dbPTM

CSK22_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CSK22_HUMAN
UniProt AC	P19784
Protein Name	Casein kinase II subunit alpha'
Gene Name	CSNK2A2
Organism	Homo sapiens (Human).
Sequence Length	350
Subcellular Localization
Protein Description	Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV..
Protein Sequence	MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Nitration	AGSRARVYAEVNSLR CCCHHEEEEEHHHHH	7.47	-
13	Phosphorylation	AGSRARVYAEVNSLR CCCHHEEEEEHHHHH	7.47	28796482
18	Phosphorylation	RVYAEVNSLRSREYW EEEEEHHHHHCCCCC	30.27	28176443
21	Phosphorylation	AEVNSLRSREYWDYE EEHHHHHCCCCCCEE	34.45	17192257
24	Phosphorylation	NSLRSREYWDYEAHV HHHHCCCCCCEEECC	11.50	28796482
27	Phosphorylation	RSREYWDYEAHVPSW HCCCCCCEEECCCCC	10.81	28796482
33	Ubiquitination	DYEAHVPSWGNQDDY CEEECCCCCCCHHHH	46.67	24816145
45	Ubiquitination	DDYQLVRKLGRGKYS HHHHHHHHHCCCCHH	48.06	22817900
50	Ubiquitination	VRKLGRGKYSEVFEA HHHHCCCCHHHHHHE	44.22	22817900
50	Acetylation	VRKLGRGKYSEVFEA HHHHCCCCHHHHHHE	44.22	25953088
51	Phosphorylation	RKLGRGKYSEVFEAI HHHCCCCHHHHHHEE	16.94	20090780
52	Phosphorylation	KLGRGKYSEVFEAIN HHCCCCHHHHHHEEE	30.67	20071362
62	Ubiquitination	FEAINITNNERVVVK HHEEECCCCCEEEEE	44.56	24816145
69	Ubiquitination	NNERVVVKILKPVKK CCCEEEEEEEHHCCH	30.61	-
72	Ubiquitination	RVVVKILKPVKKKKI EEEEEEEHHCCHHHC	51.76	-
75	Acetylation	VKILKPVKKKKIKRE EEEEHHCCHHHCHHH	68.36	25953088
84	Ubiquitination	KKIKREVKILENLRG HHCHHHHHHHHHCCC	36.50	29967540
90	Methylation	VKILENLRGGTNIIK HHHHHHCCCCCEEHH	53.75	-
97	Acetylation	RGGTNIIKLIDTVKD CCCCEEHHHHHHCCC	35.28	19608861
103	Malonylation	IKLIDTVKDPVSKTP HHHHHHCCCCCCCCC	59.41	26320211
103	Acetylation	IKLIDTVKDPVSKTP HHHHHHCCCCCCCCC	59.41	23236377
103	Succinylation	IKLIDTVKDPVSKTP HHHHHHCCCCCCCCC	59.41	23954790
111	Ubiquitination	DPVSKTPALVFEYIN CCCCCCCCHHEEECC	22.91	22817900
116	Phosphorylation	TPALVFEYINNTDFK CCCHHEEECCCCCHH	9.48	-
119	Ubiquitination	LVFEYINNTDFKQLY HHEEECCCCCHHHHH	31.31	24816145
123	Ubiquitination	YINNTDFKQLYQILT ECCCCCHHHHHHHHH	42.05	22817900
124	Ubiquitination	INNTDFKQLYQILTD CCCCCHHHHHHHHHH	45.45	22817900
140	Ubiquitination	DIRFYMYELLKALDY HHHHHHHHHHHHHHH	30.97	22817900
152	Ubiquitination	LDYCHSKGIMHRDVK HHHHHHCCCCCCCCC	26.01	22817900
153	Ubiquitination	DYCHSKGIMHRDVKP HHHHHCCCCCCCCCC	2.12	22817900
159	Ubiquitination	GIMHRDVKPHNVMID CCCCCCCCCCCEEEE	44.86	29967540
159	Acetylation	GIMHRDVKPHNVMID CCCCCCCCCCCEEEE	44.86	26051181
164	Sulfoxidation	DVKPHNVMIDHQQKK CCCCCCEEEECCHHH	3.46	30846556
