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Protein

Retinoblastoma-associated protein

Gene

RB1

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

Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. 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).By similarity1 Publication
(Microbial infection) In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.5 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, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-69200 Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69231 Cyclin D associated events in G1
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-8940973 RUNX2 regulates osteoblast differentiation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P06400

SIGNOR Signaling Network Open Resource

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SIGNORi
P06400

<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:
Retinoblastoma-associated protein
Alternative name(s):
p105-Rb
pRb
Short name:
Rb
pp110
<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:RB1
<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 13

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000139687.13

Human Gene Nomenclature Database

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HGNCi
HGNC:9884 RB1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
614041 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P06400

<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

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

Childhood cancer retinoblastoma (RB)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCongenital malignant tumor that arises from the nuclear layers of the retina. It occurs in about 1:20'000 live births and represents about 2% of childhood malignancies. It is bilateral in about 30% of cases. Although most RB appear sporadically, about 20% are transmitted as an autosomal dominant trait with incomplete penetrance. The diagnosis is usually made before the age of 2 years when strabismus or a gray to yellow reflex from pupil ('cat eye') is investigated.
See also OMIM:180200
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_00557272E → Q in RB. 1 Publication1
Natural variantiVAR_005573137E → D in RB; unilateral form. 1 PublicationCorresponds to variant dbSNP:rs3092902EnsemblClinVar.1
Natural variantiVAR_005574185I → T in RB. 1 Publication1
Natural variantiVAR_010045310G → E in RB; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200844292EnsemblClinVar.1
Natural variantiVAR_010046358R → G in RB. 1 Publication1
Natural variantiVAR_005575358R → Q in RB. Corresponds to variant dbSNP:rs767011440EnsemblClinVar.1
Natural variantiVAR_010048447K → Q in RB. 1 Publication1
Natural variantiVAR_005576457M → R in RB. 1 Publication1
Natural variantiVAR_005577480Missing in RB; mild form. 1 Publication1
Natural variantiVAR_011580500R → G in RB. 1 Publication1
Natural variantiVAR_010049530K → R in RB. 1 Publication1
Natural variantiVAR_005578549H → Y in RB. 1 PublicationCorresponds to variant dbSNP:rs1050717570Ensembl.1
Natural variantiVAR_005579567S → L in RB. 2 PublicationsCorresponds to variant dbSNP:rs137853292EnsemblClinVar.1
Natural variantiVAR_011581616K → E in RB. 1 Publication1
Natural variantiVAR_005580635A → P in RB. 1 Publication1
Natural variantiVAR_005581654V → E in RB. 1 Publication1
Natural variantiVAR_010050657L → P in RB. 1 Publication1
Natural variantiVAR_005582661R → W in RB; mild form. 4 PublicationsCorresponds to variant dbSNP:rs137853294EnsemblClinVar.1
Natural variantiVAR_005583662L → P in RB. 1 Publication1
Natural variantiVAR_005584673H → P in RB. 1
Natural variantiVAR_005585685Q → P in RB. 1 Publication1
Natural variantiVAR_005586706C → Y in RB. 1
Natural variantiVAR_005587712C → R in RB. 1 PublicationCorresponds to variant dbSNP:rs137853296EnsemblClinVar.1
Natural variantiVAR_005588803N → K in RB. 1 Publication1
Bladder cancer (BLC)
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences.
See also OMIM:109800
Osteogenic sarcoma (OSRC)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA sarcoma originating in bone-forming cells, affecting the ends of long bones.
See also OMIM:259500

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>Mutagenesisi821T → A: Abolishes interaction with Pocket domain; when associated with A-826. 1 Publication1
Mutagenesisi826T → A: Abolishes interaction with Pocket domain; when associated with A-821. 1 Publication1
Mutagenesisi860K → R: Abolishes monomethylation by SMYD2 and subsequent interaction with L3MBTL1. 1 Publication1
Mutagenesisi870K → R: Does not affect the ability to be methylated by SMYD2; when associated with 873-R-R-874. 1 Publication1
Mutagenesisi873 – 874KK → R: Does not affect the ability to be methylated by SMYD2; when associated with 873-R-R-874. 2 Publications2
Mutagenesisi873 – 874KK → RR: Does not alter Rb localization in cycling cells, but mislocalizes to the cytoplasm during keratinocytes differentiation. 2 Publications2

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNET

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DisGeNETi
5925

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
RB1

MalaCards human disease database

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MalaCardsi
RB1
MIMi109800 phenotype
180200 phenotype
259500 phenotype

Open Targets

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OpenTargetsi
ENSG00000139687

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

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Orphaneti
357027 Hereditary retinoblastoma
1587 Monosomy 13q14
357034 Non-hereditary retinoblastoma
668 Osteosarcoma
70573 Small cell lung cancer

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA295

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5288

Drug and drug target database

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DrugBanki
DB00030 Insulin Human
DB00071 Insulin Pork

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RB1

Domain mapping of disease mutations (DMDM)

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DMDMi
132164

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00001678362 – 928Retinoblastoma-associated proteinAdd BLAST927

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-dimethylprolineBy similarity1
Modified residuei37PhosphoserineCombined sources1
Modified residuei249Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei252Phosphothreonine; by CDK1Combined sources1 Publication1
Modified residuei356PhosphothreonineCombined sources1
Modified residuei373Phosphothreonine; by CDK1Combined sources1 Publication1
Modified residuei567Phosphoserine; by CDK21 Publication1
Modified residuei608PhosphoserineBy similarity1
Modified residuei612Phosphoserine; by CHEK2 and CHEK1Combined sources1 Publication1
Modified residuei624PhosphoserineCombined sources1
Modified residuei780PhosphoserineCombined sources1
Modified residuei788PhosphoserineCombined sources1
Modified residuei795PhosphoserineCombined sources1
Modified residuei807Phosphoserine; by CDK1 and CDK3Combined sources2 Publications1
Modified residuei810N6-methyllysine; by SMYD21 Publication1
Modified residuei811Phosphoserine; by CDK1 and CDK3Combined sources2 Publications1
Modified residuei821Phosphothreonine; by CDK6Combined sources2 Publications1
Modified residuei823PhosphothreonineCombined sources1
Modified residuei826Phosphothreonine; by CDK4Combined sources2 Publications1
Modified residuei841PhosphothreonineCombined sources1
Modified residuei855PhosphoserineCombined sources1
Modified residuei860N6-methyllysine; by SMYD21 Publication1
Modified residuei873N6-acetyllysine; by PCAF1 Publication1
Modified residuei874N6-acetyllysine; by PCAF1 Publication1

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

Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-567 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. SV40 large T antigen, HPV E7 and adenovirus E1A bind to the underphosphorylated, active form of pRb. Phosphorylation at Thr-821 and Thr-826 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-795 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-807 and Ser-811 is required for G0-G1 transition. Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis (By similarity).By similarity
N-terminus is methylated by METTL11A/NTM1 (By similarity). Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression. Monomethylation at Lys-860 by SMYD2 promotes interaction with L3MBTL1.By similarity9 Publications
Acetylation at Lys-873 and Lys-874 regulates subcellular localization, at least during keratinocytes differentiation.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P06400

MaxQB - The MaxQuant DataBase

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MaxQBi
P06400

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

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PaxDbi
P06400

PeptideAtlas

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PeptideAtlasi
P06400

PRoteomics IDEntifications database

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PRIDEi
P06400

ProteomicsDB human proteome resource

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ProteomicsDBi
51900

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P06400

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

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PhosphoSitePlusi
P06400

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P06400

<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 retina.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000139687 Expressed in 229 organ(s), highest expression level in endometrium

CleanEx database of gene expression profiles

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CleanExi
HS_RB1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P06400 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P06400 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000095
CAB016687
HPA050082

