UniProtKB - P13405 (RB_MOUSE)
Retinoblastoma-associated protein
Rb1
Functioni
GO - Molecular functioni
- disordered domain specific binding Source: MGI
- enzyme binding Source: UniProtKB
- identical protein binding Source: MGI
- importin-alpha family protein binding Source: MGI
- kinase binding Source: UniProtKB
- phosphoprotein binding Source: MGI
- RNA polymerase II activating transcription factor binding Source: BHF-UCL
- RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: GO_Central
- transcription factor binding Source: UniProtKB
- ubiquitin protein ligase binding Source: MGI
GO - Biological processi
- aortic valve morphogenesis Source: BHF-UCL
- cell cycle arrest Source: MGI
- cell differentiation Source: GO_Central
- cell division Source: MGI
- cell morphogenesis involved in neuron differentiation Source: MGI
- cellular response to xenobiotic stimulus Source: MGI
- chromatin organization Source: UniProtKB-KW
- digestive tract development Source: MGI
- enucleate erythrocyte differentiation Source: MGI
- G1/S transition of mitotic cell cycle Source: MGI
- glial cell apoptotic process Source: MGI
- hepatocyte apoptotic process Source: MGI
- maintenance of mitotic sister chromatid cohesion Source: MGI
- myoblast differentiation Source: UniProtKB
- negative regulation of apoptotic signaling pathway Source: MGI
- negative regulation of cell cycle Source: MGI
- negative regulation of cell growth Source: UniProtKB
- negative regulation of cell population proliferation Source: MGI
- negative regulation of cold-induced thermogenesis Source: YuBioLab
- negative regulation of epithelial cell proliferation Source: MGI
- negative regulation of G1/S transition of mitotic cell cycle Source: MGI
- negative regulation of gene expression Source: MGI
- negative regulation of hepatocyte apoptotic process Source: MGI
- negative regulation of inflammatory response Source: BHF-UCL
- negative regulation of mitotic cell cycle Source: MGI
- negative regulation of myofibroblast differentiation Source: BHF-UCL
- negative regulation of protein kinase activity Source: UniProtKB
- negative regulation of protein serine/threonine kinase activity Source: MGI
- negative regulation of smoothened signaling pathway Source: MGI
- negative regulation of tau-protein kinase activity Source: MGI
- negative regulation of transcription, DNA-templated Source: MGI
- negative regulation of transcription by RNA polymerase II Source: MGI
- negative regulation of transcription involved in G1/S transition of mitotic cell cycle Source: BHF-UCL
- neuron apoptotic process Source: MGI
- neuron differentiation Source: MGI
- neuron maturation Source: MGI
- neuron projection development Source: MGI
- positive regulation of collagen fibril organization Source: BHF-UCL
- positive regulation of extracellular matrix organization Source: BHF-UCL
- positive regulation of macrophage differentiation Source: MGI
- positive regulation of mitotic metaphase/anaphase transition Source: MGI
- positive regulation of transcription by RNA polymerase II Source: MGI
- positive regulation of transcription regulatory region DNA binding Source: MGI
- protein localization to chromosome, centromeric region Source: MGI
- Ras protein signal transduction Source: Ensembl
- regulation of cell cycle Source: MGI
- regulation of cell growth Source: MGI
- regulation of cohesin loading Source: MGI
- regulation of lipid kinase activity Source: UniProtKB
- regulation of mitotic cell cycle Source: MGI
- sister chromatid biorientation Source: MGI
- skeletal muscle cell differentiation Source: MGI
- striated muscle cell differentiation Source: MGI
- tissue homeostasis Source: MGI
Keywordsi
Molecular function | Chromatin regulator, DNA-binding, Repressor |
Biological process | Cell cycle, Transcription, Transcription regulation |
Enzyme and pathway databases
Reactomei | R-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1 R-MMU-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 R-MMU-2299718, Condensation of Prophase Chromosomes R-MMU-2559584, Formation of Senescence-Associated Heterochromatin Foci (SAHF) R-MMU-69200, Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes R-MMU-69202, Cyclin E associated events during G1/S transition R-MMU-69231, Cyclin D associated events in G1 R-MMU-69656, Cyclin A:Cdk2-associated events at S phase entry |
Names & Taxonomyi
Protein namesi | Recommended name: Retinoblastoma-associated proteinAlternative name(s): p110-RB11 Publication pRb Short name: Rb pp105 |
Gene namesi | Name:Rb1 Synonyms:Rb-1 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:97874, Rb1 |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Note: During keratinocyte differentiation, acetylation by KAT2B/PCAF is required for nuclear localization.By similarity
Cytoskeleton
- spindle Source: MGI
Nucleus
- cyclin/CDK positive transcription elongation factor complex Source: Ensembl
- nucleoplasm Source: MGI
- nucleus Source: UniProtKB
- PML body Source: UniProtKB
Other locations
- chromatin Source: GO_Central
- Rb-E2F complex Source: UniProtKB
- transcription regulator complex Source: MGI
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 733 – 769 | Missing : Loss of exclusive nuclear localization. Complete loss of nuclear localization, loss of growth inhibition, when transfected in Saos-2 cells and loss of interaction with SV40 large T antigen, adenovirus E1a and E2F1; when associated with 866-N--Q-869. 1 PublicationAdd BLAST | 37 | |
Mutagenesisi | 746 | I → A: Abolishes the interaction with many chromatin regulators but not that with KMT5B and KMT5C; when associated with A-750 and A-754. 1 Publication | 1 | |
Mutagenesisi | 750 | N → A: Abolishes the interaction with many chromatin regulators but not that with KMT5B and KMT5C; when associated with A-746 and A-754. 1 Publication | 1 | |
Mutagenesisi | 754 | M → A: Abolishes the interaction with many chromatin regulators but not that with KMT5B and KMT5C; when associated with A-746 and A-750. 1 Publication | 1 | |
Mutagenesisi | 769 – 872 | Missing : Loss of exclusive nuclear localization and loss of growth inhibition, when transfected in Saos-2 cells. No effect on the interaction with SV40 large T antigen. 1 PublicationAdd BLAST | 104 | |
Mutagenesisi | 853 – 869 | Missing : Loss of exclusive nuclear localization. Decreased growth inhibition activity, when transfected in Saos-2 cells. No effect on the interaction with SV40 large T antigen, adenovirus E1a, nor E2F1. 1 PublicationAdd BLAST | 17 | |
Mutagenesisi | 866 – 869 | KKLR → NKLQ: Loss of exclusive nuclear localization, no effect on the interaction with SV40 large T antigen, adenovirus E1a, nor E2F1. Decreased growth inhibition activity, when transfected in Saos-2 cells. Complete loss of nuclear localization, loss of growth inhibition, when transfected in Saos-2 cells and loss of interaction with SV40 large T antigen, adenovirus E1a and E2F1; when associated with 733-K--P-769. 1 Publication | 4 |
Keywords - Diseasei
Tumor suppressorPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000167837 | 2 – 921 | Retinoblastoma-associated proteinAdd BLAST | 920 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N,N-dimethylproline; by NTM11 Publication | 1 | |
Modified residuei | 31 | PhosphoserineCombined sources | 1 | |
Modified residuei | 243 | PhosphoserineCombined sources | 1 | |
Modified residuei | 246 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 350 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 364 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 367 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 561 | Phosphoserine; by CDK2By similarity | 1 | |
Modified residuei | 601 | PhosphoserineCombined sources | 1 | |
Modified residuei | 605 | PhosphoserineCombined sources | 1 | |
Modified residuei | 617 | PhosphoserineBy similarity | 1 | |
Modified residuei | 773 | PhosphoserineCombined sources | 1 | |
Modified residuei | 781 | PhosphoserineBy similarity | 1 | |
Modified residuei | 788 | PhosphoserineBy similarity | 1 | |
Modified residuei | 800 | PhosphoserineCombined sources | 1 | |
Modified residuei | 803 | N6-methyllysine; by SMYD2By similarity | 1 | |
Modified residuei | 804 | PhosphoserineCombined sources | 1 | |
Modified residuei | 814 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 816 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 819 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 834 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 848 | PhosphoserineCombined sources | 1 | |
Modified residuei | 853 | N6-methyllysine; by SMYD2By similarity | 1 | |
Modified residuei | 866 | N6-acetyllysine; by PCAFBy similarity | 1 | |
Modified residuei | 867 | N6-acetyllysine; by PCAFBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Methylation, PhosphoproteinProteomic databases
EPDi | P13405 |
jPOSTi | P13405 |
MaxQBi | P13405 |
PaxDbi | P13405 |
PeptideAtlasi | P13405 |
PRIDEi | P13405 |
PTM databases
iPTMneti | P13405 |
PhosphoSitePlusi | P13405 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSMUSG00000022105, Expressed in blood and 307 other tissues |
ExpressionAtlasi | P13405, baseline and differential |
Genevisiblei | P13405, 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/E2F, E2F3, E2F4 or E2F5, or TFDP2 and E2F4 (PubMed:8336704, PubMed:20940255). The unphosphorylated form interacts with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and THOC1.
