dbPTM

XPC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	XPC_HUMAN
UniProt AC	Q01831
Protein Name	DNA repair protein complementing XP-C cells
Gene Name	XPC
Organism	Homo sapiens (Human).
Sequence Length	940
Subcellular Localization	Nucleus. Cytoplasm. Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions.
Protein Description	Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity.; The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1..
Protein Sequence	MARKRAAGGEPRGRELRSQKSKAKSKARREEEEEDAFEDEKPPKKSLLSKVSQGKRKRGCSHPGGSADGPAKKKVAKVTVKSENLKVIKDEALSDGDDLRDFPSDLKKAHHLKRGATMNEDSNEEEEESENDWEEVEELSEPVLGDVRESTAFSRSLLPVKPVEIEIETPEQAKTRERSEKIKLEFETYLRRAMKRFNKGVHEDTHKVHLLCLLANGFYRNNICSQPDLHAIGLSIIPARFTRVLPRDVDTYYLSNLVKWFIGTFTVNAELSASEQDNLQTTLERRFAIYSARDDEELVHIFLLILRALQLLTRLVLSLQPIPLKSATAKGKKPSKERLTADPGGSSETSSQVLENHTKPKTSKGTKQEETFAKGTCRPSAKGKRNKGGRKKRSKPSSSEEDEGPGDKQEKATQRRPHGRERRVASRVSYKEESGSDEAGSGSDFELSSGEASDPSDEDSEPGPPKQRKAPAPQRTKAGSKSASRTHRGSHRKDPSLPAASSSSSSSKRGKKMCSDGEKAEKRSIAGIDQWLEVFCEQEEKWVCVDCVHGVVGQPLTCYKYATKPMTYVVGIDSDGWVRDVTQRYDPVWMTVTRKCRVDAEWWAETLRPYQSPFMDREKKEDLEFQAKHMDQPLPTAIGLYKNHPLYALKRHLLKYEAIYPETAAILGYCRGEAVYSRDCVHTLHSRDTWLKKARVVRLGEVPYKMVKGFSNRARKARLAEPQLREENDLGLFGYWQTEEYQPPVAVDGKVPRNEFGNVYLFLPSMMPIGCVQLNLPNLHRVARKLDIDCVQAITGFDFHGGYSHPVTDGYIVCEEFKDVLLTAWENEQAVIERKEKEKKEKRALGNWKLLAKGLLIRERLKRRYGPKSEAAAPHTDAGGGLSSDEEEGTSSQAEAARILAASWPQNREDEEKQKLKGGPKKTKREKKAAASHLFPFEQL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
41	Sumoylation	EDAFEDEKPPKKSLL HHHCCCCCCCCHHHH	78.07	28112733
44	Acetylation	FEDEKPPKKSLLSKV CCCCCCCCHHHHHHH	64.62	20167786
45	Acetylation	EDEKPPKKSLLSKVS CCCCCCCHHHHHHHH	52.70	20167786
46	Phosphorylation	DEKPPKKSLLSKVSQ CCCCCCHHHHHHHHC	40.44	24719451
50	Acetylation	PKKSLLSKVSQGKRK CCHHHHHHHHCCCCC	45.97	20167786
50	Ubiquitination	PKKSLLSKVSQGKRK CCHHHHHHHHCCCCC	45.97	-
58	Methylation	VSQGKRKRGCSHPGG HHCCCCCCCCCCCCC	56.22	115920121
61	Phosphorylation	GKRKRGCSHPGGSAD CCCCCCCCCCCCCCC	35.22	25159151
66	Phosphorylation	GCSHPGGSADGPAKK CCCCCCCCCCCHHCC	29.15	25627689
72	Acetylation	GSADGPAKKKVAKVT CCCCCHHCCEEEEEE	57.15	25953088
79	Phosphorylation	KKKVAKVTVKSENLK CCEEEEEEEECCCEE	22.85	-
81	Sumoylation	KVAKVTVKSENLKVI EEEEEEEECCCEEEE	42.56	-
81	Sumoylation	KVAKVTVKSENLKVI EEEEEEEECCCEEEE	42.56	28112733
81	Ubiquitination	KVAKVTVKSENLKVI EEEEEEEECCCEEEE	42.56	-
81	Acetylation	KVAKVTVKSENLKVI EEEEEEEECCCEEEE	42.56	25953088
86	Ubiquitination	TVKSENLKVIKDEAL EEECCCEEEEEHHHC	54.20	-
89	Sumoylation	SENLKVIKDEALSDG CCCEEEEEHHHCCCC	53.13	28112733
94	Phosphorylation	VIKDEALSDGDDLRD EEEHHHCCCCCCHHC	46.74	29255136
104	Phosphorylation	DDLRDFPSDLKKAHH CCHHCCCHHHHHHHH	56.41	23927012
117	Phosphorylation	HHLKRGATMNEDSNE HHHHCCCCCCCCCCH	24.29	17081983
122	Phosphorylation	GATMNEDSNEEEEES CCCCCCCCCHHHHHH	39.71	22617229
