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Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (Melanoma differentiation-associated protein 6) (MDA-6) (p21)

 CDN1A_HUMAN             Reviewed;         164 AA.
P38936; Q14010; Q6FI05; Q9BUT4;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 201.
RecName: Full=Cyclin-dependent kinase inhibitor 1;
AltName: Full=CDK-interacting protein 1;
AltName: Full=Melanoma differentiation-associated protein 6;
Short=MDA-6;
AltName: Full=p21;
Name=CDKN1A; Synonyms=CAP20, CDKN1, CIP1, MDA6, PIC1, SDI1, WAF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
PubMed=8242751; DOI=10.1016/0092-8674(93)90499-G;
Harper J.W., Adami G.R., Wei N., Keyomarsi K., Elledge S.J.;
"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1
cyclin-dependent kinases.";
Cell 75:805-816(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=8242752; DOI=10.1016/0092-8674(93)90500-P;
El-Deiry W.S., Tokino T., Velculescu V.E., Levy D.B., Parsons R.,
Trent J.M., Lin D., Mercer W.E., Kinzler K.W., Vogelstein B.;
"WAF1, a potential mediator of p53 tumor suppression.";
Cell 75:817-825(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8259214; DOI=10.1038/366701a0;
Xiong Y., Hannon G.J., Zhang H., Casso D., Kobayashi R., Beach D.;
"p21 is a universal inhibitor of cyclin kinases.";
Nature 366:701-704(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Jiang H., Fisher P.B.;
"Use of a sensitive and efficient subtraction hybridization protocol
for the identification of genes differentially regulated during the
induction of differentiation in human melanoma cells.";
Mol. Cell. Differ. 1:285-299(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7753561;
Jiang H., Lin J., Su Z.Z., Herlyn M., Kerbel R.S., Weissman B.E.,
Welch D.R., Fisher P.B.;
"The melanoma differentiation-associated gene mda-6, which encodes the
cyclin-dependent kinase inhibitor p21, is differentially expressed
during growth, differentiation and progression in human melanoma
cells.";
Oncogene 10:1855-1864(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8125163; DOI=10.1006/excr.1994.1063;
Noda A., Ning Y., Venable S.F., Pereira-Smith O.M., Smith J.R.;
"Cloning of senescent cell-derived inhibitors of DNA synthesis using
an expression screen.";
Exp. Cell Res. 211:90-98(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-31.
PubMed=7655464; DOI=10.1093/hmg/4.6.1089;
Mousses S., Oezcelik H., Lee P.D., Malkin D., Bull S.B.,
Andrulis I.L.;
"Two variants of the CIP1/WAF1 gene occur together and are associated
with human cancer.";
Hum. Mol. Genet. 4:1089-1092(1995).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-31.
NIEHS SNPs program;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[9]
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-31.
TISSUE=Eye, and Lung;
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).
[15]
PROTEIN SEQUENCE OF 2-16, ACETYLATION AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=15574338; DOI=10.1016/j.molcel.2004.11.011;
Chen X., Chi Y., Bloecher A., Aebersold R., Clurman B.E.,
Roberts J.M.;
"N-acetylation and ubiquitin-independent proteasomal degradation of
p21(Cip1).";
Mol. Cell 16:839-847(2004).
[16]
PROTEIN SEQUENCE OF 136-148, PHOSPHORYLATION AT THR-145; SER-146 AND
SER-160, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10753973; DOI=10.1074/jbc.275.15.11529;
Scott M.T., Morrice N., Ball K.L.;
"Reversible phosphorylation at the C-terminal regulatory domain of
p21(Waf1/Cip1) modulates proliferating cell nuclear antigen binding.";
J. Biol. Chem. 275:11529-11537(2000).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDK4 AND CCND1 IN
THE CYCLIN D-CDK4-CDKN1A COMPLEX.
PubMed=9106657; DOI=10.1101/gad.11.7.847;
LaBaer J., Garrett M.D., Stevenson L.F., Slingerland J.M., Sandhu C.,
Chou H.S., Fattaey A., Harlow E.;
"New functional activities for the p21 family of CDK inhibitors.";
Genes Dev. 11:847-862(1997).
[18]
INTERACTION WITH PSMA3.
