Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Retinoblastoma-associated protein

Gene

Rb1

Organism
Rattus norvegicus (Rat)
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.1 Publication

<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

  • kinase binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: GO_Central
  • RNA polymerase II regulatory region DNA binding Source: GO_Central
  • transcription factor binding Source: RGD

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

<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):
pRb
Short name:
Rb
pp105
<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
Synonyms:Rb-1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3540 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

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

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>Mutagenesisi772S → A: Decreased association with HDAC1; when associated with A-780 and A-787. 1 Publication1
Mutagenesisi780S → A: Decreased association with HDAC1; when associated with A-772 and A-787. 1 Publication1
Mutagenesisi787S → A: Decreased association with HDAC1; when associated with A-772 and A-780. 1 Publication1

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_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_00001678382 – 920Retinoblastoma-associated proteinAdd BLAST919

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 residuei30PhosphoserineCombined sources1
Modified residuei242Phosphoserine; by CDK1By similarity1
Modified residuei245Phosphothreonine; by CDK1By similarity1
Modified residuei349PhosphothreonineBy similarity1
Modified residuei363PhosphothreonineCombined sources1
Modified residuei366PhosphothreonineCombined sources1
Modified residuei560Phosphoserine; by CDK2By similarity1
Modified residuei600PhosphoserineBy similarity1
Modified residuei604Phosphoserine; by CHEK2 and CHEK1By similarity1
Modified residuei616PhosphoserineBy similarity1
Modified residuei772PhosphoserineSequence analysisBy similarity1
Modified residuei780PhosphoserineSequence analysisBy similarity1
Modified residuei787Phosphoserine1 Publication1
Modified residuei799PhosphoserineCombined sources1
Modified residuei802N6-methyllysine; by SMYD2By similarity1
Modified residuei803Phosphoserine; by CDK1 and CDK3By similarity1
Modified residuei813Phosphothreonine; by CDK6By similarity1
Modified residuei815PhosphothreonineBy similarity1
Modified residuei818Phosphothreonine; by CDK4By similarity1
Modified residuei833PhosphothreonineBy similarity1
Modified residuei847PhosphoserineBy similarity1
Modified residuei852N6-methyllysine; by SMYD2By similarity1
Modified residuei865N6-acetyllysine; by PCAFBy similarity1
Modified residuei866N6-acetyllysine; by PCAFBy similarity1

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

Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-560 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. CDK3/cyclin-C-mediated phosphorylation at Ser-799 and Ser-803 is required for G0-G1 transition (By similarity). Dephosphorylated at Ser-787 by calcineruin upon calcium stimulation.By similarity2 Publications
N-terminus is methylated by METTL11A/NTM1. Monomethylation at Lys-802 by SMYD2 enhances phosphorylation at Ser-799 and Ser-803, and promotes cell cycle progression. Monomethylation at Lys-852 by SMYD2 promotes interaction with L3MBTL1 (By similarity).By similarity
Acetylation at Lys-865 and Lys-866 regulates subcellular localization, at least during keratinocytes differentiation.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P33568

PRoteomics IDEntifications database

More...
PRIDEi
P33568

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P33568

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

More...
PhosphoSitePlusi
P33568

<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

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, ATAD5, 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, LIMD1 and USP4. Interacts with PRMT2. Interacts (when methylated at Lys-852) with L3MBTL. Interacts with CHEK2; phosphorylates RB1 (By similarity). Interacts with SMARCA4/BRG1 and HDAC1. Binds to CDK1 and CDK2. P-TEFB complex interacts with RB1; promotes phosphorylation of RB1 (By similarity).By similarity3 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246837, 5 interactors

Protein interaction database and analysis system

More...
IntActi
P33568, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000021752

<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

More...
SMRi
P33568

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni366 – 763Pocket; binds T and E1ABy similarityAdd BLAST398
Regioni366 – 572Domain ABy similarityAdd BLAST207
Regioni573 – 631SpacerBy similarityAdd BLAST59
Regioni632 – 763Domain BBy similarityAdd BLAST132
Regioni755 – 920Interaction with LIMD1By similarityAdd BLAST166
Regioni763 – 920Domain C; mediates interaction with E4F1By similarityAdd 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>Motifi862 – 868Nuclear localization signalBy similarity7

<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

More...
eggNOGi
KOG1010 Eukaryota
ENOG410XQF7 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000136539

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG008967

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P33568

KEGG Orthology (KO)

More...
KOi
K06618

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P33568

TreeFam database of animal gene trees

More...
TreeFami
TF105568

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00043 CYCLIN, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

