Q8N726 (CD2A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase inhibitor 2A, isoform 4

Alternative name(s):
p14ARF
p19ARF

Gene names

Name:	CDKN2A
Synonyms:	CDKN2, MLM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	132 AA.
Sequence status	Complete.
Protein existence	Evidence 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 is stabilized 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	Nucleus › nucleolus. Nucleus › nucleoplasm 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 process	Apoptosis Cell cycle Transcription Transcription regulation Ubl conjugation pathway rRNA processing
Cellular component	Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Ligand	DNA-binding
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype PubMed 12082630. Source: BHF-UCL apoptotic DNA fragmentation 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 induction of apoptosis Inferred from mutant phenotype PubMed 12082630. Source: BHF-UCL negative regulation of B cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL 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 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 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 protein export from nucleus Inferred from mutant phenotype PubMed 10360174. Source: BHF-UCL somatic stem cell division Inferred from sequence or structural similarity. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion 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 protein complex Inferred from direct assay PubMed 9529249. Source: BHF-UCL
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase inhibitor activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
C1QBP	Q07021	3	EBI-625922,EBI-347528
DAXX	Q9UER7	8	EBI-625922,EBI-77321
EBNA-LP	Q8AZK7	5	EBI-625922,EBI-1185167	From a different organism.
HUWE1	Q7Z6Z7	4	EBI-625922,EBI-625934
MDM2	Q00987	3	EBI-625922,EBI-389668

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 132	132	Cyclin-dependent kinase inhibitor 2A, isoform 4		PRO_0000144180
Natural variations
	Alternative sequence	1 – 47	47	Missing in isoform 6.		VSP_044962
	Natural variant	17	1	P → S. Ref.3 Corresponds to variant rs3731190 [ dbSNP | Ensembl ].		VAR_029287
	Natural variant	106	1	G → R. Corresponds to variant rs4987127 [ dbSNP | Ensembl ].		VAR_053033
	Natural variant	113	1	P → L. Corresponds to variant rs34886500 [ dbSNP | Ensembl ].		VAR_053034
	Natural variant	116	1	G → D. Corresponds to variant rs35741010 [ dbSNP | Ensembl ].		VAR_053035
Experimental info
	Sequence conflict	28 – 30	3	PRL → SWF in AAH15960. Ref.6
	Sequence conflict	28 – 30	3	PRL → SWF in AAH21998. Ref.6
	Sequence conflict	28 – 30	3	PRL → SWF in AAP35666. Ref.7
	Sequence conflict	94	1	P → L in AAB01737. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 4 (p14ARF) (p19ARF) (ARF) [UniParc]. Last modified April 18, 2012. Version 2. Checksum: 7739A9050C21BC96	FASTA	132	13,903
	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
	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	FASTA	85	8,731
	10 20 30 40 50 60 MLLRSQRLGQ QPLPRRPGHD DGQRPSGGAA AAPRRGAQLR RPRHSHPTRA RRCPGGLPGH 70 80 AGGAAPGRGA AGRARCLGPS ARGPG

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

Web resources

NIEHS-SNPs

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.
IPI	IPI00478390.
PIR	I39004.
RefSeq	NP_478102.2. NM_058195.3.
UniGene	Hs.512599.
3D structure databases
ProteinModelPortal	Q8N726.
SMR	Q8N726. Positions 1-37.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-24171N.
IntAct	Q8N726. 14 interactions.
MINT	MINT-2502129.
Polymorphism databases
DMDM	74751077.
Proteomic databases
PaxDb	Q8N726.
PeptideAtlas	Q8N726.
PRIDE	Q8N726.
Protocols and materials databases
DNASU	1029.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361570; ENSP00000355153; ENSG00000147889. ENST00000530628; ENSP00000432664; ENSG00000147889. ENST00000579755; ENSP00000462950; ENSG00000147889.
GeneID	1029.
KEGG	hsa:1029.
UCSC	uc003zpl.3. human.
Organism-specific databases
CTD	1029.
GeneCards	GC09M021957.
HGNC	HGNC:1787. CDKN2A.
HPA	CAB000093. CAB000445. CAB018232.
MIM	600160. gene.
neXtProt	NX_Q8N726.
Orphanet	618. Familial melanoma. 1333. Familial pancreatic carcinoma. 252206. Melanoma neural system tumor syndrome. 51013. Melanoma-pancreatic cancer syndrome. 99860. Precursor B-cell acute lymphoblastic leukemia. 99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKB	PA106.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG42176.
HOGENOM	HOG000111485.
HOVERGEN	HBG071056.
InParanoid	Q8N726.
KO	K06621.
Enzyme and pathway databases
Pathway_Interaction_DB	pi3kciaktpathway. Class I PI3K signaling events mediated by Akt. foxm1pathway. FOXM1 transcription factor network. hif1apathway. Hypoxic and oxygen homeostasis regulation of HIF-1-alpha.
Gene expression databases
ArrayExpress	Q8N726.
Bgee	Q8N726.
CleanEx	HS_CDKN2A.
Genevestigator	Q8N726.
GermOnline	ENSG00000147889. Homo sapiens.
Family and domain databases
InterPro	IPR010868. Cyclin_kinase-Inhib_2A. [Graphical view]
PANTHER	PTHR21414. PTHR21414. 1 hit.
Pfam	PF07392. P19Arf_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1029.
NextBio	4323.
SOURCE	Search...

Entry information

Entry name

CD2A2_HUMAN

Accession

Primary (citable) accession number: Q8N726
Secondary accession number(s): D3DRK2 , Q13195, Q13399, Q16360, Q7KZR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	April 18, 2012
Last modified:	April 3, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.