dbPTM

ERCC6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERCC6_HUMAN
UniProt AC	Q03468
Protein Name	DNA excision repair protein ERCC-6
Gene Name	ERCC6
Organism	Homo sapiens (Human).
Sequence Length	1493
Subcellular Localization	Nucleus .
Protein Description	Essential factor involved in transcription-coupled nucleotide excision repair which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for transcription-coupled repair complex formation. It recruits the CSA complex (DCX(ERCC8) complex), nucleotide excision repair proteins and EP300 to the at sites of RNA polymerase II-blocking lesions..
Protein Sequence	MPNEGIPHSSQTQEQDCLQSQPVSNNEEMAIKQESGGDGEVEEYLSFRSVGDGLSTSAVGCASAAPRRGPALLHIDRHQIQAVEPSAQALELQGLGVDVYDQDVLEQGVLQQVDNAIHEASRASQLVDVEKEYRSVLDDLTSCTTSLRQINKIIEQLSPQAATSRDINRKLDSVKRQKYNKEQQLKKITAKQKHLQAILGGAEVKIELDHASLEEDAEPGPSSLGSMLMPVQETAWEELIRTGQMTPFGTQIPQKQEKKPRKIMLNEASGFEKYLADQAKLSFERKKQGCNKRAARKAPAPVTPPAPVQNKNKPNKKARVLSKKEERLKKHIKKLQKRALQFQGKVGLPKARRPWESDMRPEAEGDSEGEESEYFPTEEEEEEEDDEVEGAEADLSGDGTDYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVGRYRDDGDEDYYKQRLRRWNKLRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGSNYRFEGLGPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRRMKSDVKMSLSLPDKNEQVLFCRLTDEQHKVYQNFVDSKEVYRILNGEMQIFSGLIALRKICNHPDLFSGGPKNLKGLPDDELEEDQFGYWKRSGKMIVVESLLKIWHKQGQRVLLFSQSRQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLLTAGTIEEKIYHRQIFKQFLTNRVLKDPKQRRFFKSNDLYELFTLTSPDASQSTETSAIFAGTGSDVQTPKCHLKRRIQPAFGADHDVPKRKKFPASNISVNDATSSEEKSEAKGAEVNAVTSNRSDPLKDDPHMSSNVTSNDRLGEETNAVSGPEELSVISGNGECSNSSGTGKTSMPSGDESIDEKLGLSYKRERPSQAQTEAFWENKQMENNFYKHKSKTKHHSVAEEETLEKHLRPKQKPKNSKHCRDAKFEGTRIPHLVKKRRYQKQDSENKSEAKEQSNDDYVLEKLFKKSVGVHSVMKHDAIMDGASPDYVLVEAEANRVAQDALKALRLSRQRCLGAVSGVPTWTGHRGISGAPAGKKSRFGKKRNSNFSVQHPSSTSPTEKCQDGIMKKEGKDNVPEHFSGRAEDADSSSGPLASSSLLAKMRARNHLILPERLESESGHLQEASALLPTTEHDDLLVEMRNFIAFQAHTDGQASTREILQEFESKLSASQSCVFRELLRNLCTFHRTSGGEGIWKLKPEYC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	PNEGIPHSSQTQEQD CCCCCCCCCCCCCHH	20.84	23663014
10	Phosphorylation	NEGIPHSSQTQEQDC CCCCCCCCCCCCHHH	33.92	23663014
12	Phosphorylation	GIPHSSQTQEQDCLQ CCCCCCCCCCHHHHH	35.70	23663014
20	Phosphorylation	QEQDCLQSQPVSNNE CCHHHHHCCCCCCCH	24.41	23663014
32	Sumoylation	NNEEMAIKQESGGDG CCHHEEEEECCCCCC	38.17	-
35	Phosphorylation	EMAIKQESGGDGEVE HEEEEECCCCCCCHH	45.65	28985074
44	Phosphorylation	GDGEVEEYLSFRSVG CCCCHHEEEEEEECC	8.30	27642862
46	Phosphorylation	GEVEEYLSFRSVGDG CCHHEEEEEEECCCC	20.08	28102081
55	Phosphorylation	RSVGDGLSTSAVGCA EECCCCCCCCCCCCC	26.33	22210691
57	Phosphorylation	VGDGLSTSAVGCASA CCCCCCCCCCCCCCC	19.99	28555341
124	Phosphorylation	IHEASRASQLVDVEK HHHHHHHHHHCCHHH	23.96	20068231
124	Phosphorylation	IHEASRASQLVDVEK HHHHHHHHHHCCHHH	23.96	20068231
131	Ubiquitination	SQLVDVEKEYRSVLD HHHCCHHHHHHHHHH	60.95	-
158	Phosphorylation	NKIIEQLSPQAATSR HHHHHHHCHHHHHHH	18.05	16964243
158	Phosphorylation	NKIIEQLSPQAATSR HHHHHHHCHHHHHHH	18.05	29255136
163	Phosphorylation	QLSPQAATSRDINRK HHCHHHHHHHHHHHH	27.58	23663014
164	Phosphorylation	LSPQAATSRDINRKL HCHHHHHHHHHHHHH	24.19	23663014
170	Methylation	TSRDINRKLDSVKRQ HHHHHHHHHHHHHHH	52.75	18438403
173	Phosphorylation	DINRKLDSVKRQKYN HHHHHHHHHHHHHCC	39.72	-
173	Phosphorylation	DINRKLDSVKRQKYN HHHHHHHHHHHHHCC	39.72	22673903
212	Phosphorylation	KIELDHASLEEDAEP EEEECCCCHHCCCCC	32.66	-
242	Phosphorylation	AWEELIRTGQMTPFG HHHHHHHHCCCCCCC	25.44	-
242	Phosphorylation	AWEELIRTGQMTPFG HHHHHHHHCCCCCCC	25.44	-
246	Phosphorylation	LIRTGQMTPFGTQIP HHHHCCCCCCCCCCC	13.95	25627689
246	Phosphorylation	LIRTGQMTPFGTQIP HHHHCCCCCCCCCCC	13.95	21815630
250	Phosphorylation	GQMTPFGTQIPQKQE CCCCCCCCCCCCCCC	24.57	-
250	Phosphorylation	GQMTPFGTQIPQKQE CCCCCCCCCCCCCCC	24.57	-
255	Acetylation	FGTQIPQKQEKKPRK CCCCCCCCCCCCCCE	55.88	26051181
255	Sumoylation	FGTQIPQKQEKKPRK CCCCCCCCCCCCCCE	55.88	28112733
262	Sumoylation	KQEKKPRKIMLNEAS CCCCCCCEEEECCCC	40.78	-
262	Sumoylation	KQEKKPRKIMLNEAS CCCCCCCEEEECCCC	40.78	-
297	Methylation	CNKRAARKAPAPVTP CCHHHHHCCCCCCCC	54.73	18438403
303	Phosphorylation	RKAPAPVTPPAPVQN HCCCCCCCCCCCCCC	23.61	25627689
303	Phosphorylation	RKAPAPVTPPAPVQN HCCCCCCCCCCCCCC	23.61	30266825
345	Ubiquitination	RALQFQGKVGLPKAR HHHHHCCCCCCCCCC	23.50	-
429	Phosphorylation	IDDDFFPSSGEEAEA CCCCCCCCCCHHHHH	45.90	18669648
429	Phosphorylation	IDDDFFPSSGEEAEA CCCCCCCCCCHHHHH	45.90	25159151
430	Phosphorylation	DDDFFPSSGEEAEAA CCCCCCCCCHHHHHH	50.92	18669648
430	Phosphorylation	DDDFFPSSGEEAEAA CCCCCCCCCHHHHHH	50.92	23927012
438	Phosphorylation	GEEAEAASVGEGGGG CHHHHHHCCCCCCCC	37.39	17081983
438	Phosphorylation	GEEAEAASVGEGGGG CHHHHHHCCCCCCCC	37.39	23927012
448	Methylation	EGGGGGRKVGRYRDD CCCCCCCCCCCCCCC	52.93	18438403
486	Phosphorylation	RLKLEDDSEESDAEF CCCCCCCCHHCHHCC	56.43	22167270
489	Phosphorylation	LEDDSEESDAEFDEG CCCCCHHCHHCCCCC	37.76	22167270
554	Phosphorylation	AGLSYSKIRTRGSNY HCCCHHHHHCCCCCC	4.46	25850435
554	Phosphorylation	AGLSYSKIRTRGSNY HCCCHHHHHCCCCCC	4.46	25850435
556	Phosphorylation	LSYSKIRTRGSNYRF CCHHHHHCCCCCCCC	42.74	24719451
560	Phosphorylation	KIRTRGSNYRFEGLG HHHCCCCCCCCCCCC	34.52	23090842
560	Phosphorylation	KIRTRGSNYRFEGLG HHHCCCCCCCCCCCC	34.52	23090842
561	Phosphorylation	IRTRGSNYRFEGLGP HHCCCCCCCCCCCCC	20.55	23090842
