| IED ID | IndEnz0002012222 |
| Enzyme Type ID | protease012222 |
| Protein Name |
Retinoblastoma-like protein 1 107 kDa retinoblastoma-associated protein p107 pRb1 |
| Gene Name | Rbl1 |
| 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 | MFEDEPHAEGAAAVAAAREALQALCQELNLDEGSAAEALDDFTAIRGNYSLEGEVIHWLACSLYVACRKSIIPTVGKGVMEGNCVSLTRILRSAKLSLIQFFSKMKKWMDMSNLPQEFRERIERLERNFEVSTVIFKKFEPIFLDIFQNPYEEPPKLPRSRKQRRIPCSVKDLFNFCWTLFVYTKGNFRMIGDDLVNSYHLLLCCLDLIFANAIMCPNRRDLLNPSFKGLPSDFHAPDFKAAEEPPCIIAVLCDLHDGLLVEAKGIKEHYFKPYISKLFDKKILKGECLLDLSSFTDNSKAVNKEYEEYVLTVGDFDERIFLGADAEEEIGTPRKFTADTPFGKLTSQASVECNLQQHFEKKRSFAPSTPLTGRRYLQEKEAVTTPVASATQSVSRLQSIVAGLKSAPSEQLLNIFESCMRNPMGNIIKIVKGIGETFCQHYTQSTDKQPGSHIDFAVNRLKLAEILYYKILETIMVQETRRLHGMDMSVLLEQDIFHKSLMACCLEIVLFAYSSPRTFPWIIEVLDLQPFYFYKVIEVVIRSEEGLSRDMVKHLNSIEEQILESLAWTNNSALWEALHASANRVPSCEEVIFPNNFEIGNGGNVQGHLPMMPMSPIIHPRVKEVRTDSGSLRQDMQPLSPISVHERYSSPAAGSAKRRLFGDDPPKDTLMDKIMAEGTKLKIAPSSVTAESLSISPGQALLTMATTTVTGTTGRKVTVPLHGIANDAGEITLVPISMNPTQESTAESPVSLTAQSLIGTSPKQTHLTKAQDAHLTGVSKPKRTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFTLVHCPDLMKDRHLDQLLLCAFYIMAKVTKEERTFQEIMKSYRNQPQANSHVYRSVLLKSIPGGVVVYNGDCEMTDGDIEDATKTPNCSSEPVKEERGDLIKFYNTVYVGRVKSFALKYDLSNQDHIMDAPPLSPFPHIKQQPGSPRRISQQHSLYVSPHKNGAGLTPRSALLYKFNGSPSKSLKDINNMIRQGEQKTKKRVIAISGDADSPAKRLCQENDDVLLKRLQDVVSERANH |
| Enzyme Length | 1063 |
| Uniprot Accession Number | Q64701 |
| 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 (By similarity). Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation (PubMed:15750587). Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression (PubMed:15750587). Controls histone H4 'Lys-20' trimethylation (PubMed:15750587). Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters (PubMed:15750587). Potent inhibitor of E2F-mediated trans-activation (By similarity). May act as a tumor suppressor (By similarity). {ECO:0000250|UniProtKB:P28749, ECO:0000269|PubMed:15750587}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Modified residue (13); Region (4); Sequence conflict (4) |
| Keywords | Alternative splicing;Cell cycle;Chromatin regulator;Nucleus;Phosphoprotein;Reference proteome;Repressor;Transcription;Transcription regulation;Tumor suppressor |
| Interact With | Q155P7 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. |
| Modified Residue | MOD_RES 332; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 369; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 385; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 640; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 650; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 748; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 761; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 959; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 970; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 983; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 992; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 1004; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P28749"; MOD_RES 1036; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079" |
| Post Translational Modification | PTM: Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-959 and Ser-970 by CDK4. {ECO:0000250|UniProtKB:P28749}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10082561; 10508527; 10630640; 10788617; 11114892; 11114893; 11217851; 12086466; 12096340; 12177046; 12242027; 12379853; 12466851; 12520002; 12627794; 12702649; 12810584; 12853964; 12860570; 14555653; 14610273; 14688262; 14716294; 14732703; 15070741; 15124025; 15148303; 15188427; 15190215; 15193257; 15210943; 15231717; 15353549; 15574596; 15631990; 15664192; 15701640; 15827088; 15843406; 15939381; 16258171; 16271529; 16338659; 16465443; 16602821; 16672052; 16884701; 17080083; 17235288; 17257418; 17363591; 17502351; 17563750; 17591923; 17608565; 17923680; 17932945; 17936268; 17956737; 18300254; 18799693; 18818403; 18940733; 18981186; 19341623; 19509021; 19564414; 19649275; 19706423; 19786571; 19864318; 19887370; 19887614; 20019750; 20059953; 20100864; 20585628; 20679727; 20713602; 20946988; 21059851; 21172336; 21194568; 21423694; 21515735; 21677750; 21779340; 21816922; 21840489; 21875955; 21993628; 22237625; 22286767; 22484813; 22560297; 22714890; 22864477; 22942253; 23145321; 23146901; 23558950; 23615279; 23669396; 23765217; 23803733; 24013229; 24056077; 24086435; 24143284; 24227978; 24238961; 24449206; 24662053; 24710275; 25017070; 25100735; 25142465; 25182511; 25249236; 25252918; 25533675; 26238783; 26317218; 26365184; 26628093; 26639898; 26935419; 27001308; 27966456; 28107452; 28165337; 28192409; 28233396; 28402854; 28550162; 28928282; 30383332; 31239386; 31270502; 31613797; 34270926; 34645816; 7797074; 8077211; 8197461; 8682293; 8682294; 8862413; 8945939; 9110405; 9150384; 9192872; 9418868; 9464541; 9508781; 9620848; 9751770; 9819431; 9878593; |
| Motif | |
| Gene Encoded By | |
| Mass | 119,456 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |