MRGBP_HUMAN - dbPTM
MRGBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRGBP_HUMAN
UniProt AC Q9NV56
Protein Name MRG/MORF4L-binding protein
Gene Name MRGBP
Organism Homo sapiens (Human).
Sequence Length 204
Subcellular Localization Nucleus.
Protein Description Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage..
Protein Sequence MGEAEVGGGGAAGDKGPGEAATSPAEETVVWSPEVEVCLFHAMLGHKPVGVNRHFHMICIRDKFSQNIGRQVPSKVIWDHLSTMYDMQALHESEILPFPNPERNFVLPEEIIQEVREGKVMIEEEMKEEMKEDVDPHNGADDVFSSSGSLGKASEKSSKDKEKNSSDLGCKEGADKRKRSRVTDKVLTANSNPSSPSAAKRRRT
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------MGEAEVGGG
------CCCCCCCCC		42.7019413330
22PhosphorylationKGPGEAATSPAEETV
CCCCCCCCCCHHHCE		42.1428348404
23PhosphorylationGPGEAATSPAEETVV
CCCCCCCCCHHHCEE		19.8625159151
28PhosphorylationATSPAEETVVWSPEV
CCCCHHHCEECCCCH		16.3228348404
63AcetylationHMICIRDKFSQNIGR
EEEEECHHHHCCCCC		36.7525953088
127SumoylationVMIEEEMKEEMKEDV
CCCCHHHHHHHHHCC		54.5228112733
145PhosphorylationNGADDVFSSSGSLGK
CCHHHHHHCCCCCHH		24.3626471730
146PhosphorylationGADDVFSSSGSLGKA
CHHHHHHCCCCCHHH		27.5326471730
147PhosphorylationADDVFSSSGSLGKAS
HHHHHHCCCCCHHHC		31.0725159151
149PhosphorylationDVFSSSGSLGKASEK
HHHHCCCCCHHHCHH		35.5825849741
152AcetylationSSSGSLGKASEKSSK
HCCCCCHHHCHHCCC		54.7723236377
152UbiquitinationSSSGSLGKASEKSSK
HCCCCCHHHCHHCCC		54.7729967540
166PhosphorylationKDKEKNSSDLGCKEG
CHHHCCHHHCCCHHH		46.3728985074
171AcetylationNSSDLGCKEGADKRK
CHHHCCCHHHCCHHH		58.3425953088
183PhosphorylationKRKRSRVTDKVLTAN
HHHHHHHCCCEECCC		29.0624732914
185AcetylationKRSRVTDKVLTANSN
HHHHHCCCEECCCCC		29.7623954790
188PhosphorylationRVTDKVLTANSNPSS
HHCCCEECCCCCCCC		27.1230266825
191PhosphorylationDKVLTANSNPSSPSA
CCEECCCCCCCCHHH		47.8829255136
194PhosphorylationLTANSNPSSPSAAKR
ECCCCCCCCHHHHHH		60.1629255136
195PhosphorylationTANSNPSSPSAAKRR
CCCCCCCCHHHHHHC		24.9129255136
197PhosphorylationNSNPSSPSAAKRRRT
CCCCCCHHHHHHCCC		42.6929255136
200AcetylationPSSPSAAKRRRT---
CCCHHHHHHCCC---		46.2725953088
204PhosphorylationSAAKRRRT-------
HHHHHCCC-------		40.9426074081
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 MRGBP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MRGBP_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 MRGBP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRD8_HUMANBRD8physical
20051959
TRRAP_HUMANTRRAPphysical
12963728
BRD8_HUMANBRD8physical
12963728
EPC1_HUMANEPC1physical
12963728
HSP74_HUMANHSPA4physical
12963728
RL1D1_HUMANRSL1D1physical
12963728
DMAP1_HUMANDMAP1physical
12963728
KAT5_HUMANKAT5physical
12963728
RUVB1_HUMANRUVBL1physical
12963728
RUVB2_HUMANRUVBL2physical
12963728
ING1_HUMANING1physical
12963728
ACL6A_HUMANACTL6Aphysical
12963728
MO4L1_HUMANMORF4L1physical
12963728
MO4L2_HUMANMORF4L2physical
12963728
YETS4_HUMANYEATS4physical
12963728
EAF6_HUMANMEAF6physical
12963728
DIP2A_HUMANDIP2Aphysical
18218781
VPS72_HUMANVPS72physical
18218781
SRCAP_HUMANSRCAPphysical
17573780
BRD8_HUMANBRD8physical
17573780
EPC1_HUMANEPC1physical
17573780
EPC2_HUMANEPC2physical
17573780
IMB1_HUMANKPNB1physical
17573780
HNRPU_HUMANHNRNPUphysical
17573780
MBTD1_HUMANMBTD1physical
17573780
HSP74_HUMANHSPA4physical
17573780
HNRPM_HUMANHNRNPMphysical
17573780
LMNA_HUMANLMNAphysical
17573780
MO4L1_HUMANMORF4L1physical
17573780
DMAP1_HUMANDMAP1physical
17573780
HNRPK_HUMANHNRNPKphysical
17573780
TBB2A_HUMANTUBB2Aphysical
17573780
TBA1A_HUMANTUBA1Aphysical
17573780
IMA1_HUMANKPNA2physical
17573780
KAT5_HUMANKAT5physical
17573780
RBBP7_HUMANRBBP7physical
17573780
RUVB1_HUMANRUVBL1physical
17573780
RUVB2_HUMANRUVBL2physical
17573780
ACL6A_HUMANACTL6Aphysical
17573780
ACTS_HUMANACTA1physical
17573780
ACTB_HUMANACTBphysical
17573780
ACTG_HUMANACTG1physical
17573780
MO4L2_HUMANMORF4L2physical
17573780
MOFA1_HUMANMRFAP1physical
17573780
H2AV_HUMANH2AFVphysical
17573780
H2B2E_HUMANHIST2H2BEphysical
17573780
SIN3B_HUMANSIN3Bphysical
17573780
KR107_HUMANKRTAP10-7physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
DMAP1_HUMANDMAP1physical
26344197
MO4L1_HUMANMORF4L1physical
28514442
MO4L2_HUMANMORF4L2physical
28514442
CP250_HUMANCEP250physical
28514442
MBTD1_HUMANMBTD1physical
28514442
BRD8_HUMANBRD8physical
28514442
EP400_HUMANEP400physical
28514442
KAT5_HUMANKAT5physical
28514442
EPC1_HUMANEPC1physical
28514442
KCD21_HUMANKCTD21physical
28514442
EPC2_HUMANEPC2physical
28514442
ING3_HUMANING3physical
28514442
TRRAP_HUMANTRRAPphysical
28514442
VPS72_HUMANVPS72physical
28514442
YETS4_HUMANYEATS4physical
28514442
RUVB1_HUMANRUVBL1physical
28514442
DMAP1_HUMANDMAP1physical
28514442
IMA3_HUMANKPNA4physical
28514442
UBR7_HUMANUBR7physical
28514442
RUVB2_HUMANRUVBL2physical
28514442
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 MRGBP_HUMAN

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Related Literatures of Post-Translational Modification
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-191 AND SER-195, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-194; SER-195AND SER-197, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-195, ANDMASS SPECTROMETRY.

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