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Protein

Cyclin-dependent kinase inhibitor 1B

Gene

Cdkn1b

Organism
Mus musculus (Mouse)
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 (PubMed:8033213, PubMed:12972555). Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA (By similarity). Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes (PubMed:8033213). 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.By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei90Required for interaction with NUP501

<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

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

More...
Reactomei
R-MMU-176408 Regulation of APC/C activators between G1/S and early anaphase
R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21
R-MMU-198323 AKT phosphorylates targets in the cytosol
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence
R-MMU-6804116 TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest
R-MMU-69202 Cyclin E associated events during G1/S transition
R-MMU-69231 Cyclin D associated events in G1
R-MMU-69563 p53-Dependent G1 DNA Damage Response
R-MMU-69656 Cyclin A:Cdk2-associated events at S phase entry
R-MMU-8849470 PTK6 Regulates Cell Cycle

<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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:104565 Cdkn1b

<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

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 in G(0) phase. No change in cMYC-induced CDK2-mediated phosphorylation. Rapid dissociation from the cyclin E/CDK2 complex after induction by cMYC. Loss of protein stability in G(0) phase. No change in protein stability at S-phase. 2 Publications1
Mutagenesisi90R → G: Loss of interaction with NUP50. No cyclin E-mediated degradation of phosphorylated p27KIP1. 1 Publication1
Mutagenesisi187T → E: Loss of cMyc-induced CDK2-mediated phosphorylation. Rapid dissociation from the cyclin E/CDK2 complex after induction by c-Myc. 1 Publication1
Mutagenesisi187T → V: Loss of cMYC-induced CDK2-mediated phosphorylation Dissociates very slowly from the cyclin E/CDK2 complex after induction by cMYC. Cell cycle arrest. 1 Publication1

<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_00001900851 – 197Cyclin-dependent kinase inhibitor 1BAdd BLAST197

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 sources2 Publications1
Modified residuei74Phosphotyrosine; by SRCBy similarity1
Modified residuei88Phosphotyrosine; by ABL, LYN, SRC and JAK2By similarity1
Modified residuei89PhosphotyrosineBy similarity1
Modified residuei170Phosphothreonine; by CaMK11 Publication1
Modified residuei187Phosphothreonine; by PKB/AKT1, CDK1 and CDK21 Publication1
Modified residuei197Phosphothreonine; by CaMK1, PKB/AKT1, RPS6KA1, RPS6KA3 and PIM1By similarity1

<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, MYC and in certain cancer cell lines. The phosphorylated form found in the cytoplasm is inactivate. Phosphorylation on Thr-197 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 (By similarity). Dephosphorylated on Thr-187 by PPM1H, leading to CDKN1B stability (By similarity).By similarity
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 (By similarity).By similarity
Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P46414

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

More...
PaxDbi
P46414

PeptideAtlas

More...
PeptideAtlasi
P46414

PRoteomics IDEntifications database

More...
PRIDEi
P46414

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P46414

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

More...
PhosphoSitePlusi
P46414

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000003031 Expressed in 292 organ(s), highest expression level in cerebellar vermis

CleanEx database of gene expression profiles

More...
CleanExi
MM_CDKN1B

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P46414 MM

<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-197-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. Interacts with AKT1 and LYN; the interactions lead to cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of cell cycle arrest. 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. 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. Interacts with PIM1. Identified in a complex with SKP1, SKP2 and CKS1B. Interacts with UHMK1; the interaction leads to cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of cell cycle arrest. Interacts also with CDK1. Dephosphorylated on Thr-187 by PPM1H, leading to CDKN1B stability (By similarity).By similarity8 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)

More...
BioGridi
198652, 23 interactors

Database of interacting proteins

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DIPi
DIP-445N

Protein interaction database and analysis system

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IntActi
P46414, 9 interactors

Molecular INTeraction database

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MINTi
P46414

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000003115

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P46414

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

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SMRi
P46414

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 CDK2By similarityAdd 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.By similarity

<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

More...
GeneTreei
ENSGT00940000159852

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000294081

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG073988

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P46414

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
EOG091G19PZ

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>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.

