dbPTM

ERCC5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERCC5_HUMAN
UniProt AC	P28715
Protein Name	DNA repair protein complementing XP-G cells
Gene Name	ERCC5
Organism	Homo sapiens (Human).
Sequence Length	1186
Subcellular Localization	Nucleus .
Protein Description	Single-stranded structure-specific DNA endonuclease involved in DNA excision repair. Makes the 3'incision in DNA nucleotide excision repair (NER). Acts as a cofactor for a DNA glycosylase that removes oxidized pyrimidines from DNA. May also be involved in transcription-coupled repair of this kind of damage, in transcription by RNA polymerase II, and perhaps in other processes too..
Protein Sequence	MGVQGLWKLLECSGRQVSPEALEGKILAVDISIWLNQALKGVRDRHGNSIENPHLLTLFHRLCKLLFFRIRPIFVFDGDAPLLKKQTLVKRRQRKDLASSDSRKTTEKLLKTFLKRQAIKTAFRSKRDEALPSLTQVRRENDLYVLPPLQEEEKHSSEEEDEKEWQERMNQKQALQEEFFHNPQAIDIESEDFSSLPPEVKHEILTDMKEFTKRRRTLFEAMPEESDDFSQYQLKGLLKKNYLNQHIEHVQKEMNQQHSGHIRRQYEDEGGFLKEVESRRVVSEDTSHYILIKGIQAKTVAEVDSESLPSSSKMHGMSFDVKSSPCEKLKTEKEPDATPPSPRTLLAMQAALLGSSSEEELESENRRQARGRNAPAAVDEGSISPRTLSAIKRALDDDEDVKVCAGDDVQTGGPGAEEMRINSSTENSDEGLKVRDGKGIPFTATLASSSVNSAEEHVASTNEGREPTDSVPKEQMSLVHVGTEAFPISDESMIKDRKDRLPLESAVVRHSDAPGLPNGRELTPASPTCTNSVSKNETHAEVLEQQNELCPYESKFDSSLLSSDDETKCKPNSASEVIGPVSLQETSSIVSVPSEAVDNVENVVSFNAKEHENFLETIQEQQTTESAGQDLISIPKAVEPMEIDSEESESDGSFIEVQSVISDEELQAEFPETSKPPSEQGEEELVGTREGEAPAESESLLRDNSERDDVDGEPQEAEKDAEDSLHEWQDINLEELETLESNLLAQQNSLKAQKQQQERIAATVTGQMFLESQELLRLFGIPYIQAPMEAEAQCAILDLTDQTSGTITDDSDIWLFGARHVYRNFFNKNKFVEYYQYVDFHNQLGLDRNKLINLAYLLGSDYTEGIPTVGCVTAMEILNEFPGHGLEPLLKFSEWWHEAQKNPKIRPNPHDTKVKKKLRTLQLTPGFPNPAVAEAYLKPVVDDSKGSFLWGKPDLDKIREFCQRYFGWNRTKTDESLFPVLKQLDAQQTQLRIDSFFRLAQQEKEDAKRIKSQRLNRAVTCMLRKEKEAAASEIEAVSVAMEKEFELLDKAKGKTQKRGITNTLEESSSLKRKRLSDSKGKNTCGGFLGETCLSESSDGSSSEDAESSSLMNVQRRTAAKEPKTSASDSQNSVKEAPVKNGGATTSSSSDSDDDGGKEKMVLVTARSVFGKKRRKLRRARGRKRKT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Acetylation	MGVQGLWKLLECSGR CCHHHHHHHHHCCCC	48.51	19608861
8	Ubiquitination	MGVQGLWKLLECSGR CCHHHHHHHHHCCCC	48.51	19608861
64	Acetylation	TLFHRLCKLLFFRIR HHHHHHHHHHHHHCC	53.46	25953088
64	Ubiquitination	TLFHRLCKLLFFRIR HHHHHHHHHHHHHCC	53.46	23000965
85	Ubiquitination	GDAPLLKKQTLVKRR CCCCHHHHHHHHHHH	48.78	-
99	Phosphorylation	RQRKDLASSDSRKTT HHHHHHCCCCCHHHH	41.81	20068231
100	Phosphorylation	QRKDLASSDSRKTTE HHHHHCCCCCHHHHH	33.72	20068231
102	Phosphorylation	KDLASSDSRKTTEKL HHHCCCCCHHHHHHH	37.31	20873877