561	Phosphorylation	IRTRGSNYRFEGLGP HHCCCCCCCCCCCCC	20.55	23090842
576	Phosphorylation	TVIVCPTTVMHQWVK EEEEECHHHHHHHHH	10.85	24719451
623	Phosphorylation	HCHGILITSYSYIRL HHCCEEEECHHHHHH	20.40	20860994
624	Phosphorylation	CHGILITSYSYIRLM HCCEEEECHHHHHHH	12.70	-
625	Phosphorylation	HGILITSYSYIRLMQ CCEEEECHHHHHHHH	9.24	-
626	Phosphorylation	GILITSYSYIRLMQD CEEEECHHHHHHHHC	17.53	20860994
663	Ubiquitination	AAVTLACKQFRTPHR HHHHHHHHHCCCCCE	47.03	-
729	Ubiquitination	VQVKTAYKCACVLRD CCCHHHHHHHHHHHH	16.94	-
748	Phosphorylation	YLLRRMKSDVKMSLS HHHHHHHCCCEEEEE	37.99	29759185
755	Phosphorylation	SDVKMSLSLPDKNEQ CCCEEEEECCCCCCE	30.46	29759185
759	Ubiquitination	MSLSLPDKNEQVLFC EEEECCCCCCEEEEE	61.52	-
774	Ubiquitination	RLTDEQHKVYQNFVD EECHHHHHHHHHCCC	42.19	-
776	Phosphorylation	TDEQHKVYQNFVDSK CHHHHHHHHHCCCHH	11.53	26270265
782	Phosphorylation	VYQNFVDSKEVYRIL HHHHCCCHHHHHHHH	25.97	26270265
783	Ubiquitination	YQNFVDSKEVYRILN HHHCCCHHHHHHHHC	46.89	-
817	Ubiquitination	DLFSGGPKNLKGLPD HHHCCCCCCCCCCCC	77.51	-
820	Ubiquitination	SGGPKNLKGLPDDEL CCCCCCCCCCCCCCC	68.73	-
836	Ubiquitination	EDQFGYWKRSGKMIV CCCCCCHHHCCCEEE	28.36	-
846	Phosphorylation	GKMIVVESLLKIWHK CCEEEEEHHHHHHHH	27.65	24719451
862	Phosphorylation	GQRVLLFSQSRQMLD CCEEEEEECHHHHHH	27.50	22468782
864	Phosphorylation	RVLLFSQSRQMLDIL EEEEEECHHHHHHHH	24.23	22468782
888	Phosphorylation	TYLKMDGTTTIASRQ EEEEECCCEEEEECC	19.26	28450419
889	Phosphorylation	YLKMDGTTTIASRQP EEEECCCEEEEECCC	23.02	28450419
890	Phosphorylation	LKMDGTTTIASRQPL EEECCCEEEEECCCE	17.87	28450419
893	Phosphorylation	DGTTTIASRQPLITR CCCEEEEECCCEEEE	27.83	28450419
932	Phosphorylation	GANRVVIYDPDWNPS CCCEEEEECCCCCCC	15.15	22817900
955	Ubiquitination	AWRIGQKKQVTVYRL HHHHCCCCEEEEEEE	41.96	-
1009	Phosphorylation	YELFTLTSPDASQST HHEEEECCCCCCCCC	24.72	18669648
1054	Methylation	DHDVPKRKKFPASNI CCCCCCCCCCCCCCC	65.96	18438403
1062	Phosphorylation	KFPASNISVNDATSS CCCCCCCCCCCCCCH	21.08	28555341
1067	Phosphorylation	NISVNDATSSEEKSE CCCCCCCCCHHHHHH	35.33	28450419
1068	Phosphorylation	ISVNDATSSEEKSEA CCCCCCCCHHHHHHH	37.16	21815630
1069	Phosphorylation	SVNDATSSEEKSEAK CCCCCCCHHHHHHHC	45.48	28450419
1084	Phosphorylation	GAEVNAVTSNRSDPL CCCCEEEECCCCCCC	20.20	23312004
1085	Phosphorylation	AEVNAVTSNRSDPLK CCCEEEECCCCCCCC	24.52	23312004
1088	Phosphorylation	NAVTSNRSDPLKDDP EEEECCCCCCCCCCC	48.07	23312004
1102	Phosphorylation	PHMSSNVTSNDRLGE CCCCCCCCCCCCCCC	26.51	22210691
1111	Phosphorylation	NDRLGEETNAVSGPE CCCCCCCCCCCCCCC	24.95	22210691
1115	Phosphorylation	GEETNAVSGPEELSV CCCCCCCCCCCCCEE	46.34	30175587
1133	Phosphorylation	NGECSNSSGTGKTSM CCCCCCCCCCCCCCC	44.62	22210691
