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Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p14ARF)

 ARF_HUMAN               Reviewed;         132 AA.
Q8N726; D3DRK2; Q13195; Q13399; Q16360; Q7KZR9;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
18-APR-2012, sequence version 2.
25-OCT-2017, entry version 150.
RecName: Full=Tumor suppressor ARF {ECO:0000305};
AltName: Full=Alternative reading frame {ECO:0000303|PubMed:9724636};
Short=ARF {ECO:0000303|PubMed:9724636};
AltName: Full=Cyclin-dependent kinase inhibitor 2A {ECO:0000312|HGNC:HGNC:1787};
AltName: Full=p14ARF {ECO:0000303|PubMed:9724636};
Name=CDKN2A {ECO:0000312|EMBL:AAM77919.1, ECO:0000312|HGNC:HGNC:1787};
Synonyms=CDKN2 {ECO:0000312|EMBL:AAC60649.1}, MLM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000312|EMBL:AAC60649.1}
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7606716;
Stone S., Jiang P., Dayananth P., Tavtigian S.V., Katcher H.,
Parry D., Peters G., Kamb A.;
"Complex structure and regulation of the P16 (MTS1) locus.";
Cancer Res. 55:2988-2994(1995).
[2] {ECO:0000305, ECO:0000312|EMBL:AAB01737.1}
NUCLEOTIDE SEQUENCE [MRNA].
Linnenbach A.J.;
"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.";
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305, ECO:0000312|EMBL:AAB01737.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-17.
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000312|EMBL:CAH70601.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5] {ECO:0000305, ECO:0000312|EMBL:AAB01737.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7] {ECO:0000305, ECO:0000312|EMBL:AAA82236.1}
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hematopoietic {ECO:0000312|EMBL:AAA82236.1};
PubMed=7624129;
Duro D., Bernard O., Della Valle V., Berger R., Larsen C.J.;
"A new type of p16INK4/MTS1 gene transcript expressed in B-cell
malignancies.";
Oncogene 11:21-29(1995).
[8] {ECO:0000305, ECO:0000312|EMBL:AAB01737.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000305}
FUNCTION, AND INTERACTION WITH MDM2.
PubMed=9724636; DOI=10.1093/emboj/17.17.5001;
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.;
"The alternative product from the human CDKN2A locus, p14(ARF),
participates in a regulatory feedback loop with p53 and MDM2.";
EMBO J. 17:5001-5014(1998).
[10] {ECO:0000305}
FUNCTION, AND INTERACTION WITH TOP1.
PubMed=11314011; DOI=10.1038/sj.onc.1204170;
Karayan L., Riou J.-F., Seite P., Migeon J., Cantereau A.,
Larsen C.-J.;
"Human ARF protein interacts with topoisomerase I and stimulates its
activity.";
Oncogene 20:836-848(2001).
[11] {ECO:0000305}
FUNCTION, AND INTERACTION WITH E2F1.
PubMed=11314038; DOI=10.1038/sj.onc.1204220;
Eymin B., Karayan L., Seite P., Brambilla C., Brambilla E.,
Larsen C.-J., Gazzeri S.;
"Human ARF binds E2F1 and inhibits its transcriptional activity.";
Oncogene 20:1033-1041(2001).
[12]
INTERACTION WITH CDKN2AIP.
PubMed=12154087; DOI=10.1074/jbc.M204177200;
Hasan M.K., Yaguchi T., Sugihara T., Kumar P.K.R., Taira K.,
Reddel R.R., Kaul S.C., Wadhwa R.;
"CARF is a novel protein that cooperates with mouse p19ARF (human
p14ARF) in activating p53.";
J. Biol. Chem. 277:37765-37770(2002).
[13]
INTERACTION WITH CDKN2AIP.
PubMed=12581788; DOI=10.1016/S0531-5565(02)00180-8;
Wadhwa R., Sugihara T., Hasan M.K., Duncan E.L., Taira K., Kaul S.C.;
"A novel putative collaborator of p19ARF.";
Exp. Gerontol. 38:245-252(2003).
[14]
INTERACTION WITH E4F1.