129	Phosphorylation	SNEEEEESENDWEEV CCHHHHHHHCCHHHH	45.00	22617229
140	Phosphorylation	WEEVEELSEPVLGDV HHHHHHHCCCCCCCH	43.04	20068231
150	Phosphorylation	VLGDVRESTAFSRSL CCCCHHHHCCCCCCC	17.93	-
154	Phosphorylation	VRESTAFSRSLLPVK HHHHCCCCCCCCCCC	20.63	-
156	Phosphorylation	ESTAFSRSLLPVKPV HHCCCCCCCCCCCCE	32.81	21712546
161	Ubiquitination	SRSLLPVKPVEIEIE CCCCCCCCCEEEEEE	41.21	21890473
161	Acetylation	SRSLLPVKPVEIEIE CCCCCCCCCEEEEEE	41.21	23236377
161	Sumoylation	SRSLLPVKPVEIEIE CCCCCCCCCEEEEEE	41.21	28112733
169	Phosphorylation	PVEIEIETPEQAKTR CEEEEEECHHHHHHH	37.47	25159151
174	Ubiquitination	IETPEQAKTRERSEK EECHHHHHHHHHHHH	48.05	21890473
181	Ubiquitination	KTRERSEKIKLEFET HHHHHHHHHHHHHHH	46.52	-
183	Ubiquitination	RERSEKIKLEFETYL HHHHHHHHHHHHHHH	53.70	-
188	Phosphorylation	KIKLEFETYLRRAMK HHHHHHHHHHHHHHH	32.93	25841592
189	Phosphorylation	IKLEFETYLRRAMKR HHHHHHHHHHHHHHH	7.33	25841592
291	Phosphorylation	ERRFAIYSARDDEEL HHHEEEEECCCHHHH	15.66	23090842
318	Phosphorylation	LLTRLVLSLQPIPLK HHHHHHHHCCCCCCC	19.92	28152594
326	Phosphorylation	LQPIPLKSATAKGKK CCCCCCCCCCCCCCC	38.24	28152594
328	Phosphorylation	PIPLKSATAKGKKPS CCCCCCCCCCCCCCC	35.67	28152594
335	Phosphorylation	TAKGKKPSKERLTAD CCCCCCCCHHCCCCC	56.90	23898821
340	Phosphorylation	KPSKERLTADPGGSS CCCHHCCCCCCCCCC	34.92	23927012
346	Phosphorylation	LTADPGGSSETSSQV CCCCCCCCCHHHHHH	30.80	23401153
347	Phosphorylation	TADPGGSSETSSQVL CCCCCCCCHHHHHHH	48.44	23401153
349	Phosphorylation	DPGGSSETSSQVLEN CCCCCCHHHHHHHHH	35.31	23927012
350	Phosphorylation	PGGSSETSSQVLENH CCCCCHHHHHHHHHC	18.09	25159151
351	Phosphorylation	GGSSETSSQVLENHT CCCCHHHHHHHHHCC	31.56	17525332
358	Phosphorylation	SQVLENHTKPKTSKG HHHHHHCCCCCCCCC	61.70	23927012
359	Ubiquitination	QVLENHTKPKTSKGT HHHHHCCCCCCCCCC	36.65	21890473
359	Acetylation	QVLENHTKPKTSKGT HHHHHCCCCCCCCCC	36.65	26051181
361	Ubiquitination	LENHTKPKTSKGTKQ HHHCCCCCCCCCCCC	67.97	-
367	Ubiquitination	PKTSKGTKQEETFAK CCCCCCCCCCCCCCC	65.46	-
371	O-linked_Glycosylation	KGTKQEETFAKGTCR CCCCCCCCCCCCCCC	28.30	30379171
374	Ubiquitination	KQEETFAKGTCRPSA CCCCCCCCCCCCCCC	51.03	-
374	Acetylation	KQEETFAKGTCRPSA CCCCCCCCCCCCCCC	51.03	25953088
394	Phosphorylation	KGGRKKRSKPSSSEE CCCCCCCCCCCCCCC	58.77	23403867
397	Phosphorylation	RKKRSKPSSSEEDEG CCCCCCCCCCCCCCC	50.67	25159151
398	Phosphorylation	KKRSKPSSSEEDEGP CCCCCCCCCCCCCCC	50.74	26055452
399	Phosphorylation	KRSKPSSSEEDEGPG CCCCCCCCCCCCCCC	49.71	26055452
453	Phosphorylation	ELSSGEASDPSDEDS CCCCCCCCCCCCCCC	45.83	24275569
456	Phosphorylation	SGEASDPSDEDSEPG CCCCCCCCCCCCCCC	59.63	24275569
460	Phosphorylation	SDPSDEDSEPGPPKQ CCCCCCCCCCCCCCC	43.58	24275569
482	Phosphorylation	RTKAGSKSASRTHRG CCCCCCCCCCCCCCC	32.92	24719451
484	Phosphorylation	KAGSKSASRTHRGSH CCCCCCCCCCCCCCC	44.81	24719451
493	Ubiquitination	THRGSHRKDPSLPAA CCCCCCCCCCCCCCC	69.44	-
496	Phosphorylation	GSHRKDPSLPAASSS CCCCCCCCCCCCCCC	58.06	25159151
501	Phosphorylation	DPSLPAASSSSSSSK CCCCCCCCCCCCCCC	32.62	25627689
502	Phosphorylation	PSLPAASSSSSSSKR CCCCCCCCCCCCCCC	29.52	25627689
503	Phosphorylation	SLPAASSSSSSSKRG CCCCCCCCCCCCCCC	31.57	25627689
504	Phosphorylation	LPAASSSSSSSKRGK CCCCCCCCCCCCCCC	35.87	25627689
505	Phosphorylation	PAASSSSSSSKRGKK CCCCCCCCCCCCCCC	40.35	25627689
506	Phosphorylation	AASSSSSSSKRGKKM CCCCCCCCCCCCCCC	41.65	25627689
507	Phosphorylation	ASSSSSSSKRGKKMC CCCCCCCCCCCCCCC	28.46	25627689
508	Ubiquitination	SSSSSSSKRGKKMCS CCCCCCCCCCCCCCC	68.09	-
515	Phosphorylation	KRGKKMCSDGEKAEK CCCCCCCCCCHHHHH	45.19	24719451
560	Ubiquitination	GQPLTCYKYATKPMT CCCEEEEEECCCCEE	30.47	-
567	Phosphorylation	KYATKPMTYVVGIDS EECCCCEEEEEEECC	22.99	27762562
619	Ubiquitination	SPFMDREKKEDLEFQ CCCCCHHHHHHHHHH	63.46	-
620	Ubiquitination	PFMDREKKEDLEFQA CCCCHHHHHHHHHHH	52.27	-
628	Ubiquitination	EDLEFQAKHMDQPLP HHHHHHHHHCCCCCC	28.78	-
642	Ubiquitination	PTAIGLYKNHPLYAL CCHHHHHCCCHHHHH	54.55	-
650	Ubiquitination	NHPLYALKRHLLKYE CCHHHHHHHHHHHHH	29.60	-
655	Sumoylation	ALKRHLLKYEAIYPE HHHHHHHHHHHHCHH	47.61	-
655	Sumoylation	ALKRHLLKYEAIYPE HHHHHHHHHHHHCHH	47.61	-
656	Phosphorylation	LKRHLLKYEAIYPET HHHHHHHHHHHCHHH	15.57	21406692
660	Phosphorylation	LLKYEAIYPETAAIL HHHHHHHCHHHHHHH	11.32	21406692
663	Phosphorylation	YEAIYPETAAILGYC HHHHCHHHHHHHHHH	19.51	21406692
669	Phosphorylation	ETAAILGYCRGEAVY HHHHHHHHHCCCEEE	3.89	21406692
676	Phosphorylation	YCRGEAVYSRDCVHT HHCCCEEECCCCHHH	12.68	-
677	Phosphorylation	CRGEAVYSRDCVHTL HCCCEEECCCCHHHH	18.29	-
693	Ubiquitination	SRDTWLKKARVVRLG CCCCHHHHCEEEEEC	38.97	-
704	Phosphorylation	VRLGEVPYKMVKGFS EEECCCCHHHHCCCC	19.52	20068231
705	Ubiquitination	RLGEVPYKMVKGFSN EECCCCHHHHCCCCH	31.02	-
708	Ubiquitination	EVPYKMVKGFSNRAR CCCHHHHCCCCHHHH	51.22	-
711	Phosphorylation	YKMVKGFSNRARKAR HHHHCCCCHHHHHHH	33.79	20068231
711	O-linked_Glycosylation	YKMVKGFSNRARKAR HHHHCCCCHHHHHHH	33.79	30379171
750	Ubiquitination	PPVAVDGKVPRNEFG CCEEECCEECCCCCC	44.60	21890473
785	Ubiquitination	NLHRVARKLDIDCVQ CHHHHHHHCCCCHHH	40.55	-
812	Ubiquitination	HPVTDGYIVCEEFKD CCCCCCEEEEHHHHH	3.32	21890473
849	Ubiquitination	KRALGNWKLLAKGLL HHHHCCHHHHHHHHH	37.31	21890473
853	Ubiquitination	GNWKLLAKGLLIRER CCHHHHHHHHHHHHH	50.49	-
865	Phosphorylation	RERLKRRYGPKSEAA HHHHHHHHCCCCCCC	41.64	23312004
869	Phosphorylation	KRRYGPKSEAAAPHT HHHHCCCCCCCCCCC	35.28	22167270
876	Phosphorylation	SEAAAPHTDAGGGLS CCCCCCCCCCCCCCC	26.87	19664994
883	Phosphorylation	TDAGGGLSSDEEEGT CCCCCCCCCCCCCCC	38.73	29255136
884	Phosphorylation	DAGGGLSSDEEEGTS CCCCCCCCCCCCCCC	54.83	29255136
890	Phosphorylation	SSDEEEGTSSQAEAA CCCCCCCCCHHHHHH	28.60	29255136
891	Phosphorylation	SDEEEGTSSQAEAAR CCCCCCCCHHHHHHH	31.17	29255136
892	Phosphorylation	DEEEGTSSQAEAARI CCCCCCCHHHHHHHH	32.99	17525332
903	Phosphorylation	AARILAASWPQNRED HHHHHHHHCCCCCCH	33.41	25159151
921	2-Hydroxyisobutyrylation	QKLKGGPKKTKREKK HHHCCCCCCCHHHHH	76.09	-
932	Phosphorylation	REKKAAASHLFPFEQ HHHHHHHHHCCCHHH	18.92	24850871

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
94	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
129	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	DDB2	Q92466	PMID:16527807

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RD23A_HUMAN	RAD23A	physical	9164480
CETN2_HUMAN	CETN2	physical	11279143
RD23B_HUMAN	RAD23B	physical	11279143
ERCC3_HUMAN	ERCC3	physical	10734143
SNF5_HUMAN	SMARCB1	physical	19805520
H2AX_HUMAN	H2AFX	physical	19805520
DDB1_HUMAN	DDB1	physical	15882621
DDB2_HUMAN	DDB2	physical	15882621
XPA_HUMAN	XPA	physical	17154534
CETN2_HUMAN	CETN2	physical	17154534
RD23B_HUMAN	RAD23B	physical	17154534
RD23A_HUMAN	RAD23A	physical	9372924
RD23B_HUMAN	RAD23B	physical	9372924
HMGB1_HUMAN	HMGB1	physical	19446504
RD23B_HUMAN	RAD23B	physical	10873465
RD23B_HUMAN	RAD23B	physical	9164480
MDM2_HUMAN	MDM2	physical	24258024
RD23A_HUMAN	RAD23A	physical	24258024
RD23B_HUMAN	RAD23B	physical	24258024
UBP7_HUMAN	USP7	physical	25118285
RD23B_HUMAN	RAD23B	physical	22431748
TDG_HUMAN	TDG	physical	12505994
H2B1O_HUMAN	HIST1H2BO	physical	28514442
H2B1D_HUMAN	HIST1H2BD	physical	28514442
H2B1C_HUMAN	HIST1H2BD	physical	28514442
CETN2_HUMAN	CETN2	physical	28514442
PARP2_HUMAN	PARP2	physical	28514442
CETN3_HUMAN	CETN3	physical	28514442
ABC3C_HUMAN	APOBEC3C	physical	28514442
H2AW_HUMAN	H2AFY2	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
PARP1_HUMAN	PARP1	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
H2AY_HUMAN	H2AFY	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
278720	Xeroderma pigmentosum complementation group C (XP-C)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of XPC_HUMAN

Related Literatures of Post-Translational Modification

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-883 AND SER-884, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND SER-884, ANDMASS SPECTROMETRY.	18318008 [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-94; THR-169; SER-883;SER-884 AND SER-891, AND MASS SPECTROMETRY.	18669648 [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-883 AND SER-884, ANDMASS SPECTROMETRY.	18220336 [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-347; SER-351; SER-883;SER-884 AND SER-892, AND MASS SPECTROMETRY.	17525332 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND SER-884, ANDMASS SPECTROMETRY.	17487921 [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-94, AND MASSSPECTROMETRY.	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 SER-883 AND SER-884, ANDMASS SPECTROMETRY.	15302935 [Abstract]