as: p12;

The sequence of this isoform can be found in the external entry P42771.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform 5 (identifier: P42771-4)

Also known as: p16gamma;

The sequence of this isoform can be found in the external entry P42771.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Barely detectable in non-tumor cells.
Isoform 6 (identifier: Q8N726-2)

Also known as: smARF;

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 132132Cyclin-dependent kinase inhibitor 2A, isoform 4
PRO_0000144180

Natural variations

Alternative sequence1 – 4747Missing in isoform 6.
VSP_044962
Natural variant171P → S. Ref.3
Corresponds to variant rs3731190 [ dbSNP | Ensembl ].
VAR_029287
Natural variant1061G → R.
Corresponds to variant rs4987127 [ dbSNP | Ensembl ].
VAR_053033
Natural variant1131P → L.
Corresponds to variant rs34886500 [ dbSNP | Ensembl ].
VAR_053034
Natural variant1161G → D.
Corresponds to variant rs35741010 [ dbSNP | Ensembl ].
VAR_053035

Experimental info

Sequence conflict28 – 303PRL → SWF in AAH15960. Ref.6
Sequence conflict28 – 303PRL → SWF in AAH21998. Ref.6
Sequence conflict28 – 303PRL → SWF in AAP35666. Ref.7
Sequence conflict941P → L in AAB01737. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 (p14ARF) (p19ARF) (ARF) [UniParc].

Last modified April 18, 2012. Version 2.
Checksum: 7739A9050C21BC96

FASTA13213,903
        10         20         30         40         50         60 
MVRRFLVTLR IRRACGPPRV RVFVVHIPRL TGEWAAPGAP AAVALVLMLL RSQRLGQQPL 

        70         80         90        100        110        120 
PRRPGHDDGQ RPSGGAAAAP RRGAQLRRPR HSHPTRARRC PGGLPGHAGG AAPGRGAAGR 

       130 
ARCLGPSARG PG 

« Hide

Isoform 1 (p16INK4a) [UniParc].

See P42771.

Isoform 2 [UniParc].

See P42771.

Isoform 3 (p12) [UniParc].

See P42771.

Isoform 5 (p16gamma) [UniParc].

See P42771.

Isoform 6 (smARF) [UniParc].

Checksum: 4C9E739D74BEC556
Show »

FASTA858,731

References

« Hide 'large scale' references
[1]"Complex structure and regulation of the P16 (MTS1) locus."
Stone S., Jiang P., Dayananth P., Tavtigian S.V., Katcher H., Parry D., Peters G., Kamb A.
Cancer Res. 55:2988-2994(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"mRNA isoform with alternate first exon-encoded sequences at the cyclin-dependent kinase inhibitor 2 (p16INK4/MTS1) locus and mapping analysis of the region by using long-PCR."
Linnenbach A.J.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]NIEHS SNPs program
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-17.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Skin.
[7]"A new type of p16INK4/MTS1 gene transcript expressed in B-cell malignancies."
Duro D., Bernard O., Della Valle V., Berger R., Larsen C.J.
Oncogene 11:21-29(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hematopoietic.
[8]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]"The alternative product from the human CDKN2A locus, p14(ARF), participates in a regulatory feedback loop with p53 and MDM2."
Stott F.J., Bates S., James M.C., McConnell B.B., Starborg M., Brookes S., Palmero I., Ryan K., Hara E., Vousden K.H., Peters G.
EMBO J. 17:5001-5014(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDM2.
[10]"Human ARF protein interacts with topoisomerase I and stimulates its activity."
Karayan L., Riou J.-F., Seite P., Migeon J., Cantereau A., Larsen C.-J.
Oncogene 20:836-848(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TOP1.
[11]"Human ARF binds E2F1 and inhibits its transcriptional activity."
Eymin B., Karayan L., Seite P., Brambilla C., Brambilla E., Larsen C.-J., Gazzeri S.
Oncogene 20:1033-1041(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH E2F1.
[12]"CARF is a novel protein that cooperates with mouse p19ARF (human p14ARF) in activating p53."
Hasan M.K., Yaguchi T., Sugihara T., Kumar P.K.R., Taira K., Reddel R.R., Kaul S.C., Wadhwa R.
J. Biol. Chem. 277:37765-37770(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDKN2AIP.
[13]"A novel putative collaborator of p19ARF."
Wadhwa R., Sugihara T., Hasan M.K., Duncan E.L., Taira K., Kaul S.C.
Exp. Gerontol. 38:245-252(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDKN2AIP.
[14]"Association of p14ARF with the p120E4F transcriptional repressor enhances cell cycle inhibition."
Rizos H., Diefenbach E., Badhwar P., Woodruff S., Becker T.M., Rooney R.J., Kefford R.F.
J. Biol. Chem. 278:4981-4989(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E4F1.
[15]"Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation."
Itahana K., Bhat K.P., Jin A., Itahana Y., Hawke D., Kobayashi R., Zhang Y.
Mol. Cell 12:1151-1164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NPM1.
[16]"p14ARF induces G2 arrest and apoptosis independently of p53 leading to regression of tumours established in nude mice."
Eymin B., Leduc C., Coll J.-L., Brambilla E., Gazzeri S.
Oncogene 22:1822-1835(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Human Arf tumor suppressor specifically interacts with chromatin containing the promoter of rRNA genes."
Ayrault O., Andrique L., Larsen C.-J., Seite P.
Oncogene 23:8097-8104(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TOP1.
[18]"The ARF tumor suppressor inhibits BCL6-mediated transcriptional repression."
Suzuki H., Kurita M., Mizumoto K., Moriyama M., Aiso S., Nishimoto I., Matsuoka M.
Biochem. Biophys. Res. Commun. 326:242-248(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BCL6.
[19]"ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor."
Chen D., Kon N., Li M., Zhang W., Qin J., Gu W.
Cell 121:1071-1083(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HUWE1.
[20]"p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes the sumoylation of its binding partners."
Rizos H., Woodruff S., Kefford R.F.
Cell Cycle 4:597-603(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBE2I.
[21]"A short mitochondrial form of p19ARF induces autophagy and caspase-independent cell death."
Reef S., Zalckvar E., Shifman O., Bialik S., Sabanay H., Oren M., Kimchi A.
Mol. Cell 22:463-475(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 6), SUBCELLULAR LOCATION (ISOFORM 6).
[22]"A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains chromosomal stability."
Tompkins V.S., Hagen J., Frazier A.A., Lushnikova T., Fitzgerald M.P., di Tommaso A.D., Ladeveze V., Domann F.E., Eischen C.M., Quelle D.E.
J. Biol. Chem. 282:1322-1333(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TBRG1.
[23]"The autophagic inducer smARF interacts with and is stabilized by the mitochondrial p32 protein."
Reef S., Shifman O., Oren M., Kimchi A.
Oncogene 26:6677-6683(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C1QBP.
[24]"Tumor suppressor ARF promotes non-classic proteasome-independent polyubiquitination of COMMD1."
Huang Y., Wu M., Li H.Y.
J. Biol. Chem. 283:11453-11460(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COMMD1, FUNCTION, SUBCELLULAR LOCATION.
[25]"Transcription-independent ARF regulation in oncogenic stress-mediated p53 responses."
Chen D., Shan J., Zhu W.G., Qin J., Gu W.
Nature 464:624-627(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY TRIP12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S78535 mRNA. Translation: AAC60649.1. Different initiation.
U38945 mRNA. Translation: AAB01737.1. Different initiation.
AF527803 Genomic DNA. Translation: AAM77919.1. Different initiation.
AL449423 Genomic DNA. Translation: CAH70601.1. Different initiation.
CH471071 Genomic DNA. Translation: EAW58600.1. Different initiation.
CH471071 Genomic DNA. Translation: EAW58601.1. Different initiation.
BC015960 mRNA. Translation: AAH15960.3. Different initiation.
BC021998 mRNA. Translation: AAH21998.3. Different initiation.
U26727 mRNA. Translation: AAA82236.1.
BT007020 mRNA. Translation: AAP35666.1.
PIRI39004.
RefSeqNP_478102.2. NM_058195.3.
UniGeneHs.512599.

3D structure databases

DisProtDP00336.
ProteinModelPortalQ8N726.
SMRQ8N726. Positions 1-37.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107463. 133 interactions.
DIPDIP-24171N.
IntActQ8N726. 21 interactions.
MINTMINT-2502129.

Polymorphism databases

DMDM384872321.

Proteomic databases

PaxDbQ8N726.
PeptideAtlasQ8N726.
PRIDEQ8N726.

Protocols and materials databases

DNASU1029.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361570; ENSP00000355153; ENSG00000147889.
ENST00000530628; ENSP00000432664; ENSG00000147889. [Q8N726-1]
ENST00000579755; ENSP00000462950; ENSG00000147889. [Q8N726-1]
GeneID1029.
KEGGhsa:1029.
UCSCuc003zpl.3. human. [Q8N726-1]

Organism-specific databases

CTD1029.
GeneCardsGC09M021957.
HGNCHGNC:1787. CDKN2A.
HPACAB000093.
CAB000445.
CAB018232.
HPA047838.
MIM600160. gene.
neXtProtNX_Q8N726.
PharmGKBPA106.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42176.
HOGENOMHOG000111485.
HOVERGENHBG071056.
InParanoidQ8N726.
KOK06621.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ8N726.
BgeeQ8N726.
CleanExHS_CDKN2A.
GenevestigatorQ8N726.

Family and domain databases

InterProIPR010868. Cyclin_kinase-Inhib_2A.
[Graphical view]
PfamPF07392. P19Arf_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi1029.
NextBio4323.
SOURCESearch...

Entry information

Entry nameCD2A2_HUMAN
AccessionPrimary (citable) accession number: Q8N726
Secondary accession number(s): D3DRK2 expand/collapse secondary AC list , Q13195, Q13399, Q16360, Q7KZR9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: April 18, 2012
Last modified: April 16, 2014
This is version 114 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM