| Tag | Content |
|---|
| CPLM ID | CPLM-016641 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Retinoblastoma-binding protein 5 |
Protein Synonyms/Alias | RBBP-5 |
Gene Name | Rbbp5 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 244 | GEPEPMQKLQDLVNR | ubiquitination | [1] |
|
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] |
Functional Description | As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal. |
Sequence Annotation | REPEAT 22 63 WD 1.
REPEAT 64 103 WD 2.
REPEAT 148 188 WD 3.
REPEAT 196 235 WD 4.
REPEAT 249 291 WD 5.
REPEAT 293 331 WD 6.
MOD_RES 252 252 Phosphothreonine; by CDK1 (By
MOD_RES 350 350 Phosphoserine (By similarity).
MOD_RES 388 388 Phosphoserine (By similarity).
MOD_RES 389 389 Phosphoserine (By similarity).
MOD_RES 497 497 Phosphoserine; by CDK1 (By similarity).
MOD_RES 525 525 Phosphoserine (By similarity). |
Keyword | 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; WD repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 538 AA |
Protein Sequence | MNLELLESFG QNYPEEADGT LDCISMALTC TFNRWGTLLA VGCNDGRIVI WDFLTRGIAK 60
IISAHIHPVC SLCWSRDGHK LVSASTDNIV SQWDVLSGDC DQRFRFPSPI LKVQYHPRDQ 120
NKVLVCPMKS APVMLTLSDS KHVVLPVDDD SDLNVVASFD RRGEYIYTGN AKGKILVLKT 180
DSQDLVASFR VTTGTSNTTA IKSIEFARKG SCFLINTADR IIRVYDGREI LTCGRDGEPE 240
PMQKLQDLVN RTPWKKCCFS GDGEYIVAGS ARQHALYIWE KSIGNLVKIL HGTRGELLLD 300
VAWHPVRPII ASISSGVVSI WAQNQVENWS AFAPDFKELD ENVEYEERES EFDIEDEDKS 360
EPEQTGADAA EDEEVDVTSV DPIAAFCSSD EELEDSKALL YLPIAPEVED PEENPYGPPP 420
DAVPSSLMDE GASSEKKRQS SADGSQPPKK KPKTTNIELQ GVPNDEVHPL LGVKGDGKSK 480
KKQAGRPKGS KGKEKDSPFK PKLYKGDRGL PLEGSTKGKV QAELSQSLAA GGAISELL 538 |
Gene Ontology | GO:0071339; C:MLL1 complex; ISS:UniProtKB. GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB. GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:Compara. GO:0044212; F:transcription regulatory region DNA binding; IEA:Compara. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006974; P:response to DNA damage stimulus; ISO:MGI. GO:0043627; P:response to estrogen stimulus; IEA:Compara. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |