P38936 (CDN1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase inhibitor 1

Alternative name(s):
CDK-interacting protein 1
Melanoma differentiation-associated protein 6
Short name=MDA-6
p21

Gene names

Name:	CDKN1A
Synonyms:	CAP20, CDKN1, CIP1, MDA6, PIC1, SDI1, WAF1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	164 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be the important intermediate by which p53/TP53 mediates its role as an inhibitor 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. Ref.1 Ref.13
Subunit structure	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. Interacts with PSMA3. Interacts with PCNA. 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. 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. Interacts with PIM1. Ref.13 Ref.14 Ref.16 Ref.19 Ref.21 Ref.23 Ref.24
Subcellular location	Cytoplasm. Nucleus Ref.13 Ref.15 Ref.16.
Tissue specificity	Expressed in all adult human tissues, with 5-fold lower levels observed in the brain.
Induction	Activated by p53/TP53, mezerein (antileukemic compound) and IFNB1. Repressed by HDAC1. Ref.1 Ref.2
Domain	The PIP-box K+4 motif mediates both the interaction with PCNA and the recuitment 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. Ref.19 Ref.21 The C-terminal is required for nuclear localization of the cyclin D-CDK4 complex. Ref.19 Ref.21
Post-translational modification	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. 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. Ref.19 Ref.20 Ref.21 Ref.24 Ref.25 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.
Sequence similarities	Belongs to the CDI family.
Sequence caution	The sequence AAB59559.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAB59560.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Protein kinase inhibitor
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Inferred from direct assay. Source: BHF-UCL G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Inferred from direct assay. Source: BHF-UCL G2/M transition of mitotic cell cycle Inferred from mutant phenotype. Source: BHF-UCL Ras protein signal transduction Inferred from expression pattern. Source: BHF-UCL S phase of mitotic cell cycle Traceable author statement. Source: Reactome cell cycle arrest Inferred from direct assay. Source: BHF-UCL cellular response to extracellular stimulus Inferred from mutant phenotype. Source: BHF-UCL cellular response to ionizing radiation Inferred from mutant phenotype. Source: BHF-UCL induction of apoptosis by intracellular signals Traceable author statement. Source: ProtInc negative regulation of cell growth Inferred from direct assay. Source: BHF-UCL negative regulation of cell proliferation Inferred from direct assay. Source: BHF-UCL positive regulation of fibroblast proliferation Inferred from mutant phenotype. Source: BHF-UCL positive regulation of reactive oxygen species metabolic process Inferred from mutant phenotype. Source: BHF-UCL stress-induced premature senescence Traceable author statement. Source: BHF-UCL
Cellular component	PCNA-p21 complex Inferred from direct assay Ref.19. Source: UniProtKB cyclin-dependent protein kinase holoenzyme complex Inferred from direct assay. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular function	cyclin-dependent protein kinase activating kinase activity Inferred from direct assay Ref.13. Source: UniProtKB cyclin-dependent protein kinase activity Inferred from experiment. Source: Reactome cyclin-dependent protein kinase inhibitor activity Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCNA1	P78396	2	EBI-375077,EBI-375065
CCNA2	P20248	2	EBI-375077,EBI-457097
CCND1	P24385	5	EBI-375077,EBI-375001
CCND3	P30281	3	EBI-375077,EBI-375013
CCNE1	P24864	7	EBI-375077,EBI-519526
CCNE2	O96020	2	EBI-375077,EBI-375033
CDK14	O94921	7	EBI-375077,EBI-1043945
CDK2	P24941	9	EBI-375077,EBI-375096
CDK4	P11802	4	EBI-375077,EBI-295644
CDK5	Q00535	2	EBI-375077,EBI-1041567
OBFC2B	Q9BQ15	7	EBI-375077,EBI-2120336
PCNA	P12004	4	EBI-375077,EBI-358311
SIPA1	Q96FS4	2	EBI-375077,EBI-1054981

