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UniProtKB - P13405 (RB_MOUSE)

Protein

Retinoblastoma-associated protein

Gene

Rb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 similarity2 Publications

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
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

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoblastoma-associated protein
Alternative name(s):
pRb
Short name:
Rb
pp105
Gene namesi
Name:Rb1
Synonyms:Rb-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:97874 Rb1

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001678372 – 921Retinoblastoma-associated proteinAdd BLAST920

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Post-translational modificationi

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 similarity
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
Acetylation at Lys-866 and Lys-867 regulates subcellular localization, at least during keratinocytes differentiation.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP13405
MaxQBiP13405
PaxDbiP13405
PeptideAtlasiP13405
PRIDEiP13405

PTM databases

iPTMnetiP13405
PhosphoSitePlusiP13405

Expressioni

Tissue specificityi

Expressed in the cell nuclei of renal tubules, hepatocytes and skeletal muscles. Colocalizes with RB1CC1 in various tissues.1 Publication

Gene expression databases

BgeeiENSMUSG00000022105 Expressed in 293 organ(s), highest expression level in blood
CleanExiMM_RB1
ExpressionAtlasiP13405 baseline and differential
GenevisibleiP13405 MM

Interactioni

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, 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).By similarity7 Publications

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi202815, 36 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

Structurei

3D structure databases

ProteinModelPortaliP13405
SMRiP13405
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi863 – 869Nuclear localization signalBy similarity7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi9 – 12Poly-Ala4
Compositional biasi14 – 22Poly-Pro9

Sequence similaritiesi

Belongs to the retinoblastoma protein (RB) family.Curated

Phylogenomic databases

eggNOGiKOG1010 Eukaryota
ENOG410XQF7 LUCA
GeneTreeiENSGT00530000063235
HOGENOMiHOG000136539
HOVERGENiHBG008967
InParanoidiP13405
KOiK06618
OMAiEMQRTPR
OrthoDBiEOG091G0398
TreeFamiTF105568

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

Sequence (1+)i

Sequence statusi: Complete.

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
Checksum:iAE81D35A07ADB493
GO

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:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti867 – 868KL → NV in AAA39964 (PubMed:2671991).Curated2

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
UniGeneiMm.273862

Genome annotation databases

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

Similar proteinsi

Cross-referencesi

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
UniGeneiMm.273862

3D structure databases

ProteinModelPortaliP13405
SMRiP13405
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202815, 36 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
MaxQBiP13405
PaxDbiP13405
PeptideAtlasiP13405
PRIDEiP13405

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5925
MGIiMGI:97874 Rb1

Phylogenomic databases

eggNOGiKOG1010 Eukaryota
ENOG410XQF7 LUCA
GeneTreeiENSGT00530000063235
HOGENOMiHOG000136539
HOVERGENiHBG008967
InParanoidiP13405
KOiK06618
OMAiEMQRTPR
OrthoDBiEOG091G0398
TreeFamiTF105568

Enzyme and pathway databases

ReactomeiR-MMU-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
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

PROiPR:P13405
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022105 Expressed in 293 organ(s), highest expression level in blood
CleanExiMM_RB1
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
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
ProtoNetiSearch...

Entry informationi

Entry nameiRB_MOUSE
AccessioniPrimary (citable) accession number: P13405
Secondary accession number(s): Q4VA62
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 27, 2011
Last modified: November 7, 2018
This is version 198 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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