dbPTM

RBBP7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBBP7_HUMAN
UniProt AC	Q16576
Protein Name	Histone-binding protein RBBP7
Gene Name	RBBP7
Organism	Homo sapiens (Human).
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..
Protein Sequence	MASKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALQWPSLTVQWLPEVTKPEGKDYALHWLVLGTHTSDEQNHLVVARVHIPNDDAQFDASHCDSDKGEFGGFGSVTGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSDVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAIFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHTFESHKDEIFQVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEESDVTTSELEGQGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 2)	Acetylation	-	29.34	20068231
2	Acetylation	------MASKEMFED ------CCCHHHHHH	29.34	22814378
3	Phosphorylation	-----MASKEMFEDT -----CCCHHHHHHH	28.05	29255136
4	Sumoylation	----MASKEMFEDTV ----CCCHHHHHHHH	43.59	-
4	2-Hydroxyisobutyrylation	----MASKEMFEDTV ----CCCHHHHHHHH	43.59	-
4	Sumoylation	----MASKEMFEDTV ----CCCHHHHHHHH	43.59	28112733
4	Acetylation	----MASKEMFEDTV ----CCCHHHHHHHH	43.59	19608861
4	Ubiquitination	----MASKEMFEDTV ----CCCHHHHHHHH	43.59	19608861
6	Sulfoxidation	--MASKEMFEDTVEE --CCCHHHHHHHHHH	5.25	21406390
10	Phosphorylation	SKEMFEDTVEERVIN CHHHHHHHHHHHHHC	23.71	21712546
13 (in isoform 2)	Phosphorylation	-	48.16	30108239
14	Methylation	FEDTVEERVINEEYK HHHHHHHHHHCHHHH	22.55	115490439
20	Phosphorylation	ERVINEEYKIWKKNT HHHHCHHHHHHHCCC	11.12	25106551
21	Sumoylation	RVINEEYKIWKKNTP HHHCHHHHHHHCCCH	45.42	-
21	Acetylation	RVINEEYKIWKKNTP HHHCHHHHHHHCCCH	45.42	22636321
21	Ubiquitination	RVINEEYKIWKKNTP HHHCHHHHHHHCCCH	45.42	21890473
21	Sumoylation	RVINEEYKIWKKNTP HHHCHHHHHHHCCCH	45.42	-
24	Ubiquitination	NEEYKIWKKNTPFLY CHHHHHHHCCCHHHH	39.35	21890473
25	Ubiquitination	EEYKIWKKNTPFLYD HHHHHHHCCCHHHHH	51.57	-
27	Phosphorylation	YKIWKKNTPFLYDLV HHHHHCCCHHHHHHH	25.05	30177828
31	Phosphorylation	KKNTPFLYDLVMTHA HCCCHHHHHHHHHHH	13.96	30177828
36	Phosphorylation	FLYDLVMTHALQWPS HHHHHHHHHHHHCCC	9.12	30177828
60	Phosphorylation	TKPEGKDYALHWLVL CCCCCCCEEEEEEEE	17.97	28152594
65	Ubiquitination	KDYALHWLVLGTHTS CCEEEEEEEEECCCC	1.26	21890473
68	Ubiquitination	ALHWLVLGTHTSDEQ EEEEEEEECCCCCCC	14.15	21890473
95	Phosphorylation	DDAQFDASHCDSDKG CCCCCCHHHCCCCCC	26.88	23401153
99	Phosphorylation	FDASHCDSDKGEFGG CCHHHCCCCCCCCCC	46.76	29255136
101	Ubiquitination	ASHCDSDKGEFGGFG HHHCCCCCCCCCCCC	65.38	-
101	2-Hydroxyisobutyrylation	ASHCDSDKGEFGGFG HHHCCCCCCCCCCCC	65.38	-
101	Acetylation	ASHCDSDKGEFGGFG HHHCCCCCCCCCCCC	65.38	23749302
109	Phosphorylation	GEFGGFGSVTGKIEC CCCCCCCEECEEEEE	17.78	24732914
111	Phosphorylation	FGGFGSVTGKIECEI CCCCCEECEEEEEEE	34.16	24732914
113	Sumoylation	GFGSVTGKIECEIKI CCCEECEEEEEEEEE	26.43	-
113	Acetylation	GFGSVTGKIECEIKI CCCEECEEEEEEEEE	26.43	26051181
113	Ubiquitination	GFGSVTGKIECEIKI CCCEECEEEEEEEEE	26.43	-
119	Sumoylation	GKIECEIKINHEGEV EEEEEEEEECCCCCC	18.37	-
119	Acetylation	GKIECEIKINHEGEV EEEEEEEEECCCCCC	18.37	16916647
