RBBP4_HUMAN - dbPTM
RBBP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBBP4_HUMAN
UniProt AC Q09028
Protein Name Histone-binding protein RBBP4
Gene Name RBBP4
Organism Homo sapiens (Human).
Sequence Length 425
Subcellular Localization Nucleus.
Protein Description Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex..
Protein Sequence MADKEAAFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEKGEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIATKTPSSDVLVFDYTKHPSKPDPSGECNPDLRLRGHQKEGYGLSWNPNLSGHLLSASDDHTICLWDISAVPKEGKVVDAKTIFTGHTAVVEDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQMAENIYNDEDPEGSVDPEGQGS
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
2Acetylation------MADKEAAFD
------CCCHHHHHC		36.2622223895
4Sumoylation----MADKEAAFDDA
----CCCHHHHHCHH		39.4528112733
4Acetylation----MADKEAAFDDA
----CCCHHHHHCHH		39.4519608861
4 (in isoform 2)Ubiquitination-39.45-
4Ubiquitination----MADKEAAFDDA
----CCCHHHHHCHH		39.4533845483
15MethylationFDDAVEERVINEEYK
HCHHHHHHHHCHHHH		22.55115490383
21AcetylationERVINEEYKIWKKNT
HHHHCHHHHHHHCCC		11.1219608861
21PhosphorylationERVINEEYKIWKKNT
HHHHCHHHHHHHCCC		11.1225106551
21UbiquitinationERVINEEYKIWKKNT
HHHHCHHHHHHHCCC		11.1223000965
22SumoylationRVINEEYKIWKKNTP
HHHCHHHHHHHCCCH		45.42-
22SumoylationRVINEEYKIWKKNTP
HHHCHHHHHHHCCCH		45.4219608861
22UbiquitinationRVINEEYKIWKKNTP
HHHCHHHHHHHCCCH		45.4223000965
22AcetylationRVINEEYKIWKKNTP
HHHCHHHHHHHCCCH		45.4223749302
24UbiquitinationINEEYKIWKKNTPFL
HCHHHHHHHCCCHHH		11.0421890473
25UbiquitinationNEEYKIWKKNTPFLY
CHHHHHHHCCCHHHH		39.3523000965
26UbiquitinationEEYKIWKKNTPFLYD
HHHHHHHCCCHHHHH		51.5723000965
55MethylationQWLPDVTRPEGKDFS
EECCCCCCCCCCCCE		27.4124390899
67UbiquitinationDFSIHRLVLGTHTSD
CCEEEEEEECCCCCC		4.7029967540
96PhosphorylationDDAQFDASHYDSEKG
CCCCCCHHHCCCCCC		25.1528796482
98PhosphorylationAQFDASHYDSEKGEF
CCCCHHHCCCCCCCC		20.7628796482
100PhosphorylationFDASHYDSEKGEFGG
CCHHHCCCCCCCCCC		33.7628796482
101UbiquitinationDASHYDSEKGEFGGF
CHHHCCCCCCCCCCC		63.2829967540
102UbiquitinationASHYDSEKGEFGGFG
HHHCCCCCCCCCCCC		68.6329967540
108UbiquitinationEKGEFGGFGSVSGKI
CCCCCCCCCCCCCEE		7.2521963094
110PhosphorylationGEFGGFGSVSGKIEI
CCCCCCCCCCCEEEE		15.7330266825
112PhosphorylationFGGFGSVSGKIEIEI
CCCCCCCCCEEEEEE		35.7530266825
121UbiquitinationKIEIEIKINHEGEVN
EEEEEEEECCCCCCC		8.5921963094
125UbiquitinationEIKINHEGEVNRARY
EEEECCCCCCCCEEE		36.2821963094
142UbiquitinationQNPCIIATKTPSSDV
CCCEEEEECCCCCCE		25.6621963094
143UbiquitinationNPCIIATKTPSSDVL
CCEEEEECCCCCCEE		49.7921963094
144PhosphorylationPCIIATKTPSSDVLV
CEEEEECCCCCCEEE		24.8530266825
146PhosphorylationIIATKTPSSDVLVFD
EEEECCCCCCEEEEE		44.3930266825
147PhosphorylationIATKTPSSDVLVFDY
EEECCCCCCEEEEEC		32.7030266825
154PhosphorylationSDVLVFDYTKHPSKP
CCEEEEECCCCCCCC		13.2628152594
