CPLM-005720

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-005720

UniProt Accession

RBL1_HUMAN; P28749; A8K2W5; Q4VXA0; Q8N5K6; Q9H1L5; Q9H1M1

Genbank Protein ID

L14812; AK290380; AL136172; AL365505; AL391114; AL365505; AL136172; AL391114; AL391114; AL136172; AL365505; AL365505; AL136172; AL391114; AL391114; AL136172; AL365505; AL136172; AL365505; AL391114; CH471077; BC032247; M74547; S78664

Genbank Nucleotide ID

AAA02489.1; BAF83069.1; CAI95716.1; CAI95716.1; CAI95716.1; CAI95177.1; CAI95177.1; CAI95177.1; CAI95151.1; CAI95151.1; CAI95151.1; CAI95178.1; CAI95178.1; CAI95178.1; CAI95152.1; CAI95152.1; CAI95152.1; CAI95717.1; CAI95717.1; CAI95717.1; EAW76088.1; AAH32247.1; AAA36397.1; AAD14290.1

Protein Name

Retinoblastoma-like protein 1

Protein Synonyms/Alias

107 kDa retinoblastoma-associated protein; p107; pRb1

Gene Name

RBL1

Gene Synonyms/Alias

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
1056	ENDDVLLKRLQDVVS	acetylation	[1]

Reference

[1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]

Functional Description

Key regulator of entry into cell division. 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 SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation. Forms a complex with adenovirus E1A and with SV40 large T antigen. May bind and modulate functionally certain cellular proteins with which T and E1A compete for pocket binding. May act as a tumor suppressor.

Sequence Annotation

REGION 385 949 Pocket; binds T and E1A.
REGION 385 584 Domain A.
REGION 585 780 Spacer.
REGION 781 949 Domain B.
MOD_RES 332 332 Phosphothreonine; by CDK2.
MOD_RES 369 369 Phosphothreonine; by CDK4.
MOD_RES 385 385 Phosphothreonine; by CDK2.
MOD_RES 640 640 Phosphoserine; by CDK2 and CDK4.
MOD_RES 650 650 Phosphoserine.
MOD_RES 749 749 Phosphoserine.
MOD_RES 762 762 Phosphoserine; by CDK2.
MOD_RES 964 964 Phosphoserine; by CDK2 and CDK4.
MOD_RES 975 975 Phosphoserine; by CDK2 and CDK4.
MOD_RES 988 988 Phosphoserine; by CDK2.
MOD_RES 997 997 Phosphothreonine; by CDK2.
MOD_RES 1009 1009 Phosphoserine; by CDK2.

Keyword

3D-structure; Alternative splicing; Cell cycle; Chromatin regulator; Complete proteome; Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation; Tumor suppressor.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

1068 AA

Protein Sequence

MFEDKPHAEG AAVVAAAGEA LQALCQELNL DEGSAAEALD DFTAIRGNYS LEGEVTHWLA 60
CSLYVACRKS IIPTVGKGIM EGNCVSLTRI LRSAKLSLIQ FFSKMKKWMD MSNLPQEFRE 120
RIERLERNFE VSTVIFKKYE PIFLDIFQNP YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL 180
FVYTKGNFRM IGDDLVNSYH LLLCCLDLIF ANAIMCPNRQ DLLNPSFKGL PSDFHTADFT 240
ASEEPPCIIA VLCELHDGLL VEAKGIKEHY FKPYISKLFD RKILKGECLL DLSSFTDNSK 300
AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTRDT PLGKLTAQAN VEYNLQQHFE 360
KKRSFAPSTP LTGRRYLREK EAVITPVASA TQSVSRLQSI VAGLKNAPSD QLINIFESCV 420
RNPVENIMKI LKGIGETFCQ HYTQSTDEQP GSHIDFAVNR LKLAEILYYK ILETVMVQET 480
RRLHGMDMSV LLEQDIFHRS LMACCLEIVL FAYSSPRTFP WIIEVLNLQP FYFYKVIEVV 540
IRSEEGLSRD MVKHLNSIEE QILESLAWSH DSALWEALQV SANKVPTCEE VIFPNNFETG 600
NGGNVQGHLP LMPMSPLMHP RVKEVRTDSG SLRRDMQPLS PISVHERYSS PTAGSAKRRL 660
FGEDPPKEML MDKIITEGTK LKIAPSSSIT AENVSILPGQ TLLTMATAPV TGTTGHKVTI 720
PLHGVANDAG EITLIPLSMN TNQESKVKSP VSLTAHSLIG ASPKQTNLTK AQEVHSTGIN 780
RPKRTGSLAL FYRKVYHLAS VRLRDLCLKL DVSNELRRKI WTCFEFTLVH CPDLMKDRHL 840
DQLLLCAFYI MAKVTKEERT FQEIMKSYRN QPQANSHVYR SVLLKSIPRE VVAYNKNIND 900
DFEMIDCDLE DATKTPDCSS GPVKEERGDL IKFYNTIYVG RVKSFALKYD LANQDHMMDA 960
PPLSPFPHIK QQPGSPRRIS QQHSIYISPH KNGSGLTPRS ALLYKFNGSP SKSLKDINNM 1020
IRQGEQRTKK RVIAIDSDAE SPAKRVCQEN DDVLLKRLQD VVSERANH 1068

Gene Ontology

GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0005667; C:transcription factor complex; IEA:Compara.
GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
GO:0000278; P:mitotic cell cycle; TAS:Reactome.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO:0051726; P:regulation of cell cycle; IEA:InterPro.
GO:0043550; P:regulation of lipid kinase activity; IDA:UniProtKB.
GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

Interpro

IPR013763; Cyclin-like.
IPR024599; DUF3452_retinoblatoma-assoc.
IPR002720; RB_A.
IPR002719; RB_B.
IPR015030; Rb_C.

Pfam

PF11934; DUF3452
PF01858; RB_A
PF01857; RB_B
PF08934; Rb_C

SMART

SM00385; CYCLIN

PROSITE

PRINTS