119	2-Hydroxyisobutyrylation	GKIECEIKINHEGEV EEEEEEEEECCCCCC	18.37	-
119	Sumoylation	GKIECEIKINHEGEV EEEEEEEEECCCCCC	18.37	-
119	Ubiquitination	GKIECEIKINHEGEV EEEEEEEEECCCCCC	18.37	-
119	Malonylation	GKIECEIKINHEGEV EEEEEEEEECCCCCC	18.37	26320211
130	Methylation	EGEVNRARYMPQNPH CCCCCCEEECCCCCC	25.66	115490431
142	Ubiquitination	NPHIIATKTPSSDVL CCCEEEECCCCCCEE	49.79	21890473
143	Phosphorylation	PHIIATKTPSSDVLV CCEEEECCCCCCEEE	24.85	30266825
145	Phosphorylation	IIATKTPSSDVLVFD EEEECCCCCCEEEEE	44.39	30266825
146	Phosphorylation	IATKTPSSDVLVFDY EEECCCCCCEEEEEC	32.70	30266825
153	Phosphorylation	SDVLVFDYTKHPAKP CCEEEEECCCCCCCC	13.26	28152594
154	Phosphorylation	DVLVFDYTKHPAKPD CEEEEECCCCCCCCC	25.40	28152594
155	Acetylation	VLVFDYTKHPAKPDP EEEEECCCCCCCCCC	41.17	25953088
155	Sumoylation	VLVFDYTKHPAKPDP EEEEECCCCCCCCCC	41.17	28112733
155	Ubiquitination	VLVFDYTKHPAKPDP EEEEECCCCCCCCCC	41.17	-
159	Methylation	DYTKHPAKPDPSGEC ECCCCCCCCCCCCCC	55.17	23644510
159	Sumoylation	DYTKHPAKPDPSGEC ECCCCCCCCCCCCCC	55.17	-
159	Acetylation	DYTKHPAKPDPSGEC ECCCCCCCCCCCCCC	55.17	23749302
159	Ubiquitination	DYTKHPAKPDPSGEC ECCCCCCCCCCCCCC	55.17	-
159	Sumoylation	DYTKHPAKPDPSGEC ECCCCCCCCCCCCCC	55.17	28112733
177	Ubiquitination	LRLRGHQKEGYGLSW CCCCCCCCCCCCCCC	47.64	-
186	Ubiquitination	GYGLSWNSNLSGHLL CCCCCCCCCCCCEEE	32.65	21890473
214	Acetylation	NAGPKEGKIVDAKAI CCCCCCCCEEECEEE	40.42	26051181
214	Ubiquitination	NAGPKEGKIVDAKAI CCCCCCCCEEECEEE	40.42	-
219	Ubiquitination	EGKIVDAKAIFTGHS CCCEEECEEEEECCC	37.24	-
257	Methylation	KLMIWDTRSNTTSKP CEEEEECCCCCCCCC	25.99	-
263	Ubiquitination	TRSNTTSKPSHLVDA CCCCCCCCCHHEEEC	48.74	-
263	Acetylation	TRSNTTSKPSHLVDA CCCCCCCCCHHEEEC	48.74	26051181
296	Phosphorylation	ATGSADKTVALWDLR ECCCCCCEEEEEEHH	16.14	21712546
303	Methylation	TVALWDLRNLKLKLH EEEEEEHHCCEEEEE	43.92	-
306	Sumoylation	LWDLRNLKLKLHTFE EEEHHCCEEEEEEEC	47.31	-
308	2-Hydroxyisobutyrylation	DLRNLKLKLHTFESH EHHCCEEEEEEECHH	36.31	-
308	Ubiquitination	DLRNLKLKLHTFESH EHHCCEEEEEEECHH	36.31	-
314	Phosphorylation	LKLHTFESHKDEIFQ EEEEEECHHCCCEEE	31.48	-
316	Ubiquitination	LHTFESHKDEIFQVH EEEECHHCCCEEEEE	67.35	21906983
325	Phosphorylation	EIFQVHWSPHNETIL CEEEEEECCCCCEEE	11.03	26714015
340	Methylation	ASSGTDRRLNVWDLS CCCCCCCCCEEEEHH	33.16	-
347	Phosphorylation	RLNVWDLSKIGEEQS CCEEEEHHHHCCCCC	21.54	21815630
348	Ubiquitination	LNVWDLSKIGEEQSA CEEEEHHHHCCCCCH	63.13	2190698
354	Phosphorylation	SKIGEEQSAEDAEDG HHHCCCCCHHHCCCC	36.58	30266825
360	Ubiquitination	QSAEDAEDGPPELLF CCHHHCCCCCCEEEE	76.30	21890473
373	Phosphorylation	LFIHGGHTAKISDFS EEEECCCEEEECCCC	32.68	23403867
377	Phosphorylation	GGHTAKISDFSWNPN CCCEEEECCCCCCCC	31.71	20068231
380	Phosphorylation	TAKISDFSWNPNEPW EEEECCCCCCCCCCE	30.82	20068231
391	Phosphorylation	NEPWVICSVSEDNIM CCCEEEEEECHHHHH	19.97	20068231
393	Phosphorylation	PWVICSVSEDNIMQI CEEEEEECHHHHHHH	23.96	20068231
408	Phosphorylation	WQMAENIYNDEESDV HHHHHHHCCCCCCCC	28.30	20068231
413	Phosphorylation	NIYNDEESDVTTSEL HHCCCCCCCCCHHHH	35.02	20068231
416	Phosphorylation	NDEESDVTTSELEGQ CCCCCCCCHHHHCCC	29.60	20068231
417	Phosphorylation	DEESDVTTSELEGQG CCCCCCCHHHHCCCC	21.76	20068231
418	Phosphorylation	EESDVTTSELEGQGS CCCCCCHHHHCCCCC	30.71	20068231
425	Phosphorylation	SELEGQGS------- HHHCCCCC-------	29.21	20068231

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
314	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBBP7_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 RBBP7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRCA1_HUMAN	BRCA1	physical	11394910
P66B_HUMAN	GATAD2B	physical	11756549
BRCA1_HUMAN	BRCA1	physical	10220405
SIN3A_HUMAN	SIN3A	physical	9651585
SAP30_HUMAN	SAP30	physical	9651585
BAF_HUMAN	BANF1	physical	19759913
P66A_HUMAN	GATAD2A	physical	16738318
P66B_HUMAN	GATAD2B	physical	16738318
BC11B_HUMAN	BCL11B	physical	16091750
H31T_HUMAN	HIST3H3	physical	20953179
HAT1_HUMAN	HAT1	physical	20953179
CHD4_HUMAN	CHD4	physical	9790534
SALL2_HUMAN	SALL2	physical	21228219
H31T_HUMAN	HIST3H3	physical	15601853
WAP53_HUMAN	WRAP53	physical	22939629
RBBP4_HUMAN	RBBP4	physical	22863883
NACC2_HUMAN	NACC2	physical	22926524
FA60A_HUMAN	FAM60A	physical	26186194
NPAT_HUMAN	NPAT	physical	26186194
SAP30_HUMAN	SAP30	physical	26186194
ING2_HUMAN	ING2	physical	26186194
HDAC1_HUMAN	HDAC1	physical	26186194
HDAC2_HUMAN	HDAC2	physical	26186194
KDM5A_HUMAN	KDM5A	physical	26186194
ARI4A_HUMAN	ARID4A	physical	26186194
SIN3A_HUMAN	SIN3A	physical	26186194
SIN3B_HUMAN	SIN3B	physical	26186194
Z512B_HUMAN	ZNF512B	physical	26186194
P66A_HUMAN	GATAD2A	physical	26186194
SP130_HUMAN	SAP130	physical	26186194
SHPRH_HUMAN	SHPRH	physical	26186194
PHF12_HUMAN	PHF12	physical	26186194
ARI4B_HUMAN	ARID4B	physical	26186194
ZN521_HUMAN	ZNF521	physical	26186194
ZN423_HUMAN	ZNF423	physical	26186194
MBD2_HUMAN	MBD2	physical	26186194
MBD3_HUMAN	MBD3	physical	26186194
CHD3_HUMAN	CHD3	physical	26186194
CHD4_HUMAN	CHD4	physical	26186194
CHD5_HUMAN	CHD5	physical	26186194
MTA2_HUMAN	MTA2	physical	26186194
MTA3_HUMAN	MTA3	physical	26186194
RBBP4_HUMAN	RBBP4	physical	26186194
SUZ12_HUMAN	SUZ12	physical	26186194
BRM1L_HUMAN	BRMS1L	physical	26186194
SMCA5_HUMAN	SMARCA5	physical	26186194
SMCA1_HUMAN	SMARCA1	physical	26186194
GATD1_HUMAN	GATAD1	physical	26186194
SP30L_HUMAN	SAP30L	physical	26186194
EZH2_HUMAN	EZH2	physical	26186194
BPTF_HUMAN	BPTF	physical	26186194
LIN9_HUMAN	LIN9	physical	26186194
EED_HUMAN	EED	physical	26186194
CDKA1_HUMAN	CDK2AP1	physical	26186194
ING1_HUMAN	ING1	physical	26186194
SDS3_HUMAN	SUDS3	physical	26186194
BC11A_HUMAN	BCL11A	physical	26186194
FOXK2_HUMAN	FOXK2	physical	26186194
FOXK1_HUMAN	FOXK1	physical	26186194
CCD71_HUMAN	CCDC71	physical	26186194
CCDC8_HUMAN	CCDC8	physical	26186194
BAP18_HUMAN	C17orf49	physical	26186194
BRMS1_HUMAN	BRMS1	physical	26186194
SALL1_HUMAN	SALL1	physical	26186194
ZBTB2_HUMAN	ZBTB2	physical	26186194
MTF2_HUMAN	MTF2	physical	26186194
BAHC1_HUMAN	BAHCC1	physical	26186194
CA122_HUMAN	C1orf122	physical	26186194
GNL3_HUMAN	GNL3	physical	26344197