106	Phosphorylation	SSDSRKTTEKLLKTF CCCCHHHHHHHHHHH	33.87	30576142
111	Ubiquitination	KTTEKLLKTFLKRQA HHHHHHHHHHHHHHH	47.90	-
120	Ubiquitination	FLKRQAIKTAFRSKR HHHHHHHHHHHHHHH	36.49	29967540
121	Phosphorylation	LKRQAIKTAFRSKRD HHHHHHHHHHHHHHH	25.56	21964256
126	Ubiquitination	IKTAFRSKRDEALPS HHHHHHHHHHHCCCC	60.66	29967540
133	Phosphorylation	KRDEALPSLTQVRRE HHHHCCCCCCCCCCC	44.92	28555341
144	Phosphorylation	VRRENDLYVLPPLQE CCCCCCEEEECCCCH	11.64	22496350
156	Phosphorylation	LQEEEKHSSEEEDEK CCHHHCCCCHHHHHH	50.98	23927012
157	Phosphorylation	QEEEKHSSEEEDEKE CHHHCCCCHHHHHHH	49.07	25159151
172	Ubiquitination	WQERMNQKQALQEEF HHHHHHHHHHHHHHH	32.31	29967540
209	Ubiquitination	HEILTDMKEFTKRRR HHHHHCHHHHHHHHH	53.11	29967540
213	Ubiquitination	TDMKEFTKRRRTLFE HCHHHHHHHHHHHHH	49.59	-
217	Phosphorylation	EFTKRRRTLFEAMPE HHHHHHHHHHHHCCC	33.71	28122231
235	Ubiquitination	DFSQYQLKGLLKKNY CCHHHHHHHHHHHHH	31.80	29967540
240	Ubiquitination	QLKGLLKKNYLNQHI HHHHHHHHHHHHHHH	51.28	29967540
252	Ubiquitination	QHIEHVQKEMNQQHS HHHHHHHHHHHHHCC	58.82	29967540
274	Ubiquitination	EDEGGFLKEVESRRV ECCCCCCHHHHHCEE	58.41	29967540
287	O-linked_Glycosylation	RVVSEDTSHYILIKG EEECCCCCEEEEEEC	26.98	30379171
287	Phosphorylation	RVVSEDTSHYILIKG EEECCCCCEEEEEEC	26.98	25003641
289	Phosphorylation	VSEDTSHYILIKGIQ ECCCCCEEEEEECCE	9.37	28796482
293	Ubiquitination	TSHYILIKGIQAKTV CCEEEEEECCEEEEE	46.66	21890473
293 (in isoform 1)	Ubiquitination	-	46.66	21890473
293	Ubiquitination	TSHYILIKGIQAKTV CCEEEEEECCEEEEE	46.66	21890473
298	Ubiquitination	LIKGIQAKTVAEVDS EEECCEEEEEEEECC	27.44	29967540
305	Phosphorylation	KTVAEVDSESLPSSS EEEEEECCCCCCCCC	33.97	27251275
307	Phosphorylation	VAEVDSESLPSSSKM EEEECCCCCCCCCHH	49.92	21815630
310	O-linked_Glycosylation	VDSESLPSSSKMHGM ECCCCCCCCCHHCCC	53.16	30379171
310	Phosphorylation	VDSESLPSSSKMHGM ECCCCCCCCCHHCCC	53.16	21815630
311	Phosphorylation	DSESLPSSSKMHGMS CCCCCCCCCHHCCCC	31.85	25159151
312	Phosphorylation	SESLPSSSKMHGMSF CCCCCCCCHHCCCCE	38.03	21815630
313	Acetylation	ESLPSSSKMHGMSFD CCCCCCCHHCCCCEE	36.54	25953088
313	Ubiquitination	ESLPSSSKMHGMSFD CCCCCCCHHCCCCEE	36.54	29967540
318	Phosphorylation	SSKMHGMSFDVKSSP CCHHCCCCEECCCCH	23.92	25159151
322	Ubiquitination	HGMSFDVKSSPCEKL CCCCEECCCCHHHHC	47.24	29967540
323	Phosphorylation	GMSFDVKSSPCEKLK CCCEECCCCHHHHCC	39.08	28450419
324	Phosphorylation	MSFDVKSSPCEKLKT CCEECCCCHHHHCCC	28.05	27422710
331	Phosphorylation	SPCEKLKTEKEPDAT CHHHHCCCCCCCCCC	63.83	23927012