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

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

Interacts with ATAD5. Interacts with PRMT2, CDK1 and CDK2 (By similarity). The hypophosphorylated form interacts with and sequesters the E2F1 transcription factor. Interacts with heterodimeric E2F/DP transcription factor complexes containing TFDP1 and either E2F1, E2F3, E2F4 or E2F5, or TFDP2 and E2F4. The unphosphorylated form interacts with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and THOC1. Interacts with the N-terminal domain of TAF1. Interacts with SNW1, AATF, DNMT1, LIN9, LMNA, KMT5B, KMT5C, PELP1, UHRF2 and TMPO-alpha. 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 (By similarity). Interacts with PSMA3 and USP4. Interacts (when methylated at Lys-860) with L3MBTL1. Interacts with CHEK2; phosphorylates RB1. Interacts with CEBPA (PubMed:15107404). P-TEFB complex interacts with RB1; promotes phosphorylation of RB1 (PubMed:12037672).By similarity32 Publications
(Microbial infection) Interacts with adenovirus E1A protein.1 Publication
(Microbial infection) Interacts with HPV E7 protein.1 Publication
(Microbial infection) Interacts with SV40 large T antigen.2 Publications
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL123.1 Publication
(Microbial infection) Interacts with molluscum contagiosum virus protein MC007.1 Publication

<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

WithEntry#Exp.IntActNotes
itself3EBI-491274,EBI-491274
P030706EBI-491274,EBI-617698From Simian virus 40.
P032543EBI-491274,EBI-8599077From Human adenovirus C serotype 2.
P0325510EBI-491274,EBI-2603114From Human adenovirus C serotype 5.
P03255-12EBI-491274,EBI-6692439From a different organism.
P03255-23EBI-491274,EBI-6859460From a different organism.
AGO2Q9UKV83EBI-491274,EBI-528269
CCNCP248634EBI-491274,EBI-395261
CDK2P249413EBI-491274,EBI-375096
Cdk4P302852EBI-491274,EBI-847225From Mus musculus.
CenpfQ155P74EBI-491274,EBI-2211248From Mus musculus.
CHEK1O147573EBI-491274,EBI-974488
CHEK2O960173EBI-491274,EBI-1180783
DGKZQ13574-26EBI-491274,EBI-715527
DYRK1AQ136273EBI-491274,EBI-1053596
DYRK1BQ9Y4633EBI-491274,EBI-634187
E2F1Q0109421EBI-491274,EBI-448924
E2F2Q142093EBI-491274,EBI-718476
E2F3O007164EBI-491274,EBI-765551
E7A0MPS72EBI-491274,EBI-7014709From Human papillomavirus type 16.
E7P0312922EBI-491274,EBI-866453From Human papillomavirus type 16.
E7P040203EBI-491274,EBI-7005254From Human papillomavirus type 11.
E7P064643EBI-491274,EBI-6944797From Human papillomavirus type 6b.
E7P064652EBI-491274,EBI-963841From Human papillomavirus type 1.
E7P067883EBI-491274,EBI-1776887From Human papillomavirus type 18.
FOXO3O435242EBI-491274,EBI-1644164
FRKP426853EBI-491274,EBI-1383583
GATA1P159762EBI-491274,EBI-3909284
GRB2P629934EBI-491274,EBI-401755
HBP1O603812EBI-491274,EBI-954175
HDAC1Q1354716EBI-491274,EBI-301834
Hmga2P529275EBI-491274,EBI-912574From Mus musculus.
Ifi202Q9R0025EBI-491274,EBI-3043899From Mus musculus.
IRF3Q146532EBI-491274,EBI-2650369
KDM5AP293752EBI-491274,EBI-1560836
MAPK14Q165394EBI-491274,EBI-73946
MDM2Q009875EBI-491274,EBI-389668
MDM4O151514EBI-491274,EBI-398437
MRPS18BQ9Y6762EBI-491274,EBI-750085
NCOA6Q146863EBI-491274,EBI-78670
NEFMP071972EBI-491274,EBI-1105035
ospFQ8VSP92EBI-491274,EBI-6506625From Shigella flexneri.
PA2G4Q9UQ804EBI-491274,EBI-924893
PPP1CAP621362EBI-491274,EBI-357253
PRMT2P553453EBI-491274,EBI-78458
Psmd10Q9Z2X23EBI-491274,EBI-8377084From Mus musculus.
PURAQ005776EBI-491274,EBI-1045860
RAF1P040493EBI-491274,EBI-365996
RBBP8Q997082EBI-491274,EBI-745715
RNF40O751503EBI-491274,EBI-744408
SETD7Q8WTS64EBI-491274,EBI-1268586
Sirt1Q923E44EBI-491274,EBI-1802585From Mus musculus.
Smarca4Q3TKT44EBI-491274,EBI-1210244From Mus musculus.
UHRF2Q96PU44EBI-491274,EBI-625304
USP7Q930098EBI-491274,EBI-302474