170	Ubiquitination	VMIDHQQKKLRLIDW EEEECCHHHHHHHHH	47.40	24816145
180	Ubiquitination	RLIDWGLAEFYHPAQ HHHHHHHHHHCCHHH	10.83	27667366
193	Ubiquitination	AQEYNVRVASRYFKG HHHCCCEEEHHHCCC	5.03	24816145
195	Phosphorylation	EYNVRVASRYFKGPE HCCCEEEHHHCCCCE	25.34	28355574
197	Ubiquitination	NVRVASRYFKGPELL CCEEEHHHCCCCEEE	13.72	22817900
197	Phosphorylation	NVRVASRYFKGPELL CCEEEHHHCCCCEEE	13.72	23186163
209	Ubiquitination	ELLVDYQMYDYSLDM EEEEEEECCCCCHHH	1.93	22817900
210	Ubiquitination	LLVDYQMYDYSLDMW EEEEEECCCCCHHHH	9.01	22817900
210	Phosphorylation	LLVDYQMYDYSLDMW EEEEEECCCCCHHHH	9.01	-
222	Ubiquitination	DMWSLGCMLASMIFR HHHHHHHHHHHHHHH	3.12	24816145
240	Phosphorylation	FFHGQDNYDQLVRIA CCCCCCCHHHHHHHH	17.23	22817900
248	Ubiquitination	DQLVRIAKVLGTEEL HHHHHHHHHHCHHHH	35.30	22817900
256	Phosphorylation	VLGTEELYGYLKKYH HHCHHHHHHHHHHHC	13.65	12628006
260	Acetylation	EELYGYLKKYHIDLD HHHHHHHHHHCCCCC	42.68	25953088
260	Ubiquitination	EELYGYLKKYHIDLD HHHHHHHHHHCCCCC	42.68	21906983
261	Ubiquitination	ELYGYLKKYHIDLDP HHHHHHHHHCCCCCH	39.19	33845483
266	Ubiquitination	LKKYHIDLDPHFNDI HHHHCCCCCHHHHHH	12.49	27667366
279	Ubiquitination	DILGQHSRKRWENFI HHCCHHHHHHHHHHC	30.36	24816145
280	Ubiquitination	ILGQHSRKRWENFIH HCCHHHHHHHHHHCC	65.95	-
280	Malonylation	ILGQHSRKRWENFIH HCCHHHHHHHHHHCC	65.95	26320211
288	Phosphorylation	RWENFIHSENRHLVS HHHHHCCCCCCCCCC	31.58	17192257
304	Ubiquitination	EALDLLDKLLRYDHQ HHHHHHHHHHCCCHH	49.76	-
308	Phosphorylation	LLDKLLRYDHQQRLT HHHHHHCCCHHHCCC	20.11	26074081
315	Phosphorylation	YDHQQRLTAKEAMEH CCHHHCCCHHHHHHC	37.56	26074081
317	Ubiquitination	HQQRLTAKEAMEHPY HHHCCCHHHHHHCCC	40.55	27667366
324	Phosphorylation	KEAMEHPYFYPVVKE HHHHHCCCCHHHCCC	20.04	26074081
326	Phosphorylation	AMEHPYFYPVVKEQS HHHCCCCHHHCCCCC	6.83	26074081
330	Ubiquitination	PYFYPVVKEQSQPCA CCCHHHCCCCCCCCC	50.71	32015554
330	Acetylation	PYFYPVVKEQSQPCA CCCHHHCCCCCCCCC	50.71	26051181
333	Phosphorylation	YPVVKEQSQPCADNA HHHCCCCCCCCCCCC	36.86	25159151
343	Phosphorylation	CADNAVLSSGLTAAR CCCCCHHCCCCCCCC	18.76	27050516
347	O-linked_Glycosylation	AVLSSGLTAAR---- CHHCCCCCCCC----	23.07	28657654

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	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CSK22_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 CSK22_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUCL_HUMAN	NCL	physical	8663258
KLF1_HUMAN	KLF1	physical	9722526
PTEN_HUMAN	PTEN	physical	12297295
TF3B_HUMAN	BRF1	physical	11997511
TOP1_HUMAN	TOP1	physical	2998765
TF65_HUMAN	RELA	physical	10938077
MGMT_HUMAN	MGMT	physical	10667577
CSK2B_HUMAN	CSNK2B	physical	10799509
FGF1_HUMAN	FGF1	physical	12145206
FGF2_HUMAN	FGF2	physical	12145206
MAF1_HUMAN	MAF1	physical	21383183
MAF1_YEAST	MAF1	physical	21383183
ABCA1_HUMAN	ABCA1	physical	15218032
HDAC6_HUMAN	HDAC6	physical	21486957
CSK2B_HUMAN	CSNK2B	physical	21486957
CSK2B_HUMAN	CSNK2B	physical	22939629
TOP2A_HUMAN	TOP2A	physical	22939629
PAF1_HUMAN	PAF1	physical	22939629
TGM2_HUMAN	TGM2	physical	21988832
LAMC3_HUMAN	LAMC3	physical	21988832
DCPS_HUMAN	DCPS	physical	21988832
CSK2B_HUMAN	CSNK2B	physical	21988832
H12_HUMAN	HIST1H1C	physical	21988832
PDIA1_HUMAN	P4HB	physical	21988832
EI2BB_HUMAN	EIF2B2	physical	21988832
ZNHI3_HUMAN	ZNHIT3	physical	21988832
TTL12_HUMAN	TTLL12	physical	21988832
ZN219_HUMAN	ZNF219	physical	21988832
SNX6_HUMAN	SNX6	physical	21988832
ZN670_HUMAN	ZNF670	physical	21988832
NAP1_YEAST	NAP1	physical	18086883
SAP18_HUMAN	SAP18	physical	23455922
NRP1_HUMAN	NRP1	physical	23455922
PLRG1_HUMAN	PLRG1	physical	23455922
EFC14_HUMAN	EFCAB14	physical	23455922
GPC4_HUMAN	GPC4	physical	23455922
EIF3J_HUMAN	EIF3J	physical	23455922
SPF27_HUMAN	BCAS2	physical	23455922
BCR_HUMAN	BCR	physical	23455922
CD11B_HUMAN	CDK11B	physical	23455922
BRD2_HUMAN	BRD2	physical	23455922
SDC2_HUMAN	SDC2	physical	23455922
DEK_HUMAN	DEK	physical	23455922
COIL_HUMAN	COIL	physical	23455922
ECHA_HUMAN	HADHA	physical	23455922
PI42A_HUMAN	PIP4K2A	physical	23455922
ECHB_HUMAN	HADHB	physical	23455922
EIF3B_HUMAN	EIF3B	physical	23455922
DCAF7_HUMAN	DCAF7	physical	23455922
WDR5_HUMAN	WDR5	physical	23455922
CSK2B_HUMAN	CSNK2B	physical	23455922
CSK21_HUMAN	CSNK2A1	physical	23455922
PI42B_HUMAN	PIP4K2B	physical	23455922
KMT2A_HUMAN	KMT2A	physical	23455922
RING1_HUMAN	RING1	physical	23455922
TCOF_HUMAN	TCOF1	physical	23455922
SQSTM_HUMAN	SQSTM1	physical	23455922
RRP1B_HUMAN	RRP1B	physical	23455922
NOLC1_HUMAN	NOLC1	physical	23455922
PCGF3_HUMAN	PCGF3	physical	23455922
HAGHL_HUMAN	HAGHL	physical	23455922
RN111_HUMAN	RNF111	physical	23455922
CK057_HUMAN	C11orf57	physical	23455922
HDGR2_HUMAN	HDGFRP2	physical	23455922
PCGF5_HUMAN	PCGF5	physical	23455922
ZCH18_HUMAN	ZC3H18	physical	23455922
YAF2_HUMAN	YAF2	physical	23455922
SRRM1_HUMAN	SRRM1	physical	23455922
ZN687_HUMAN	ZNF687	physical	23455922
RYBP_HUMAN	RYBP	physical	23455922
NKAP_HUMAN	NKAP	physical	23455922
PI42C_HUMAN	PIP4K2C	physical	23455922
AUTS2_HUMAN	AUTS2	physical	23455922
CR025_HUMAN	C18orf25	physical	23455922
CCNL2_HUMAN	CCNL2	physical	23455922
CDC5L_HUMAN	CDC5L	physical	23455922
RING2_HUMAN	RNF2	physical	23455922
ANM1_HUMAN	PRMT1	physical	23455922
HIRP3_HUMAN	HIRIP3	physical	23455922
MK67I_HUMAN	NIFK	physical	23455922
NOG1_HUMAN	GTPBP4	physical	23455922
PININ_HUMAN	PNN	physical	23455922
FBRS_HUMAN	FBRS	physical	23455922
FBSL_HUMAN	FBRSL1	physical	23455922
SDA1_HUMAN	SDAD1	physical	23455922
GPTC2_HUMAN	GPATCH2	physical	23455922
TAP26_HUMAN	CCDC59	physical	23455922
S30BP_HUMAN	SAP30BP	physical	23455922
CCNL1_HUMAN	CCNL1	physical	23455922
PRP19_HUMAN	PRPF19	physical	23455922
CD11A_HUMAN	CDK11A	physical	23455922
TR150_HUMAN	THRAP3	physical	23455922
PRC2C_HUMAN	PRRC2C	physical	23455922
TRI41_HUMAN	TRIM41	physical	25416956
LAC1_YEAST	LAC1	physical	25429105
SIR1_MOUSE	Sirt1	physical	19680552
KDM1A_HUMAN	KDM1A	physical	25999347
CSK2B_HUMAN	CSNK2B	physical	23555304
DEC1_HUMAN	DEC1	physical	23555304
BHE41_HUMAN	BHLHE41	physical	23555304
NR1D2_HUMAN	NR1D2	physical	23555304
PCGF3_HUMAN	PCGF3	physical	26186194
PHRF1_HUMAN	PHRF1	physical	26186194
NKAP_HUMAN	NKAP	physical	26186194
BCLF1_HUMAN	BCLAF1	physical	26186194
LC7L2_HUMAN	LUC7L2	physical	26186194
CK057_HUMAN	C11orf57	physical	26186194
KMT2A_HUMAN	KMT2A	physical	26186194
CDC5L_HUMAN	CDC5L	physical	26186194
BCR_HUMAN	BCR	physical	26186194
CD11B_HUMAN	CDK11B	physical	26186194
ZN687_HUMAN	ZNF687	physical	26186194
CR025_HUMAN	C18orf25	physical	26186194
PKCB1_HUMAN	ZMYND8	physical	26186194
GPT2L_HUMAN	GPATCH2L	physical	26186194
EIF3J_HUMAN	EIF3J	physical	26186194
RYBP_HUMAN	RYBP	physical	26186194
AUTS2_HUMAN	AUTS2	physical	26186194
FBRS_HUMAN	FBRS	physical	26186194
CSK21_HUMAN	CSNK2A1	physical	26186194
RN111_HUMAN	RNF111	physical	26186194
ZN592_HUMAN	ZNF592	physical	26186194
RING2_HUMAN	RNF2	physical	26186194
RING1_HUMAN	RING1	physical	26186194
GPTC2_HUMAN	GPATCH2	physical	26186194
NKTR_HUMAN	NKTR	physical	26186194
HAGHL_HUMAN	HAGHL	physical	26186194
FBSL_HUMAN	FBRSL1	physical	26186194
DDX54_HUMAN	DDX54	physical	26186194
TSYL2_HUMAN	TSPYL2	physical	26186194
XPC_HUMAN	XPC	physical	26186194
YAF2_HUMAN	YAF2	physical	26186194
ZN106_HUMAN	ZNF106	physical	26186194
HIRP3_HUMAN	HIRIP3	physical	26186194
CSK21_HUMAN	CSNK2A1	physical	26344197
SIN3A_HUMAN	SIN3A	physical	26344197
SPT5H_HUMAN	SUPT5H	physical	26344197
ARRB2_HUMAN	ARRB2	physical	11877451
BTF3_HUMAN	BTF3	physical	26496610
CD11B_HUMAN	CDK11B	physical	26496610
CO5A1_HUMAN	COL5A1	physical	26496610
QOR_HUMAN	CRYZ	physical	26496610
CSK21_HUMAN	CSNK2A1	physical	26496610
CSK2B_HUMAN	CSNK2B	physical	26496610
