Rb1
entrez
24708
canonical
uniprot
P33568
canonical
ensembl
ENSRNOG00000016029
resolver
ensembl
ENSRNOG00055014785
resolver
ensembl
ENSRNOG00060018531
resolver
ensembl
ENSRNOG00065017661
resolver
ensp
ENSRNOP00000021752
resolver
ensp
ENSRNOP00055020690
resolver
ensp
ENSRNOP00060025908
resolver
ensp
ENSRNOP00065023462
resolver
enst
ENSRNOT00000021752
resolver
enst
ENSRNOT00055025330
resolver
enst
ENSRNOT00060031883
resolver
enst
ENSRNOT00065029547
resolver
genesymbol
Rb1
resolver
genesymbol_syn
Rb-1
resolver
uniprot
Q63527
resolver
uniprot_entry
RB_RAT
resolver
uniprot_sec
Q63527
resolver
amino_acid_sequence
MPPKAPRRTAAAEPPPPPPPPPEDDPAQDSDPEELPLIRLEFEKIEEPEFIALCQKLKVPDHVRERAWLTWEKVSSVDGILEGYIQKKKELWGICIFIAAVDLDEMPFTFTELQKSIETSVYKFFDLLKEIDTSTKVDNAVSRLLKKYNVLCALYSKLERTCGLIYLTQPSSGLSTEINSMLVLKVSWITFLLAKGEVVQMEDDLVISFQLMLCVLDYFIKLSPPALLREPYKTAATPINGSPRTPRRGQNRSARIAKQLESDTRTIEVLCKEHECNVDEVKNVYFKNFIPFISSLGIVSSNGLPELESLSKRYEEVYLKSKDLDARLFLDHDKTLQTDTIDSFETERTPRKSNPDEEANMVTPHTPVRTVMNTIQQLMVILNSASDQPSENLISYFSNCTVNPKENILKRVKDVGHIFKEKFASAVGQGCIDIGAQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSMLQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKVEANLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDGEGPDHLESACSLSLPLQSNHTAADMYLSPIRSPKKRTSTTRVNSAANTETQAASAFHTQKPLKSTSLSLFYKKVYRLAYLRLNTLCARLLSDHPELEHIIWTLFQHTLENEYELMKDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGSDEADGSKHLPAESKFQQKLAEMTSTRTRMQKQKLNDSMEISNKEEK
uniprot
proteins
function
FUNCTION: Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle. The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes. Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription. Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase. RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. 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 (PubMed:19081374). 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). {ECO:0000250|UniProtKB:P06400, ECO:0000250|UniProtKB:P13405, ECO:0000269|PubMed:19081374}.
uniprot
proteins
mass_dalton
105025
uniprot
proteins
mutagenesis
MUTAGEN 772; /note="S->A: Decreased association with HDAC1; when associated with A-780 and A-787."; /evidence="ECO:0000269|PubMed:19081374"; MUTAGEN 780; /note="S->A: Decreased association with HDAC1; when associated with A-772 and A-787."; /evidence="ECO:0000269|PubMed:19081374"; MUTAGEN 787; /note="S->A: Decreased association with HDAC1; when associated with A-772 and A-780."; /evidence="ECO:0000269|PubMed:19081374
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250, ECO:0000269|PubMed:10542199, ECO:0000269|PubMed:19081374}.; PTM: 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). {ECO:0000250}.; PTM: Acetylated during keratinocyte differentiation. Acetylation at Ser-799 and Ser-803 regulates subcellular localization. Can be deacetylated by SIRT1. {ECO:0000250|UniProtKB:P06400}.
uniprot
proteins
protein_family
Retinoblastoma protein (RB) family
uniprot
proteins
pubmed
10542199
uniprot
proteins
pubmed
10888886
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
19081374
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
7665085
uniprot
proteins
pubmed
8441612
uniprot
proteins
pubmed
9697699
uniprot
proteins
sequence_length
920
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13405}. Cytoplasm {ECO:0000250|UniProtKB:P13405}. Note=During keratinocyte differentiation, acetylation by KAT2B/PCAF is required for nuclear localization (By similarity). Localizes to the cytoplasm when hyperphosphorylated (By similarity). {ECO:0000250|UniProtKB:P06400, ECO:0000250|UniProtKB:P13405}.
uniprot
proteins