Interacts with the N-terminal domain of TAF1.
Interacts with SNW1, ATAD5, AATF, DNMT1, LIN9, LMNA, KMT5B, KMT5C, PELP1, UHRF2, TMPO-alpha and USP4. May interact with NDC80.
Interacts with GRIP1 and UBR4.
Interacts with ARID4A and KDM5B.
Interacts with E4F1 and LIMD1.
Interacts with SMARCA4/BRG1 and HDAC1.
Interacts with USP4.
Interacts (when methylated at Lys-853) with L3MBTL1. Binds to CDK1 and CDK2.
Interacts with CHEK2; phosphorylates RB1 (By similarity).
Interacts with PRMT2.
Interacts with CEBPA. P-TEFB complex interacts with RB1; promotes phosphorylation of RB1 (By similarity).
Interacts with RBBP9; the interaction disrupts RB1 binding to E2F1 (By similarity).
Interacts with KAT2B/PCAF and EP300/P300 (PubMed:20940255).
Interacts with PAX5 (By similarity).
By similarity9 Publications(Microbial infection) Interacts with adenovirus E1a protein.
1 Publication(Microbial infection) Interacts with SV40 large T antigen.
1 PublicationBinary interactionsi
Hide detailsP13405
GO - Molecular functioni
- disordered domain specific binding Source: MGI
- enzyme binding Source: UniProtKB
- identical protein binding Source: MGI
- importin-alpha family protein binding Source: MGI
- kinase binding Source: UniProtKB
- phosphoprotein binding Source: MGI
- RNA polymerase II activating transcription factor binding Source: BHF-UCL
- transcription factor binding Source: UniProtKB
- ubiquitin protein ligase binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 202815, 61 interactors |
ComplexPortali | CPX-160, RB1-E2F1-TFDP1 transcription repressor complex CPX-177, RB1-E2F2-TFDP1 transcription repressor complex CPX-470, L3MBTL1 complex |
CORUMi | P13405 |
DIPi | DIP-37637N |
IntActi | P13405, 26 interactors |
MINTi | P13405 |
STRINGi | 10090.ENSMUSP00000022701 |
Miscellaneous databases
RNActi | P13405, protein |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 367 – 764 | Pocket; binds T and E1ABy similarityAdd BLAST | 398 | |
Regioni | 367 – 573 | Domain ABy similarityAdd BLAST | 207 | |
Regioni | 574 – 632 | SpacerBy similarityAdd BLAST | 59 | |
Regioni | 633 – 764 | Domain BBy similarityAdd BLAST | 132 | |
Regioni | 756 – 921 | Interaction with LIMD1By similarityAdd BLAST | 166 | |
Regioni | 764 – 921 | Domain; mediates interaction with E4F1By similarityAdd BLAST | 158 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 853 – 869 | Bipartite nuclear localization signal1 PublicationAdd BLAST | 17 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 14 – 22 | Poly-Pro | 9 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1010, Eukaryota |
GeneTreei | ENSGT00950000183202 |
HOGENOMi | CLU_015754_0_0_1 |
InParanoidi | P13405 |
OMAi | VPGGNIY |
OrthoDBi | 113612at2759 |
TreeFami | TF105568 |
Family and domain databases
CDDi | cd00043, CYCLIN, 1 hit |
InterProi | View protein in InterPro IPR013763, Cyclin-like IPR036915, Cyclin-like_sf IPR002720, RB_A IPR002719, RB_B IPR015030, RB_C IPR028309, RB_fam IPR024599, RB_N |
PANTHERi | PTHR13742, PTHR13742, 1 hit |
Pfami | View protein in Pfam PF11934, DUF3452, 1 hit PF01858, RB_A, 1 hit PF01857, RB_B, 1 hit PF08934, Rb_C, 1 hit |
SMARTi | View protein in SMART SM00385, CYCLIN, 1 hit SM01367, DUF3452, 1 hit SM01368, RB_A, 1 hit SM01369, Rb_C, 1 hit |
SUPFAMi | SSF47954, SSF47954, 2 hits |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketE9Q5C5 | E9Q5C5_MOUSE | Retinoblastoma-associated protein | Rb1 | 47 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 867 – 868 | KL → NV in AAA39964 (PubMed:2671991).Curated | 2 |
