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Entry version 218 (02 Jun 2021)
Sequence version 2 (27 Jul 2011)
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Protein

Retinoblastoma-associated protein

Gene

Rb1

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

Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed:8336704).

The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes. Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription. Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase. RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation (PubMed:15750587).

Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation (PubMed:16612004).

Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity) (PubMed:15750587, PubMed:16612004, PubMed:8336704).

By similarity3 Publications

<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 functionChromatin regulator, DNA-binding, Repressor
Biological processCell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-MMU-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-2299718, Condensation of Prophase Chromosomes
R-MMU-2559584, Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-MMU-69200, Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes
R-MMU-69202, Cyclin E associated events during G1/S transition
R-MMU-69231, Cyclin D associated events in G1
R-MMU-69656, Cyclin A:Cdk2-associated events at S phase entry

<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%5Fand%5Ftaxonomy%5Fsection">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:
Retinoblastoma-associated protein
Alternative name(s):
p110-RB11 Publication
pRb
Short name:
Rb
pp105
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Rb1
Synonyms:Rb-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 14

Organism-specific databases

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

More...
MGIi
MGI:97874, Rb1

<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

Keywords - Cellular componenti

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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi733 – 769Missing : Loss of exclusive nuclear localization. Complete loss of nuclear localization, loss of growth inhibition, when transfected in Saos-2 cells and loss of interaction with SV40 large T antigen, adenovirus E1a and E2F1; when associated with 866-N--Q-869. 1 PublicationAdd BLAST37
Mutagenesisi746I → A: Abolishes the interaction with many chromatin regulators but not that with KMT5B and KMT5C; when associated with A-750 and A-754. 1 Publication1
Mutagenesisi750N → A: Abolishes the interaction with many chromatin regulators but not that with KMT5B and KMT5C; when associated with A-746 and A-754. 1 Publication1
Mutagenesisi754M → A: Abolishes the interaction with many chromatin regulators but not that with KMT5B and KMT5C; when associated with A-746 and A-750. 1 Publication1
Mutagenesisi769 – 872Missing : Loss of exclusive nuclear localization and loss of growth inhibition, when transfected in Saos-2 cells. No effect on the interaction with SV40 large T antigen. 1 PublicationAdd BLAST104
Mutagenesisi853 – 869Missing : Loss of exclusive nuclear localization. Decreased growth inhibition activity, when transfected in Saos-2 cells. No effect on the interaction with SV40 large T antigen, adenovirus E1a, nor E2F1. 1 PublicationAdd BLAST17
Mutagenesisi866 – 869KKLR → NKLQ: Loss of exclusive nuclear localization, no effect on the interaction with SV40 large T antigen, adenovirus E1a, nor E2F1. Decreased growth inhibition activity, when transfected in Saos-2 cells. Complete loss of nuclear localization, loss of growth inhibition, when transfected in Saos-2 cells and loss of interaction with SV40 large T antigen, adenovirus E1a and E2F1; when associated with 733-K--P-769. 1 Publication4

Keywords - Diseasei

Tumor suppressor

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001678372 – 921Retinoblastoma-associated proteinAdd BLAST920

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,N-dimethylproline; by NTM11 Publication1
Modified residuei31PhosphoserineCombined sources1
Modified residuei243PhosphoserineCombined sources1
Modified residuei246PhosphothreonineCombined sources1
Modified residuei350PhosphothreonineBy similarity1
Modified residuei364PhosphothreonineCombined sources1
Modified residuei367PhosphothreonineCombined sources1
Modified residuei561Phosphoserine; by CDK2By similarity1
Modified residuei601PhosphoserineCombined sources1
Modified residuei605PhosphoserineCombined sources1
Modified residuei617PhosphoserineBy similarity1
Modified residuei773PhosphoserineCombined sources1
Modified residuei781PhosphoserineBy similarity1
Modified residuei788PhosphoserineBy similarity1
Modified residuei800PhosphoserineCombined sources1
Modified residuei803N6-methyllysine; by SMYD2By similarity1
Modified residuei804PhosphoserineCombined sources1
Modified residuei814PhosphothreonineCombined sources1
Modified residuei816PhosphothreonineBy similarity1
Modified residuei819PhosphothreonineCombined sources1
Modified residuei834PhosphothreonineBy similarity1
Modified residuei848PhosphoserineCombined sources1
Modified residuei853N6-methyllysine; by SMYD2By similarity1
Modified residuei866N6-acetyllysine; by PCAFBy similarity1
Modified residuei867N6-acetyllysine; by PCAFBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 (PubMed:8336704). Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-561 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. Phosphorylation of threonine residues in domain C promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes. Dephosphorylated at Ser-788 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-800 and Ser-804 is required for G0-G1 transition (By similarity). Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis (By similarity).By similarity1 Publication
Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression. Monomethylation at Lys-853 by SMYD2 promotes interaction with L3MBTL1 (By similarity). N-terminus is methylated by METTL11A/NTM1.By similarity1 Publication
Acetylated in the skin (PubMed:20940255). Acetylation at Lys-866 and Lys-867 regulates subcellular localization during keratinocytes differentiation (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P13405