338	Phosphorylation	TEKEPDATPPSPRTL CCCCCCCCCCCHHHH	43.01	29255136
341	Phosphorylation	EPDATPPSPRTLLAM CCCCCCCCHHHHHHH	28.37	29255136
344	Phosphorylation	ATPPSPRTLLAMQAA CCCCCHHHHHHHHHH	29.52	26074081
355	Phosphorylation	MQAALLGSSSEEELE HHHHHHCCCCHHHHH	30.57	21955146
356	Phosphorylation	QAALLGSSSEEELES HHHHHCCCCHHHHHH	39.71	21955146
357	Phosphorylation	AALLGSSSEEELESE HHHHCCCCHHHHHHH	51.21	21955146
363	Phosphorylation	SSEEELESENRRQAR CCHHHHHHHHHHHHC	53.44	20363803
382	Phosphorylation	PAAVDEGSISPRTLS CCCCCCCCCCHHHHH	20.18	29255136
384	Phosphorylation	AVDEGSISPRTLSAI CCCCCCCCHHHHHHH	15.27	19664994
387	Phosphorylation	EGSISPRTLSAIKRA CCCCCHHHHHHHHHH	28.57	26074081
389	Phosphorylation	SISPRTLSAIKRALD CCCHHHHHHHHHHCC	27.60	25159151
392	Acetylation	PRTLSAIKRALDDDE HHHHHHHHHHCCCCC	31.19	25953088
392	Ubiquitination	PRTLSAIKRALDDDE HHHHHHHHHHCCCCC	31.19	29967540
402	Ubiquitination	LDDDEDVKVCAGDDV CCCCCCCEEECCCCC	43.87	21963094
423	Phosphorylation	AEEMRINSSTENSDE CCEECCCCCCCCCCC	35.94	25159151
424	Phosphorylation	EEMRINSSTENSDEG CEECCCCCCCCCCCC	34.94	25159151
425	Phosphorylation	EMRINSSTENSDEGL EECCCCCCCCCCCCC	38.72	21712546
428	Phosphorylation	INSSTENSDEGLKVR CCCCCCCCCCCCCCC	30.70	25159151
433	Ubiquitination	ENSDEGLKVRDGKGI CCCCCCCCCCCCCCC	46.19	33845483
438	Acetylation	GLKVRDGKGIPFTAT CCCCCCCCCCCCEEE	58.94	25953088
477	Phosphorylation	SVPKEQMSLVHVGTE CCCHHHHCEEEECCC	27.25	28555341
489	Phosphorylation	GTEAFPISDESMIKD CCCEECCCCHHHCCC	35.25	28555341
511	Phosphorylation	ESAVVRHSDAPGLPN CHHEECCCCCCCCCC	25.55	28555341
523	Phosphorylation	LPNGRELTPASPTCT CCCCCEECCCCCCCC	16.44	30266825
526	Phosphorylation	GRELTPASPTCTNSV CCEECCCCCCCCCCC	23.19	19664994
528	Phosphorylation	ELTPASPTCTNSVSK EECCCCCCCCCCCCC	29.48	30266825
530	Phosphorylation	TPASPTCTNSVSKNE CCCCCCCCCCCCCCH	32.76	30266825
532	Phosphorylation	ASPTCTNSVSKNETH CCCCCCCCCCCCHHH	15.04	30278072
534	Phosphorylation	PTCTNSVSKNETHAE CCCCCCCCCCHHHHH	29.59	23927012
538	Phosphorylation	NSVSKNETHAEVLEQ CCCCCCHHHHHHHHH	35.46	22210691
552	Phosphorylation	QQNELCPYESKFDSS HHHCCCCCCCCCCHH	31.66	27732954
554	Phosphorylation	NELCPYESKFDSSLL HCCCCCCCCCCHHHC	32.55	26074081
558	Phosphorylation	PYESKFDSSLLSSDD CCCCCCCHHHCCCCC	26.47	30266825
559	Phosphorylation	YESKFDSSLLSSDDE CCCCCCHHHCCCCCC	34.86	30266825
562	Phosphorylation	KFDSSLLSSDDETKC CCCHHHCCCCCCCCC	36.69	29255136
563	Phosphorylation	FDSSLLSSDDETKCK CCHHHCCCCCCCCCC	49.39	29255136
567	Phosphorylation	LLSSDDETKCKPNSA HCCCCCCCCCCCCCH	49.05	29255136