PubMed=11350925; DOI=10.1093/emboj/20.10.2367;
Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J.,
Allday M.J.;
"A degradation signal located in the C-terminus of p21WAF1/CIP1 is a
binding site for the C8 alpha-subunit of the 20S proteasome.";
EMBO J. 20:2367-2375(2001).
[19]
FUNCTION, AND INTERACTION WITH PCNA.
PubMed=11595739; DOI=10.1074/jbc.M106990200;
Ducoux M., Urbach S., Baldacci G., Huebscher U., Koundrioukoff S.,
Christensen J., Hughes P.;
"Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA
replication through a conserved p21(Cip1)-like PCNA-binding motif
present in the third subunit of human DNA polymerase delta.";
J. Biol. Chem. 276:49258-49266(2001).
[20]
PHOSPHORYLATION AT THR-145, MUTAGENESIS OF THR-145 AND SER-146, AND
SUBCELLULAR LOCATION.
PubMed=11463845; DOI=10.1128/MCB.21.16.5644-5657.2001;
Roessig L., Jadidi A.S., Urbich C., Badorff C., Zeiher A.M.,
Dimmeler S.;
"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and
proliferation of endothelial cells.";
Mol. Cell. Biol. 21:5644-5657(2001).
[21]
PHOSPHORYLATION AT THR-145 BY PIM1, SUBCELLULAR LOCATION, AND
INTERACTION WITH PIM1.
PubMed=12431783; DOI=10.1016/S0167-4889(02)00347-6;
Wang Z., Bhattacharya N., Mixter P.F., Wei W., Sedivy J.,
Magnuson N.S.;
"Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1
kinase.";
Biochim. Biophys. Acta 1593:45-55(2002).
[22]
UBIQUITINATION AT SER-2.
PubMed=15226418; DOI=10.1128/MCB.24.14.6140-6150.2004;
Coulombe P., Rodier G., Bonneil E., Thibault P., Meloche S.;
"N-Terminal ubiquitination of extracellular signal-regulated kinase 3
and p21 directs their degradation by the proteasome.";
Mol. Cell. Biol. 24:6140-6150(2004).
[23]
PHOSPHORYLATION AT THR-145.
PubMed=16982699; DOI=10.1128/MCB.00201-06;
Heron-Milhavet L., Franckhauser C., Rana V., Berthenet C., Fisher D.,
Hemmings B.A., Fernandez A., Lamb N.J.;
"Only Akt1 is required for proliferation, while Akt2 promotes cell
cycle exit through p21 binding.";
Mol. Cell. Biol. 26:8267-8280(2006).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[25]
UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, INTERACTION WITH PCNA,
MUTAGENESIS OF SER-114 AND 144-GLN--PHE-150, AND PHOSPHORYLATION AT
SER-114.
PubMed=18794347; DOI=10.1101/gad.1676108;
Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A.;
"PCNA-dependent regulation of p21 ubiquitylation and degradation via
the CRL4Cdt2 ubiquitin ligase complex.";
Genes Dev. 22:2496-2506(2008).
[26]
UBIQUITINATION.
PubMed=18794348; DOI=10.1101/gad.1703708;
Kim Y., Starostina N.G., Kipreos E.T.;
"The CRL4Cdt2 ubiquitin ligase targets the degradation of p21Cip1 to
control replication licensing.";
Genes Dev. 22:2507-2519(2008).
[27]
UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, MUTAGENESIS OF
147-MET--TYR-151 AND 154-LYS--ARG-156, AND INTERACTION WITH PCNA.
PubMed=18703516; DOI=10.1074/jbc.M806045200;
Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T.,
Tsurimoto T.;
"CDK inhibitor p21 is degraded by a proliferating cell nuclear
antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV
irradiation.";
J. Biol. Chem. 283:29045-29052(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
REVIEW ON DNA REPAIR, AND INTERACTION WITH CDK2.
PubMed=19445729; DOI=10.1186/1747-1028-4-9;
Satyanarayana A., Kaldis P.;
"A dual role of Cdk2 in DNA damage response.";
Cell Div. 4:9-9(2009).
[30]
UBIQUITINATION, AND INTERACTION WITH MKRN1.