PubMed=12446718; DOI=10.1074/jbc.M210978200;
Rizos H., Diefenbach E., Badhwar P., Woodruff S., Becker T.M.,
Rooney R.J., Kefford R.F.;
"Association of p14ARF with the p120E4F transcriptional repressor
enhances cell cycle inhibition.";
J. Biol. Chem. 278:4981-4989(2003).
[15] {ECO:0000305}
FUNCTION, AND INTERACTION WITH NPM1.
PubMed=14636574; DOI=10.1016/S1097-2765(03)00431-3;
Itahana K., Bhat K.P., Jin A., Itahana Y., Hawke D., Kobayashi R.,
Zhang Y.;
"Tumor suppressor ARF degrades B23, a nucleolar protein involved in
ribosome biogenesis and cell proliferation.";
Mol. Cell 12:1151-1164(2003).
[16] {ECO:0000305}
FUNCTION.
PubMed=12660818; DOI=10.1038/sj.onc.1206303;
Eymin B., Leduc C., Coll J.-L., Brambilla E., Gazzeri S.;
"p14ARF induces G2 arrest and apoptosis independently of p53 leading
to regression of tumours established in nude mice.";
Oncogene 22:1822-1835(2003).
[17] {ECO:0000305}
FUNCTION, AND INTERACTION WITH TOP1.
PubMed=15361825; DOI=10.1038/sj.onc.1207968;
Ayrault O., Andrique L., Larsen C.-J., Seite P.;
"Human Arf tumor suppressor specifically interacts with chromatin
containing the promoter of rRNA genes.";
Oncogene 23:8097-8104(2004).
[18] {ECO:0000305}
FUNCTION, AND INTERACTION WITH BCL6.
PubMed=15567177; DOI=10.1016/j.bbrc.2004.11.016;
Suzuki H., Kurita M., Mizumoto K., Moriyama M., Aiso S., Nishimoto I.,
Matsuoka M.;
"The ARF tumor suppressor inhibits BCL6-mediated transcriptional
repression.";
Biochem. Biophys. Res. Commun. 326:242-248(2005).
[19] {ECO:0000305}
FUNCTION, AND INTERACTION WITH HUWE1.
PubMed=15989956; DOI=10.1016/j.cell.2005.03.037;
Chen D., Kon N., Li M., Zhang W., Qin J., Gu W.;
"ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor.";
Cell 121:1071-1083(2005).
[20] {ECO:0000305}
FUNCTION, AND INTERACTION WITH UBE2I.
PubMed=15876874;
Rizos H., Woodruff S., Kefford R.F.;
"p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes
the sumoylation of its binding partners.";
Cell Cycle 4:597-603(2005).
[21]
INTERACTION WITH CDK5RAP3 AND MDM2, SUBCELLULAR LOCATION, AND REGION.
PubMed=16173922; DOI=10.1042/BJ20050960;
Wang J., He X., Luo Y., Yarbrough W.G.;
"A novel ARF-binding protein (LZAP) alters ARF regulation of HDM2.";
Biochem. J. 393:489-501(2006).
[22]
FUNCTION (ISOFORM SMARF), ALTERNATIVE SPLICING (ISOFORM SMARF), AND
SUBCELLULAR LOCATION (ISOFORM SMARF).
PubMed=16713577; DOI=10.1016/j.molcel.2006.04.014;
Reef S., Zalckvar E., Shifman O., Bialik S., Sabanay H., Oren M.,
Kimchi A.;
"A short mitochondrial form of p19ARF induces autophagy and caspase-
independent cell death.";
Mol. Cell 22:463-475(2006).
[23]
INTERACTION WITH TBRG1.
PubMed=17110379; DOI=10.1074/jbc.M609612200;
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.;
"A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains
chromosomal stability.";
J. Biol. Chem. 282:1322-1333(2007).
[24]
INTERACTION WITH C1QBP.
PubMed=17486078; DOI=10.1038/sj.onc.1210485;
Reef S., Shifman O., Oren M., Kimchi A.;
"The autophagic inducer smARF interacts with and is stabilized by the
mitochondrial p32 protein.";
Oncogene 26:6677-6683(2007).