HAT1_HUMAN	HAT1	physical	26344197
HDAC1_HUMAN	HDAC1	physical	26344197
HDAC2_HUMAN	HDAC2	physical	26344197
RBBP4_HUMAN	RBBP4	physical	26344197
DDB1_HUMAN	DDB1	physical	25795299
HDAC1_HUMAN	HDAC1	physical	25885317
SUZ12_HUMAN	SUZ12	physical	28514442
PHF12_HUMAN	PHF12	physical	28514442
MTF2_HUMAN	MTF2	physical	28514442
ZN521_HUMAN	ZNF521	physical	28514442
Z512B_HUMAN	ZNF512B	physical	28514442
CHD5_HUMAN	CHD5	physical	28514442
KDM5A_HUMAN	KDM5A	physical	28514442
MTA3_HUMAN	MTA3	physical	28514442
ZN423_HUMAN	ZNF423	physical	28514442
BPTF_HUMAN	BPTF	physical	28514442
BRM1L_HUMAN	BRMS1L	physical	28514442
NPAT_HUMAN	NPAT	physical	28514442
P66A_HUMAN	GATAD2A	physical	28514442
SP30L_HUMAN	SAP30L	physical	28514442
MBD3_HUMAN	MBD3	physical	28514442
MBD2_HUMAN	MBD2	physical	28514442
ARI4B_HUMAN	ARID4B	physical	28514442
SIN3B_HUMAN	SIN3B	physical	28514442
SDS3_HUMAN	SUDS3	physical	28514442
HDAC1_HUMAN	HDAC1	physical	28514442
SHPRH_HUMAN	SHPRH	physical	28514442
EZH2_HUMAN	EZH2	physical	28514442
SP130_HUMAN	SAP130	physical	28514442
EED_HUMAN	EED	physical	28514442
SIN3A_HUMAN	SIN3A	physical	28514442
ARI4A_HUMAN	ARID4A	physical	28514442
SMCA1_HUMAN	SMARCA1	physical	28514442
CHD4_HUMAN	CHD4	physical	28514442
SAP30_HUMAN	SAP30	physical	28514442
ZBTB2_HUMAN	ZBTB2	physical	28514442
CDKA1_HUMAN	CDK2AP1	physical	28514442
LIN9_HUMAN	LIN9	physical	28514442
CHD3_HUMAN	CHD3	physical	28514442
BC11A_HUMAN	BCL11A	physical	28514442
ING1_HUMAN	ING1	physical	28514442
BAHC1_HUMAN	BAHCC1	physical	28514442
SMCA5_HUMAN	SMARCA5	physical	28514442
FOXK2_HUMAN	FOXK2	physical	28514442
CA122_HUMAN	C1orf122	physical	28514442
MTA2_HUMAN	MTA2	physical	28514442
FOXK1_HUMAN	FOXK1	physical	28514442
GATD1_HUMAN	GATAD1	physical	28514442
RBBP4_HUMAN	RBBP4	physical	28514442
SALL1_HUMAN	SALL1	physical	28514442
HDAC2_HUMAN	HDAC2	physical	28514442
ASF1A_HUMAN	ASF1A	physical	28514442
CCD71_HUMAN	CCDC71	physical	28514442
CCDC8_HUMAN	CCDC8	physical	28514442
DNMT1_HUMAN	DNMT1	physical	28143904
HAT1_HUMAN	HAT1	physical	28143904
ZN827_HUMAN	ZNF827	physical	25150861

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 RBBP7_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, UBIQUITINATION [LARGESCALE ANALYSIS] AT LYS-4, AND MASS SPECTROMETRY.	18781797 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-413 AND THR-416,ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19007248 [Abstract]
"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 LYS-21, AND MASSSPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-119, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"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-354, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-413 AND THR-416,ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND THR-416, ANDMASS SPECTROMETRY.	17287340 [Abstract]
Ubiquitylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, UBIQUITINATION [LARGESCALE ANALYSIS] AT LYS-4, AND MASS SPECTROMETRY.	18781797 [Abstract]