| Tag | Content |
|---|---|
| UniProt Accession | RBL2_HUMAN; Q08999; |
| Entrez ID | 5934 |
| GenBank Protein ID | NM_001323608.1; NM_005611.3; |
| GenBank Nucleotide ID | NP_001310537.1; NP_005602.3; |
| Protein Name | Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2) |
| Gene Name | RBL2; RB2 |
| 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, 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 (Fasta) | MPSGGDQSPP PPPPPPAAAA SDEEEEDDGE AEDAAPPAES PTPQIQQRFD ELCSRLNMDE 60 AARAEAWDSY RSMSESYTLE GNDLHWLACA LYVACRKSVP TVSKGTVEGN YVSLTRILKC 120 SEQSLIEFFN KMKKWEDMAN LPPHFRERTE RLERNFTVSA VIFKKYEPIF QDIFKYPQEE 180 QPRQQRGRKQ RRQPCTVSEI FHFCWVLFIY AKGNFPMISD DLVNSYHLLL CALDLVYGNA 240 LQCSNRKELV NPNFKGLSED FHAKDSKPSS DPPCIIEKLC SLHDGLVLEA KGIKEHFWKP 300 YIRKLYEKKL LKGKEENLTG FLEPGNFGES FKAINKAYEE YVLSVGNLDE RIFLGEDAEE 360 EIGTLSRCLN AGSGTETAER VQMKNILQQH FDKSKALRIS TPLTGVRYIK ENSPCVTPVS 420 TATHSLSRLH TMLTGLRNAP SEKLEQILRT CSRDPTQAIA NRLKEMFEIY SQHFQPDEDF 480 SNCAKEIASK HFRFAEMLYY KVLESVIEQE QKRLGDMDLS GILEQDAFHR SLLACCLEVV 540 TFSYKPPGNF PFITEIFDVP LYHFYKVIEV FIRAEDGLCR EVVKHLNQIE EQILDHLAWK 600 PESPLWEKIR DNENRVPTCE EVMPPQNLER ADEICIAGSP LTPRRVTEVR ADTGGLGRSI 660 TSPTTLYDRY SSPPASTTRR RLFVENDSPS DGGTPGRMPP QPLVNAVPVQ NVSGETVSVT 720 PVPGQTLVTM ATATVTANNG QTVTIPVQGI ANENGGITFF PVQVNVGGQA QAVTGSIQPL 780 SAQALAGSLS SQQVTGTTLQ VPGQVAIQQI SPGGQQQKQG QSVTSSSNRP RKTSSLSLFF 840 RKVYHLAAVR LRDLCAKLDI SDELRKKIWT CFEFSIIQCP ELMMDRHLDQ LLMCAIYVMA 900 KVTKEDKSFQ NIMRCYRTQP QARSQVYRSV LIKGKRKRRN SGSSDSRSHQ NSPTELNKDR 960 TSRDSSPVMR SSSTLPVPQP SSAPPTPTRL TGANSDMEEE ERGDLIQFYN NIYIKQIKTF 1020 AMKYSQANMD APPLSPYPFV RTGSPRRIQL SQNHPVYISP HKNETMLSPR EKIFYYFSNS 1080 PSKRLREINS MIRTGETPTK KRGILLEDGS ESPAKRICPE NHSALLRRLQ DVANDRGSH 1140 |
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| Database | Annotation |
|---|---|
| CTD (Curated) (count: 3) | MESH:D008106
; Liver Cirrhosis, Experimental MESH:D015451 ; Leukemia, Lymphocytic, Chronic, B-Cell MESH:D010051 ; Ovarian Neoplasms |
| GWASdb (count: 8) (view all) | rs1074182; Tuberculosis; tuberculosis
rs16952252; Multiple complex diseases; Null rs9929873; Multiple complex diseases; Null rs7204496; Multiple complex diseases; Null rs8061388; Multiple complex diseases; Null rs8043918; Multiple complex diseases; Null |
| PTM | Modification Sites |
|---|---|
| Phosphorylation (count: 68) (view all) | 1019 IYIKQIKTFAMKYSQ dbPAF
1035 NMDAPPLSPYPFVRT dbPAF 1037 DAPPLSPYPFVRTGS dbPAF 1042 SPYPFVRTGSPRRIQ dbPAF 1044 YPFVRTGSPRRIQLS dbPAF 1051 SPRRIQLSQNHPVYI dbPAF |
| Ubiquitination (count: 1) | 384 TAERVQMKNILQQHF PLMD |