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Protein

Cyclin-dependent kinase inhibitor 1

Gene

CDKN1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).3 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri13 – 41C4-typeSequence analysisAdd BLAST29

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • cyclin binding Source: BHF-UCL
  • cyclin-dependent protein kinase activating kinase activity Source: UniProtKB
  • cyclin-dependent protein serine/threonine kinase activity Source: Reactome
  • cyclin-dependent protein serine/threonine kinase inhibitor activity Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein-containing complex binding Source: CAFA
  • protein kinase binding Source: CAFA
  • protein kinase inhibitor activity Source: CAFA
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionProtein kinase inhibitor
Biological processCell cycle
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-198323 AKT phosphorylates targets in the cytosol
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6804116 TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69231 Cyclin D associated events in G1
R-HSA-69563 p53-Dependent G1 DNA Damage Response
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-69895 Transcriptional activation of cell cycle inhibitor p21
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8866911 TFAP2 (AP-2) family regulates transcription of cell cycle factors
R-HSA-8878166 Transcriptional regulation by RUNX2
R-HSA-8941855 RUNX3 regulates CDKN1A transcription

SIGNOR Signaling Network Open Resource

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SIGNORi
P38936

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P38936 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cyclin-dependent kinase inhibitor 1
Alternative name(s):
CDK-interacting protein 1
Melanoma differentiation-associated protein 6
Short name:
MDA-6
p21
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CDKN1A
Synonyms:CAP20, CDKN1, CIP1, MDA6, PIC1, SDI1, WAF1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000124762.13

Human Gene Nomenclature Database

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HGNCi
HGNC:1784 CDKN1A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
116899 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P38936

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi80T → A: Abolishes UV radiation-induced phosphorylation and subsequent degradation. 1 Publication1
Mutagenesisi114S → E: Phosphomimetic mutant, increases ubiquitination by the DCX(DTL) complex. 1 Publication1
Mutagenesisi144 – 150QTSMTDF → ATSATDA: Abolishes interaction with PCNA and subsequent degradation by the proteasome. 1 Publication7
Mutagenesisi145T → A: Reduces phosphorylation by Akt; no change in interaction with PCNA, CDK2 or CDK4; no change in subcellular location. 1 Publication1
Mutagenesisi145T → D: No interaction with PCNA; 59% inhibition of CDK2 binding; modest inhibition of CDK4 binding; no change in subcellular location. 1 Publication1
Mutagenesisi146S → A: No change in interaction with PCNA. Abolishes UV radiation-induced phosphorylation and subsequent degradation. 2 Publications1
Mutagenesisi146S → D: Reduces interaction with PCNA. 1 Publication1
Mutagenesisi147 – 151MTDFY → ATDAAA: Abolishes interaction with PCNA and subsequent degradation by the proteasome. 1 Publication5
Mutagenesisi154 – 156KRR → AAA: Abolishes degradation by the proteasome without affecting the interaction with PCNA. 1 Publication3

Organism-specific databases

DisGeNET

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DisGeNETi
1026

MalaCards human disease database

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MalaCardsi
CDKN1A

Open Targets

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OpenTargetsi
ENSG00000124762

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
652 Multiple endocrine neoplasia type 1

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA104

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5021

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CDKN1A

Domain mapping of disease mutations (DMDM)

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DMDMi
729143

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001900792 – 164Cyclin-dependent kinase inhibitor 1Add BLAST163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki2Glycyl serine ester (Ser-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei80Phosphothreonine; by LKB11 Publication1
Modified residuei114Phosphoserine; by GSK3-beta1 Publication1
Modified residuei130PhosphoserineCombined sources1
Modified residuei145Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM25 Publications1
Modified residuei146Phosphoserine; by PKC and NUAK12 Publications1
Modified residuei160Phosphoserine; by PKC; in vitro1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.7 Publications
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.1 Publication
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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P38936

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P38936

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P38936

PeptideAtlas

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PeptideAtlasi
P38936

PRoteomics IDEntifications database

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PRIDEi
P38936

ProteomicsDB human proteome resource

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ProteomicsDBi
55307

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P38936

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P38936

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P38936

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in all adult tissues, with 5-fold lower levels observed in the brain.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Activated by p53/TP53, mezerein (antileukemic compound) and IFNB1. Repressed by HDAC1.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000124762 Expressed in 229 organ(s), highest expression level in left coronary artery