More...
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 1 potential isoform that is computationally mapped.Show allAlign All

P33568-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPPKAPRRTA AAEPPPPPPP PPEDDPAQDS DPEELPLIRL EFEKIEEPEF
60 70 80 90 100
IALCQKLKVP DHVRERAWLT WEKVSSVDGI LEGYIQKKKE LWGICIFIAA
110 120 130 140 150
VDLDEMPFTF TELQKSIETS VYKFFDLLKE IDTSTKVDNA VSRLLKKYNV
160 170 180 190 200
LCALYSKLER TCGLIYLTQP SSGLSTEINS MLVLKVSWIT FLLAKGEVVQ
210 220 230 240 250
MEDDLVISFQ LMLCVLDYFI KLSPPALLRE PYKTAATPIN GSPRTPRRGQ
260 270 280 290 300
NRSARIAKQL ESDTRTIEVL CKEHECNVDE VKNVYFKNFI PFISSLGIVS
310 320 330 340 350
SNGLPELESL SKRYEEVYLK SKDLDARLFL DHDKTLQTDT IDSFETERTP
360 370 380 390 400
RKSNPDEEAN MVTPHTPVRT VMNTIQQLMV ILNSASDQPS ENLISYFSNC
410 420 430 440 450
TVNPKENILK RVKDVGHIFK EKFASAVGQG CIDIGAQRYK LGVRLYYRVM
460 470 480 490 500
ESMLKSEEER LSIQNFSKLL NDNIFHMSLL ACALEVVMAT YSRSMLQNLD
510 520 530 540 550
SGTDLSFPWI LNVLNLKAFD FYKVIESFIK VEANLTREMI KHLERCEHRI
560 570 580 590 600
MESLAWLSDS PLFDLIKQSK DGEGPDHLES ACSLSLPLQS NHTAADMYLS
610 620 630 640 650
PIRSPKKRTS TTRVNSAANT ETQAASAFHT QKPLKSTSLS LFYKKVYRLA
660 670 680 690 700
YLRLNTLCAR LLSDHPELEH IIWTLFQHTL ENEYELMKDR HLDQIMMCSM
710 720 730 740 750
YGICKVKNID LKFKIIVTAY KDLPHAAQET FKRVLIREEE FDSIIVFYNS
760 770 780 790 800
VFMQRLKTNI LQYASTRPPT LSPIPHIPRS PYKFSSSPLR IPGGNIYISP
810 820 830 840 850
LKSPYKISEG LPTPTKMTPR SRILVSIGES FGTSEKFQKI NQMVCNSDRV
860 870 880 890 900
LKRSAEGGNP PKPLKKLRFD IEGSDEADGS KHLPAESKFQ QKLAEMTSTR
910 920
TRMQKQKLND SMEISNKEEK
Length:920
Mass (Da):105,025
Last modified:February 9, 2010 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3BA735EA59927301
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
R9PXV5R9PXV5_RAT
Retinoblastoma-associated protein
Rb1
892Annotation 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 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 conflicti668L → P in BAA04958 (PubMed:7665085).Curated1
Sequence conflicti798I → M in BAA04958 (PubMed:7665085).Curated1
Sequence conflicti866 – 867KL → TW in AAA42090 (PubMed:8441612).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D25233 mRNA Translation: BAA04958.1
L07126 mRNA Translation: AAA42090.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S35544

NCBI Reference Sequences

More...
RefSeqi
NP_058741.1, NM_017045.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.55115

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24708

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24708

UCSC genome browser

More...
UCSCi
RGD:3540 rat

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D25233 mRNA Translation: BAA04958.1
L07126 mRNA Translation: AAA42090.1
PIRiS35544
RefSeqiNP_058741.1, NM_017045.1
UniGeneiRn.55115

3D structure databases

SMRiP33568
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246837, 5 interactors
IntActiP33568, 3 interactors
STRINGi10116.ENSRNOP00000021752

PTM databases

iPTMnetiP33568
PhosphoSitePlusiP33568

Proteomic databases

PaxDbiP33568
PRIDEiP33568

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24708
KEGGirno:24708
UCSCiRGD:3540 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5925
RGDi3540 Rb1

Phylogenomic databases

eggNOGiKOG1010 Eukaryota
ENOG410XQF7 LUCA
HOGENOMiHOG000136539
HOVERGENiHBG008967
InParanoidiP33568
KOiK06618
PhylomeDBiP33568
TreeFamiTF105568

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P33568

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

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRB_RAT
<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: P33568
Secondary accession number(s): Q63527
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 9, 2010
Last modified: November 7, 2018
This is version 168 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again