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Q8N726

- CD2A2_HUMAN

UniProt

Q8N726 - CD2A2_HUMAN

Protein

Cyclin-dependent kinase inhibitor 2A, isoform 4

Gene

CDKN2A

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

    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.10 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. MDM2/MDM4 family protein binding Source: BHF-UCL
    3. p53 binding Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. transcription factor binding Source: BHF-UCL
    6. ubiquitin-protein transferase inhibitor activity Source: BHF-UCL

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
    2. apoptotic mitochondrial changes Source: BHF-UCL
    3. cell cycle arrest Source: BHF-UCL
    4. cellular senescence Source: BHF-UCL
    5. negative regulation of B cell proliferation Source: BHF-UCL
    6. negative regulation of cell proliferation Source: UniProtKB
    7. negative regulation of immature T cell proliferation in thymus Source: BHF-UCL
    8. negative regulation of protein kinase activity Source: BHF-UCL
    9. negative regulation of ubiquitin-protein transferase activity Source: BHF-UCL
    10. positive regulation of cell cycle arrest Source: BHF-UCL
    11. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    12. positive regulation of protein sumoylation Source: BHF-UCL
    13. positive regulation of transcription, DNA-templated Source: UniProtKB
    14. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    15. protein destabilization Source: BHF-UCL
    16. protein K63-linked ubiquitination Source: UniProtKB
    17. protein polyubiquitination Source: UniProtKB
    18. protein stabilization Source: BHF-UCL
    19. regulation of apoptotic DNA fragmentation Source: BHF-UCL
    20. regulation of G2/M transition of mitotic cell cycle Source: BHF-UCL
    21. regulation of protein export from nucleus Source: BHF-UCL
    22. regulation of protein stability Source: BHF-UCL
    23. rRNA processing Source: UniProtKB-KW
    24. somatic stem cell division Source: BHF-UCL
    25. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Apoptosis, Cell cycle, rRNA processing, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase inhibitor 2A, isoform 4
    Alternative name(s):
    p14ARF
    p19ARF
    Gene namesi
    Name:CDKN2AImported
    Synonyms:CDKN2, MLM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:1787. CDKN2A.

    Subcellular locationi

    Nucleusnucleolus 1 Publication. Nucleusnucleoplasm 1 Publication
    Isoform 6 : Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nucleolus Source: BHF-UCL
    3. nucleoplasm Source: BHF-UCL
    4. nucleus Source: BHF-UCL
    5. protein complex Source: BHF-UCL

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA106.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 132132Cyclin-dependent kinase inhibitor 2A, isoform 4PRO_0000144180Add
    BLAST

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ8N726.
    PaxDbiQ8N726.
    PeptideAtlasiQ8N726.
    PRIDEiQ8N726.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8N726.
    BgeeiQ8N726.
    CleanExiHS_CDKN2A.
    GenevestigatoriQ8N726.

    Organism-specific databases

    HPAiCAB000093.
    CAB000445.
    CAB018232.
    HPA047838.

    Interactioni

    Subunit structurei

    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.14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    C1QBPQ070213EBI-625922,EBI-347528
    DAXXQ9UER78EBI-625922,EBI-77321
    EBNA-LPQ8AZK75EBI-625922,EBI-1185167From a different organism.
    EGR1P181464EBI-625922,EBI-2834611
    HUWE1Q7Z6Z74EBI-625922,EBI-625934
    MDM2Q009875EBI-625922,EBI-389668
    MYCNP041983EBI-625922,EBI-878369
    NPM1P067482EBI-625922,EBI-78579
    ZNF420Q8TAQ58EBI-625922,EBI-3923307

    Protein-protein interaction databases

    BioGridi107463. 135 interactions.
    DIPiDIP-24171N.
    IntActiQ8N726. 21 interactions.
    MINTiMINT-2502129.

    Structurei

    3D structure databases

    DisProtiDP00336.
    ProteinModelPortaliQ8N726.
    SMRiQ8N726. Positions 1-37.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG42176.
    HOGENOMiHOG000111485.
    HOVERGENiHBG071056.
    InParanoidiQ8N726.
    KOiK06621.

    Family and domain databases

    InterProiIPR010868. Cyclin_kinase-Inhib_2A.
    [Graphical view]
    PfamiPF07392. P19Arf_N. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    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.By similarity

    Isoform 41 Publication (identifier: Q8N726-1) [UniParc]FASTAAdd to Basket

    Also known as: p14ARF1 Publication

    , p19ARF, ARF1 Publication

    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

    MVRRFLVTLR IRRACGPPRV RVFVVHIPRL TGEWAAPGAP AAVALVLMLL    50
    RSQRLGQQPL PRRPGHDDGQ RPSGGAAAAP RRGAQLRRPR HSHPTRARRC 100
    PGGLPGHAGG AAPGRGAAGR ARCLGPSARG PG 132
    Length:132
    Mass (Da):13,903
    Last modified:April 18, 2012 - v2
    Checksum:i7739A9050C21BC96
    GO
    Isoform 1Curated (identifier: P42771-1) [UniParc]FASTAAdd to Basket

    Also known as: p16INK4aCurated

    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.
    Length:156
    Mass (Da):16,533
    GO
    Isoform 2Curated (identifier: P42771-2) [UniParc]FASTAAdd to Basket

    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.
    Length:105
    Mass (Da):11,215
    GO
    Isoform 3Curated (identifier: P42771-3) [UniParc]FASTAAdd to Basket

    Also known as: p12Curated

    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.
    Length:116
    Mass (Da):12,213
    GO
    Isoform 5 (identifier: P42771-4) [UniParc]FASTAAdd to Basket

    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.