1138	Phosphorylation	NSSGTGKTSMPSGDE CCCCCCCCCCCCCCC	31.44	22199227
1139	Phosphorylation	SSGTGKTSMPSGDES CCCCCCCCCCCCCCC	31.98	22199227
1142	Phosphorylation	TGKTSMPSGDESIDE CCCCCCCCCCCCHHH	50.68	25159151
1146	Phosphorylation	SMPSGDESIDEKLGL CCCCCCCCHHHHHCC	39.83	25159151
1156	Ubiquitination	EKLGLSYKRERPSQA HHHCCCCCCCCCCHH	44.39	-
1189	Phosphorylation	KSKTKHHSVAEEETL CCCCCCCCCCCHHHH	23.81	29978859
1195	Phosphorylation	HSVAEEETLEKHLRP CCCCCHHHHHHHCCC	43.42	30631047
1198	Ubiquitination	AEEETLEKHLRPKQK CCHHHHHHHCCCCCC	51.56	-
1216	Acetylation	SKHCRDAKFEGTRIP CCCCCCCCCCCCCHH	48.51	26051181
1254	Ubiquitination	NDDYVLEKLFKKSVG CHHHHHHHHHHHCCC	55.87	-
1258	Ubiquitination	VLEKLFKKSVGVHSV HHHHHHHHCCCCCHH	42.93	-
1276	Phosphorylation	DAIMDGASPDYVLVE HHHCCCCCCCEEEEE	24.67	25159151
1279	Phosphorylation	MDGASPDYVLVEAEA CCCCCCCEEEEEHHH	10.08	21712546
1295	Ubiquitination	RVAQDALKALRLSRQ HHHHHHHHHHHHHHH	47.28	-
1337	Phosphorylation	RFGKKRNSNFSVQHP CCCCCCCCCCCCCCC	43.20	25159151
1340	Phosphorylation	KKRNSNFSVQHPSST CCCCCCCCCCCCCCC	25.72	25159151
1345	Phosphorylation	NFSVQHPSSTSPTEK CCCCCCCCCCCCCHH	44.09	23401153
1346	Phosphorylation	FSVQHPSSTSPTEKC CCCCCCCCCCCCHHH	37.04	22167270
1347	Phosphorylation	SVQHPSSTSPTEKCQ CCCCCCCCCCCHHHC	42.96	22167270
1348	Phosphorylation	VQHPSSTSPTEKCQD CCCCCCCCCCHHHCC	31.60	22167270
1350	Phosphorylation	HPSSTSPTEKCQDGI CCCCCCCCHHHCCCH	48.09	22167270
1352	Ubiquitination	SSTSPTEKCQDGIMK CCCCCCHHHCCCHHH	39.41	-
1359	Ubiquitination	KCQDGIMKKEGKDNV HHCCCHHHCCCCCCC	45.83	-
1363	Ubiquitination	GIMKKEGKDNVPEHF CHHHCCCCCCCCCHH	47.42	-
1379	Phosphorylation	GRAEDADSSSGPLAS CCCCCCCCCCCCCCC	28.29	30576142
1380	Phosphorylation	RAEDADSSSGPLASS CCCCCCCCCCCCCCH	39.60	20873877
1381	Phosphorylation	AEDADSSSGPLASSS CCCCCCCCCCCCCHH	48.67	20873877
1388	Phosphorylation	SGPLASSSLLAKMRA CCCCCCHHHHHHHHH	25.55	25627689
1392	Ubiquitination	ASSSLLAKMRARNHL CCHHHHHHHHHHCCC	28.96	-
1457	Ubiquitination	ILQEFESKLSASQSC HHHHHHHHCCHHHHH	38.98	21890473
1461	Phosphorylation	FESKLSASQSCVFRE HHHHCCHHHHHHHHH	21.17	17525332
1487	Ubiquitination	SGGEGIWKLKPEYC- CCCCCCEECCCCCC-	44.72	-

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
10	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
158	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
932	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	ERCC8	Q13216	PMID:16751180

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
10	S	Phosphorylation	29203878
Phosphorylated in a cell cycle-dependent manner at Ser-158 by cyclin A-CDK2 and at Ser-10 by ATM in response to DNA damage.