CleanEx database of gene expression profiles

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CleanExi
HS_CDKN1A

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P38936 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P38936 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000064
CAB069401
HPA005946

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).By similarity10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107460, 281 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P38936

Database of interacting proteins

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DIPi
DIP-246N

Protein interaction database and analysis system

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IntActi
P38936, 183 interactors

Molecular INTeraction database

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MINTi
P38936

STRING: functional protein association networks

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STRINGi
9606.ENSP00000244741

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P38936

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1164
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AXCX-ray2.60B/D/F139-160[»]
2ZVVX-ray2.00X/Y139-160[»]
2ZVWX-ray2.50I/J/K/L/M/N/O/P139-160[»]
4RJFX-ray2.01B/D/F139-160[»]
5E0UX-ray1.93D/E/F139-160[»]
6CBIX-ray2.75H/I/J/K139-152[»]
6CEJNMR-A139-152[»]
6CIVNMR-C139-152[»]
6CIXNMR-B139-152[»]

Database of protein disorder

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DisProti
DP00016

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P38936

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P38936

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P38936

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni17 – 24Required for binding cyclins8
Regioni53 – 58Required for binding CDKs6

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi140 – 164PIP-box K+4 motifAdd BLAST25
Motifi141 – 156Nuclear localization signalSequence analysisAdd BLAST16

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.
The C-terminal is required for nuclear localization of the cyclin D-CDK4 complex.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the CDI family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri13 – 41C4-typeSequence analysisAdd BLAST29

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4743 Eukaryota
ENOG410XXN5 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159918

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000285999

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050868

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P38936

KEGG Orthology (KO)

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KOi
K06625

Identification of Orthologs from Complete Genome Data

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OMAi
LEGNFAW

Database of Orthologous Groups

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OrthoDBi
1595421at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P38936

TreeFam database of animal gene trees

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TreeFami
TF101038

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003175 CDI
IPR029841 CDKN1A_vertebrate

The PANTHER Classification System

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PANTHERi
PTHR10265 PTHR10265, 1 hit
PTHR10265:SF16 PTHR10265:SF16, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02234 CDI, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P38936-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEPAGDVRQ NPCGSKACRR LFGPVDSEQL SRDCDALMAG CIQEARERWN
60 70 80 90 100
FDFVTETPLE GDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA
110 120 130 140 150
LLQGTAEEDH VDLSLSCTLV PRSGEQAEGS PGGPGDSQGR KRRQTSMTDF
160
YHSKRRLIFS KRKP
Length:164
Mass (Da):18,119
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i98D1E7C519ADFCA9
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB59559 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB59560 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0486864P → L. Corresponds to variant dbSNP:rs4986866Ensembl.1
Natural variantiVAR_01187031S → R3 PublicationsCorresponds to variant dbSNP:rs1801270EnsemblClinVar.1
Natural variantiVAR_04868763F → L. Corresponds to variant dbSNP:rs4986867Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
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
BT006719 mRNA Translation: AAP35365.1
AB451290 mRNA Translation: BAG70104.1
AB451422 mRNA Translation: BAG70236.1
CR536533 mRNA Translation: CAG38770.1
Z85996 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03904.1
BC000275 mRNA Translation: AAH00275.1
BC000312 mRNA Translation: AAH00312.1
BC001935 mRNA Translation: AAH01935.1
BC013967 mRNA Translation: AAH13967.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS4824.1

Protein sequence database of the Protein Information Resource

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PIRi
I54380
I68674

NCBI Reference Sequences

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RefSeqi
NP_000380.1, NM_000389.4
NP_001207706.1, NM_001220777.1
NP_001207707.1, NM_001220778.1
NP_001278478.1, NM_001291549.1
NP_510867.1, NM_078467.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.370771
Hs.732576

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000244741; ENSP00000244741; ENSG00000124762
ENST00000373711; ENSP00000362815; ENSG00000124762
ENST00000405375; ENSP00000384849; ENSG00000124762
ENST00000448526; ENSP00000409259; ENSG00000124762
ENST00000615513; ENSP00000482768; ENSG00000124762

