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Protein

Cyclin-dependent kinase inhibitor 1B

Gene

CDKN1B

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

Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA (PubMed:28666995). Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry.6 Publications

Miscellaneous

Decreased levels of p27Kip1, mainly due to proteasomal degradation, are found in various epithelial tumors originating from lung, breast, colon, ovary, esophagus, thyroid and prostate.

<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

  • chaperone binding Source: GO_Central
  • cyclin binding Source: CAFA
  • cyclin-dependent protein serine/threonine kinase activity Source: Reactome
  • cyclin-dependent protein serine/threonine kinase inhibitor activity Source: UniProtKB
  • Hsp70 protein binding Source: Ensembl
  • protein-containing complex binding Source: CAFA
  • protein kinase binding Source: CAFA
  • protein kinase inhibitor activity Source: CAFA
  • protein phosphatase binding Source: BHF-UCL
  • transforming growth factor beta receptor, cytoplasmic mediator activity Source: ProtInc

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

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-5625900 RHO GTPases activate CIT
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
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-8849470 PTK6 Regulates Cell Cycle

SIGNOR Signaling Network Open Resource

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SIGNORi
P46527

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P46527 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 1B
Alternative name(s):
Cyclin-dependent kinase inhibitor p271 Publication
p27Kip11 Publication
<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:CDKN1B
Synonyms:KIP1
<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 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000111276.10

Human Gene Nomenclature Database

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HGNCi
HGNC:1785 CDKN1B

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600778 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P46527

<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, Endosome, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Multiple endocrine neoplasia 4 (MEN4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionMultiple endocrine neoplasia (MEN) syndromes are inherited cancer syndromes of the thyroid. MEN4 is a MEN-like syndrome with a phenotypic overlap of both MEN1 and MEN2.
See also OMIM:610755

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>Mutagenesisi10S → A: Loss of phosphorylation by UHMK1. No translocation to the cytoplasm. Greater cell cycle arrest. 3 Publications1
Mutagenesisi10S → D: Exported to the cytoplasm. Inhibits cell cycle arrest. 3 Publications1
Mutagenesisi10S → E: Increased stability in vivo and in vitro. 3 Publications1
Mutagenesisi74Y → F: No change in binding CDK4 and no inhibition of CDK4 activity. Translocates to nucleus. No effect on in vitro phosphorylation of CDK4 by CCNH-CDK7. 2 Publications1
Mutagenesisi88Y → F: Abolishes LYN-mediated phosphorylation, reduces CDK2-mediated phosphorylation on T-187, has greater cell cycle arrest into S-phase, no effect on binding CDK2 complexes, reduced CDK4 binding and inhibits CDK4 enzyme activity. No nuclear translocation. No effect on in vitro phosphorylation of CDK4 by CCNH-CDK7. Completely abolishes CDK4 binding; when associated with F-89. 3 Publications1
Mutagenesisi89Y → F: No effect on binding CDK2 complexes, reduced CDK4 binding and greatly inhibits CDK4 enzyme activity. No nuclear translocation. Inhibits in vitro phosphorylation of CDK4 by CCNH-CDK7. Completely abolishes CDK4 binding; when associated with F-88. 3 Publications1
Mutagenesisi157T → A: Greatly reduced PKB/AKT1-mediated phosphorylation. Nuclear location. Inhibits cyclin E/CDK2 cell cycle progression. No effect on binding AKT1. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation; when associated with A-198. 5 Publications1
Mutagenesisi161S → A: No change in PKB/AKT1-mediated phosphorylation. 1 Publication1
Mutagenesisi162T → A: No change in PKB/AKT1-mediated phosphorylation. 1 Publication1
Mutagenesisi185E → A, D or Q: Strongly reduced ubiquitination by a TRIM21-containing SCF(SKP2) complex. 1 Publication1
Mutagenesisi187T → A or D: No change in PKB/AKT1- nor UHMK1-mediated phosphorylation. 5 Publications1
Mutagenesisi187T → A: Abolishes phosphorylation-dependent ubiquitination. 5 Publications1
Mutagenesisi198T → A or D: Abolishes PKB/AKT1-mediated phosphorylation. 46% cytoplasmic location. Greatly reduced binding to YWHAQ. Equally reduced binding; when associated with A-10 and A-187. No nuclear import; when associated with A-157. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation; when associated with A-157. 3 Publications1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNET

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DisGeNETi
1027

MalaCards human disease database

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MalaCardsi
CDKN1B
MIMi610755 phenotype

Open Targets

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OpenTargetsi
ENSG00000111276

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

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Orphaneti
652 Multiple endocrine neoplasia type 1
276152 Multiple endocrine neoplasia type 4

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA105

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CDKN1B

<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 ‘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_00001900841 – 198Cyclin-dependent kinase inhibitor 1BAdd BLAST198

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 residuei10Phosphoserine; by UHMK1Combined sources4 Publications1
Modified residuei74Phosphotyrosine; by SRC1 Publication1
Modified residuei88Phosphotyrosine; by ABL, LYN, SRC and JAK24 Publications1
Modified residuei89Phosphotyrosine1 Publication1
Modified residuei157Phosphothreonine; by CaMK1, PKB/AKT1 and PIM14 Publications1
Modified residuei170PhosphothreonineBy similarity1
Modified residuei187Phosphothreonine; by PKB/AKT1, CDK1 and CDK24 Publications1
Modified residuei198Phosphothreonine; by CaMK1, PKB/AKT1, RPS6KA1, RPS6KA3 and PIM15 Publications1

<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

Phosphorylated; phosphorylation occurs on serine, threonine and tyrosine residues. Phosphorylation on Ser-10 is the major site of phosphorylation in resting cells, takes place at the G0-G1 phase and leads to protein stability. Phosphorylation on other sites is greatly enhanced by mitogens, growth factors, cMYC and in certain cancer cell lines. The phosphorylated form found in the cytoplasm is inactivate. Phosphorylation on Thr-198 is required for interaction with 14-3-3 proteins. Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation. Tyrosine phosphorylation promotes this process. Phosphorylation by PKB/AKT1 can be suppressed by LY294002, an inhibitor of the catalytic subunit of PI3K. Phosphorylation on Tyr-88 and Tyr-89 has no effect on binding CDK2, but is required for binding CDK4. Dephosphorylated on tyrosine residues by G-CSF.14 Publications
Ubiquitinated; in the cytoplasm by the KPC complex (composed of RNF123/KPC1 and UBAC1/KPC2) and, in the nucleus, by SCF(SKP2). The latter requires prior phosphorylation on Thr-187. Ubiquitinated; by a TRIM21-containing SCF(SKP2)-like complex; leads to its degradation.4 Publications
Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P46527

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P46527

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

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PaxDbi
P46527

PeptideAtlas

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PeptideAtlasi
P46527

PRoteomics IDEntifications database

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PRIDEi
P46527

ProteomicsDB human proteome resource

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ProteomicsDBi
55741

Consortium for Top Down Proteomics

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TopDownProteomicsi
P46527

2D gel databases

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

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SWISS-2DPAGEi
P46527

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P46527

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

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PhosphoSitePlusi
P46527

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P46527

<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 tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney.

<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

Maximal levels in quiescence cells and early G1. Levels decrease after mitogen stimulation as cells progress toward S-phase.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000111276 Expressed in 243 organ(s), highest expression level in pigmented layer of retina

CleanEx database of gene expression profiles

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CleanExi
HS_CDKN1B

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P46527 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P46527 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB003691
CAB021888
HPA059086