[25]
INTERACTION WITH COMMD1, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18305112; DOI=10.1074/jbc.M708544200;
Huang Y., Wu M., Li H.Y.;
"Tumor suppressor ARF promotes non-classic proteasome-independent
polyubiquitination of COMMD1.";
J. Biol. Chem. 283:11453-11460(2008).
[26]
UBIQUITINATION BY TRIP12.
PubMed=20208519; DOI=10.1038/nature08820;
Chen D., Shan J., Zhu W.G., Qin J., Gu W.;
"Transcription-independent ARF regulation in oncogenic stress-mediated
p53 responses.";
Nature 464:624-627(2010).
[27]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22094112; DOI=10.1016/j.yexcr.2011.10.019;
Watari A., Li Y., Higashiyama S., Yutsudo M.;
"A novel proapoptotic gene PANO encodes a post-translational modulator
of the tumor suppressor p14ARF.";
Exp. Cell Res. 318:187-195(2012).
[28]
INTERACTION WITH NOP53, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=27323397; DOI=10.18632/oncotarget.9957;
Lee S., Cho Y.E., Kim S.H., Kim Y.J., Park J.H.;
"GLTSCR2 promotes the nucleoplasmic translocation and subsequent
degradation of nucleolar ARF.";
Oncotarget 8:16293-16302(2017).
-!- 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 smARF may be involved in regulation of
autophagy and caspase-independent cell death; the short-lived
mitochondrial isoform is stabilized by C1QBP.
{ECO:0000269|PubMed:11314011, ECO:0000269|PubMed:11314038,
ECO:0000269|PubMed:12660818, ECO:0000269|PubMed:14636574,
ECO:0000269|PubMed:15361825, ECO:0000269|PubMed:15567177,
ECO:0000269|PubMed:15876874, ECO:0000269|PubMed:15989956,
ECO:0000269|PubMed:16713577, ECO:0000269|PubMed:18305112,
ECO:0000269|PubMed:22094112, ECO:0000269|PubMed:9724636}.
-!- SUBUNIT: 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. Interacts with CDK5RAP3 and MDM2; form a
ternary complex involved in regulation of p53/TP53
(PubMed:16173922). Isoform smARF interacts with C1QBP. Interacts
with NOP53; the interaction is direct and promotes ARF
nucleoplasmic relocalization and ubiquitin-mediated proteasomal
degradation (PubMed:27323397). {ECO:0000269|PubMed:11314011,
ECO:0000269|PubMed:11314038, ECO:0000269|PubMed:12154087,
ECO:0000269|PubMed:12446718, ECO:0000269|PubMed:12581788,
ECO:0000269|PubMed:14636574, ECO:0000269|PubMed:15361825,
ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:15876874,
ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:16173922,
ECO:0000269|PubMed:17110379, ECO:0000269|PubMed:17486078,
ECO:0000269|PubMed:18305112, ECO:0000269|PubMed:27323397,
ECO:0000269|PubMed:9724636}.
-!- INTERACTION:
Q07021:C1QBP; NbExp=3; IntAct=EBI-625922, EBI-347528;
Q9UER7:DAXX; NbExp=8; IntAct=EBI-625922, EBI-77321;
Q8AZK7:EBNA-LP (xeno); NbExp=5; IntAct=EBI-625922, EBI-1185167;
P18146:EGR1; NbExp=4; IntAct=EBI-625922, EBI-2834611;
Q7Z6Z7:HUWE1; NbExp=5; IntAct=EBI-625922, EBI-625934;
Q00987:MDM2; NbExp=5; IntAct=EBI-625922, EBI-389668;
Q13330:MTA1; NbExp=2; IntAct=EBI-625922, EBI-714236;
P04198:MYCN; NbExp=3; IntAct=EBI-625922, EBI-878369;
P06748:NPM1; NbExp=2; IntAct=EBI-625922, EBI-78579;
P08047:SP1; NbExp=4; IntAct=EBI-625922, EBI-298336;
Q14669:TRIP12; NbExp=4; IntAct=EBI-625922, EBI-308443;
Q8TAQ5:ZNF420; NbExp=8; IntAct=EBI-625922, EBI-3923307;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:16173922, ECO:0000269|PubMed:18305112,
ECO:0000269|PubMed:22094112, ECO:0000269|PubMed:27323397}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:18305112,
ECO:0000269|PubMed:27323397}.