154NitrationSDVLVFDYTKHPSKP
CCEEEEECCCCCCCC		13.26-
155PhosphorylationDVLVFDYTKHPSKPD
CEEEEECCCCCCCCC		25.4028152594
155UbiquitinationDVLVFDYTKHPSKPD
CEEEEECCCCCCCCC		25.4021963094
156UbiquitinationVLVFDYTKHPSKPDP
EEEEECCCCCCCCCC		47.4921963094
156AcetylationVLVFDYTKHPSKPDP
EEEEECCCCCCCCCC		47.4925953088
159PhosphorylationFDYTKHPSKPDPSGE
EECCCCCCCCCCCCC		57.44-
159UbiquitinationFDYTKHPSKPDPSGE
EECCCCCCCCCCCCC		57.4421963094
160UbiquitinationDYTKHPSKPDPSGEC
ECCCCCCCCCCCCCC		58.8721963094
160SumoylationDYTKHPSKPDPSGEC
ECCCCCCCCCCCCCC		58.87-
160SumoylationDYTKHPSKPDPSGEC
ECCCCCCCCCCCCCC		58.87-
160AcetylationDYTKHPSKPDPSGEC
ECCCCCCCCCCCCCC		58.8723749302
177UbiquitinationDLRLRGHQKEGYGLS
CCCCCCCCCCCCCCC		48.6029967540
178UbiquitinationLRLRGHQKEGYGLSW
CCCCCCCCCCCCCCC		47.6429967540
185UbiquitinationKEGYGLSWNPNLSGH
CCCCCCCCCCCCCCE		29.3729967540
190O-linked_GlycosylationLSWNPNLSGHLLSAS
CCCCCCCCCEEEECC		30.7023301498
215AcetylationSAVPKEGKVVDAKTI
CCCCCCCCEECCEEE		39.9323749302
219UbiquitinationKEGKVVDAKTIFTGH
CCCCEECCEEEECCC		10.1629967540
220UbiquitinationEGKVVDAKTIFTGHT
CCCEECCEEEECCCE		37.3829967540
229UbiquitinationIFTGHTAVVEDVSWH
EECCCEEEEEEHHHH		5.2129967540
258MethylationKLMIWDTRSNNTSKP
EEEEEECCCCCCCCC		34.61-
263UbiquitinationDTRSNNTSKPSHSVD
ECCCCCCCCCCCCCC		44.7029967540
264AcetylationTRSNNTSKPSHSVDA
CCCCCCCCCCCCCCC		48.8026051181
264UbiquitinationTRSNNTSKPSHSVDA
CCCCCCCCCCCCCCC		48.8029967540
274UbiquitinationHSVDAHTAEVNCLSF
CCCCCCEEEEEEEEC		14.6329967540
278GlutathionylationAHTAEVNCLSFNPYS
CCEEEEEEEECCCCC		3.9922555962
280PhosphorylationTAEVNCLSFNPYSEF
EEEEEEEECCCCCCE		25.7728152594
282UbiquitinationEVNCLSFNPYSEFIL
EEEEEECCCCCCEEE		31.0932015554
284PhosphorylationNCLSFNPYSEFILAT
EEEECCCCCCEEEEC		23.1828152594
285PhosphorylationCLSFNPYSEFILATG
EEECCCCCCEEEECC		27.5628152594
291PhosphorylationYSEFILATGSADKTV
CCCEEEECCCCCCEE		28.3728152594
293PhosphorylationEFILATGSADKTVAL
CEEEECCCCCCEEEE		29.0128152594
297PhosphorylationATGSADKTVALWDLR
ECCCCCCEEEEEEHH		16.1421712546
304MethylationTVALWDLRNLKLKLH
EEEEEEHHCCEEEEE		43.92-
307SumoylationLWDLRNLKLKLHSFE
EEEHHCCEEEEEEEH		47.31-
308UbiquitinationWDLRNLKLKLHSFES
EEHHCCEEEEEEEHH		8.8729967540
309UbiquitinationDLRNLKLKLHSFESH
EHHCCEEEEEEEHHH		42.4329967540
312PhosphorylationNLKLKLHSFESHKDE
CCEEEEEEEHHHCCC		40.9429038488
314UbiquitinationKLKLHSFESHKDEIF
EEEEEEEHHHCCCEE		55.7521963094
316UbiquitinationKLHSFESHKDEIFQV
EEEEEHHHCCCEEEE		34.1032015554
317UbiquitinationLHSFESHKDEIFQVQ
EEEEHHHCCCEEEEE		67.3532015554
326PhosphorylationEIFQVQWSPHNETIL
CEEEEEECCCCCEEE		10.13-
341MethylationASSGTDRRLNVWDLS
CCCCCCCCCCEEEHH		33.16-
348UbiquitinationRLNVWDLSKIGEEQS
CCCEEEHHHCCCCCC		21.5421963094
348PhosphorylationRLNVWDLSKIGEEQS
CCCEEEHHHCCCCCC		21.5421815630
349UbiquitinationLNVWDLSKIGEEQSP
CCEEEHHHCCCCCCH		63.1321963094
