| IED ID | IndEnz0002011610 |
| Enzyme Type ID | protease011610 |
| Protein Name |
Retinoblastoma-like protein 2 130 kDa retinoblastoma-associated protein p130 Retinoblastoma-related protein 2 RBR-2 pRb2 |
| Gene Name | Rbl2 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MASGGNQSPPPPPAAAASSEEEEEDGDAADRAQPAGSPSHQIQQRFEELCSRLNMDEAARAEAWSSYRSMSESYTLEGNDLHWLACALYVACRKSVPTVSKGTAEGNYVSLTRILRCSEQSLIEFFNKMKKWEDMANLPPHFRERTERLERNFTVSAVIFKKYEPIFQDIFKYPQEEQPRQQRGRKQRRQPCTTSEIFHFCWVLFIYAKGNFPMISDDLVNSYHLLLCALDLVYGNALQCSNRKELVNPNFKGLSEDCHPKDSKASSDPPCVIEKLCSLHDGLVLEAKGIKEHFWKPYIRKLFEKKLLKGKEENLTGFLEPGNFGESFKAVNKAYEEYVLAAGNLDERVFLGEDAEEEVGTLSRCLSAASGTESAERTQMRDILQQHLDKSKALRVCTPLTGVRYVQENSPCVTPVSTAAHSLSRLHTMLSGLRNAPSEKLERILRSCSRDPTQAIADRLKEMYEIYSQHFQPDENFSNCAKEIANKHFRFAEMLYYKVLESVIEQEQKRLGDMDLSGVLEHDAFHRSLLACCLEVVAFSHKPPGNFPFIAEIFDVPHYHFYKVIEVFIRAEDGLCREVVKHLNQIEEQILDHLAWKTKSPLWDRIRDNENRVPTCEEVMPPQNLERTDEIYIAGSPLTPRRVGEVRADAGGLGRSITSPTTLYDRYSSPTVSTTRRRLFENDSPSEGSTSGRIPPQPLVNAVPVQNVPGETVSVTPVPGQTLVTMATATVTANNGQTVTIPVQGIANENGGITFFPVQVNVGGQAQAVAGSIQPLSAQALAGSLSSQQVTGTTLQVPGPVAIQQISPGGQQQNPGQPLTSSSIRPRKTSSLALFFRKVYYLAGVRLRDLCIKLDISDELRKKIWTCFEFSIIQCTELMMDRHLDQLLMCAIYVMAKVTKEDRSFQNIMRCYRTQPQARSQVYRSVLIKGKRRNSGSSESRSHQNSPTELNTDRASRDSSPVMRSNSTLPVPQPSSAPPTPTRLTGASSDVEEEERGDLIQFYNNIYRKQIQAFAMKYSQANAQTDTPPLSPYPFVRTGSPRRVQLSQSHPIYISPHNNEAMPSPREKIFYYFSNSPSKRLREINSMIRTGETPTKKRGILLDDGSESPAKRICPENHSALLRRLQDVANDRGSQ |
| Enzyme Length | 1135 |
| Uniprot Accession Number | Q64700 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: 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 KMT5B and KMT5C, 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. {ECO:0000269|PubMed:15750587}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (3); Modified residue (20); Region (7); Sequence conflict (13) |
| Keywords | Cell cycle;Chromatin regulator;DNA-binding;Nucleus;Phosphoprotein;Reference proteome;Repressor;Transcription;Transcription regulation;Tumor suppressor |
| Interact With | Q155P7 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus. |
| Modified Residue | MOD_RES 410; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 414; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 636; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 639; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 659; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 669; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 684; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 942; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 946; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 960; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 965; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 967; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 968; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 975; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 976; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 980; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1031; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 1064; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 1076; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999"; MOD_RES 1108; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q08999" |
| Post Translational Modification | PTM: During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-636 and on 5 sites within the domain B. Phosphorylation on Ser-669 in G1 leads to its ubiquitin-dependent proteolysis (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10082561; 10630640; 10760507; 11114892; 11114893; 11798183; 11956760; 12031714; 12086466; 12177046; 12242027; 12379853; 12520002; 12538525; 12627794; 12702649; 12860570; 12941628; 14555653; 14688262; 15124025; 15188427; 15231717; 15247284; 15574596; 15664192; 15743840; 15827088; 15843406; 15867156; 15939381; 16258171; 16338659; 16465443; 16513252; 16672052; 16880527; 16884701; 17235288; 17257418; 17385710; 17502351; 17627279; 17765889; 17932948; 17956737; 18287052; 18311151; 18385796; 18420946; 18818403; 18940733; 18981186; 19151761; 19341623; 19509021; 19644500; 19649275; 19703998; 19864318; 19887370; 19887614; 20059953; 20100864; 20406986; 20650264; 21059851; 21350014; 21423694; 21631154; 21677172; 21816922; 21825075; 21840489; 21875955; 21983857; 21993628; 22237625; 22464334; 22544282; 22560297; 22714890; 22942253; 23029429; 23615279; 23669396; 24013229; 24078773; 24086435; 24143284; 24189068; 24194600; 24227978; 24531128; 24710275; 24820054; 24828495; 25017070; 25056122; 25100735; 25131634; 25142465; 25252918; 25533675; 25576924; 26238783; 26365184; 26639898; 27298335; 27373157; 27374332; 27452466; 27581360; 27750399; 27966456; 28107452; 28192409; 28402854; 28489825; 28490518; 28550162; 28928282; 29222391; 30777870; 30841904; 31043741; 31239386; 31833833; 31883968; 32473656; 8247552; 8682293; 8682294; 9110405; 9150384; 9192872; 9383278; 9418868; 9464541; 9501314; 9508781; 9751770; 9806916; 9819431; |
| Motif | |
| Gene Encoded By | |
| Mass | 127,485 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |