| Tag | Content |
|---|---|
| UniProt Accession | RBL1_HUMAN; P28749; |
| Entrez ID | 5933 |
| GenBank Protein ID | NM_002895.4; NM_183404.3; |
| GenBank Nucleotide ID | NP_002886.2; NP_899662.1; |
| Protein Name | Retinoblastoma-like protein 1 (107 kDa retinoblastoma-associated protein) (p107) (pRb1) |
| Gene Name | RBL1 |
| Organism | Homo sapiens |
| NCBI Taxa ID | 9606 |
| 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 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. 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 (Fasta) | 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 1069 |
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| Database | Annotation |
|---|---|
| GWASdb (count: 1) | rs6073285; Multiple complex diseases; Null |
| PTM | Modification Sites |
|---|---|
| Phosphorylation (count: 47) (view all) | 1000 GSGLTPRSALLYKFN dbPAF
1004 TPRSALLYKFNGSPS dbPAF 1009 LLYKFNGSPSKSLKD dbPAF 1011 YKFNGSPSKSLKDIN dbPAF 103 LSLIQFFSKMKKWMD dbPAF 1037 KRVIAIDSDAESPAK dbPAF |
| Acetylation (count: 1) | 1056 ENDDVLLKRLQDVVS PLMD |
| Ubiquitination (count: 2) | 138 VSTVIFKKYEPIFLD PLMD
304 DNSKAVNKEYEEYVL PLMD |