PubMed=19536131; DOI=10.1038/emboj.2009.164;
Lee E.-W., Lee M.-S., Camus S., Ghim J., Yang M.-R., Oh W., Ha N.-C.,
Lane D.P., Song J.;
"Differential regulation of p53 and p21 by MKRN1 E3 ligase controls
cell cycle arrest and apoptosis.";
EMBO J. 28:2100-2113(2009).
[31]
UBIQUITINATION.
PubMed=19332548; DOI=10.1074/jbc.M808810200;
Stuart S.A., Wang J.Y.;
"Ionizing radiation induces ATM-independent degradation of p21Cip1 in
transformed cells.";
J. Biol. Chem. 284:15061-15070(2009).
[32]
PHOSPHORYLATION AT THR-145 BY PIM2.
PubMed=20307683; DOI=10.1016/j.biocel.2010.03.012;
Wang Z., Zhang Y., Gu J.J., Davitt C., Reeves R., Magnuson N.S.;
"Pim-2 phosphorylation of p21(Cip1/WAF1) enhances its stability and
inhibits cell proliferation in HCT116 cells.";
Int. J. Biochem. Cell Biol. 42:1030-1038(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[34]
UBIQUITINATION BY RNF114.
PubMed=23645206; DOI=10.1038/cdd.2013.33;
Han J., Kim Y.L., Lee K.W., Her N.G., Ha T.K., Yoon S., Jeong S.I.,
Lee J.H., Kang M.J., Lee M.G., Ryu B.K., Baik J.H., Chi S.G.;
"ZNF313 is a novel cell cycle activator with an E3 ligase activity
inhibiting cellular senescence by destabilizing p21(WAF1.).";
Cell Death Differ. 20:1055-1067(2013).
[35]
FUNCTION, INTERACTION WITH STK11 AND NUAK1, PHOSPHORYLATION AT THR-80
AND SER-146, AND MUTAGENESIS OF THR-80 AND SER-146.
PubMed=25329316; DOI=10.1371/journal.pgen.1004721;
Esteve-Puig R., Gil R., Gonzalez-Sanchez E., Bech-Serra J.J.,
Grueso J., Hernandez-Losa J., Moline T., Canals F., Ferrer B.,
Cortes J., Bastian B., Cajal S.R.Y., Martin-Caballero J., Flores J.M.,
Vivancos A., Garcia-Patos V., Recio J.A.;
"A mouse model uncovers LKB1 as an UVB-induced DNA damage sensor
mediating CDKN1A (p21WAF1/CIP1) degradation.";
PLoS Genet. 10:E1004721-E1004721(2014).
[36]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 139-160 IN COMPLEX WITH PCNA.
PubMed=8861913; DOI=10.1016/S0092-8674(00)81347-1;
Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J.;
"Structure of the C-terminal region of p21(WAF1/CIP1) complexed with
human PCNA.";
Cell 87:297-306(1996).
-!- FUNCTION: May be involved in p53/TP53 mediated inhibition of
cellular proliferation in response to DNA damage. Binds to and
inhibits cyclin-dependent kinase activity, preventing
phosphorylation of critical cyclin-dependent kinase substrates and
blocking cell cycle progression. Functions in the nuclear
localization and assembly of cyclin D-CDK4 complex and promotes
its kinase activity towards RB1. At higher stoichiometric ratios,
inhibits the kinase activity of the cyclin D-CDK4 complex.
Inhibits DNA synthesis by DNA polymerase delta by competing with
POLD3 for PCNA binding (PubMed:11595739).
{ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:8242751,
ECO:0000269|PubMed:9106657}.
-!- SUBUNIT: Interacts with HDAC1; the interaction is prevented by
competitive binding of C10orf90/FATS to HDAC1 facilitating
acetylation and protein stabilization of CDKN1A/p21 (By
similarity). Interacts with MKRN1 (PubMed:19536131). Interacts
with PSMA3 (PubMed:11350925). Interacts with PCNA
(PubMed:11595739, PubMed:18794347, PubMed:18703516,
PubMed:8861913). Component of the ternary complex, cyclin D-CDK4-
CDKN1A. Interacts (via its N-terminal domain) with CDK4; the
interaction promotes the assembly of the cyclin D-CDK4 complex,
its nuclear translocation and promotes the cyclin D-dependent
enzyme activity of CDK4 (PubMed:9106657). Binding to CDK2 leads to
CDK2/cyclin E inactivation at the G1-S phase DNA damage
checkpoint, thereby arresting cells at the G1-S transition during
DNA repair (PubMed:19445729). Interacts with PIM1
(PubMed:12431783). Interacts with STK11 and NUAK1
(PubMed:25329316). {ECO:0000250|UniProtKB:P39689,
ECO:0000269|PubMed:11350925, ECO:0000269|PubMed:11595739,
ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:18703516,
ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:19445729,
ECO:0000269|PubMed:19536131, ECO:0000269|PubMed:25329316,
ECO:0000269|PubMed:8861913, ECO:0000269|PubMed:9106657}.