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111860, 242 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-155 RB1-E2F1-TFDP1 transcription repressor complex
CPX-175 RB1-E2F2-TFDP1 transcription repressor complex
CPX-469 L3MBTL1 complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P06400

Database of interacting proteins

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DIPi
DIP-582N

Protein interaction database and analysis system

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IntActi
P06400, 141 interactors

Molecular INTeraction database

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MINTi
P06400

STRING: functional protein association networks

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STRINGi
9606.ENSP00000267163

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P06400

<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

1928
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P06400

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

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SMRi
P06400

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P06400

<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>Regioni373 – 771Pocket; binds T and E1AAdd BLAST399
Regioni373 – 579Domain AAdd BLAST207
Regioni580 – 639SpacerAdd BLAST60
Regioni640 – 771Domain BAdd BLAST132
Regioni763 – 928Interaction with LIMD11 PublicationAdd BLAST166
Regioni771 – 928Domain C; mediates interaction with E4F11 PublicationAdd BLAST158

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>Motifi870 – 876Nuclear localization signalCurated7

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi10 – 18Poly-Ala9
Compositional biasi20 – 29Poly-Pro10

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

The Pocket domain binds to the threonine-phosphorylated domain C, thereby preventing interaction with heterodimeric E2F/DP transcription factor complexes.

<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
ENOG410XQF7 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155912

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG008967

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P06400

KEGG Orthology (KO)

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KOi
K06618

Identification of Orthologs from Complete Genome Data

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OMAi
EMQRTPR

Database of Orthologous Groups

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OrthoDBi
EOG091G0398

Database for complete collections of gene phylogenies

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PhylomeDBi
P06400

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
IPR033057 RB1
IPR002720 RB_A
IPR002719 RB_B
IPR015030 RB_C
IPR028309 RB_fam
IPR024599 RB_N

The PANTHER Classification System

More...
PANTHERi
PTHR13742 PTHR13742, 1 hit
PTHR13742:SF17 PTHR13742:SF17, 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

More...
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_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.