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 |
CCDSi | CCDS27267.1 |
PIRi | A33718 |
RefSeqi | NP_033055.2, NM_009029.2 |
Genome annotation databases
Ensembli | ENSMUST00000022701; ENSMUSP00000022701; ENSMUSG00000022105 |
GeneIDi | 19645 |
KEGGi | mmu:19645 |
UCSCi | uc007upp.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 |
CCDSi | CCDS27267.1 |
PIRi | A33718 |
RefSeqi | NP_033055.2, NM_009029.2 |
3D structure databases
SMRi | P13405 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 202815, 61 interactors |
ComplexPortali | CPX-160, RB1-E2F1-TFDP1 transcription repressor complex CPX-177, RB1-E2F2-TFDP1 transcription repressor complex CPX-470, L3MBTL1 complex |
CORUMi | P13405 |
DIPi | DIP-37637N |
IntActi | P13405, 26 interactors |
MINTi | P13405 |
STRINGi | 10090.ENSMUSP00000022701 |
PTM databases
iPTMneti | P13405 |
PhosphoSitePlusi | P13405 |
Proteomic databases
EPDi | P13405 |
jPOSTi | P13405 |
MaxQBi | P13405 |
PaxDbi | P13405 |
PeptideAtlasi | P13405 |
PRIDEi | P13405 |
Protocols and materials databases
Antibodypediai | 3758, 3331 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000022701; ENSMUSP00000022701; ENSMUSG00000022105 |
GeneIDi | 19645 |
KEGGi | mmu:19645 |
UCSCi | uc007upp.2, mouse |
Organism-specific databases
CTDi | 5925 |
MGIi | MGI:97874, Rb1 |
Phylogenomic databases
eggNOGi | KOG1010, Eukaryota |
GeneTreei | ENSGT00950000183202 |
HOGENOMi | CLU_015754_0_0_1 |
InParanoidi | P13405 |
OMAi | VPGGNIY |
OrthoDBi | 113612at2759 |
TreeFami | TF105568 |
Enzyme and pathway databases
Reactomei | R-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1 R-MMU-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 R-MMU-2299718, Condensation of Prophase Chromosomes R-MMU-2559584, Formation of Senescence-Associated Heterochromatin Foci (SAHF) R-MMU-69200, Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes R-MMU-69202, Cyclin E associated events during G1/S transition R-MMU-69231, Cyclin D associated events in G1 R-MMU-69656, Cyclin A:Cdk2-associated events at S phase entry |
Miscellaneous databases
BioGRID-ORCSi | 19645, 3 hits in 20 CRISPR screens |
ChiTaRSi | Rb1, mouse |
PROi | PR:P13405 |
RNActi | P13405, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000022105, Expressed in blood and 307 other tissues |
ExpressionAtlasi | P13405, baseline and differential |
Genevisiblei | P13405, MM |
Family and domain databases
CDDi | cd00043, CYCLIN, 1 hit |
InterProi | View protein in InterPro IPR013763, Cyclin-like IPR036915, Cyclin-like_sf IPR002720, RB_A IPR002719, RB_B IPR015030, RB_C IPR028309, RB_fam IPR024599, RB_N |
PANTHERi | PTHR13742, PTHR13742, 1 hit |
Pfami | View protein in Pfam PF11934, DUF3452, 1 hit PF01858, RB_A, 1 hit PF01857, RB_B, 1 hit PF08934, Rb_C, 1 hit |
SMARTi | View protein in SMART SM00385, CYCLIN, 1 hit SM01367, DUF3452, 1 hit SM01368, RB_A, 1 hit SM01369, Rb_C, 1 hit |
SUPFAMi | SSF47954, SSF47954, 2 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RB_MOUSE | |
Accessioni | P13405Primary (citable) accession number: P13405 Secondary accession number(s): Q4VA62 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1990 |
Last sequence update: | July 27, 2011 | |
Last modified: | February 10, 2021 | |
This is version 216 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families