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11

Chain

2 – 164

163

Cyclin-dependent kinase inhibitor 1

PRO_0000190079

Regions

Zinc finger

13 – 41

29

C4-type Potential

Region

17 – 24

8

Required for binding cyclins

Region

53 – 58

6

Required for binding CDKs

Motif

140 – 164

25

PIP-box K+4 motif

Motif

141 – 156

16

Nuclear localization signal Potential

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.11

Modified residue

114

1

Phosphoserine; by GSK3-beta Ref.19

Modified residue

130

1

Phosphoserine Ref.18 Ref.22

Modified residue

145

1

Phosphothreonine; by PKA; PKB/AKT1, PIM1 and PIM2 Ref.12 Ref.15 Ref.16 Ref.17 Ref.26

Modified residue

146

1

Phosphoserine; by PKC Ref.12

Modified residue

160

1

Phosphoserine; by PKC; in vitro Ref.12

Natural variations

Natural variant

4

1

P → L. [dbSNP:rs4986866]

VAR_048686

Natural variant

31

1

S → R. [dbSNP:rs1801270] Ref.7 Ref.8 Ref.10

VAR_011870

Natural variant

63

1

F → L. [dbSNP:rs4986867]

VAR_048687

Natural variant

149

1

D → G. [dbSNP:rs1801724]

VAR_014875

Experimental info

Mutagenesis

114

1

S → E: Phosphomimetic mutant, increases ubiquitination by the DCX(DTL) complex. Ref.19

Mutagenesis

144 – 150

7

QTSMTDF → ATSATDA: Abolishes interaction with PCNA and subsequent degradation by the proteasome. Ref.19

Mutagenesis

145

1

T → A: Reduces phosphorylation by Akt; no change in interaction with PCNA, CDK2 or CDK4; no change in subcellular location. Ref.15

Mutagenesis

145

1

T → D: No interaction with PCNA; 59% inhibition of CDK2 binding; modest inhibition of CDK4 binding; no change in subcellular location. Ref.15

Mutagenesis

146

1

S → A: No change in interaction with PCNA. Ref.15

Mutagenesis

146

1

S → D: Reduces interaction with PCNA. Ref.15

Mutagenesis

147 – 151

5

MTDFY → ATDAAA: Abolishes interaction with PCNA and subsequent degradation by the proteasome. Ref.21

Mutagenesis

154 – 156

3

KRR → AAA: Abolishes degradation by the proteasome without affecting the interaction with PCNA. Ref.21

Secondary structure

1

.

.

.

.

.

164

Helix Strand Turn

Details...