Database of genes from NCBI RefSeq genomes

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GeneIDi
1026

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1026

UCSC genome browser

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UCSCi
uc003omm.5 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
BT006719 mRNA Translation: AAP35365.1
AB451290 mRNA Translation: BAG70104.1
AB451422 mRNA Translation: BAG70236.1
CR536533 mRNA Translation: CAG38770.1
Z85996 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03904.1
BC000275 mRNA Translation: AAH00275.1
BC000312 mRNA Translation: AAH00312.1
BC001935 mRNA Translation: AAH01935.1
BC013967 mRNA Translation: AAH13967.1
CCDSiCCDS4824.1
PIRiI54380
I68674
RefSeqiNP_000380.1, NM_000389.4
NP_001207706.1, NM_001220777.1
NP_001207707.1, NM_001220778.1
NP_001278478.1, NM_001291549.1
NP_510867.1, NM_078467.2
UniGeneiHs.370771
Hs.732576

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AXCX-ray2.60B/D/F139-160[»]
2ZVVX-ray2.00X/Y139-160[»]
2ZVWX-ray2.50I/J/K/L/M/N/O/P139-160[»]
4RJFX-ray2.01B/D/F139-160[»]
5E0UX-ray1.93D/E/F139-160[»]
6CBIX-ray2.75H/I/J/K139-152[»]
6CEJNMR-A139-152[»]
6CIVNMR-C139-152[»]
6CIXNMR-B139-152[»]
DisProtiDP00016
ProteinModelPortaliP38936
SMRiP38936
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107460, 281 interactors
CORUMiP38936
DIPiDIP-246N
IntActiP38936, 183 interactors
MINTiP38936
STRINGi9606.ENSP00000244741

Chemistry databases

BindingDBiP38936
ChEMBLiCHEMBL5021

Protein family/group databases

MoonDBiP38936 Predicted

PTM databases

iPTMnetiP38936
PhosphoSitePlusiP38936

Polymorphism and mutation databases

BioMutaiCDKN1A
DMDMi729143

2D gel databases

SWISS-2DPAGEiP38936

Proteomic databases

EPDiP38936
jPOSTiP38936
PaxDbiP38936
PeptideAtlasiP38936
PRIDEiP38936
ProteomicsDBi55307

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1026
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244741; ENSP00000244741; ENSG00000124762
ENST00000373711; ENSP00000362815; ENSG00000124762
ENST00000405375; ENSP00000384849; ENSG00000124762
ENST00000448526; ENSP00000409259; ENSG00000124762
ENST00000615513; ENSP00000482768; ENSG00000124762
GeneIDi1026
KEGGihsa:1026
UCSCiuc003omm.5 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1026
DisGeNETi1026
EuPathDBiHostDB:ENSG00000124762.13

GeneCards: human genes, protein and diseases

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GeneCardsi
CDKN1A
HGNCiHGNC:1784 CDKN1A
HPAiCAB000064
CAB069401
HPA005946
MalaCardsiCDKN1A
MIMi116899 gene
neXtProtiNX_P38936
OpenTargetsiENSG00000124762
Orphaneti652 Multiple endocrine neoplasia type 1
PharmGKBiPA104

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4743 Eukaryota
ENOG410XXN5 LUCA
GeneTreeiENSGT00940000159918
HOGENOMiHOG000285999
HOVERGENiHBG050868
InParanoidiP38936
KOiK06625
OMAiLEGNFAW
OrthoDBi1595421at2759
PhylomeDBiP38936
TreeFamiTF101038

Enzyme and pathway databases

ReactomeiR-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-198323 AKT phosphorylates targets in the cytosol
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6804116 TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69231 Cyclin D associated events in G1
R-HSA-69563 p53-Dependent G1 DNA Damage Response
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-69895 Transcriptional activation of cell cycle inhibitor p21
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8866911 TFAP2 (AP-2) family regulates transcription of cell cycle factors
R-HSA-8878166 Transcriptional regulation by RUNX2
R-HSA-8941855 RUNX3 regulates CDKN1A transcription
SIGNORiP38936

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CDKN1A human
EvolutionaryTraceiP38936

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
P21

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
1026

Protein Ontology

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PROi
PR:P38936

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000124762 Expressed in 229 organ(s), highest expression level in left coronary artery
CleanExiHS_CDKN1A
ExpressionAtlasiP38936 baseline and differential
GenevisibleiP38936 HS

Family and domain databases

InterProiView protein in InterPro
IPR003175 CDI
IPR029841 CDKN1A_vertebrate
PANTHERiPTHR10265 PTHR10265, 1 hit
PTHR10265:SF16 PTHR10265:SF16, 1 hit
PfamiView protein in Pfam
PF02234 CDI, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDN1A_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P38936
Secondary accession number(s): Q14010, Q6FI05, Q9BUT4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 214 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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