RBBP5_HUMAN - dbPTM
RBBP5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBBP5_HUMAN
UniProt AC Q15291
Protein Name Retinoblastoma-binding protein 5
Gene Name RBBP5
Organism Homo sapiens (Human).
Sequence Length 538
Subcellular Localization Nucleus .
Protein Description 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 (By similarity). 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..
Protein Sequence MNLELLESFGQNYPEEADGTLDCISMALTCTFNRWGTLLAVGCNDGRIVIWDFLTRGIAKIISAHIHPVCSLCWSRDGHKLVSASTDNIVSQWDVLSGDCDQRFRFPSPILKVQYHPRDQNKVLVCPMKSAPVMLTLSDSKHVVLPVDDDSDLNVVASFDRRGEYIYTGNAKGKILVLKTDSQDLVASFRVTTGTSNTTAIKSIEFARKGSCFLINTADRIIRVYDGREILTCGRDGEPEPMQKLQDLVNRTPWKKCCFSGDGEYIVAGSARQHALYIWEKSIGNLVKILHGTRGELLLDVAWHPVRPIIASISSGVVSIWAQNQVENWSAFAPDFKELDENVEYEERESEFDIEDEDKSEPEQTGADAAEDEEVDVTSVDPIAAFCSSDEELEDSKALLYLPIAPEVEDPEENPYGPPPDAVQTSLMDEGASSEKKRQSSADGSQPPKKKPKTTNIELQGVPNDEVHPLLGVKGDGKSKKKQAGRPKGSKGKEKDSPFKPKLYKGDRGLPLEGSAKGKVQAELSQPLTAGGAISELL
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
8PhosphorylationMNLELLESFGQNYPE
CCHHHHHHHCCCCCH		34.3522817900
13PhosphorylationLESFGQNYPEEADGT
HHHHCCCCCHHCCCC		12.2522817900
20PhosphorylationYPEEADGTLDCISMA
CCHHCCCCHHHHHHH		21.7022817900
55PhosphorylationIVIWDFLTRGIAKII
EEEEECHHHHHHHHH		27.1820860994
108PhosphorylationDQRFRFPSPILKVQY
CCCCCCCCCEEEEEE		23.1224719451
112UbiquitinationRFPSPILKVQYHPRD
CCCCCEEEEEECCCC		28.19-
122UbiquitinationYHPRDQNKVLVCPMK
ECCCCCCCEEEEECC		31.17-
129SumoylationKVLVCPMKSAPVMLT
CEEEEECCCCCEEEE		28.7128112733
129UbiquitinationKVLVCPMKSAPVMLT
CEEEEECCCCCEEEE		28.71-
130PhosphorylationVLVCPMKSAPVMLTL
EEEEECCCCCEEEEC		31.3919664994
136PhosphorylationKSAPVMLTLSDSKHV
CCCCEEEECCCCCEE		13.2021406692
138PhosphorylationAPVMLTLSDSKHVVL
CCEEEECCCCCEEEE		34.3020068231
140PhosphorylationVMLTLSDSKHVVLPV
EEEECCCCCEEEEEC		22.6821406692
162MethylationVVASFDRRGEYIYTG
EEEEEECCCCEEEEC		44.11115490407
165PhosphorylationSFDRRGEYIYTGNAK
EEECCCCEEEECCCC		11.3120068231
167PhosphorylationDRRGEYIYTGNAKGK
ECCCCEEEECCCCCE		14.0020068231
168PhosphorylationRRGEYIYTGNAKGKI
CCCCEEEECCCCCEE		17.8820068231
172UbiquitinationYIYTGNAKGKILVLK
EEEECCCCCEEEEEE		65.81-
180PhosphorylationGKILVLKTDSQDLVA
CEEEEEECCCCCEEE		36.4020068231
182PhosphorylationILVLKTDSQDLVASF
EEEEECCCCCEEEEE		30.7217525332
188PhosphorylationDSQDLVASFRVTTGT
CCCCEEEEEEEEECC		13.2020068231
193PhosphorylationVASFRVTTGTSNTTA
EEEEEEEECCCCCCE		35.2917525332
195PhosphorylationSFRVTTGTSNTTAIK
EEEEEECCCCCCEEE		19.4020860994