-!- SUBCELLULAR LOCATION: Isoform smARF: Mitochondrion
{ECO:0000269|PubMed:16713577}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Isoform 1 and isoform tumor suppressor ARF 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.
{ECO:0000250|UniProtKB:Q64364};
Name=tumor suppressor ARF {ECO:0000303|PubMed:11314011};
Synonyms=p14ARF {ECO:0000303|PubMed:9724636}, p19ARF;
IsoId=Q8N726-1; Sequence=Displayed;
Name=1 {ECO:0000305}; Synonyms=p16INK4a {ECO:0000305};
IsoId=P42771-1; Sequence=External;
Name=2 {ECO:0000305};
IsoId=P42771-2; Sequence=External;
Name=3 {ECO:0000305}; Synonyms=p12 {ECO:0000305};
IsoId=P42771-3; Sequence=External;
Name=5; Synonyms=p16gamma;
IsoId=P42771-4; Sequence=External;
Note=Barely detectable in non-tumor cells.;
Name=smARF;
IsoId=Q8N726-2; Sequence=VSP_044962;
-!- PTM: 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 proteasomal
degradation. In cancer cells, however, TRIP12 is located in a
different cell compartment, preventing ubiquitination and
degradation. {ECO:0000269|PubMed:20208519,
ECO:0000269|PubMed:27323397}.
-!- CAUTION: The proteins described here are encoded by the gene
CDKN2A, but are completely unrelated in term of sequence and
function to cyclin-dependent kinase inhibitor 2A (AC P42771) which
is encoded by the same gene. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB01737.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAC60649.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH15960.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH21998.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAM77919.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAH70601.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=EAW58600.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=EAW58601.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdkn2a/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CDKN2aID146.html";
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EMBL; S78535; AAC60649.1; ALT_INIT; mRNA.
EMBL; U38945; AAB01737.1; ALT_INIT; mRNA.
EMBL; AF527803; AAM77919.1; ALT_INIT; Genomic_DNA.
EMBL; AL449423; CAH70601.1; ALT_INIT; Genomic_DNA.
EMBL; CH471071; EAW58600.1; ALT_INIT; Genomic_DNA.
EMBL; CH471071; EAW58601.1; ALT_INIT; Genomic_DNA.
EMBL; BC015960; AAH15960.3; ALT_INIT; mRNA.
EMBL; BC021998; AAH21998.3; ALT_INIT; mRNA.
EMBL; U26727; AAA82236.1; -; mRNA.
EMBL; BT007020; AAP35666.1; -; mRNA.
CCDS; CCDS6511.2; -. [Q8N726-1]
PIR; I39004; I39004.
RefSeq; NP_478102.2; NM_058195.3. [Q8N726-1]
UniGene; Hs.512599; -.
ProteinModelPortal; Q8N726; -.
SMR; Q8N726; -.
BioGrid; 107463; 163.
CORUM; Q8N726; -.
DIP; DIP-24171N; -.
IntAct; Q8N726; 50.
MINT; MINT-2502129; -.
iPTMnet; Q8N726; -.
BioMuta; UBR5; -.
DMDM; 384872321; -.
MaxQB; Q8N726; -.
PeptideAtlas; Q8N726; -.
PRIDE; Q8N726; -.
DNASU; 1029; -.
Ensembl; ENST00000530628; ENSP00000432664; ENSG00000147889. [Q8N726-1]
Ensembl; ENST00000579755; ENSP00000462950; ENSG00000147889. [Q8N726-1]
GeneID; 1029; -.
UCSC; uc003zpl.4; human. [Q8N726-1]
CTD; 1029; -.
DisGeNET; 1029; -.
EuPathDB; HostDB:ENSG00000147889.16; -.
GeneCards; CDKN2A; -.
HGNC; HGNC:1787; CDKN2A.
HPA; CAB000093; -.
HPA; CAB000445; -.
HPA; CAB018232; -.
HPA; HPA047838; -.
MalaCards; CDKN2A; -.
MIM; 600160; gene.
neXtProt; NX_Q8N726; -.
OpenTargets; ENSG00000147889; -.
PharmGKB; PA106; -.
GeneTree; ENSGT00390000004527; -.
HOGENOM; HOG000111485; -.
HOVERGEN; HBG071056; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3232118; SUMOylation of transcription factors.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-69541; Stabilization of p53.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
SIGNOR; Q8N726; -.
ChiTaRS; CDKN2A; human.
GenomeRNAi; 1029; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000147889; -.
CleanEx; HS_CDKN2A; -.
ExpressionAtlas; Q8N726; baseline and differential.
Genevisible; Q8N726; HS.
GO; GO:0005739; C:mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:BHF-UCL.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:CAFA.
GO; GO:0055105; F:ubiquitin-protein transferase inhibitor activity; ISS:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:BHF-UCL.
GO; GO:1990000; P:amyloid fibril formation; IMP:CAFA.
GO; GO:0008637; P:apoptotic mitochondrial changes; IMP:BHF-UCL.
GO; GO:0000422; P:autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0007050; P:cell cycle arrest; IMP:BHF-UCL.
GO; GO:0090398; P:cellular senescence; IMP:BHF-UCL.
GO; GO:0051882; P:mitochondrial depolarization; IMP:ParkinsonsUK-UCL.
GO; GO:0030889; P:negative regulation of B cell proliferation; ISS:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; ISS:BHF-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:BHF-UCL.
GO; GO:2000435; P:negative regulation of protein neddylation; IDA:CAFA.
GO; GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:CAFA.
GO; GO:1903051; P:negative regulation of proteolysis involved in cellular protein catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IDA:CAFA.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISS:BHF-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:BHF-UCL.
GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:CAFA.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:UniProtKB.
GO; GO:0033235; P:positive regulation of protein sumoylation; IMP:BHF-UCL.
GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IDA:BHF-UCL.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:1902510; P:regulation of apoptotic DNA fragmentation; IMP:BHF-UCL.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0046825; P:regulation of protein export from nucleus; IMP:BHF-UCL.
GO; GO:0031647; P:regulation of protein stability; ISS:BHF-UCL.
GO; GO:1903214; P:regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
GO; GO:0048103; P:somatic stem cell division; ISS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR010868; Tumor_suppres_ARF.
Pfam; PF07392; P19Arf_N; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Cell cycle; Complete proteome;
DNA-binding; Mitochondrion; Nucleus; Polymorphism; Reference proteome;
rRNA processing; Transcription; Transcription regulation;
Tumor suppressor; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 132 Tumor suppressor ARF.
/FTId=PRO_0000144180.
REGION 1 64 Interaction with CDK5RAP3 and MDM2.
{ECO:0000269|PubMed:16173922}.
VAR_SEQ 1 47 Missing (in isoform smARF).
{ECO:0000305}.
/FTId=VSP_044962.
VARIANT 17 17 P -> S (in dbSNP:rs3731190).
{ECO:0000269|Ref.3}.
/FTId=VAR_029287.
VARIANT 106 106 G -> R (in dbSNP:rs4987127).
/FTId=VAR_053033.
VARIANT 113 113 P -> L (in dbSNP:rs34886500).
/FTId=VAR_053034.
VARIANT 116 116 G -> D (in dbSNP:rs35741010).
/FTId=VAR_053035.
CONFLICT 28 30 PRL -> SWF (in Ref. 6; AAH15960/AAH21998
and 7; AAP35666). {ECO:0000305}.
CONFLICT 94 94 P -> L (in Ref. 2; AAB01737).
{ECO:0000305}.
SEQUENCE 132 AA; 13903 MW; 7739A9050C21BC96 CRC64;
MVRRFLVTLR IRRACGPPRV RVFVVHIPRL TGEWAAPGAP AAVALVLMLL RSQRLGQQPL
PRRPGHDDGQ RPSGGAAAAP RRGAQLRRPR HSHPTRARRC PGGLPGHAGG AAPGRGAAGR
ARCLGPSARG PG


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