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

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P06400-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPPKTPRKTA ATAAAAAAEP PAPPPPPPPE EDPEQDSGPE DLPLVRLEFE
60 70 80 90 100
ETEEPDFTAL CQKLKIPDHV RERAWLTWEK VSSVDGVLGG YIQKKKELWG
110 120 130 140 150
ICIFIAAVDL DEMSFTFTEL QKNIEISVHK FFNLLKEIDT STKVDNAMSR
160 170 180 190 200
LLKKYDVLFA LFSKLERTCE LIYLTQPSSS ISTEINSALV LKVSWITFLL
210 220 230 240 250
AKGEVLQMED DLVISFQLML CVLDYFIKLS PPMLLKEPYK TAVIPINGSP
260 270 280 290 300
RTPRRGQNRS ARIAKQLEND TRIIEVLCKE HECNIDEVKN VYFKNFIPFM
310 320 330 340 350
NSLGLVTSNG LPEVENLSKR YEEIYLKNKD LDARLFLDHD KTLQTDSIDS
360 370 380 390 400
FETQRTPRKS NLDEEVNVIP PHTPVRTVMN TIQQLMMILN SASDQPSENL
410 420 430 440 450
ISYFNNCTVN PKESILKRVK DIGYIFKEKF AKAVGQGCVE IGSQRYKLGV
460 470 480 490 500
RLYYRVMESM LKSEEERLSI QNFSKLLNDN IFHMSLLACA LEVVMATYSR
510 520 530 540 550
STSQNLDSGT DLSFPWILNV LNLKAFDFYK VIESFIKAEG NLTREMIKHL
560 570 580 590 600
ERCEHRIMES LAWLSDSPLF DLIKQSKDRE GPTDHLESAC PLNLPLQNNH
610 620 630 640 650
TAADMYLSPV RSPKKKGSTT RVNSTANAET QATSAFQTQK PLKSTSLSLF
660 670 680 690 700
YKKVYRLAYL RLNTLCERLL SEHPELEHII WTLFQHTLQN EYELMRDRHL
710 720 730 740 750
DQIMMCSMYG ICKVKNIDLK FKIIVTAYKD LPHAVQETFK RVLIKEEEYD
760 770 780 790 800
SIIVFYNSVF MQRLKTNILQ YASTRPPTLS PIPHIPRSPY KFPSSPLRIP
810 820 830 840 850
GGNIYISPLK SPYKISEGLP TPTKMTPRSR ILVSIGESFG TSEKFQKINQ
860 870 880 890 900
MVCNSDRVLK RSAEGSNPPK PLKKLRFDIE GSDEADGSKH LPGESKFQQK
910 920
LAEMTSTRTR MQKQKMNDSM DTSNKEEK
Length:928
Mass (Da):106,159
Last modified:January 1, 1990 - 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:iC8E746111E19CC32
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8Y743A0A2R8Y743_HUMAN
Retinoblastoma-associated protein
RB1
110Annotation 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>
Q92728Q92728_HUMAN
Mutated retinoblastoma protein
RB1
53Annotation 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>
A0A2R8YFL6A0A2R8YFL6_HUMAN
Retinoblastoma-associated protein
RB1
103Annotation 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 conflicti500 – 501RS → SN in AAN64133 (Ref. 7) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00557272E → Q in RB. 1 Publication1
Natural variantiVAR_051909133N → H. Corresponds to variant dbSNP:rs3092900Ensembl.1
Natural variantiVAR_005573137E → D in RB; unilateral form. 1 PublicationCorresponds to variant dbSNP:rs3092902EnsemblClinVar.1
Natural variantiVAR_069376173Y → H1 Publication1
Natural variantiVAR_005574185I → T in RB. 1 Publication1
Natural variantiVAR_010045310G → E in RB; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200844292EnsemblClinVar.1
Natural variantiVAR_010046358R → G in RB. 1 Publication1
Natural variantiVAR_005575358R → Q in RB. Corresponds to variant dbSNP:rs767011440EnsemblClinVar.1
Natural variantiVAR_019379436Q → K1 PublicationCorresponds to variant dbSNP:rs4151534EnsemblClinVar.1
Natural variantiVAR_010048447K → Q in RB. 1 Publication1
Natural variantiVAR_005576457M → R in RB. 1 Publication1
Natural variantiVAR_005577480Missing in RB; mild form. 1 Publication1
Natural variantiVAR_011580500R → G in RB. 1 Publication1
Natural variantiVAR_019380525A → G1 PublicationCorresponds to variant dbSNP:rs4151539EnsemblClinVar.1
Natural variantiVAR_010049530K → R in RB. 1 Publication1
Natural variantiVAR_005578549H → Y in RB. 1 PublicationCorresponds to variant dbSNP:rs1050717570Ensembl.1
Natural variantiVAR_005579567S → L in RB. 2 PublicationsCorresponds to variant dbSNP:rs137853292EnsemblClinVar.1
Natural variantiVAR_051910569L → F. Corresponds to variant dbSNP:rs3092895Ensembl.1
Natural variantiVAR_011581616K → E in RB. 1 Publication1
Natural variantiVAR_005580635A → P in RB. 1 Publication1
Natural variantiVAR_005581654V → E in RB. 1 Publication1
Natural variantiVAR_010050657L → P in RB. 1 Publication1
Natural variantiVAR_005582661R → W in RB; mild form. 4 PublicationsCorresponds to variant dbSNP:rs137853294EnsemblClinVar.1
Natural variantiVAR_005583662L → P in RB. 1 Publication1
Natural variantiVAR_005584673H → P in RB. 1
Natural variantiVAR_005585685Q → P in RB. 1 Publication1
Natural variantiVAR_051911697D → E. Corresponds to variant dbSNP:rs3092903EnsemblClinVar.1
Natural variantiVAR_005586706C → Y in RB. 1
Natural variantiVAR_005587712C → R in RB. 1 PublicationCorresponds to variant dbSNP:rs137853296EnsemblClinVar.1
Natural variantiVAR_034442746E → G. Corresponds to variant dbSNP:rs3092905Ensembl.1
Natural variantiVAR_005588803N → K in RB. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M15400 mRNA Translation: AAA69807.1 Sequence problems.
M28419 mRNA Translation: AAA69808.1
M33647 mRNA Translation: AAA69806.1
L41870 mRNA Translation: AAB59465.1
M27866
, M27845, M27846, M27847, M27849, M27850, M27851, L35146, M27852, M27853, M27854, M27855, M27856, M27857, M27858, M27859, M27860, L35147, M27862, M27863, M27864, M27865 Genomic DNA Translation: AAA53484.1
L41889 Genomic DNA Translation: AAB59467.1
L41890 Genomic DNA Translation: AAA65735.1
L41891 Genomic DNA Translation: AAA65736.1
L41893 Genomic DNA Translation: AAA65737.1
L41894 Genomic DNA Translation: AAA65738.1
L41895 Genomic DNA Translation: AAA65739.1
L41896 Genomic DNA Translation: AAA65740.1
L41897 Genomic DNA Translation: AAA65741.1
L41898 Genomic DNA Translation: AAB59471.1
L41899 Genomic DNA Translation: AAB59473.1
L41997 Genomic DNA Translation: AAB59482.1
X16439 Genomic DNA Translation: CAA34462.1
AF551763 Genomic DNA Translation: AAN64133.1
AK291258 mRNA Translation: BAF83947.1
AL136960 Genomic DNA No translation available.
AL392048 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08793.1
BC039060 mRNA Translation: AAH39060.1
BC040540 mRNA Translation: AAH40540.1
L11910 Genomic DNA Translation: AAA53483.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS31973.1

