RBBP7_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RBBP7_MOUSE
• UniProt AC: Q60973
• Protein Name: Histone-binding protein RBBP7
• Gene Name: Rbbp7
• Organism: Mus musculus (Mouse).
• Sequence Length: 425
• Subcellular Localization: Nucleus.
• Protein Description: Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases 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 type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; 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; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex (By similarity)..
• Protein Sequence: MASKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALQWPSLTVQWLPEVTKPEGKDYALHWLVLGTHTSDEQNHLVVARVHIPNDDAQFDASHCDSDKGEFGGFGSVTGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSDVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAIFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHTFESHKDEIFQVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEESDVTASELEGQGS

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
2	Acetylation	------MASKEMFED ------CCCHHHHHH	29.34	23806337
3	Phosphorylation	-----MASKEMFEDT -----CCCHHHHHHH	28.05	25266776
4	Acetylation	----MASKEMFEDTV ----CCCHHHHHHHH	43.59	23806337
10	Phosphorylation	SKEMFEDTVEERVIN CHHHHHHHHHHHHHC	23.71	28066266
25	Ubiquitination	EEYKIWKKNTPFLYD HHHHHHHCCCHHHHH	51.57	-
45	Phosphorylation	ALQWPSLTVQWLPEV HHHCCCEEEEECCCC	18.26	-
53	Phosphorylation	VQWLPEVTKPEGKDY EEECCCCCCCCCCCE	38.94	-
95	Phosphorylation	DDAQFDASHCDSDKG CCCCCCHHHCCCCCC	26.88	25619855
99	Phosphorylation	FDASHCDSDKGEFGG CCHHHCCCCCCCCCC	46.76	22817900
101	Ubiquitination	ASHCDSDKGEFGGFG HHHCCCCCCCCCCCC	65.38	-
109	Phosphorylation	GEFGGFGSVTGKIEC CCCCCCCEECEEEEE	17.78	28066266
111	Phosphorylation	FGGFGSVTGKIECEI CCCCCEECEEEEEEE	34.16	28066266
119	Acetylation	GKIECEIKINHEGEV EEEEEEEEECCCCCC	18.37	23806337
119	Malonylation	GKIECEIKINHEGEV EEEEEEEEECCCCCC	18.37	26320211
143	Phosphorylation	PHIIATKTPSSDVLV CCEEEECCCCCCEEE	24.85	28066266
145	Phosphorylation	IIATKTPSSDVLVFD EEEECCCCCCEEEEE	44.39	28833060
146	Phosphorylation	IATKTPSSDVLVFDY EEECCCCCCEEEEEC	32.70	26643407
153	Phosphorylation	SDVLVFDYTKHPAKP CCEEEEECCCCCCCC	13.26	25777480
154	Phosphorylation	DVLVFDYTKHPAKPD CEEEEECCCCCCCCC	25.40	25777480
159	Acetylation	DYTKHPAKPDPSGEC ECCCCCCCCCCCCCC	55.17	23806337
166	Glutathionylation	KPDPSGECNPDLRLR CCCCCCCCCCCCCCC	11.62	24333276
166	S-nitrosocysteine	KPDPSGECNPDLRLR CCCCCCCCCCCCCCC	11.62	-
166	S-nitrosylation	KPDPSGECNPDLRLR CCCCCCCCCCCCCCC	11.62	21278135
171	Methylation	GECNPDLRLRGHQKE CCCCCCCCCCCCCCC	29.71	24333051
200	O-linked_Glycosylation	LSASDDHTVCLWDIN EECCCCCEEEEEECC	21.65	51588379
256	Phosphorylation	QKLMIWDTRSNTTSK CCEEEEECCCCCCCC	22.47	22006019
265	Phosphorylation	SNTTSKPSHLVDAHT CCCCCCCHHEEECCC	32.94	23649490
279	Phosphorylation	TAEVNCLSFNPYSEF CCEEEEEECCCCCCE	25.77	23649490
347	Phosphorylation	RLNVWDLSKIGEEQS CCEEEEHHHHCCCCC	21.54	27600695
354	Phosphorylation	SKIGEEQSAEDAEDG HHHCCCCCHHHCCCC	36.58	26824392
373	Phosphorylation	LFIHGGHTAKISDFS EEEECCCEEEECCCC	32.68	25619855

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RBBP7_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RBBP7_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RBBP7_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC1_MOUSE	Hdac1	physical	20211142
SUMO1_MOUSE	Sumo1	physical	19189660

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.
PubMed: 19367708