DSC2_HUMAN	DSC2	physical	26496610
TTC3_HUMAN	TTC3	physical	26496610
SF01_HUMAN	SF1	physical	26496610
IFT88_HUMAN	IFT88	physical	26496610
RBM10_HUMAN	RBM10	physical	26496610
RABE1_HUMAN	RABEP1	physical	26496610
REPS2_HUMAN	REPS2	physical	26496610
BCL7B_HUMAN	BCL7B	physical	26496610
WDR46_HUMAN	WDR46	physical	26496610
MED21_HUMAN	MED21	physical	26496610
PITM1_HUMAN	PITPNM1	physical	26496610
MED6_HUMAN	MED6	physical	26496610
HUWE1_HUMAN	HUWE1	physical	26496610
CEPT1_HUMAN	CEPT1	physical	26496610
HPS5_HUMAN	HPS5	physical	26496610
KIF1B_HUMAN	KIF1B	physical	26496610
CAMP2_HUMAN	CAMSAP2	physical	26496610
SYNEM_HUMAN	SYNM	physical	26496610
PKCB1_HUMAN	ZMYND8	physical	26496610
ASCC1_HUMAN	ASCC1	physical	26496610
SPN90_HUMAN	NCKIPSD	physical	26496610
CCHCR_HUMAN	CCHCR1	physical	26496610
NDE1_HUMAN	NDE1	physical	26496610
EMSY_HUMAN	C11orf30	physical	26496610
RHG39_HUMAN	ARHGAP39	physical	26496610
T126A_HUMAN	TMEM126A	physical	26496610
MAK16_HUMAN	MAK16	physical	26496610
DPP9_HUMAN	DPP9	physical	26496610
PR14L_HUMAN	PRR14L	physical	26496610
GPTC2_HUMAN	GPATCH2	physical	28514442
NKAP_HUMAN	NKAP	physical	28514442
PCGF3_HUMAN	PCGF3	physical	28514442
FBRS_HUMAN	FBRS	physical	28514442
EIF3J_HUMAN	EIF3J	physical	28514442
PHRF1_HUMAN	PHRF1	physical	28514442
PKCB1_HUMAN	ZMYND8	physical	28514442
ZN687_HUMAN	ZNF687	physical	28514442
AUTS2_HUMAN	AUTS2	physical	28514442
RN111_HUMAN	RNF111	physical	28514442
ZN592_HUMAN	ZNF592	physical	28514442
RYBP_HUMAN	RYBP	physical	28514442
FBSL_HUMAN	FBRSL1	physical	28514442
HAGHL_HUMAN	HAGHL	physical	28514442
BCR_HUMAN	BCR	physical	28514442
KMT2A_HUMAN	KMT2A	physical	28514442
CR025_HUMAN	C18orf25	physical	28514442
CD11B_HUMAN	CDK11B	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
HIRP3_HUMAN	HIRIP3	physical	28514442
RING2_HUMAN	RNF2	physical	28514442
RING1_HUMAN	RING1	physical	28514442
ZN106_HUMAN	ZNF106	physical	28514442
TSYL2_HUMAN	TSPYL2	physical	28514442
LC7L2_HUMAN	LUC7L2	physical	28514442
DDX41_HUMAN	DDX41	physical	28514442
XPC_HUMAN	XPC	physical	28514442
CDC5L_HUMAN	CDC5L	physical	28514442
MDM2_HUMAN	MDM2	physical	10561590
CSK2B_HUMAN	CSNK2B	physical	10561590

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 CSK22_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-97, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13; SER-18; SER-21;TYR-240; SER-288 AND SER-343, AND MASS SPECTROMETRY.	19369195 [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-18; SER-21 AND SER-288,AND MASS SPECTROMETRY.	18691976 [Abstract]