Helix

147 – 149

3

Beta strand

151 – 158

8

Sequences

	Sequence		Length	Mass (Da)
	P38936 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 98D1E7C519ADFCA9	FASTA	164	18,119
	10 20 30 40 50 60 MSEPAGDVRQ NPCGSKACRR LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLE 70 80 90 100 110 120 GDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLV 130 140 150 160 PRSGEQAEGS PGGPGDSQGR KRRQTSMTDF YHSKRRLIFS KRKP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases." Harper J.W., Adami G.R., Wei N., Keyomarsi K., Elledge S.J. Cell 75:805-816(1993) [PubMed: 8242751] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION.
[2]	"WAF1, a potential mediator of p53 tumor suppression." 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. Cell 75:817-825(1993) [PubMed: 8242752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[3]	"p21 is a universal inhibitor of cyclin kinases." Xiong Y., Hannon G.J., Zhang H., Casso D., Kobayashi R., Beach D. Nature 366:701-704(1993) [PubMed: 8259214] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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." Jiang H., Fisher P.B. Mol. Cell. Differ. 1:285-299(1993) Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"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." Jiang H., Lin J., Su Z.Z., Herlyn M., Kerbel R.S., Weissman B.E., Welch D.R., Fisher P.B. Oncogene 10:1855-1864(1995) [PubMed: 7753561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen." Noda A., Ning Y., Venable S.F., Pereira-Smith O.M., Smith J.R. Exp. Cell Res. 211:90-98(1994) [PubMed: 8125163] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	"Two variants of the CIP1/WAF1 gene occur together and are associated with human cancer." Mousses S., Oezcelik H., Lee P.D., Malkin D., Bull S.B., Andrulis I.L. Hum. Mol. Genet. 4:1089-1092(1995) [PubMed: 7655464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-31.
[8]	NIEHS SNPs program Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-31.
[9]	"The DNA sequence and analysis of human chromosome 6." 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. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-31. Tissue: Eye and Lung.
[11]	"N-acetylation and ubiquitin-independent proteasomal degradation of p21(Cip1)." Chen X., Chi Y., Bloecher A., Aebersold R., Clurman B.E., Roberts J.M. Mol. Cell 16:839-847(2004) [PubMed: 15574338] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16, ACETYLATION AT SER-2, MASS SPECTROMETRY.
[12]	"Reversible phosphorylation at the C-terminal regulatory domain of p21(Waf1/Cip1) modulates proliferating cell nuclear antigen binding." Scott M.T., Morrice N., Ball K.L. J. Biol. Chem. 275:11529-11537(2000) [PubMed: 10753973] [Abstract] Cited for: PROTEIN SEQUENCE OF 136-148, PHOSPHORYLATION AT THR-145; SER-146 AND SER-160, MASS SPECTROMETRY.
[13]	"New functional activities for the p21 family of CDK inhibitors." LaBaer J., Garrett M.D., Stevenson L.F., Slingerland J.M., Sandhu C., Chou H.S., Fattaey A., Harlow E. Genes Dev. 11:847-862(1997) [PubMed: 9106657] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDK4 AND CCND1 IN THE CYCLIN D-CDK4-CDKN1A COMPLEX.
[14]	"A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome." Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J., Allday M.J. EMBO J. 20:2367-2375(2001) [PubMed: 11350925] [Abstract] Cited for: INTERACTION WITH PSMA3.
[15]	"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells." Roessig L., Jadidi A.S., Urbich C., Badorff C., Zeiher A.M., Dimmeler S. Mol. Cell. Biol. 21:5644-5657(2001) [PubMed: 11463845] [Abstract] Cited for: PHOSPHORYLATION AT THR-145, MUTAGENESIS OF THR-145 AND SER-146, SUBCELLULAR LOCATION.
[16]	"Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1 kinase." Wang Z., Bhattacharya N., Mixter P.F., Wei W., Sedivy J., Magnuson N.S. Biochim. Biophys. Acta 1593:45-55(2002) [PubMed: 12431783] [Abstract] Cited for: PHOSPHORYLATION AT THR-145 BY PIM1, SUBCELLULAR LOCATION, INTERACTION WITH PIM1.
[17]	"Only Akt1 is required for proliferation, while Akt2 promotes cell cycle exit through p21 binding." Heron-Milhavet L., Franckhauser C., Rana V., Berthenet C., Fisher D., Hemmings B.A., Fernandez A., Lamb N.J. Mol. Cell. Biol. 26:8267-8280(2006) [PubMed: 16982699] [Abstract] Cited for: PHOSPHORYLATION AT THR-145.
[18]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex." Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A. Genes Dev. 22:2496-2506(2008) [PubMed: 18794347] [Abstract] Cited for: UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, INTERACTION WITH PCNA, MUTAGENESIS OF SER-114 AND 144-GLN--PHE-150, PHOSPHORYLATION AT SER-114.
[20]	"The CRL4Cdt2 ubiquitin ligase targets the degradation of p21Cip1 to control replication licensing." Kim Y., Starostina N.G., Kipreos E.T. Genes Dev. 22:2507-2519(2008) [PubMed: 18794348] [Abstract] Cited for: UBIQUITINATION.
[21]	"CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation." Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T., Tsurimoto T. J. Biol. Chem. 283:29045-29052(2008) [PubMed: 18703516] [Abstract] Cited for: UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, MUTAGENESIS OF 147-MET--TYR-151 AND 154-LYS--ARG-156, INTERACTION WITH PCNA.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"A dual role of Cdk2 in DNA damage response." Satyanarayana A., Kaldis P. Cell Div. 4:9-9(2009) [PubMed: 19445729] [Abstract] Cited for: REVIEW ON DNA REPAIR, INTERACTION WITH CDK2.
[24]	"Differential regulation of p53 and p21 by MKRN1 E3 ligase controls cell cycle arrest and apoptosis." Lee E.-W., Lee M.-S., Camus S., Ghim J., Yang M.-R., Oh W., Ha N.-C., Lane D.P., Song J. EMBO J. 28:2100-2113(2009) [PubMed: 19536131] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH MKRN1.
[25]	"Ionizing radiation induces ATM-independent degradation of p21Cip1 in transformed cells." Stuart S.A., Wang J.Y. J. Biol. Chem. 284:15061-15070(2009) [PubMed: 19332548] [Abstract] Cited for: UBIQUITINATION.
[26]	"Pim-2 phosphorylation of p21(Cip1/WAF1) enhances its stability and inhibits cell proliferation in HCT116 cells." Wang Z., Zhang Y., Gu J.J., Davitt C., Reeves R., Magnuson N.S. Int. J. Biochem. Cell Biol. 42:1030-1038(2010) [PubMed: 20307683] [Abstract] Cited for: PHOSPHORYLATION AT THR-145 BY PIM2.
[27]	"Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA." Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J. Cell 87:297-306(1996) [PubMed: 8861913] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 139-160 IN COMPLEX WITH PCNA.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L25610 mRNA. Translation: AAA16109.1.
S67388 mRNA. Translation: AAB29246.1.
U09579 mRNA. Translation: AAA85641.1.
U03106 mRNA. Translation: AAC04313.1.
L26165 mRNA. Translation: AAA19811.1.
L47232 mRNA. Translation: AAB59559.1. Different initiation.
L47233 mRNA. Translation: AAB59560.1. Different initiation.
AF497972 Genomic DNA. Translation: AAM11787.1.
Z85996 Genomic DNA. Translation: CAB06656.1.
BC000275 mRNA. Translation: AAH00275.1.
BC000312 mRNA. Translation: AAH00312.1.
BC001935 mRNA. Translation: AAH01935.1.
BC013967 mRNA. Translation: AAH13967.1.

