| Tag | Content |
|---|
| CPLM ID | CPLM-014663 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Retinoblastoma-like protein 2 |
Protein Synonyms/Alias | 130 kDa retinoblastoma-associated protein; p130; Retinoblastoma-related protein 2; RBR-2; pRb2 |
Gene Name | Rbl2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 101 | KSVPTVSKGTAEGNY | ubiquitination | [1] | | 128 | SLIEFFNKMKKWEDM | acetylation | [2] | | 130 | IEFFNKMKKWEDMAN | acetylation | [2] | | 1068 | AMPSPREKIFYYFSN | acetylation | [2] | | 1079 | YFSNSPSKRLREINS | acetylation | [2] | | 1111 | DGSESPAKRICPENH | acetylation | [2] |
|
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] [2] Cell cycle-dependent acetylation of Rb2/p130 in NIH3T3 cells. Schwarze F, Meraner J, Lechner M, Loidl A, Stasyk T, Laich A, Loidl P. Oncogene. 2010 Oct 21;29(42):5755-60. [ PMID: 20676144] |
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, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor. |
Sequence Annotation | REGION 414 1021 Pocket; binds E1A.
REGION 414 613 Domain A.
REGION 614 824 Spacer.
REGION 825 1021 Domain B.
MOD_RES 410 410 Phosphoserine.
MOD_RES 414 414 Phosphothreonine.
MOD_RES 636 636 Phosphoserine.
MOD_RES 639 639 Phosphothreonine.
MOD_RES 659 659 Phosphoserine (By similarity).
MOD_RES 669 669 Phosphoserine (By similarity).
MOD_RES 942 942 Phosphoserine.
MOD_RES 946 946 Phosphoserine (By similarity).
MOD_RES 960 960 Phosphoserine (By similarity).
MOD_RES 976 976 Phosphoserine (By similarity).
MOD_RES 980 980 Phosphothreonine (By similarity).
MOD_RES 1027 1027 Phosphothreonine.
MOD_RES 1031 1031 Phosphoserine (By similarity). |
Keyword | Cell cycle; Chromatin regulator; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation; Tumor suppressor. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1135 AA |
Protein Sequence | MASGGNQSPP PPPAAAASSE EEEEDGDAAD RAQPAGSPSH QIQQRFEELC SRLNMDEAAR 60
AEAWSSYRSM SESYTLEGND LHWLACALYV ACRKSVPTVS KGTAEGNYVS LTRILRCSEQ 120
SLIEFFNKMK KWEDMANLPP HFRERTERLE RNFTVSAVIF KKYEPIFQDI FKYPQEEQPR 180
QQRGRKQRRQ PCTTSEIFHF CWVLFIYAKG NFPMISDDLV NSYHLLLCAL DLVYGNALQC 240
SNRKELVNPN FKGLSEDCHP KDSKASSDPP CVIEKLCSLH DGLVLEAKGI KEHFWKPYIR 300
KLFEKKLLKG KEENLTGFLE PGNFGESFKA VNKAYEEYVL AAGNLDERVF LGEDAEEEVG 360
TLSRCLSAAS GTESAERTQM RDILQQHLDK SKALRVCTPL TGVRYVQENS PCVTPVSTAA 420
HSLSRLHTML SGLRNAPSEK LERILRSCSR DPTQAIADRL KEMYEIYSQH FQPDENFSNC 480
AKEIANKHFR FAEMLYYKVL ESVIEQEQKR LGDMDLSGVL EHDAFHRSLL ACCLEVVAFS 540
HKPPGNFPFI AEIFDVPHYH FYKVIEVFIR AEDGLCREVV KHLNQIEEQI LDHLAWKTKS 600
PLWDRIRDNE NRVPTCEEVM PPQNLERTDE IYIAGSPLTP RRVGEVRADA GGLGRSITSP 660
TTLYDRYSSP TVSTTRRRLF ENDSPSEGST SGRIPPQPLV NAVPVQNVPG ETVSVTPVPG 720
QTLVTMATAT VTANNGQTVT IPVQGIANEN GGITFFPVQV NVGGQAQAVA GSIQPLSAQA 780
LAGSLSSQQV TGTTLQVPGP VAIQQISPGG QQQNPGQPLT SSSIRPRKTS SLALFFRKVY 840
YLAGVRLRDL CIKLDISDEL RKKIWTCFEF SIIQCTELMM DRHLDQLLMC AIYVMAKVTK 900
EDRSFQNIMR CYRTQPQARS QVYRSVLIKG KRRNSGSSES RSHQNSPTEL NTDRASRDSS 960
PVMRSNSTLP VPQPSSAPPT PTRLTGASSD VEEEERGDLI QFYNNIYRKQ IQAFAMKYSQ 1020
ANAQTDTPPL SPYPFVRTGS PRRVQLSQSH PIYISPHNNE AMPSPREKIF YYFSNSPSKR 1080
LREINSMIRT GETPTKKRGI LLDDGSESPA KRICPENHSA LLRRLQDVAN DRGSQ 1135 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:Compara. GO:0005730; C:nucleolus; IEA:Compara. GO:0005667; C:transcription factor complex; IDA:MGI. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0007049; P:cell cycle; IEA:UniProtKB-KW. GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. GO:0051726; P:regulation of cell cycle; IEA:InterPro. GO:0043550; P:regulation of lipid kinase activity; IEA:Compara. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
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Pfam | |
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