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Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF)

 ARF_MOUSE               Reviewed;         169 AA.
Q64364; Q4U255; Q9QXC7; Q9R051;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 142.
RecName: Full=Tumor suppressor ARF {ECO:0000305};
AltName: Full=Alternative reading frame;
Short=ARF;
AltName: Full=Cyclin-dependent kinase inhibitor 2A;
AltName: Full=p19ARF;
Name=Cdkn2a {ECO:0000312|EMBL:AAB35770.1, ECO:0000312|MGI:MGI:104738};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB35770.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8521522; DOI=10.1016/0092-8674(95)90214-7;
Quelle D.E., Zindy F., Ashmun R.A., Sherr C.J.;
"Alternative reading frames of the INK4a tumor suppressor gene encode
two unrelated proteins capable of inducing cell cycle arrest.";
Cell 83:993-1000(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary tumor;
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).
[3] {ECO:0000305, ECO:0000312|EMBL:CAB65598.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
STRAIN=129/SvJ {ECO:0000312|EMBL:CAB65598.1};
PubMed=10753221; DOI=10.1093/carcin/21.4.817;
Melendez B., Malumbres M., de Castro I.P., Santos J., Pellicer A.,
Fernandez-Piqueras J.;
"Characterization of the murine p19ARF promoter CpG island and its
methylation pattern in primary lymphomas.";
Carcinogenesis 21:817-821(2000).
[4] {ECO:0000305, ECO:0000312|EMBL:AAC00053.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
STRAIN=020 {ECO:0000269|PubMed:9021155},
129/J {ECO:0000312|EMBL:AAC00054.1},
A/J {ECO:0000312|EMBL:AAC00054.1}, A/Wy {ECO:0000312|EMBL:AAC00054.1},
AKR/J {ECO:0000312|EMBL:AAC00054.1},
B10.A {ECO:0000312|EMBL:AAC00054.1},
B10.D2(58N) {ECO:0000312|EMBL:AAC00054.1},
BALB/cJ {ECO:0000269|PubMed:9021155},
C3H/21BG {ECO:0000269|PubMed:9021155},
C3H/HeJ {ECO:0000269|PubMed:9021155},
C57BL/10ScNJ {ECO:0000312|EMBL:AAC00054.1},
C57BL/10SN {ECO:0000312|EMBL:AAC00054.1},
C57BL/6By {ECO:0000312|EMBL:AAC00054.1},
C57BL/6J {ECO:0000269|PubMed:9021155},
C57BR/cdJ {ECO:0000312|EMBL:AAC00054.1},
CBA/J {ECO:0000269|PubMed:9021155},
DBA/2J {ECO:0000312|EMBL:AAC00054.1},
HS/IBG {ECO:0000312|EMBL:AAC00054.1},
LP/J {ECO:0000312|EMBL:AAC00054.1},
LS/IBG {ECO:0000312|EMBL:AAC00054.1},
MA/M4J {ECO:0000312|EMBL:AAC00053.1},
PL/J {ECO:0000269|PubMed:9021155}, RF/J {ECO:0000312|EMBL:AAC00054.1},
Sencar {ECO:0000269|PubMed:9021155},
SJL/J {ECO:0000312|EMBL:AAC00054.1},
SM/J {ECO:0000312|EMBL:AAC00054.1},
ST/J {ECO:0000312|EMBL:AAC00054.1}, and
SWR/J {ECO:0000312|EMBL:AAC00054.1};
TISSUE=Lung {ECO:0000269|PubMed:9021155};
PubMed=9021155; DOI=10.1007/s003359900352;
Herzog C.R., You M.;
"Sequence variation and chromosomal mapping of the murine Cdkn2a tumor
suppressor gene.";
Mamm. Genome 8:65-66(1997).
[5] {ECO:0000305, ECO:0000312|EMBL:AAD33245.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
STRAIN=129/SvjE {ECO:0000312|EMBL:AAD33245.1};
PubMed=10097151; DOI=10.1073/pnas.96.7.3993;
Inoue K., Roussel M.F., Sherr C.J.;
"Induction of ARF tumor suppressor gene expression and cell cycle
arrest by transcription factor DMP1.";
Proc. Natl. Acad. Sci. U.S.A. 96:3993-3998(1999).
[6] {ECO:0000305}
FUNCTION.
PubMed=9393858; DOI=10.1016/S0092-8674(00)80452-3;
Kamijo T., Zindy F., Roussel M.F., Quelle D.E., Downing J.R.,
Ashmun R.A., Grosveld G., Sherr C.J.;
"Tumor suppression at the mouse INK4a locus mediated by the
alternative reading frame product p19ARF.";
Cell 91:649-659(1997).