IPI

IPI00009384.

PIR

I54380.
I68674.

RefSeq

NP_000380.1. NM_000389.4.
NP_001207706.1. NM_001220777.1.
NP_001207707.1. NM_001220778.1.
NP_510867.1. NM_078467.2.

UniGene

Hs.370771.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AXC	X-ray	2.60	B/D/F	139-160	[»]
2ZVV	X-ray	2.00	X/Y	139-160	[»]
2ZVW	X-ray	2.50	I/J/K/L/M/N/O/P	139-160	[»]

ProteinModelPortal

P38936.

SMR

P38936. Positions 14-79.

DisProt

DP00016.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-246N.
DIP-458N.

IntAct

P38936. 50 interactions.

MINT

MINT-104203.

STRING

P38936.

PTM databases

PhosphoSite

P38936.

Polymorphism databases

DMDM

729143.

2D gel databases

SWISS-2DPAGE

P38936.

Proteomic databases

PRIDE

P38936.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000244741; ENSP00000244741; ENSG00000124762.
ENST00000373711; ENSP00000362815; ENSG00000124762.
ENST00000405375; ENSP00000384849; ENSG00000124762.
ENST00000448526; ENSP00000409259; ENSG00000124762.

GeneID

1026.

KEGG

hsa:1026.

UCSC

uc003omm.2. human.

Organism-specific databases

CTD

1026.

GeneCards

GC06P036649.

H-InvDB

HIX0200868.

HGNC

HGNC:1784. CDKN1A.

HPA

CAB000064.

MIM

116899. gene.

neXtProt

NX_P38936.

PharmGKB

PA104.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05825.

HOVERGEN

HBG050868.

InParanoid

P38936.

OrthoDB

EOG437RG1.

PhylomeDB

P38936.

Enzyme and pathway databases

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.
prlsignalingeventspathway. Signaling events mediated by PRL.

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P38936.

Bgee

P38936.

CleanEx

HS_CDKN1A.

Genevestigator

P38936.

GermOnline

ENSG00000124762. Homo sapiens.

Family and domain databases

InterPro

IPR003175. CDI.
[Graphical view]

KO

K06625.

PANTHER

PTHR10265. CDI. 1 hit.

Pfam

PF02234. CDI. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

4309.

SOURCE

Search...

Entry information

Entry name

CDN1A_HUMAN

Accession

Primary (citable) accession number: P38936
Secondary accession number(s): Q14010, Q9BUT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

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