Protein sequence database of the Protein Information Resource

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PIRi
JS0276 RBHU

NCBI Reference Sequences

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RefSeqi
NP_000312.2, NM_000321.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.408528

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000267163; ENSP00000267163; ENSG00000139687

Database of genes from NCBI RefSeq genomes

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GeneIDi
5925

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5925

UCSC genome browser

More...
UCSCi
uc001vcb.4 human

Keywords - Coding sequence diversityi

Polymorphism

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

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

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

RB1base

RB1 mutation db

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

Retinoblastoma protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15400 mRNA Translation: AAA69807.1 Sequence problems.
M28419 mRNA Translation: AAA69808.1
M33647 mRNA Translation: AAA69806.1
L41870 mRNA Translation: AAB59465.1
M27866
, M27845, M27846, M27847, M27849, M27850, M27851, L35146, M27852, M27853, M27854, M27855, M27856, M27857, M27858, M27859, M27860, L35147, M27862, M27863, M27864, M27865 Genomic DNA Translation: AAA53484.1
L41889 Genomic DNA Translation: AAB59467.1
L41890 Genomic DNA Translation: AAA65735.1
L41891 Genomic DNA Translation: AAA65736.1
L41893 Genomic DNA Translation: AAA65737.1
L41894 Genomic DNA Translation: AAA65738.1
L41895 Genomic DNA Translation: AAA65739.1
L41896 Genomic DNA Translation: AAA65740.1
L41897 Genomic DNA Translation: AAA65741.1
L41898 Genomic DNA Translation: AAB59471.1
L41899 Genomic DNA Translation: AAB59473.1
L41997 Genomic DNA Translation: AAB59482.1
X16439 Genomic DNA Translation: CAA34462.1
AF551763 Genomic DNA Translation: AAN64133.1
AK291258 mRNA Translation: BAF83947.1
AL136960 Genomic DNA No translation available.
AL392048 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08793.1
BC039060 mRNA Translation: AAH39060.1
BC040540 mRNA Translation: AAH40540.1
L11910 Genomic DNA Translation: AAA53483.1
CCDSiCCDS31973.1
PIRiJS0276 RBHU
RefSeqiNP_000312.2, NM_000321.2
UniGeneiHs.408528

