RBBP5_MOUSE - dbPTM
RBBP5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBBP5_MOUSE
UniProt AC Q8BX09
Protein Name Retinoblastoma-binding protein 5
Gene Name Rbbp5
Organism Mus musculus (Mouse).
Sequence Length 538
Subcellular Localization Nucleus.
Protein 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..
Protein Sequence MNLELLESFGQNYPEEADGTLDCISMALTCTFNRWGTLLAVGCNDGRIVIWDFLTRGIAKIISAHIHPVCSLCWSRDGHKLVSASTDNIVSQWDVLSGDCDQRFRFPSPILKVQYHPRDQNKVLVCPMKSAPVMLTLSDSKHVVLPVDDDSDLNVVASFDRRGEYIYTGNAKGKILVLKTDSQDLVASFRVTTGTSNTTAIKSIEFARKGSCFLINTADRIIRVYDGREILTCGRDGEPEPMQKLQDLVNRTPWKKCCFSGDGEYIVAGSARQHALYIWEKSIGNLVKILHGTRGELLLDVAWHPVRPIIASISSGVVSIWAQNQVENWSAFAPDFKELDENVEYEERESEFDIEDEDKSEPEQTGADAAEDEEVDVTSVDPIAAFCSSDEELEDSKALLYLPIAPEVEDPEENPYGPPPDAVPSSLMDEGASSEKKRQSSADGSQPPKKKPKTTNIELQGVPNDEVHPLLGVKGDGKSKKKQAGRPKGSKGKEKDSPFKPKLYKGDRGLPLEGSTKGKVQAELSQSLAAGGAISELL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
192PhosphorylationLVASFRVTTGTSNTT
EEEEEEEEECCCCCC
18.4329895711
193PhosphorylationVASFRVTTGTSNTTA
EEEEEEEECCCCCCE
35.2929895711
195PhosphorylationSFRVTTGTSNTTAIK
EEEEEECCCCCCEEE
19.4029895711
196PhosphorylationFRVTTGTSNTTAIKS
EEEEECCCCCCEEEE
33.2629895711
198PhosphorylationVTTGTSNTTAIKSIE
EEECCCCCCEEEEEE
19.8529895711
209AcetylationKSIEFARKGSCFLIN
EEEEEHHCCCEEEEE
52.317712699
244UbiquitinationGEPEPMQKLQDLVNR
CCCCHHHHHHHHHHC
41.6922790023
252PhosphorylationLQDLVNRTPWKKCCF
HHHHHHCCCCCCCCC
28.44-
345PhosphorylationELDENVEYEERESEF
HHHHCCCHHHHHCCC
20.8626643407
350PhosphorylationVEYEERESEFDIEDE
CCHHHHHCCCCCCCC
50.1925521595
388PhosphorylationDPIAAFCSSDEELED
CHHHHHCCCCHHHCC
34.0825195567
389PhosphorylationPIAAFCSSDEELEDS
HHHHHCCCCHHHCCC
50.6625195567
440PhosphorylationSSEKKRQSSADGSQP
CCHHHHHCCCCCCCC
31.3725266776
441PhosphorylationSEKKRQSSADGSQPP
CHHHHHCCCCCCCCC
23.2623684622
445PhosphorylationRQSSADGSQPPKKKP
HHCCCCCCCCCCCCC
39.8129550500
497PhosphorylationSKGKEKDSPFKPKLY
CCCCCCCCCCCCCCC
43.2225266776
515PhosphorylationRGLPLEGSTKGKVQA
CCCCCCCCCCCHHHH
19.99-
516PhosphorylationGLPLEGSTKGKVQAE
CCCCCCCCCCHHHHH
55.46-
525PhosphorylationGKVQAELSQSLAAGG
CHHHHHHHHHHHHCC
14.82-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
252TPhosphorylationKinaseCDK1P11440
Uniprot
497SPhosphorylationKinaseCDK1P11440
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBBP5_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RBBP5_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR5_MOUSEWdr5physical
17825402
ASH2L_MOUSEAsh2lphysical
17825402
PHF20_MOUSEPhf20physical
23452852

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBBP5_MOUSE

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Related Literatures of Post-Translational Modification

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