196PhosphorylationFRVTTGTSNTTAIKS
EEEEECCCCCCEEEE		33.2629759185
198PhosphorylationVTTGTSNTTAIKSIE
EEECCCCCCEEEEEE		19.8520860994
199PhosphorylationTTGTSNTTAIKSIEF
EECCCCCCEEEEEEE		30.5420860994
202MalonylationTSNTTAIKSIEFARK
CCCCCEEEEEEEHHC		42.8026320211
202UbiquitinationTSNTTAIKSIEFARK
CCCCCEEEEEEEHHC		42.80-
202AcetylationTSNTTAIKSIEFARK
CCCCCEEEEEEEHHC		42.8026051181
209AcetylationKSIEFARKGSCFLIN
EEEEEHHCCCEEEEE		52.3126051181
211PhosphorylationIEFARKGSCFLINTA
EEEHHCCCEEEEECC		12.5323927012
244 (in isoform 2)Ubiquitination-41.6921890473
244UbiquitinationGEPEPMQKLQDLVNR
CCCCHHHHHHHHHHC		41.6921890473
252PhosphorylationLQDLVNRTPWKKCCF
HHHHHHCCCCCCCCC		28.4425159151
256UbiquitinationVNRTPWKKCCFSGDG
HHCCCCCCCCCCCCC		32.16-
279 (in isoform 1)Ubiquitination-8.0721890473
281AcetylationHALYIWEKSIGNLVK
CCEEEEHHHHHHHHH		32.1719608861
345PhosphorylationELDENVEYEERESEF
HHHHCCCHHHHHCCC		20.8623917254
350PhosphorylationVEYEERESEFDIEDE
CCHHHHHCCCCCCCC		50.1928355574
378PhosphorylationEDEEVDVTSVDPIAA
CCCCCCCCEECHHHH		20.6927251275
379PhosphorylationDEEVDVTSVDPIAAF
CCCCCCCEECHHHHH		25.1127251275
388PhosphorylationDPIAAFCSSDEELED
CHHHHHCCCCHHHCC		34.0817081983
389PhosphorylationPIAAFCSSDEELEDS
HHHHHCCCCHHHCCC		50.6617081983
396PhosphorylationSDEELEDSKALLYLP
CCHHHCCCCEEEEEE		15.5126074081
397SumoylationDEELEDSKALLYLPI
CHHHCCCCEEEEEEC		56.21-
401PhosphorylationEDSKALLYLPIAPEV
CCCCEEEEEECCCCC		15.9826074081
425PhosphorylationPPPDAVQTSLMDEGA
CCCCHHHHHHCCCCC		19.7528348404
426PhosphorylationPPDAVQTSLMDEGAS
CCCHHHHHHCCCCCC		12.4722210691
433PhosphorylationSLMDEGASSEKKRQS
HHCCCCCCCHHHHHC		50.3028348404
434PhosphorylationLMDEGASSEKKRQSS
HCCCCCCCHHHHHCC		53.5622210691
440PhosphorylationSSEKKRQSSADGSQP
CCHHHHHCCCCCCCC		31.3728985074
441PhosphorylationSEKKRQSSADGSQPP
CHHHHHCCCCCCCCC		23.2625262027
445PhosphorylationRQSSADGSQPPKKKP
HHCCCCCCCCCCCCC		39.8120446291
455PhosphorylationPKKKPKTTNIELQGV
CCCCCCCCCEEEECC		40.0828555341
474AcetylationVHPLLGVKGDGKSKK
CCCCCCCCCCCCCCC		49.8726051181
490 (in isoform 2)Phosphorylation-44.3420068231
497PhosphorylationSKGKEKDSPFKPKLY
CCCCCCCCCCCCCCC		43.2223401153
500AcetylationKEKDSPFKPKLYKGD
CCCCCCCCCCCCCCC		44.6323749302
515PhosphorylationRGLPLEGSAKGKVQA
CCCCCCCCCCCCEEE		19.8925159151
517AcetylationLPLEGSAKGKVQAEL
CCCCCCCCCCEEEEE		62.0525953088
525PhosphorylationGKVQAELSQPLTAGG
CCEEEEECCCCCCCC		22.6625159151
529PhosphorylationAELSQPLTAGGAISE
EEECCCCCCCCHHHH		29.9123663014
535PhosphorylationLTAGGAISELL----
CCCCCHHHHHC----		22.9720068231