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P13405

MaxQB - The MaxQuant DataBase

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MaxQBi
P13405

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

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PaxDbi
P13405

PeptideAtlas

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PeptideAtlasi
P13405

PRoteomics IDEntifications database

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PRIDEi
P13405

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
255135

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P13405

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

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PhosphoSitePlusi
P13405

<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 the cell nuclei of renal tubules, hepatocytes and skeletal muscles. Expressed in skin (at protein level) (PubMed:20940255).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000022105, Expressed in blood and 315 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P13405, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P13405, 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The hypophosphorylated form interacts with and sequesters the E2F1 transcription factor.

Interacts with heterodimeric E2F/DP transcription factor complexes containing TFDP1 and either E2F1/E2F, E2F3, E2F4 or E2F5, or TFDP2 and E2F4 (PubMed:8336704, PubMed:20940255). The unphosphorylated form interacts with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and THOC1.

Interacts with the N-terminal domain of TAF1.

Interacts with SNW1, ATAD5, AATF, DNMT1, LIN9, LMNA, KMT5B, KMT5C, PELP1, UHRF2, TMPO-alpha and USP4. May interact with NDC80.

Interacts with GRIP1 and UBR4.

Interacts with ARID4A and KDM5B.

Interacts with E4F1 and LIMD1.

Interacts with SMARCA4/BRG1 and HDAC1.

Interacts with USP4.

Interacts (when methylated at Lys-853) with L3MBTL1. Binds to CDK1 and CDK2.

Interacts with CHEK2; phosphorylates RB1 (By similarity).

Interacts with PRMT2.

Interacts with CEBPA. P-TEFB complex interacts with RB1; promotes phosphorylation of RB1 (By similarity).

Interacts with RBBP9; the interaction disrupts RB1 binding to E2F1 (By similarity).

Interacts with KAT2B/PCAF and EP300/P300 (PubMed:20940255).

Interacts with PAX5 (By similarity).

By similarity9 Publications

(Microbial infection) Interacts with adenovirus E1a protein.

1 Publication

(Microbial infection) Interacts with SV40 large T antigen.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
202815, 61 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-160, RB1-E2F1-TFDP1 transcription repressor complex
CPX-177, RB1-E2F2-TFDP1 transcription repressor complex
CPX-470, L3MBTL1 complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P13405

Database of interacting proteins

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DIPi
DIP-37637N

Protein interaction database and analysis system

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IntActi
P13405, 26 interactors

Molecular INTeraction database

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MINTi
P13405

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000022701

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P13405, protein

<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

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

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SMRi
P13405

Database of comparative protein structure models

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ModBasei
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>Regioni1 – 36DisorderedSequence analysisAdd BLAST36
Regioni341 – 360DisorderedSequence analysisAdd BLAST20
Regioni367 – 764Pocket; binds T and E1ABy similarityAdd BLAST398
Regioni367 – 573Domain ABy similarityAdd BLAST207
Regioni574 – 632SpacerBy similarityAdd BLAST59
Regioni633 – 764Domain BBy similarityAdd BLAST132
Regioni756 – 921Interaction with LIMD1By similarityAdd BLAST166
Regioni764 – 921Domain; mediates interaction with E4F1By similarityAdd BLAST158
Regioni872 – 921DisorderedSequence analysisAdd BLAST50