-!- INTERACTION:
P27958:- (xeno); NbExp=3; IntAct=EBI-375077, EBI-6377335;
P78396:CCNA1; NbExp=3; IntAct=EBI-375077, EBI-375065;
P20248:CCNA2; NbExp=3; IntAct=EBI-375077, EBI-457097;
P24385:CCND1; NbExp=15; IntAct=EBI-375077, EBI-375001;
P30279:CCND2; NbExp=14; IntAct=EBI-375077, EBI-748789;
P30281:CCND3; NbExp=17; IntAct=EBI-375077, EBI-375013;
P24864:CCNE1; NbExp=9; IntAct=EBI-375077, EBI-519526;
O96020:CCNE2; NbExp=4; IntAct=EBI-375077, EBI-375033;
O75419:CDC45; NbExp=2; IntAct=EBI-375077, EBI-374969;
Q99741:CDC6; NbExp=2; IntAct=EBI-375077, EBI-374862;
P06493:CDK1; NbExp=3; IntAct=EBI-375077, EBI-444308;
O94921:CDK14; NbExp=8; IntAct=EBI-375077, EBI-1043945;
P24941:CDK2; NbExp=25; IntAct=EBI-375077, EBI-375096;
Q00526:CDK3; NbExp=4; IntAct=EBI-375077, EBI-1245761;
P11802:CDK4; NbExp=5; IntAct=EBI-375077, EBI-295644;
Q00535:CDK5; NbExp=4; IntAct=EBI-375077, EBI-1041567;
Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-375077, EBI-747204;
Q15323:KRT31; NbExp=5; IntAct=EBI-375077, EBI-948001;
Q9UHC7:MKRN1; NbExp=5; IntAct=EBI-375077, EBI-373524;
Q9BQ15:NABP2; NbExp=7; IntAct=EBI-375077, EBI-2120336;
P12004:PCNA; NbExp=29; IntAct=EBI-375077, EBI-358311;
Q6FI35:PCNA; NbExp=2; IntAct=EBI-375077, EBI-8469539;
Q9UQR0-1:SCML2; NbExp=3; IntAct=EBI-375077, EBI-16087037;
Q96FS4:SIPA1; NbExp=2; IntAct=EBI-375077, EBI-1054981;
P63208:SKP1; NbExp=3; IntAct=EBI-375077, EBI-307486;
Q13309:SKP2; NbExp=2; IntAct=EBI-375077, EBI-456291;
P15884:TCF4; NbExp=3; IntAct=EBI-375077, EBI-533224;
Q8IYF3:TEX11; NbExp=4; IntAct=EBI-375077, EBI-742397;
P04637:TP53; NbExp=3; IntAct=EBI-375077, EBI-366083;
Q13077:TRAF1; NbExp=3; IntAct=EBI-375077, EBI-359224;
Q9BYV2:TRIM54; NbExp=5; IntAct=EBI-375077, EBI-2130429;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- TISSUE SPECIFICITY: Expressed in all adult tissues, with 5-fold
lower levels observed in the brain.
-!- INDUCTION: Activated by p53/TP53, mezerein (antileukemic compound)
and IFNB1. Repressed by HDAC1. {ECO:0000269|PubMed:8242751,
ECO:0000269|PubMed:8242752}.
-!- DOMAIN: The PIP-box K+4 motif mediates both the interaction with
PCNA and the recruitment of the DCX(DTL) complex: while the PIP-
box interacts with PCNA, the presence of the K+4 submotif,
recruits the DCX(DTL) complex, leading to its ubiquitination.