    Length:167
    Mass (Da):17,883
    GO
    Isoform 6 (identifier: Q8N726-2) [UniParc]FASTAAdd to Basket

    Also known as: smARF

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

    Show »
    Length:85
    Mass (Da):8,731
    Checksum:i4C9E739D74BEC556
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 303PRL → SWF in AAH15960. (PubMed:15489334)Curated
    Sequence conflicti28 – 303PRL → SWF in AAH21998. (PubMed:15489334)Curated
    Sequence conflicti28 – 303PRL → SWF in AAP35666. (PubMed:7624129)Curated
    Sequence conflicti94 – 941P → L in AAB01737. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171P → S.1 Publication
    Corresponds to variant rs3731190 [ dbSNP | Ensembl ].
    VAR_029287
    Natural varianti106 – 1061G → R.
    Corresponds to variant rs4987127 [ dbSNP | Ensembl ].
    VAR_053033
    Natural varianti113 – 1131P → L.
    Corresponds to variant rs34886500 [ dbSNP | Ensembl ].
    VAR_053034
    Natural varianti116 – 1161G → D.
    Corresponds to variant rs35741010 [ dbSNP | Ensembl ].
    VAR_053035

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4747Missing in isoform 6. CuratedVSP_044962Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS6511.2. [Q8N726-1]
    PIRiI39004.
    RefSeqiNP_478102.2. NM_058195.3. [Q8N726-1]
    UniGeneiHs.512599.

    Genome annotation databases

    EnsembliENST00000361570; ENSP00000355153; ENSG00000147889.
    ENST00000530628; ENSP00000432664; ENSG00000147889. [Q8N726-1]
    ENST00000579755; ENSP00000462950; ENSG00000147889. [Q8N726-1]
    GeneIDi1029.
    KEGGihsa:1029.
    UCSCiuc003zpl.3. human. [Q8N726-1]

    Polymorphism databases

    DMDMi384872321.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS6511.2. [Q8N726-1 ]
    PIRi I39004.
    RefSeqi NP_478102.2. NM_058195.3. [Q8N726-1 ]
    UniGenei Hs.512599.

    3D structure databases

    DisProti DP00336.
    ProteinModelPortali Q8N726.
    SMRi Q8N726. Positions 1-37.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107463. 135 interactions.
    DIPi DIP-24171N.
    IntActi Q8N726. 21 interactions.
    MINTi MINT-2502129.

    Polymorphism databases

    DMDMi 384872321.

    Proteomic databases

    MaxQBi Q8N726.
    PaxDbi Q8N726.
    PeptideAtlasi Q8N726.
    PRIDEi Q8N726.

    Protocols and materials databases

    DNASUi 1029.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361570 ; ENSP00000355153 ; ENSG00000147889 .
    ENST00000530628 ; ENSP00000432664 ; ENSG00000147889 . [Q8N726-1 ]
    ENST00000579755 ; ENSP00000462950 ; ENSG00000147889 . [Q8N726-1 ]
    GeneIDi 1029.
    KEGGi hsa:1029.
    UCSCi uc003zpl.3. human. [Q8N726-1 ]

    Organism-specific databases

    CTDi 1029.
    GeneCardsi GC09M021957.
    HGNCi HGNC:1787. CDKN2A.
    HPAi CAB000093.
    CAB000445.
    CAB018232.
    HPA047838.
    MIMi 600160. gene.
    neXtProti NX_Q8N726.
    PharmGKBi PA106.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42176.
    HOGENOMi HOG000111485.
    HOVERGENi HBG071056.
    InParanoidi Q8N726.
    KOi K06621.

    Enzyme and pathway databases

    Reactomei REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    GenomeRNAii 1029.
    NextBioi 4323.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N726.
    Bgeei Q8N726.
    CleanExi HS_CDKN2A.
    Genevestigatori Q8N726.

    Family and domain databases

    InterProi IPR010868. Cyclin_kinase-Inhib_2A.
    [Graphical view ]
    Pfami PF07392. P19Arf_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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: HematopoieticImported.
    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. 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. 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.

    Entry informationi

    Entry nameiCD2A2_HUMAN
    AccessioniPrimary (citable) accession number: Q8N726
    Secondary accession number(s): D3DRK2
    , Q13195, Q13399, Q16360, Q7KZR9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: April 18, 2012
    Last modified: October 1, 2014
    This is version 119 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3