<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

Forms a ternary complex composed of CCNE1, CDK2 and CDKN1B. Interacts directly with CCNE1; the interaction is inhibited by CDK2-dependent phosphorylation on Thr-187. Interacts with COPS5, subunit of the COP9 signalosome complex; the interaction leads to CDKN1B degradation. Interacts with NUP50; the interaction leads to nuclear import and degradation of phosphorylated CDKN1B. Interacts with CCND1 and SNX6 (By similarity). Interacts (Thr-198-phosphorylated form) with 14-3-3 proteins, binds strongly YWHAQ, weakly YWHAE and YWHAH, but not YWHAB nor YWHAZ; the interaction with YWHAQ results in translocation to the cytoplasm (PubMed:14504289). Interacts with AKT1 and LYN; the interactions lead to cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of cell cycle arrest (PubMed:12042314, PubMed:12244301, PubMed:17254966). Forms a ternary complex with CCNA2 and CDK2; CDKN1B inhibits the kinase activity of CDK2 through conformational rearrangements. Interacts (unphosphorylated form) with CDK2. Forms a complex with CDK2 and SPDYA, but does not directly interact with SPDYA (PubMed:12972555, PubMed:28666995). Forms a ternary complex composed of cyclin D, CDK4 and CDKN1B. Interacts (phosphorylated on Tyr-88 and Tyr-89) with CDK4; the interaction is required for cyclin D and CDK4 complex assembly, induces nuclear translocation and activates the CDK4 kinase activity. Interacts with GRB2 (PubMed:16195327). Interacts with PIM1 (PubMed:18593906). Identified in a complex with SKP1, SKP2 and CKS1B (PubMed:16209941). Interacts with UHMK1; the interaction leads to cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of cell cycle arrest (PubMed:12093740). Interacts also with CDK1 (PubMed:16007079). Dephosphorylated on Thr-187 by PPM1H, leading to CDKN1B stability (PubMed:22586611).By similarity15 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
107461, 92 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P46527

Database of interacting proteins

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DIPi
DIP-33341N

Protein interaction database and analysis system

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IntActi
P46527, 68 interactors

Molecular INTeraction database

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MINTi
P46527

STRING: functional protein association networks

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STRINGi
9606.ENSP00000228872

<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

1198
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
1H27X-ray2.20E25-35[»]
1JSUX-ray2.30C23-106[»]
2ASTX-ray2.30D181-190[»]
5UQ3X-ray3.60C1-198[»]
6ATHX-ray1.82C22-85[»]

Database of protein disorder

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DisProti
DP00018

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P46527

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

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SMRi
P46527

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

More...
EvolutionaryTracei
P46527

<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>Regioni51 – 91Interaction with CDK21 PublicationAdd BLAST41

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>Motifi153 – 169Nuclear localization signalSequence analysisAdd BLAST17

<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

A peptide sequence containing only AA 28-79 retains substantial Kip1 cyclin A/CDK2 inhibitory activity.

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4743 Eukaryota
ENOG410XXN5 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159852

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000294081

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG073988

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P46527

KEGG Orthology (KO)

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KOi
K06624

Identification of Orthologs from Complete Genome Data

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OMAi
YPKPSAC

Database of Orthologous Groups

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OrthoDBi
962484at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P46527

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
IPR029843 CDKN1B

The PANTHER Classification System

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PANTHERi
PTHR10265 PTHR10265, 1 hit
PTHR10265:SF9 PTHR10265:SF9, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P46527-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVDHEE LTRDLEKHCR
60 70 80 90 100
DMEEASQRKW NFDFQNHKPL EGKYEWQEVE KGSLPEFYYR PPRPPKGACK
110 120 130 140 150
VPAQESQDVS GSRPAAPLIG APANSEDTHL VDPKTDPSDS QTGLAEQCAG
160 170 180 190
IRKRPATDDS STQNKRANRT EENVSDGSPN AGSVEQTPKK PGLRRRQT
Length:198
Mass (Da):22,073
Last modified:November 1, 1995 - v1
<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:i1118D58901CDF3FC
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7ES52E7ES52_HUMAN
Cyclin-dependent kinase inhibitor 1...
CDKN1B
205Annotation score:

Annotation score:1 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>
H7C2T1H7C2T1_HUMAN
Cyclin-dependent kinase inhibitor 1...
CDKN1B
104Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti22E → D in AAD14244 (PubMed:7882309).Curated1

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_01187115R → W1 PublicationCorresponds to variant dbSNP:rs2066828EnsemblClinVar.1
Natural variantiVAR_06442969P → L Found in a patient with multiple endocrine tumors; germline mutation; reduced expression levels; shows impaired binding to CDK2. 1 PublicationCorresponds to variant dbSNP:rs777354267EnsemblClinVar.1
Natural variantiVAR_011872109V → G3 PublicationsCorresponds to variant dbSNP:rs2066827EnsemblClinVar.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
U10906 mRNA Translation: AAA20240.1
S76988, S76986 Genomic DNA Translation: AAD14244.1
BT019553 mRNA Translation: AAV38360.1
BT019554 mRNA Translation: AAV38361.1
AF480891 Genomic DNA Translation: AAL78041.1
BC001971 mRNA Translation: AAH01971.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS8653.1