573	Phosphorylation	ETKCKPNSASEVIGP CCCCCCCCHHHCCCC	41.52	26074081
575	Phosphorylation	KCKPNSASEVIGPVS CCCCCCHHHCCCCCC	32.02	26074081
605	Phosphorylation	DNVENVVSFNAKEHE CCCCCEECCCHHHHH	14.43	24719451
662	Phosphorylation	IEVQSVISDEELQAE EEEEEEECCHHHHHH	36.49	22817901
678	Phosphorylation	PETSKPPSEQGEEEL CCCCCCCHHHCCCCC	51.59	22817901
697	Phosphorylation	EGEAPAESESLLRDN CCCCCCCCHHHHCCC	34.29	25850435
699	Phosphorylation	EAPAESESLLRDNSE CCCCCCHHHHCCCCC	41.82	21815630
705	Phosphorylation	ESLLRDNSERDDVDG HHHHCCCCCCCCCCC	37.99	30576142
724	Phosphorylation	AEKDAEDSLHEWQDI HHHHHHHHHHHHHCC	24.11	25159151
738	Phosphorylation	INLEELETLESNLLA CCHHHHHHHHHHHHH	48.74	20068231
741	Phosphorylation	EELETLESNLLAQQN HHHHHHHHHHHHHHH	35.57	20068231
749	Phosphorylation	NLLAQQNSLKAQKQQ HHHHHHHHHHHHHHH	27.23	20068231
751	Ubiquitination	LAQQNSLKAQKQQQE HHHHHHHHHHHHHHH	48.90	29967540
830	Ubiquitination	RNFFNKNKFVEYYQY HHCCCCCCCEEEEEE	53.01	-
904	Ubiquitination	HEAQKNPKIRPNPHD HHHHHCCCCCCCCCC	61.82	29967540
920	Phosphorylation	KVKKKLRTLQLTPGF HHHHHHCCCCCCCCC	29.32	20068231
924	Phosphorylation	KLRTLQLTPGFPNPA HHCCCCCCCCCCCHH	14.38	20068231
936	Phosphorylation	NPAVAEAYLKPVVDD CHHHHHHHHCCEEEC	13.53	20068231
952	Ubiquitination	KGSFLWGKPDLDKIR CCCCCCCCCCHHHHH	24.63	29967540
971	Phosphorylation	RYFGWNRTKTDESLF HHHCCCCCCCCCHHH	34.77	23403867
972	Ubiquitination	YFGWNRTKTDESLFP HHCCCCCCCCCHHHH	51.22	29967540
973	Phosphorylation	FGWNRTKTDESLFPV HCCCCCCCCCHHHHH	44.37	23403867
976	Phosphorylation	NRTKTDESLFPVLKQ CCCCCCCHHHHHHHH	37.81	23403867
982	Ubiquitination	ESLFPVLKQLDAQQT CHHHHHHHHHCHHHH	49.39	29967540
995	Phosphorylation	QTQLRIDSFFRLAQQ HHHHHHHHHHHHHHH	24.74	24719451
1004	Ubiquitination	FRLAQQEKEDAKRIK HHHHHHHHHHHHHHH	57.46	24816145
1012	Phosphorylation	EDAKRIKSQRLNRAV HHHHHHHHHHHHHHH	20.40	24719451
1020	Phosphorylation	QRLNRAVTCMLRKEK HHHHHHHHHHHHHHH	7.39	24719451
1032	Phosphorylation	KEKEAAASEIEAVSV HHHHHHHHHHHHHHH	34.09	30576142
1050	Acetylation	KEFELLDKAKGKTQK HHHHHHHHHCCCCCC	52.55	25953088
1050	Ubiquitination	KEFELLDKAKGKTQK HHHHHHHHHCCCCCC	52.55	-
1063	Phosphorylation	QKRGITNTLEESSSL CCCCCCCHHHHCCHH	27.22	28555341
1067	Phosphorylation	ITNTLEESSSLKRKR CCCHHHHCCHHCHHH	18.82	23401153
1068	Phosphorylation	TNTLEESSSLKRKRL CCHHHHCCHHCHHHC	42.86	30576142
1069	Phosphorylation	NTLEESSSLKRKRLS CHHHHCCHHCHHHCC	47.38	25159151
1071	Methylation	LEESSSLKRKRLSDS HHHCCHHCHHHCCCC	58.80	115978467
1071	Ubiquitination	LEESSSLKRKRLSDS HHHCCHHCHHHCCCC	58.80	-