158	S	Phosphorylation	16964243
Phosphorylated in a cell cycle-dependent manner at Ser-158 by cyclin A-CDK2 and at Ser-10 by ATM in response to DNA damage.
205	K	Sumoylation	26620705
Sumoylation at Lys-205 in an UV-radiation-dependent manner is essential for its transcription-coupled nucleotide excision repair activity.

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 ERCC6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XPA_HUMAN	XPA	physical	8999876
H2B1B_HUMAN	HIST1H2BB	physical	11003660
H31_HUMAN	HIST1H3A	physical	11003660
RPA1_HUMAN	POLR1A	physical	20541997
XPA_HUMAN	XPA	physical	20541997
ERCC2_HUMAN	ERCC2	physical	20541997
XPF_HUMAN	ERCC4	physical	20541997
RPB1_HUMAN	POLR2A	physical	20541997
ERCC8_HUMAN	ERCC8	physical	20541997
DDB1_HUMAN	DDB1	physical	20541997
HMGN1_HUMAN	HMGN1	physical	20541997
PCNA_HUMAN	PCNA	physical	20541997
DPOD1_HUMAN	POLD1	physical	20541997
H2A2C_HUMAN	HIST2H2AC	physical	20541997
RPB1_HUMAN	POLR2A	physical	16916636
ERCC8_HUMAN	ERCC8	physical	16916636
ERCC3_HUMAN	ERCC3	physical	16916636
ERCC5_HUMAN	ERCC5	physical	16916636
RFA1_HUMAN	RPA1	physical	16916636
BRCA1_HUMAN	BRCA1	physical	21756275
ERCC8_HUMAN	ERCC8	physical	7664335
P53_HUMAN	TP53	physical	22032989
ERCC8_HUMAN	ERCC8	physical	22032989
MDM2_HUMAN	MDM2	physical	22032989
DDB1_HUMAN	DDB1	physical	22032989
CUL4A_HUMAN	CUL4A	physical	22032989
CUL4B_HUMAN	CUL4B	physical	22032989
CAND1_HUMAN	CAND1	physical	22032989
UBP7_HUMAN	USP7	physical	22032989
CSN3_HUMAN	COPS3	physical	22032989
CSN4_HUMAN	COPS4	physical	22032989
CSN6_HUMAN	COPS6	physical	22032989
CUL7_HUMAN	CUL7	physical	22032989
OGG1_HUMAN	OGG1	physical	20100872
SSBP_HUMAN	SSBP1	physical	20100872
PARP1_HUMAN	PARP1	physical	16107709
RPA1_HUMAN	POLR1A	physical	23667505
KAT2B_HUMAN	KAT2B	physical	23667505
UBC_HUMAN	UBC	physical	20541997
SPTA1_HUMAN	SPTA1	physical	16889989

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
133540	Cockayne syndrome B (CSB)
214150	Cerebro-oculo-facio-skeletal syndrome 1 (COFS1)
278800	De Sanctis-Cacchione syndrome (DSC)
613761	Macular degeneration, age-related, 5 (ARMD5)
600630	UV-sensitive syndrome 1 (UVSS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ERCC6_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Protein lysine methyltransferase G9a acts on non-histone targets."; Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.; Nat. Chem. Biol. 4:344-346(2008). Cited for: METHYLATION AT LYS-170; LYS-297; LYS-448 AND LYS-1054.	18438403 [Abstract]
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1142, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-158; SER-429; SER-430;SER-486; SER-489; SER-1142 AND SER-1348, AND MASS SPECTROMETRY.	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-158, 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-158, AND MASSSPECTROMETRY.	19007248 [Abstract]
"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-1461, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND MASSSPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND MASSSPECTROMETRY.	16964243 [Abstract]

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