NCBI Reference Sequences

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RefSeqi
NP_004055.1, NM_004064.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.238990

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000228872; ENSP00000228872; ENSG00000111276

Database of genes from NCBI RefSeq genomes

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GeneIDi
1027

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1027

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
U10906 mRNA Translation: AAA20240.1
S76988, S76986 Genomic DNA Translation: AAD14244.1
BT019553 mRNA Translation: AAV38360.1
BT019554 mRNA Translation: AAV38361.1
AF480891 Genomic DNA Translation: AAL78041.1
BC001971 mRNA Translation: AAH01971.1
CCDSiCCDS8653.1
RefSeqiNP_004055.1, NM_004064.4
UniGeneiHs.238990

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H27X-ray2.20E25-35[»]
1JSUX-ray2.30C23-106[»]
2ASTX-ray2.30D181-190[»]
5UQ3X-ray3.60C1-198[»]
6ATHX-ray1.82C22-85[»]
DisProtiDP00018
ProteinModelPortaliP46527
SMRiP46527
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107461, 92 interactors
CORUMiP46527
DIPiDIP-33341N
IntActiP46527, 68 interactors
MINTiP46527
STRINGi9606.ENSP00000228872

Protein family/group databases

MoonDBiP46527 Predicted

PTM databases

iPTMnetiP46527
PhosphoSitePlusiP46527

Polymorphism and mutation databases

BioMutaiCDKN1B

2D gel databases

SWISS-2DPAGEiP46527

Proteomic databases

EPDiP46527
jPOSTiP46527
PaxDbiP46527
PeptideAtlasiP46527
PRIDEiP46527
ProteomicsDBi55741
TopDownProteomicsiP46527

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1027
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228872; ENSP00000228872; ENSG00000111276
GeneIDi1027
KEGGihsa:1027

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1027
DisGeNETi1027
EuPathDBiHostDB:ENSG00000111276.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CDKN1B
HGNCiHGNC:1785 CDKN1B
HPAiCAB003691
CAB021888
HPA059086
MalaCardsiCDKN1B
MIMi600778 gene
610755 phenotype
neXtProtiNX_P46527
OpenTargetsiENSG00000111276
Orphaneti652 Multiple endocrine neoplasia type 1
276152 Multiple endocrine neoplasia type 4
PharmGKBiPA105

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4743 Eukaryota
ENOG410XXN5 LUCA
GeneTreeiENSGT00940000159852
HOGENOMiHOG000294081
HOVERGENiHBG073988
InParanoidiP46527
KOiK06624
OMAiYPKPSAC
OrthoDBi962484at2759
PhylomeDBiP46527
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-5625900 RHO GTPases activate CIT
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
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-8849470 PTK6 Regulates Cell Cycle
SIGNORiP46527

Miscellaneous databases

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

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ChiTaRSi
CDKN1B human
EvolutionaryTraceiP46527

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
CDKN1B

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

More...
GenomeRNAii
1027
PMAP-CutDBiP46527

Protein Ontology

More...
PROi
PR:P46527

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000111276 Expressed in 243 organ(s), highest expression level in pigmented layer of retina
CleanExiHS_CDKN1B
ExpressionAtlasiP46527 baseline and differential
GenevisibleiP46527 HS

Family and domain databases

InterProiView protein in InterPro
IPR003175 CDI
IPR029843 CDKN1B
PANTHERiPTHR10265 PTHR10265, 1 hit
PTHR10265:SF9 PTHR10265:SF9, 1 hit
PfamiView protein in Pfam
PF02234 CDI, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiCDN1B_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: P46527
Secondary accession number(s): Q16307, Q5U0H2, Q9BUS6
<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: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 16, 2019
This is version 206 of the entry and version 1 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
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