CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004116
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Retinoblastoma-associated protein 
Protein Synonyms/Alias
 pRb; Rb; pp105 
Gene Name
 Rb1 
Gene Synonyms/Alias
 Rb-1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
803NIYISPLKSPYKISEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 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, SUV420H1 and SUV420H2, 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). 
Sequence Annotation
 REGION 367 764 Pocket; binds T and E1A (By similarity).
 REGION 367 573 Domain A (By similarity).
 REGION 574 632 Spacer (By similarity).
 REGION 633 764 Domain B (By similarity).
 REGION 756 921 Interaction with LIMD1 (By similarity).
 REGION 764 921 Domain; mediates interaction with E4F1
 MOTIF 863 869 Nuclear localization signal (By
 MOD_RES 2 2 N,N-dimethylproline; by NTM1.
 MOD_RES 31 31 Phosphoserine (By similarity).
 MOD_RES 243 243 Phosphoserine; by CDK1 (By similarity).
 MOD_RES 246 246 Phosphothreonine; by CDK1 (By
 MOD_RES 350 350 Phosphothreonine (By similarity).
 MOD_RES 367 367 Phosphothreonine; by CDK1 (By
 MOD_RES 561 561 Phosphoserine; by CDK2 (By similarity).
 MOD_RES 605 605 Phosphoserine; by CHEK2 and CHEK1 (By
 MOD_RES 788 788 Phosphoserine (By similarity).
 MOD_RES 800 800 Phosphoserine; by CDK1 and CDK3 (By
 MOD_RES 803 803 N6-methyllysine; by SMYD2 (By
 MOD_RES 804 804 Phosphoserine; by CDK1 and CDK3 (By
 MOD_RES 814 814 Phosphothreonine; by CDK6 (By
 MOD_RES 816 816 Phosphothreonine (By similarity).
 MOD_RES 819 819 Phosphothreonine; by CDK4.
 MOD_RES 834 834 Phosphothreonine (By similarity).
 MOD_RES 853 853 N6-methyllysine; by SMYD2 (By
 MOD_RES 866 866 N6-acetyllysine; by PCAF (By similarity).
 MOD_RES 867 867 N6-acetyllysine; by PCAF (By similarity).  
Keyword
 Acetylation; Cell cycle; Chromatin regulator; Complete proteome; DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 921 AA 
Protein Sequence
MPPKAPRRAA AAEPPPPPPP PPREDDPAQD SGPEELPLAR LEFEEIEEPE FIALCQKLKV 60
PDHVRERAWL TWEKVSSVDG ILEGYIQKKK ELWGICIFIA AVDLDEMPFT FTELQKSIET 120
SVYKFFDLLK EIDTSTKVDN AMSRLLKKYN VLCALYSKLE RTCELIYLTQ PSSALSTEIN 180
SMLVLKISWI TFLLAKGEVL QMEDDLVISF QLMLCVVDYF IKFSPPALLR EPYKTAAIPI 240
NGSPRTPRRG QNRSARIAKQ LENDTRIIEV LCKEHECNID EVKNVYFKNF IPFINSLGIV 300
SSNGLPEVES LSKRYEEVYL KNKDLDARLF LDHDKTLQTD PIDSFETERT PRKNNPDEEA 360
NVVTPHTPVR TVMNTIQQLM VILNSASDQP SENLISYFNN CTVNPKENIL KRVKDVGHIF 420
KEKFANAVGQ GCVDIGVQRY KLGVRLYYRV MESMLKSEEE RLSIQNFSKL LNDNIFHMSL 480
LACALEVVMA TYSRSTLQHL DSGTDLSFPW ILNVLNLKAF DFYKVIESFI KVEANLTREM 540
IKHLERCEHR IMESLAWLSD SPLFDLIKQS KDGEGPDNLE PACPLSLPLQ GNHTAADMYL 600
SPLRSPKKRT STTRVNSAAN TETQAASAFH TQKPLKSTSL ALFYKKVYRL AYLRLNTLCA 660
RLLSDHPELE HIIWTLFQHT LQNEYELMRD RHLDQIMMCS MYGICKVKNI DLKFKIIVTA 720
YKDLPHAAQE TFKRVLIREE EFDSIIVFYN SVFMQRLKTN ILQYASTRPP TLSPIPHIPR 780
SPYKFSSSPL RIPGGNIYIS PLKSPYKISE GLPTPTKMTP RSRILVSIGE SFGTSEKFQK 840
INQMVCNSDR VLKRSAEGGN PPKPLKKLRF DIEGADEADG SKHLPAESKF QQKLAEMTST 900
RTRMQKQRMN ESKDVSNKEE K 921 
Gene Ontology
 GO:0016605; C:PML body; ISS:UniProtKB.
 GO:0035189; C:Rb-E2F complex; IDA:BHF-UCL.
 GO:0005819; C:spindle; IDA:MGI.
 GO:0001047; F:core promoter binding; IEA:Compara.
 GO:0019900; F:kinase binding; ISS:UniProtKB.
 GO:0008134; F:transcription factor binding; ISS:UniProtKB.
 GO:0007050; P:cell cycle arrest; IMP:MGI.
 GO:0051301; P:cell division; IMP:MGI.
 GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0048565; P:digestive tract development; IMP:MGI.
 GO:0043353; P:enucleate erythrocyte differentiation; IGI:MGI.
 GO:0034349; P:glial cell apoptotic process; IMP:MGI.
 GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
 GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IEA:Compara.
 GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
 GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
 GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
 GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
 GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
 GO:0071930; P:negative regulation of transcription involved in G1/S phase of mitotic cell cycle; IGI:BHF-UCL.
 GO:0051402; P:neuron apoptotic process; IMP:MGI.
 GO:0042551; P:neuron maturation; IMP:MGI.
 GO:0031175; P:neuron projection development; IMP:MGI.
 GO:0045651; P:positive regulation of macrophage differentiation; IGI:MGI.
 GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0071459; P:protein localization to chromosome, centromeric region; IEA:Compara.
 GO:0007265; P:Ras protein signal transduction; IEA:Compara.
 GO:0071922; P:regulation of cohesin localization to chromatin; IEA:Compara.
 GO:0043550; P:regulation of lipid kinase activity; ISS:UniProtKB.
 GO:0031134; P:sister chromatid biorientation; IEA:Compara.
 GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR013763; Cyclin-like.
 IPR024599; DUF3452_retinoblatoma-assoc.
 IPR002720; RB_A.
 IPR015652; Rb_associated.
 IPR002719; RB_B.
 IPR015030; Rb_C. 
Pfam
 PF11934; DUF3452
 PF01858; RB_A
 PF01857; RB_B
 PF08934; Rb_C 
SMART
 SM00385; CYCLIN 
PROSITE
  
PRINTS