-!- DOMAIN: The C-terminal is required for nuclear localization of the
cyclin D-CDK4 complex.
-!- PTM: Phosphorylation of Thr-145 by Akt or of Ser-146 by PKC
impairs binding to PCNA. Phosphorylation at Ser-114 by GSK3-beta
enhances ubiquitination by the DCX(DTL) complex. Phosphorylation
of Thr-145 by PIM2 enhances CDKN1A stability and inhibits cell
proliferation. Phosphorylation of Thr-145 by PIM1 results in the
relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein
stability. UV radiation-induced phosphorylation at Thr-80 by LKB1
and at Ser-146 by NUAK1 leads to its degradation.
{ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:11463845,
ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:16982699,
ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:20307683,
ECO:0000269|PubMed:25329316}.
-!- PTM: Ubiquitinated by MKRN1; leading to polyubiquitination and 26S
proteasome-dependent degradation. Ubiquitinated by the DCX(DTL)
complex, also named CRL4(CDT2) complex, leading to its degradation
during S phase or following UV irradiation. Ubiquitination by the
DCX(DTL) complex is essential to control replication licensing and
is PCNA-dependent: interacts with PCNA via its PIP-box, while the
presence of the containing the 'K+4' motif in the PIP box, recruit
the DCX(DTL) complex, leading to its degradation. Ubiquitination
at Ser-2 leads to degradation by the proteasome pathway.
Ubiquitinated by RNF114; leading to proteasomal degradation.
{ECO:0000269|PubMed:15226418}.
-!- PTM: Acetylation leads to protein stability. Acetylated in vitro
on Lys-141, Lys-154, Lys-161 and Lys-163. Deacetylation by HDAC1
is prevented by competitive binding of C10orf90/FATS to HDAC1 (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the CDI family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB59559.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAB59560.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CDKN1AID139.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdkn1a/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L25610; AAA16109.1; -; mRNA.
EMBL; S67388; AAB29246.1; -; mRNA.
EMBL; U09579; AAA85641.1; -; mRNA.
EMBL; U03106; AAC04313.1; -; mRNA.
EMBL; L26165; AAA19811.1; -; mRNA.
EMBL; L47232; AAB59559.1; ALT_INIT; mRNA.
EMBL; L47233; AAB59560.1; ALT_INIT; mRNA.
EMBL; AF497972; AAM11787.1; -; Genomic_DNA.
EMBL; BT006719; AAP35365.1; -; mRNA.
EMBL; AB451290; BAG70104.1; -; mRNA.
EMBL; AB451422; BAG70236.1; -; mRNA.
EMBL; CR536533; CAG38770.1; -; mRNA.
EMBL; Z85996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03904.1; -; Genomic_DNA.
EMBL; BC000275; AAH00275.1; -; mRNA.
EMBL; BC000312; AAH00312.1; -; mRNA.
EMBL; BC001935; AAH01935.1; -; mRNA.
EMBL; BC013967; AAH13967.1; -; mRNA.
CCDS; CCDS4824.1; -.
PIR; I54380; I54380.
PIR; I68674; I68674.
RefSeq; NP_000380.1; NM_000389.4.
RefSeq; NP_001207706.1; NM_001220777.1.
RefSeq; NP_001207707.1; NM_001220778.1.
RefSeq; NP_001278478.1; NM_001291549.1.
RefSeq; NP_510867.1; NM_078467.2.
UniGene; Hs.370771; -.
UniGene; Hs.732576; -.
PDB; 1AXC; X-ray; 2.60 A; B/D/F=139-160.
PDB; 2ZVV; X-ray; 2.00 A; X/Y=139-160.
PDB; 2ZVW; X-ray; 2.50 A; I/J/K/L/M/N/O/P=139-160.
PDB; 4RJF; X-ray; 2.01 A; B/D/F=139-160.
PDB; 5E0U; X-ray; 1.93 A; D/E/F=139-160.
PDBsum; 1AXC; -.
PDBsum; 2ZVV; -.
PDBsum; 2ZVW; -.
PDBsum; 4RJF; -.
PDBsum; 5E0U; -.
DisProt; DP00016; -.
ProteinModelPortal; P38936; -.
SMR; P38936; -.
BioGrid; 107460; 273.
CORUM; P38936; -.