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
252TPhosphorylationKinaseCDK1P06493
Uniprot
497SPhosphorylationKinaseCDK1P06493
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBBP5_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KMT2A_HUMANKMT2Aphysical
15199122
WDR5_HUMANWDR5physical
15199122
ASCL2_HUMANASCL2physical
12482968
KMT2C_HUMANKMT2Cphysical
12482968
H32_HUMANHIST2H3Cphysical
12482968
RB_HUMANRB1physical
7558034
CXXC1_HUMANCXXC1physical
16253997
ASH2L_HUMANASH2Lphysical
16253997
SET1A_HUMANSETD1Aphysical
17355966
SET1B_HUMANSETD1Bphysical
17355966
KMT2A_HUMANKMT2Aphysical
20064463
WDR5_HUMANWDR5physical
17041588
DDB1_HUMANDDB1physical
17041588
KMT2A_HUMANKMT2Aphysical
15960975
KAT8_HUMANKAT8physical
15960975
ASH2L_HUMANASH2Lphysical
15960974
WDR5_HUMANWDR5physical
15960974
KMT2D_HUMANKMT2Dphysical
15960974
WDR5_HUMANWDR5physical
17925232
PAXI1_HUMANPAXIP1physical
17925232
ASH2L_HUMANASH2Lphysical
17925232
NCOA6_HUMANNCOA6physical
17925232
PAXI1_HUMANPAXIP1physical
17500065
NCOA6_HUMANNCOA6physical
17500065
ASH2L_HUMANASH2Lphysical
17500065
RBBP5_HUMANRBBP5physical
17500065
ASH2L_HUMANASH2Lphysical
21220120
WDR5_HUMANWDR5physical
21220120
H31T_HUMANHIST3H3physical
21124902
KMT2D_HUMANKMT2Dphysical
16603732
ASH2L_HUMANASH2Lphysical
16603732
WDR5_HUMANWDR5physical
16603732
KDM4B_HUMANKDM4Bphysical
21502505
KANL1_HUMANKANSL1physical
21502505
KMT2B_HUMANKMT2Bphysical
21502505
ESR1_HUMANESR1physical
21502505
ASH2L_HUMANASH2Lphysical
21124902
ASH2L_HUMANASH2Lphysical
20305087
CXXC1_HUMANCXXC1physical
20305087
DPY30_HUMANDPY30physical
20305087
HCFC1_HUMANHCFC1physical
20305087
SET1A_HUMANSETD1Aphysical
20305087
WDR5_HUMANWDR5physical
20305087
MEN1_HUMANMEN1physical
14992727
SET1A_HUMANSETD1Aphysical
22939629
SMRC1_HUMANSMARCC1physical
22939629
SMCE1_HUMANSMARCE1physical
22939629
SMRD2_HUMANSMARCD2physical
22939629
SRRT_HUMANSRRTphysical
22939629
SMRD1_HUMANSMARCD1physical
22939629
ASH2L_HUMANASH2Lphysical
25416956
WDR33_HUMANWDR33physical
26344197
ARCH_HUMANZBTB8OSphysical
26344197
TBA1A_HUMANTUBA1Aphysical
12482968
ASH2L_HUMANASH2Lphysical
21516116
CHD7_HUMANCHD7physical
24705355
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBBP5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-281, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND THR-193, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-388; SER-389AND SER-497, AND MASS SPECTROMETRY.

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