[7] {ECO:0000305}
MUTAGENESIS OF LEU-85; PRO-93; ARG-97; 105-GLY-HIS-106 AND ALA-120.
PubMed=9012842; DOI=10.1073/pnas.94.2.669;
Quelle D.E., Cheng M., Ashmun R.A., Sherr C.J.;
"Cancer-associated mutations at the INK4a locus cancel cell cycle
arrest by p16INK4a but not by the alternative reading frame protein
p19ARF.";
Proc. Natl. Acad. Sci. U.S.A. 94:669-673(1997).
[8] {ECO:0000305}
FUNCTION, AND INTERACTION WITH MDM2.
PubMed=9529248; DOI=10.1016/S0092-8674(00)81400-2;
Pomerantz J., Schreiber-Agus N., Liegeois N.J., Silverman A.,
Alland L., Chin L., Potes J., Chen K., Orlow I., Lee H.-W.,
Cordon-Cardo C., DePinho R.A.;
"The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2
and neutralizes MDM2's inhibition of p53.";
Cell 92:713-723(1998).
[9] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10359817; DOI=10.1073/pnas.96.12.6937;
Tao W., Levine A.J.;
"P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of
Mdm2.";
Proc. Natl. Acad. Sci. U.S.A. 96:6937-6941(1999).
[10]
INDUCTION.
PubMed=10898794;
Inoue K., Wen R., Rehg J.E., Adachi M., Cleveland J.L., Roussel M.F.,
Sherr C.J.;
"Disruption of the ARF transcriptional activator DMP1 facilitates cell
immortalization, Ras transformation, and tumorigenesis.";
Genes Dev. 14:1797-1809(2000).
[11]
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).
[12] {ECO:0000305}
DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=15105443; DOI=10.1091/mbc.E03-11-0785;
Yi Y., Shepard A., Kittrell F., Mulac-Jericevic B., Medina D.,
Said T.K.;
"p19ARF determines the balance between normal cell proliferation rate
and apoptosis during mammary gland development.";
Mol. Biol. Cell 15:2302-2311(2004).
[13] {ECO:0000305}
FUNCTION, AND INTERACTION WITH MYC.
PubMed=15361884; DOI=10.1038/nature02958;
Qi Y., Gregory M.A., Li Z., Brousal J.P., West K., Hann S.R.;
"p19ARF directly and differentially controls the functions of c-Myc
independently of p53.";
Nature 431:712-717(2004).
[14] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, 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).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=15601844; DOI=10.1128/MCB.25.1.220-232.2005;
Sreeramaneni R., Chaudhry A., McMahon M., Sherr C.J., Inoue K.;
"Ras-Raf-Arf signaling critically depends on the Dmp1 transcription
factor.";
Mol. Cell. Biol. 25:220-232(2005).
[16]
ALTERNATIVE SPLICING (ISOFORM SMARF), FUNCTION (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).
[17]
FUNCTION.
PubMed=17936562; DOI=10.1016/j.ccr.2007.08.034;
Mallakin A., Sugiyama T., Taneja P., Matise L.A., Frazier D.P.,
Choudhary M., Hawkins G.A., D'Agostino R.B. Jr., Willingham M.C.,
Inoue K.;
"Mutually exclusive inactivation of DMP1 and ARF/p53 in lung cancer.";
Cancer Cell 12:381-394(2007).
[18]
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).
[19]
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).
[20]
INDUCTION.
PubMed=17546045; DOI=10.1038/sj.onc.1210568;
Taneja P., Mallakin A., Matise L.A., Frazier D.P., Choudhary M.,
Inoue K.;
"Repression of Dmp1 and Arf transcription by anthracyclins: critical
roles of the NF-kappaB subunit p65.";
Oncogene 26:7457-7466(2007).
[21] {ECO:0000305}
STRUCTURE BY NMR OF 1-37.
PubMed=11327858; DOI=10.1021/bi0024005;
DiGiammarino E.L., Filippov I., Weber J.D., Bothner B., Kriwacki R.W.;
"Solution structure of the p53 regulatory domain of the p19Arf tumor
suppressor protein.";
Biochemistry 40:2379-2386(2001).
-!- 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 (By
similarity). 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:0000250|UniProtKB:Q8N726, ECO:0000269|PubMed:10359817,
ECO:0000269|PubMed:15361884, ECO:0000269|PubMed:15567177,
ECO:0000269|PubMed:15601844, ECO:0000269|PubMed:17936562,
ECO:0000269|PubMed:8521522, ECO:0000269|PubMed:9393858,
ECO:0000269|PubMed:9529248}.
-!- SUBUNIT: Does not interact with cyclins, CDK1, CDK2, CDK4, CDK5 or
CDK6. Interacts with COMMD1 (By similarity). Binds to BCL6, E2F1,
HUWE1, MDM2, MYC, NPM1/B23, TOP1/TOPOI and UBE2I/UBC9. Interacts
with TBRG1. Interacts with CDKN2AIP and E4F1. Isoform smARF
interacts with C1QBP. Interacts with CDK5RAP3 and MDM2; form a
ternary complex involved in regulation of p53/TP53. Interacts with
NOP53; the interaction is direct and promotes ARF nucleoplasmic
relocalization and ubiquitin-mediated proteasomal degradation (By
similarity). {ECO:0000250|UniProtKB:Q8N726,
ECO:0000269|PubMed:12154087, ECO:0000269|PubMed:15361884,
ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:17110379,
ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:9529248}.
-!- INTERACTION:
Q07021:C1QBP (xeno); NbExp=4; IntAct=EBI-1202287, EBI-347528;
Q8K4B0:Mta1; NbExp=2; IntAct=EBI-1202287, EBI-1216353;
Q8VCI5:Pex19; NbExp=4; IntAct=EBI-1202306, EBI-1810767;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000250|UniProtKB:Q8N726, ECO:0000269|PubMed:10359817,
ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:15601844,
ECO:0000269|PubMed:8521522}. Nucleus, nucleoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform smARF: Mitochondrion
{ECO:0000269|PubMed:16713577}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
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:0000269|PubMed:8521522};
Name=tumor suppressor ARF {ECO:0000303|PubMed:10097151};
Synonyms=p19ARF {ECO:0000303|PubMed:8521522};
IsoId=Q64364-1; Sequence=Displayed;
Name=1 {ECO:0000305}; Synonyms=p16INK4a {ECO:0000305};
IsoId=P51480-1; Sequence=External;
Name=2 {ECO:0000305};
IsoId=P51480-2; Sequence=External;
Name=smARF;
IsoId=Q64364-2; Sequence=VSP_044963;
-!- DEVELOPMENTAL STAGE: Not detected in 12-week virgin mammary
glands. Expression increases (at protein level) six-fold during
pregnancy and remains at this level during lactation. During
involution, a slight increase is observed at days 2 and 8 followed
by a sharp decline at day 15. {ECO:0000269|PubMed:15105443}.
-!- INDUCTION: By progesterone. Induced by activated Ras, and this
requires DMTF1. Repressed by non-classical inhibitors of NF-kappa-
B signaling such as doxorubicin, daunorubicin and UVC, and by the
NF-kappa-B p65 subunit (RELA). {ECO:0000269|PubMed:10898794,
ECO:0000269|PubMed:15105443, ECO:0000269|PubMed:15601844,
ECO:0000269|PubMed:17546045}.
-!- 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 degradation. In
cancer cells, however, TRIP12 is located in a different cell
compartment, preventing ubiquitination and degradation (By
similarity). {ECO:0000250}.
-!- 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:0000250|UniProtKB:Q8N726}.
-!- DISRUPTION PHENOTYPE: Mice lacking isoform tumor suppressor ARF of
Cdkn2a display delayed mammary gland involution.
{ECO:0000269|PubMed:15105443}.
-!- 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 P51480) which
is encoded by the same gene. {ECO:0000305}.
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EMBL; L76092; AAC42080.1; -; mRNA.
EMBL; BC058190; AAH58190.3; -; mRNA.
EMBL; S80650; AAB35770.1; -; mRNA.
EMBL; AJ238890; CAB65598.1; -; Genomic_DNA.
EMBL; U49281; AAC00053.1; -; Genomic_DNA.
EMBL; U49282; AAC00054.1; -; Genomic_DNA.
EMBL; AF120108; AAD33245.1; -; Genomic_DNA.
CCDS; CCDS18350.1; -. [Q64364-1]
RefSeq; NP_034007.1; NM_009877.2. [Q64364-1]
UniGene; Mm.4733; -.
PDB; 1HN3; NMR; -; A=1-37.
PDBsum; 1HN3; -.
DisProt; DP00335; -.
ProteinModelPortal; Q64364; -.
SMR; Q64364; -.
BioGrid; 198654; 34.
CORUM; Q64364; -.
DIP; DIP-24169N; -.
IntAct; Q64364; 10.
MINT; MINT-193442; -.
STRING; 10090.ENSMUSP00000030237; -.
iPTMnet; Q64364; -.
EPD; Q64364; -.
MaxQB; Q64364; -.
PaxDb; Q64364; -.
PeptideAtlas; Q64364; -.
PRIDE; Q64364; -.
Ensembl; ENSMUST00000107131; ENSMUSP00000102748; ENSMUSG00000044303. [Q64364-1]
GeneID; 12578; -.
UCSC; uc008toi.1; mouse. [Q64364-1]
CTD; 1029; -.