DIP; DIP-246N; -.
IntAct; P38936; 178.
MINT; MINT-104203; -.
STRING; 9606.ENSP00000244741; -.
BindingDB; P38936; -.
ChEMBL; CHEMBL5021; -.
iPTMnet; P38936; -.
PhosphoSitePlus; P38936; -.
BioMuta; CDKN1A; -.
DMDM; 729143; -.
SWISS-2DPAGE; P38936; -.
EPD; P38936; -.
PaxDb; P38936; -.
PeptideAtlas; P38936; -.
PRIDE; P38936; -.
DNASU; 1026; -.
Ensembl; ENST00000244741; ENSP00000244741; ENSG00000124762.
Ensembl; ENST00000373711; ENSP00000362815; ENSG00000124762.
Ensembl; ENST00000405375; ENSP00000384849; ENSG00000124762.
Ensembl; ENST00000448526; ENSP00000409259; ENSG00000124762.
Ensembl; ENST00000615513; ENSP00000482768; ENSG00000124762.
GeneID; 1026; -.
KEGG; hsa:1026; -.
UCSC; uc003omm.5; human.
CTD; 1026; -.
DisGeNET; 1026; -.
EuPathDB; HostDB:ENSG00000124762.13; -.
GeneCards; CDKN1A; -.
HGNC; HGNC:1784; CDKN1A.
HPA; CAB000064; -.
HPA; CAB069401; -.
HPA; HPA005946; -.
MalaCards; CDKN1A; -.
MIM; 116899; gene.
neXtProt; NX_P38936; -.
OpenTargets; ENSG00000124762; -.
Orphanet; 652; Multiple endocrine neoplasia type 1.
PharmGKB; PA104; -.
eggNOG; KOG4743; Eukaryota.
eggNOG; ENOG410XXN5; LUCA.
GeneTree; ENSGT00530000063588; -.
HOGENOM; HOG000285999; -.
HOVERGEN; HBG050868; -.
InParanoid; P38936; -.
KO; K06625; -.
OMA; FAWERVW; -.
OrthoDB; EOG091G19PZ; -.
PhylomeDB; P38936; -.
TreeFam; TF101038; -.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69563; p53-Dependent G1 DNA Damage Response.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-HSA-69895; Transcriptional activation of cell cycle inhibitor p21.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
Reactome; R-HSA-8941855; RUNX3 regulates CDKN1A transcription.
SIGNOR; P38936; -.
ChiTaRS; CDKN1A; human.
EvolutionaryTrace; P38936; -.
GeneWiki; P21; -.
GenomeRNAi; 1026; -.
PRO; PR:P38936; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124762; -.
CleanEx; HS_CDKN1A; -.
ExpressionAtlas; P38936; baseline and differential.
Genevisible; P38936; HS.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0070557; C:PCNA-p21 complex; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0030332; F:cyclin binding; IEA:Ensembl.
GO; GO:0019912; F:cyclin-dependent protein kinase activating kinase activity; IDA:UniProtKB.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; EXP:Reactome.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; TAS:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032403; F:protein complex binding; IPI:CAFA.
GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
GO; GO:0004860; F:protein kinase inhibitor activity; IMP:CAFA.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:BHF-UCL.
GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:BHF-UCL.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL.
GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
GO; GO:0090398; P:cellular senescence; IMP:BHF-UCL.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IDA:BHF-UCL.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0060574; P:intestinal epithelial cell maturation; IEA:Ensembl.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
GO; GO:0071850; P:mitotic cell cycle arrest; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:1904030; P:negative regulation of cyclin-dependent protein kinase activity; IMP:CAFA.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IGI:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0042326; P:negative regulation of phosphorylation; IDA:BHF-UCL.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0043068; P:positive regulation of programmed cell death; IEA:Ensembl.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
GO; GO:0050821; P:protein stabilization; TAS:Reactome.
GO; GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
GO; GO:2000278; P:regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0033158; P:regulation of protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0090399; P:replicative senescence; IEA:Ensembl.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
GO; GO:0090400; P:stress-induced premature senescence; TAS:BHF-UCL.
InterPro; IPR003175; CDI.
InterPro; IPR029841; CDKN1A_vertebrate.