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>Motifi853 – 869Bipartite nuclear localization signal1 PublicationAdd BLAST17

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 26Pro residuesSequence analysisAdd BLAST26
Compositional biasi341 – 356Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi872 – 886Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi906 – 921Basic and acidic residuesSequence analysisAdd BLAST16

<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 retinoblastoma protein (RB) family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1010, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00950000183202

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_015754_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P13405

Identification of Orthologs from Complete Genome Data

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OMAi
VPGGNIY

Database of Orthologous Groups

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OrthoDBi
113612at2759

TreeFam database of animal gene trees

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TreeFami
TF105568

Family and domain databases

Conserved Domains Database

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CDDi
cd00043, CYCLIN, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR013763, Cyclin-like
IPR036915, Cyclin-like_sf
IPR002720, RB_A
IPR002719, RB_B
IPR015030, RB_C
IPR028309, RB_fam
IPR024599, RB_N

The PANTHER Classification System

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PANTHERi
PTHR13742, PTHR13742, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF11934, DUF3452, 1 hit
PF01858, RB_A, 1 hit
PF01857, RB_B, 1 hit
PF08934, Rb_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00385, CYCLIN, 1 hit
SM01367, DUF3452, 1 hit
SM01368, RB_A, 1 hit
SM01369, Rb_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47954, SSF47954, 2 hits

<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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P13405-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPPKAPRRAA AAEPPPPPPP PPREDDPAQD SGPEELPLAR LEFEEIEEPE
60 70 80 90 100
FIALCQKLKV PDHVRERAWL TWEKVSSVDG ILEGYIQKKK ELWGICIFIA
110 120 130 140 150
AVDLDEMPFT FTELQKSIET SVYKFFDLLK EIDTSTKVDN AMSRLLKKYN
160 170 180 190 200
VLCALYSKLE RTCELIYLTQ PSSALSTEIN SMLVLKISWI TFLLAKGEVL
210 220 230 240 250
QMEDDLVISF QLMLCVVDYF IKFSPPALLR EPYKTAAIPI NGSPRTPRRG
260 270 280 290 300
QNRSARIAKQ LENDTRIIEV LCKEHECNID EVKNVYFKNF IPFINSLGIV
310 320 330 340 350
SSNGLPEVES LSKRYEEVYL KNKDLDARLF LDHDKTLQTD PIDSFETERT
360 370 380 390 400
PRKNNPDEEA NVVTPHTPVR TVMNTIQQLM VILNSASDQP SENLISYFNN
410 420 430 440 450
CTVNPKENIL KRVKDVGHIF KEKFANAVGQ GCVDIGVQRY KLGVRLYYRV
460 470 480 490 500
MESMLKSEEE RLSIQNFSKL LNDNIFHMSL LACALEVVMA TYSRSTLQHL
510 520 530 540 550
DSGTDLSFPW ILNVLNLKAF DFYKVIESFI KVEANLTREM IKHLERCEHR
560 570 580 590 600
IMESLAWLSD SPLFDLIKQS KDGEGPDNLE PACPLSLPLQ GNHTAADMYL
610 620 630 640 650
SPLRSPKKRT STTRVNSAAN TETQAASAFH TQKPLKSTSL ALFYKKVYRL
660 670 680 690 700
AYLRLNTLCA RLLSDHPELE HIIWTLFQHT LQNEYELMRD RHLDQIMMCS
710 720 730 740 750
MYGICKVKNI DLKFKIIVTA YKDLPHAAQE TFKRVLIREE EFDSIIVFYN
760 770 780 790 800
SVFMQRLKTN ILQYASTRPP TLSPIPHIPR SPYKFSSSPL RIPGGNIYIS
810 820 830 840 850
PLKSPYKISE GLPTPTKMTP RSRILVSIGE SFGTSEKFQK INQMVCNSDR
860 870 880 890 900
VLKRSAEGGN PPKPLKKLRF DIEGADEADG SKHLPAESKF QQKLAEMTST
910 920
RTRMQKQRMN ESKDVSNKEE K
Length:921
Mass (Da):105,367
Last modified:July 27, 2011 - 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:iAE81D35A07ADB493
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9Q5C5E9Q5C5_MOUSE
Retinoblastoma-associated protein
Rb1
47Annotation 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 conflicti867 – 868KL → NV in AAA39964 (PubMed:2671991).Curated2

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
M26391 mRNA Translation: AAA39964.1
DQ400415 mRNA Translation: ABD72475.1
BC096525 mRNA Translation: AAH96525.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS27267.1

Protein sequence database of the Protein Information Resource

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PIRi
A33718

NCBI Reference Sequences

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RefSeqi
NP_033055.2, NM_009029.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000022701; ENSMUSP00000022701; ENSMUSG00000022105

Database of genes from NCBI RefSeq genomes

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GeneIDi
19645

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:19645

UCSC genome browser

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UCSCi
uc007upp.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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">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

Wikipedia

Retinoblastoma protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26391 mRNA Translation: AAA39964.1
DQ400415 mRNA Translation: ABD72475.1
BC096525 mRNA Translation: AAH96525.1
CCDSiCCDS27267.1
PIRiA33718
RefSeqiNP_033055.2, NM_009029.2

3D structure databases

SMRiP13405
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi202815, 61 interactors
ComplexPortaliCPX-160, RB1-E2F1-TFDP1 transcription repressor complex
CPX-177, RB1-E2F2-TFDP1 transcription repressor complex
CPX-470, L3MBTL1 complex
CORUMiP13405
DIPiDIP-37637N
IntActiP13405, 26 interactors
MINTiP13405
STRINGi10090.ENSMUSP00000022701

PTM databases

iPTMnetiP13405
PhosphoSitePlusiP13405

Proteomic databases

EPDiP13405
jPOSTiP13405
MaxQBiP13405
PaxDbiP13405
PeptideAtlasiP13405
PRIDEiP13405
ProteomicsDBi255135

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
3758, 3409 antibodies

The DNASU plasmid repository

More...
DNASUi
19645

Genome annotation databases

EnsembliENSMUST00000022701; ENSMUSP00000022701; ENSMUSG00000022105
GeneIDi19645
KEGGimmu:19645
UCSCiuc007upp.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5925
MGIiMGI:97874, Rb1

Phylogenomic databases

eggNOGiKOG1010, Eukaryota
GeneTreeiENSGT00950000183202
HOGENOMiCLU_015754_0_0_1
InParanoidiP13405
OMAiVPGGNIY
OrthoDBi113612at2759
TreeFamiTF105568

Enzyme and pathway databases

ReactomeiR-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-MMU-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-2299718, Condensation of Prophase Chromosomes
R-MMU-2559584, Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-MMU-69200, Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes
R-MMU-69202, Cyclin E associated events during G1/S transition
R-MMU-69231, Cyclin D associated events in G1
R-MMU-69656, Cyclin A:Cdk2-associated events at S phase entry

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
19645, 3 hits in 56 CRISPR screens

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

More...
ChiTaRSi
Rb1, mouse

Protein Ontology

More...
PROi
PR:P13405
RNActiP13405, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000022105, Expressed in blood and 315 other tissues
ExpressionAtlasiP13405, baseline and differential
GenevisibleiP13405, MM

Family and domain databases

CDDicd00043, CYCLIN, 1 hit
InterProiView protein in InterPro
IPR013763, Cyclin-like
IPR036915, Cyclin-like_sf
IPR002720, RB_A
IPR002719, RB_B
IPR015030, RB_C
IPR028309, RB_fam
IPR024599, RB_N
PANTHERiPTHR13742, PTHR13742, 1 hit
PfamiView protein in Pfam
PF11934, DUF3452, 1 hit
PF01858, RB_A, 1 hit
PF01857, RB_B, 1 hit
PF08934, Rb_C, 1 hit
SMARTiView protein in SMART
SM00385, CYCLIN, 1 hit
SM01367, DUF3452, 1 hit
SM01368, RB_A, 1 hit
SM01369, Rb_C, 1 hit
SUPFAMiSSF47954, SSF47954, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiRB_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: P13405
Secondary accession number(s): Q4VA62
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 27, 2011
Last modified: June 2, 2021
This is version 218 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

Reference proteome

Documents

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