MGI; MGI:104738; Cdkn2a.
eggNOG; ENOG410J100; Eukaryota.
eggNOG; ENOG4111DUI; LUCA.
GeneTree; ENSGT00390000008249; -.
HOVERGEN; HBG081068; -.
InParanoid; Q64364; -.
OrthoDB; EOG091G113N; -.
PhylomeDB; Q64364; -.
EvolutionaryTrace; Q64364; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000044303; -.
CleanEx; MM_CDKN2A; -.
ExpressionAtlas; Q64364; baseline and differential.
Genevisible; Q64364; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0001652; C:granular component; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0035985; C:senescence-associated heterochromatin focus; ISO:MGI.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:MGI.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:CAFA.
GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; IPI:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0019789; F:SUMO transferase activity; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:1990948; F:ubiquitin ligase inhibitor activity; ISO:MGI.
GO; GO:0055105; F:ubiquitin-protein transferase inhibitor activity; IDA:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0007568; P:aging; IMP:MGI.
GO; GO:1990000; P:amyloid fibril formation; ISO:MGI.
GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:MGI.
GO; GO:0000422; P:autophagy of mitochondrion; ISO:MGI.
GO; GO:0007569; P:cell aging; IDA:MGI.
GO; GO:0007050; P:cell cycle arrest; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:MGI.
GO; GO:0090398; P:cellular senescence; IDA:MGI.
GO; GO:0008544; P:epidermis development; IMP:MGI.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0051882; P:mitochondrial depolarization; ISO:MGI.
GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:HGNC.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:MGI.
GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; IMP:HGNC.
GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IMP:MGI.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0042326; P:negative regulation of phosphorylation; ISO:MGI.
GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
GO; GO:2000435; P:negative regulation of protein neddylation; ISO:MGI.
GO; GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:1903051; P:negative regulation of proteolysis involved in cellular protein catabolic process; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISO:MGI.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:BHF-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IMP:MGI.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISO:MGI.
GO; GO:2000774; P:positive regulation of cellular senescence; ISO:MGI.
GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0031648; P:protein destabilization; ISO:MGI.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:1902510; P:regulation of apoptotic DNA fragmentation; ISO:MGI.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IGI:MGI.
GO; GO:0046825; P:regulation of protein export from nucleus; ISO:MGI.
GO; GO:0031647; P:regulation of protein stability; IMP:BHF-UCL.
GO; GO:1903214; P:regulation of protein targeting to mitochondrion; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0090399; P:replicative senescence; ISO:MGI.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
GO; GO:0009303; P:rRNA transcription; IGI:MGI.
GO; GO:0035986; P:senescence-associated heterochromatin focus assembly; ISO:MGI.
GO; GO:0048103; P:somatic stem cell division; IMP:HGNC.
GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI.
InterPro; IPR010868; Tumor_suppres_ARF.
Pfam; PF07392; P19Arf_N; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cell cycle;
Complete proteome; DNA-binding; Mitochondrion; Nucleus;
Reference proteome; rRNA processing; Transcription;
Transcription regulation; Tumor suppressor; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 169 Tumor suppressor ARF.
/FTId=PRO_0000144182.
REGION 1 63 Interaction with CDK5RAP3 and MDM2.
{ECO:0000250|UniProtKB:Q8N726}.
COMPBIAS 3 168 Arg-rich. {ECO:0000255}.
VAR_SEQ 1 44 Missing (in isoform smARF).
{ECO:0000305}.
/FTId=VSP_044963.
MUTAGEN 85 85 L->P,R: No effect on activity.
{ECO:0000269|PubMed:9012842}.
MUTAGEN 93 93 P->S: No effect on activity.
{ECO:0000269|PubMed:9012842}.
MUTAGEN 97 97 R->Q: No effect on activity.
{ECO:0000269|PubMed:9012842}.
MUTAGEN 105 106 Missing: No effect on activity.
{ECO:0000269|PubMed:9012842}.
MUTAGEN 120 120 A->T: No effect on activity.
{ECO:0000269|PubMed:9012842}.
HELIX 4 14 {ECO:0000244|PDB:1HN3}.
HELIX 20 29 {ECO:0000244|PDB:1HN3}.
SEQUENCE 169 AA; 19238 MW; 644505EFE1CBF478 CRC64;
MGRRFLVTVR IQRAGRPLQE RVFLVKFVRS RRPRTASCAL AFVNMLLRLE RILRRGPHRN
PGPGDDDGQR SRSSSSAQLR CRFELRGPHY LLPPGARRSA GRLPGHAGGA ARVRGSAGCA
RCLGSPAARL GPRAGTSRHR AIFAFRWVLF VFRWVVFVYR WERRPDRRA


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