P46414-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVNHEE LTRDLEKHCR
60 70 80 90 100
DMEEASQRKW NFDFQNHKPL EGRYEWQEVE RGSLPEFYYR PPRPPKSACK
110 120 130 140 150
VLAQESQDVS GSRQAVPLIG SQANSEDRHL VDQMPDSSDN PAGLAEQCPG
160 170 180 190
MRKRPAAEDS SSQNKRANRT EENVSDGSPN AGTVEQTPKK PGLRRQT
Length:197
Mass (Da):22,193
Last modified:October 3, 2012 - v2
<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:iBAC30D648B9BA3D6
GO

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 AAA21149 (PubMed:8033213).Curated1
Sequence conflicti22E → D in AAA20235 (PubMed:8033212).Curated1
Sequence conflicti22E → D in AAH14296 (PubMed:15489334).Curated1
Sequence conflicti141P → Q in AAA21149 (PubMed:8033213).Curated1
Sequence conflicti141P → Q in AAA20235 (PubMed:8033212).Curated1
Sequence conflicti141P → Q in AAH14296 (PubMed:15489334).Curated1

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

More...
DDBJi
Links Updated
U10440 mRNA Translation: AAA21149.1
U09968 mRNA Translation: AAA20235.1
AK046676 mRNA Translation: BAC32833.1
AK047669 mRNA Translation: BAC33119.1
AK050240 mRNA Translation: BAC34141.1
AC122193 Genomic DNA No translation available.
BC014296 mRNA Translation: AAH14296.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS20642.1

Protein sequence database of the Protein Information Resource

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PIRi
I49064

NCBI Reference Sequences

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RefSeqi
NP_034005.2, NM_009875.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.2958

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000003115; ENSMUSP00000003115; ENSMUSG00000003031
ENSMUST00000067327; ENSMUSP00000065832; ENSMUSG00000003031
ENSMUST00000204807; ENSMUSP00000145056; ENSMUSG00000003031

Database of genes from NCBI RefSeq genomes

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GeneIDi
12576

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:12576

UCSC genome browser

More...
UCSCi
uc009ela.2 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10440 mRNA Translation: AAA21149.1
U09968 mRNA Translation: AAA20235.1
AK046676 mRNA Translation: BAC32833.1
AK047669 mRNA Translation: BAC33119.1
AK050240 mRNA Translation: BAC34141.1
AC122193 Genomic DNA No translation available.
BC014296 mRNA Translation: AAH14296.1
CCDSiCCDS20642.1
PIRiI49064
RefSeqiNP_034005.2, NM_009875.4
UniGeneiMm.2958

3D structure databases

ProteinModelPortaliP46414
SMRiP46414
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198652, 23 interactors
DIPiDIP-445N
IntActiP46414, 9 interactors
MINTiP46414
STRINGi10090.ENSMUSP00000003115

PTM databases

iPTMnetiP46414
PhosphoSitePlusiP46414

Proteomic databases

EPDiP46414
PaxDbiP46414
PeptideAtlasiP46414
PRIDEiP46414

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003115; ENSMUSP00000003115; ENSMUSG00000003031
ENSMUST00000067327; ENSMUSP00000065832; ENSMUSG00000003031
ENSMUST00000204807; ENSMUSP00000145056; ENSMUSG00000003031
GeneIDi12576
KEGGimmu:12576
UCSCiuc009ela.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1027
MGIiMGI:104565 Cdkn1b

Phylogenomic databases

eggNOGiKOG4743 Eukaryota
ENOG410XXN5 LUCA
GeneTreeiENSGT00940000159852
HOGENOMiHOG000294081
HOVERGENiHBG073988
InParanoidiP46414
KOiK06624
OMAiYPKPSAC
OrthoDBiEOG091G19PZ
TreeFamiTF101038

Enzyme and pathway databases

ReactomeiR-MMU-176408 Regulation of APC/C activators between G1/S and early anaphase
R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21
R-MMU-198323 AKT phosphorylates targets in the cytosol
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence
R-MMU-6804116 TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest
R-MMU-69202 Cyclin E associated events during G1/S transition
R-MMU-69231 Cyclin D associated events in G1
R-MMU-69563 p53-Dependent G1 DNA Damage Response
R-MMU-69656 Cyclin A:Cdk2-associated events at S phase entry
R-MMU-8849470 PTK6 Regulates Cell Cycle

Miscellaneous databases

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

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ChiTaRSi
Cdkn1b mouse

Protein Ontology

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PROi
PR:P46414

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000003031 Expressed in 292 organ(s), highest expression level in cerebellar vermis
CleanExiMM_CDKN1B
GenevisibleiP46414 MM

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

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ProtoNeti
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<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_MOUSE
<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: P46414
Secondary accession number(s): Q8BG74
<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: October 3, 2012
Last modified: December 5, 2018
This is version 157 of the entry and version 2 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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