1124	Phosphorylation	TAAKEPKTSASDSQN HHCCCCCCCCCCCCC	39.99	27794612
1125	Phosphorylation	AAKEPKTSASDSQNS HCCCCCCCCCCCCCC	31.72	27794612
1127	Phosphorylation	KEPKTSASDSQNSVK CCCCCCCCCCCCCCC	37.25	27794612
1129	Phosphorylation	PKTSASDSQNSVKEA CCCCCCCCCCCCCCC	28.85	21712546
1132	Phosphorylation	SASDSQNSVKEAPVK CCCCCCCCCCCCCCC	27.25	21712546
1139	Acetylation	SVKEAPVKNGGATTS CCCCCCCCCCCCCCC	49.14	7711251
1145	Phosphorylation	VKNGGATTSSSSDSD CCCCCCCCCCCCCCC	26.52	-
1147	Phosphorylation	NGGATTSSSSDSDDD CCCCCCCCCCCCCCC	31.59	-
1148	Phosphorylation	GGATTSSSSDSDDDG CCCCCCCCCCCCCCC	37.62	-
1149	Phosphorylation	GATTSSSSDSDDDGG CCCCCCCCCCCCCCC	42.98	-
1151	Phosphorylation	TTSSSSDSDDDGGKE CCCCCCCCCCCCCCE	44.91	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	DTL	Q9NZJ0	PMID:25483071

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ERCC5_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 ERCC5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCNA_HUMAN	PCNA	physical	9305916
ERCC2_HUMAN	ERCC2	physical	8652557
EWS_HUMAN	EWSR1	physical	16713569
RPB1_HUMAN	POLR2A	physical	16246722
ERCC6_HUMAN	ERCC6	physical	16246722
DTL_HUMAN	DTL	physical	25483071
BRCA2_HUMAN	BRCA2	physical	26833090
PALB2_HUMAN	PALB2	physical	26833090
RAD51_HUMAN	RAD51	physical	26833090
BRCA1_HUMAN	BRCA1	physical	26833090

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
278780	Xeroderma pigmentosum complementation group G (XP-G)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ERCC5_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-8, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-384; SER-559; SER-562AND SER-563, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-384; SER-526; SER-562AND SER-563, AND MASS SPECTROMETRY.	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-156; SER-157; THR-338;SER-341; SER-355; SER-356; SER-357; SER-382; SER-384; SER-423;SER-424; SER-428; SER-559; SER-562 AND SER-563, 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-384, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND SER-526, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND SER-526, ANDMASS SPECTROMETRY.	18187866 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-157; SER-355;SER-356; SER-357; SER-384 AND SER-724, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-338; SER-341; SER-355;SER-356; SER-357; SER-384; SER-428; SER-526 AND SER-563, AND MASSSPECTROMETRY.	15302935 [Abstract]