355PhosphorylationSKIGEEQSPEDAEDG
HHCCCCCCHHHCCCC		33.2730266825
374PhosphorylationLFIHGGHTAKISDFS
EEEECCCEEEECCCC		32.68-
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

Oops, there are no upstream regulatory protein records of RBBP4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBBP4_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 RBBP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
12943729
HDAC2_HUMANHDAC2physical
12943729
HDAC1_HUMANHDAC1physical
11470869
HDAC3_HUMANHDAC3physical
11470869
P66B_HUMANGATAD2Bphysical
11756549
BRCA1_HUMANBRCA1physical
10220405
HDAC1_HUMANHDAC1physical
9150133
SIN3A_HUMANSIN3Aphysical
9651585
SAP30_HUMANSAP30physical
9651585
HDAC1_HUMANHDAC1physical
12091390
HDAC2_HUMANHDAC2physical
12091390
CBP_HUMANCREBBPphysical
10866654
XRCC6_HUMANXRCC6physical
16169070
AEBP2_HUMANAEBP2physical
15225548
EED_HUMANEEDphysical
15225548
SUZ12_HUMANSUZ12physical
15225548
BAF_HUMANBANF1physical
19759913
P66A_HUMANGATAD2Aphysical
16738318
P66B_HUMANGATAD2Bphysical
16738318
BC11B_HUMANBCL11Bphysical
16091750
MTA2_HUMANMTA2physical
11602581
SIN3A_HUMANSIN3Aphysical
11602581
HDAC1_HUMANHDAC1physical
11602581
CHD4_HUMANCHD4physical
9790534
HDAC1_HUMANHDAC1physical
17827154
HDAC2_HUMANHDAC2physical
17827154
FOG1_HUMANZFPM1physical
21047798
LIN9_HUMANLIN9physical
17671431
NR2C2_HUMANNR2C2physical
21670149
NR2C1_HUMANNR2C1physical
21670149
DNMT1_HUMANDNMT1physical
21670149
KDM1A_HUMANKDM1Aphysical
21670149
HDAC1_HUMANHDAC1physical
21670149
HDAC2_HUMANHDAC2physical
21670149
MTA2_HUMANMTA2physical
21670149
MTA1_HUMANMTA1physical
21670149
CHD4_HUMANCHD4physical
21670149
MBD3_HUMANMBD3physical
21670149
DPOD3_HUMANPOLD3physical
21670149
RBBP7_HUMANRBBP7physical
22939629
SUZ12_HUMANSUZ12physical
22939629
SMCA5_HUMANSMARCA5physical
22939629
SMCA1_HUMANSMARCA1physical
22939629
TERA_HUMANVCPphysical
22939629
H4_XENLAhist1h4aphysical
23178455
TSSK3_HUMANTSSK3physical
21988832
MTPN_HUMANMTPNphysical
22863883
PDIA3_HUMANPDIA3physical
22863883
RB_HUMANRB1physical
8350924
NACC2_HUMANNACC2physical
22926524
HAT1_HUMANHAT1physical
25416956
MTA1_HUMANMTA1physical
25416956
PHF6_HUMANPHF6physical
22720776
MTA1_HUMANMTA1physical
24920672
GNL3_HUMANGNL3physical
26344197
HAT1_HUMANHAT1physical
26344197
HDAC2_HUMANHDAC2physical
26344197
MTA1_HUMANMTA1physical
26344197
MTA2_HUMANMTA2physical
26344197
MTA3_HUMANMTA3physical
26344197
IMA5_HUMANKPNA1physical
26491019
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 RBBP4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-146, AND MASS SPECTROMETRY.
"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-4, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-146, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-4, AND MASS SPECTROMETRY.

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