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AD6X-ray2.30A378-562[»]
1GH6X-ray3.20B379-577[»]
B645-772[»]
1GUXX-ray1.85A372-589[»]
B636-787[»]
1H25X-ray2.50E868-878[»]
1N4MX-ray2.20A/B380-785[»]
1O9KX-ray2.60A/C/E/G372-589[»]
B/D/F/H636-787[»]
1PJMX-ray2.50A858-881[»]
2AZEX-ray2.55C829-874[»]
2QDJX-ray2.00A52-355[»]
2R7GX-ray1.67A/C380-787[»]
3N5UX-ray3.20C870-882[»]
3POMX-ray2.50A/B380-577[»]
A/B643-783[»]
4CRIX-ray2.35C/D802-817[»]
4ELJX-ray2.70A53-787[»]
4ELLX-ray1.98A/B380-787[»]
ProteinModelPortaliP06400
SMRiP06400
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111860, 242 interactors
ComplexPortaliCPX-155 RB1-E2F1-TFDP1 transcription repressor complex
CPX-175 RB1-E2F2-TFDP1 transcription repressor complex
CPX-469 L3MBTL1 complex
CORUMiP06400
DIPiDIP-582N
IntActiP06400, 141 interactors
MINTiP06400
STRINGi9606.ENSP00000267163

Chemistry databases

BindingDBiP06400
ChEMBLiCHEMBL5288
DrugBankiDB00030 Insulin Human
DB00071 Insulin Pork

PTM databases

iPTMnetiP06400
PhosphoSitePlusiP06400

Polymorphism and mutation databases

BioMutaiRB1
DMDMi132164

Proteomic databases

EPDiP06400
MaxQBiP06400
PaxDbiP06400
PeptideAtlasiP06400
PRIDEiP06400
ProteomicsDBi51900

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5925
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267163; ENSP00000267163; ENSG00000139687
GeneIDi5925
KEGGihsa:5925
UCSCiuc001vcb.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5925
DisGeNETi5925
EuPathDBiHostDB:ENSG00000139687.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RB1
GeneReviewsiRB1
HGNCiHGNC:9884 RB1
HPAiCAB000095
CAB016687
HPA050082
MalaCardsiRB1
MIMi109800 phenotype
180200 phenotype
259500 phenotype
614041 gene
neXtProtiNX_P06400
OpenTargetsiENSG00000139687
Orphaneti357027 Hereditary retinoblastoma
1587 Monosomy 13q14
357034 Non-hereditary retinoblastoma
668 Osteosarcoma
70573 Small cell lung cancer
PharmGKBiPA295

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1010 Eukaryota
ENOG410XQF7 LUCA
GeneTreeiENSGT00940000155912
HOVERGENiHBG008967
InParanoidiP06400
KOiK06618
OMAiEMQRTPR
OrthoDBiEOG091G0398
PhylomeDBiP06400
TreeFamiTF105568

Enzyme and pathway databases

ReactomeiR-HSA-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-69200 Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69231 Cyclin D associated events in G1
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-8940973 RUNX2 regulates osteoblast differentiation
SignaLinkiP06400
SIGNORiP06400

Miscellaneous databases

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

More...
ChiTaRSi
RB1 human
EvolutionaryTraceiP06400

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Retinoblastoma_protein

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

More...
GenomeRNAii
5925
PMAP-CutDBiP06400

Protein Ontology

More...
PROi
PR:P06400

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000139687 Expressed in 229 organ(s), highest expression level in endometrium
CleanExiHS_RB1
ExpressionAtlasiP06400 baseline and differential
GenevisibleiP06400 HS

Family and domain databases

CDDicd00043 CYCLIN, 1 hit
InterProiView protein in InterPro
IPR013763 Cyclin-like
IPR036915 Cyclin-like_sf
IPR033057 RB1
IPR002720 RB_A
IPR002719 RB_B
IPR015030 RB_C
IPR028309 RB_fam
IPR024599 RB_N
PANTHERiPTHR13742 PTHR13742, 1 hit
PTHR13742:SF17 PTHR13742:SF17, 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

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiRB_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: P06400
Secondary accession number(s): A8K5E3
, P78499, Q5VW46, Q8IZL4
<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: January 1, 1988
Last sequence update: January 1, 1990
Last modified: December 5, 2018
This is version 245 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
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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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