PANTHER; PTHR10265; PTHR10265; 1.
PANTHER; PTHR10265:SF16; PTHR10265:SF16; 1.
Pfam; PF02234; CDI; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Complete proteome; Cytoplasm;
Direct protein sequencing; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Protein kinase inhibitor; Reference proteome;
Ubl conjugation; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:15574338}.
CHAIN 2 164 Cyclin-dependent kinase inhibitor 1.
/FTId=PRO_0000190079.
ZN_FING 13 41 C4-type. {ECO:0000255}.
REGION 17 24 Required for binding cyclins.
REGION 53 58 Required for binding CDKs.
MOTIF 140 164 PIP-box K+4 motif.
MOTIF 141 156 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:15574338}.
MOD_RES 80 80 Phosphothreonine; by LKB1.
{ECO:0000269|PubMed:25329316}.
MOD_RES 114 114 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:18794347}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648}.
MOD_RES 145 145 Phosphothreonine; by PKA, PKB/AKT1, PIM1
and PIM2. {ECO:0000269|PubMed:10753973,
ECO:0000269|PubMed:11463845,
ECO:0000269|PubMed:12431783,
ECO:0000269|PubMed:16982699,
ECO:0000269|PubMed:20307683}.
MOD_RES 146 146 Phosphoserine; by PKC and NUAK1.
{ECO:0000269|PubMed:10753973,
ECO:0000269|PubMed:25329316}.
MOD_RES 160 160 Phosphoserine; by PKC; in vitro.
{ECO:0000269|PubMed:10753973}.
CROSSLNK 2 2 Glycyl serine ester (Ser-Gly) (interchain
with G-Cter in ubiquitin).
{ECO:0000305|PubMed:15226418}.
VARIANT 4 4 P -> L (in dbSNP:rs4986866).
/FTId=VAR_048686.
VARIANT 31 31 S -> R (in dbSNP:rs1801270).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7655464,
ECO:0000269|Ref.8}.
/FTId=VAR_011870.
VARIANT 63 63 F -> L (in dbSNP:rs4986867).
/FTId=VAR_048687.
MUTAGEN 80 80 T->A: Abolishes UV radiation-induced
phosphorylation and subsequent
degradation.
{ECO:0000269|PubMed:25329316}.
MUTAGEN 114 114 S->E: Phosphomimetic mutant, increases
ubiquitination by the DCX(DTL) complex.
{ECO:0000269|PubMed:18794347}.
MUTAGEN 144 150 QTSMTDF->ATSATDA: Abolishes interaction
with PCNA and subsequent degradation by
the proteasome.
{ECO:0000269|PubMed:18794347}.
MUTAGEN 145 145 T->A: Reduces phosphorylation by Akt; no
change in interaction with PCNA, CDK2 or
CDK4; no change in subcellular location.
{ECO:0000269|PubMed:11463845}.
MUTAGEN 145 145 T->D: No interaction with PCNA; 59%
inhibition of CDK2 binding; modest
inhibition of CDK4 binding; no change in
subcellular location.
{ECO:0000269|PubMed:11463845}.
MUTAGEN 146 146 S->A: No change in interaction with PCNA.
Abolishes UV radiation-induced
phosphorylation and subsequent
degradation.
{ECO:0000269|PubMed:11463845,
ECO:0000269|PubMed:25329316}.
MUTAGEN 146 146 S->D: Reduces interaction with PCNA.
{ECO:0000269|PubMed:11463845}.
MUTAGEN 147 151 MTDFY->ATDAAA: Abolishes interaction with
PCNA and subsequent degradation by the
proteasome.
{ECO:0000269|PubMed:18703516}.
MUTAGEN 154 156 KRR->AAA: Abolishes degradation by the
proteasome without affecting the
interaction with PCNA.
{ECO:0000269|PubMed:18703516}.
HELIX 147 149 {ECO:0000244|PDB:5E0U}.
STRAND 153 158 {ECO:0000244|PDB:5E0U}.
SEQUENCE 164 AA; 18119 MW; 98D1E7C519ADFCA9 CRC64;
MSEPAGDVRQ NPCGSKACRR LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLE
GDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLV
PRSGEQAEGS PGGPGDSQGR KRRQTSMTDF YHSKRRLIFS KRKP


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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