dbPTM

CO3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CO3_HUMAN
UniProt AC	P01024
Protein Name	Complement C3
Gene Name	C3
Organism	Homo sapiens (Human).
Sequence Length	1663
Subcellular Localization	Secreted.
Protein Description	C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.; Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.; C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation.; Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2. [PubMed: 8376604]
Protein Sequence	MGPTSGPSLLLLLLTHLPLALGSPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAARRRRSVQLTEKRMDKVGKYPKELRKCCEDGMRENPMRFSCQRRTRFISLGEACKKVFLDCCNYITELRRQHARASHLGLARSNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMTEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	Phosphorylation	PNILRLESEETMVLE CCEEEECCCCEEEEE	45.37	26091039
41	Phosphorylation	LRLESEETMVLEAHD EEECCCCEEEEEEEC	14.45	26091039
56	Phosphorylation	AQGDVPVTVTVHDFP CCCCCCEEEEEECCC	12.37	26091039
65	2-Hydroxyisobutyrylation	TVHDFPGKKLVLSSE EEECCCCCEEEEECC	43.08	-
70	Phosphorylation	PGKKLVLSSEKTVLT CCCEEEEECCCEEEE	29.04	26091039
71	O-linked_Glycosylation	GKKLVLSSEKTVLTP CCEEEEECCCEEEEC	38.66	OGP
85	N-linked_Glycosylation	PATNHMGNVTFTIPA CCCCCCCCEEEEEEC	23.29	17051150
85	N-linked_Glycosylation	PATNHMGNVTFTIPA CCCCCCCCEEEEEEC	23.29	17051150
107	O-linked_Glycosylation	KGRNKFVTVQATFGT CCCCCEEEEEEEECC	15.27	OGP
107	Phosphorylation	KGRNKFVTVQATFGT CCCCCEEEEEEEECC	15.27	28258704
111	O-linked_Glycosylation	KFVTVQATFGTQVVE CEEEEEEEECCCCEE	12.90	OGP
114	O-linked_Glycosylation	TVQATFGTQVVEKVV EEEEEECCCCEEEEE	17.63	OGP
124	Phosphorylation	VEKVVLVSLQSGYLF EEEEEEEECCCCEEE	19.27	28258704
127	Phosphorylation	VVLVSLQSGYLFIQT EEEEECCCCEEEEEE	34.40	28258704
137	Phosphorylation	LFIQTDKTIYTPGST EEEEECCEEECCCCE	23.25	24043423
139	Phosphorylation	IQTDKTIYTPGSTVL EEECCEEECCCCEEE	16.47	24043423
140	Phosphorylation	QTDKTIYTPGSTVLY EECCEEECCCCEEEE	19.81	24043423
143	Phosphorylation	KTIYTPGSTVLYRIF CEEECCCCEEEEEEE	19.29	24043423
144	Phosphorylation	TIYTPGSTVLYRIFT EEECCCCEEEEEEEE	22.05	24043423
147	Phosphorylation	TPGSTVLYRIFTVNH CCCCEEEEEEEECCC	9.42	24043423
219	Phosphorylation	NSPQQVFSTEFEVKE CCCCEEEEEEEEEEE	28.33	28270605
220	Phosphorylation	SPQQVFSTEFEVKEY CCCEEEEEEEEEEEE	32.98	28270605
283	Phosphorylation	QDGEQRISLPESLKR CCCCEEECCCHHHCC	39.81	-
287	Phosphorylation	QRISLPESLKRIPIE EEECCCHHHCCCCCC	36.93	23898821
289	Ubiquitination	ISLPESLKRIPIEDG ECCCHHHCCCCCCCC	58.52	2063986
297	Phosphorylation	RIPIEDGSGEVVLSR CCCCCCCCCEEEEEE	44.07	21082442
303	Phosphorylation	GSGEVVLSRKVLLDG CCCEEEEEEEEEECC	20.60	28270605
305	Ubiquitination	GEVVLSRKVLLDGVQ CEEEEEEEEEECCCC	33.58	-
350	O-linked_Glycosylation	RSGIPIVTSPYQIHF HCCCCEECCCEEEEE	25.38	OGP
358	O-linked_Glycosylation	SPYQIHFTKTPKYFK CCEEEEEECCCCCCC	21.61	OGP
426	O-linked_Glycosylation	PLSITVRTKKQELSE CEEEEEECCHHHHHH	37.95	OGP
432	O-linked_Glycosylation	RTKKQELSEAEQATR ECCHHHHHHHHHHHH	33.73	OGP
438	O-linked_Glycosylation	LSEAEQATRTMQALP HHHHHHHHHHHHHCC	26.77	OGP
459	Phosphorylation	SNNYLHLSVLRTELR CCCEEEEEEEEECCC	14.36	24719451
489	Phosphorylation	AHEAKIRYYTYLIMN HHHHHHHHEEEEEEE	12.02	21082442
490	Phosphorylation	HEAKIRYYTYLIMNK HHHHHHHEEEEEEEC	4.50	29978859
491	Phosphorylation	EAKIRYYTYLIMNKG HHHHHHEEEEEEECC	11.69	29978859
492	Phosphorylation	AKIRYYTYLIMNKGR HHHHHEEEEEEECCC	4.33	29978859
567	Phosphorylation	VGSLVVKSGQSEDRQ EEEEEEECCCCCCCC	30.38	28270605
570	Phosphorylation	LVVKSGQSEDRQPVP EEEECCCCCCCCCCC	45.02	28270605
582	Phosphorylation	PVPGQQMTLKIEGDH CCCCCEEEEEEECCC	22.14	30622161
612	Phosphorylation	LNKKNKLTQSKIWDV EECCCCCCHHHHHHH	32.19	29083192
614	Phosphorylation	KKNKLTQSKIWDVVE CCCCCCHHHHHHHHH	22.37	29083192
672	Phosphorylation	PAARRRRSVQLTEKR HHHHCHHHHHCCHHH	16.65	28355574
676	Phosphorylation	RRRSVQLTEKRMDKV CHHHHHCCHHHHHHH	23.52	-
686	Nitration	RMDKVGKYPKELRKC HHHHHCCCHHHHHHH	17.38	-
686	Phosphorylation	RMDKVGKYPKELRKC HHHHHCCCHHHHHHH	17.38	-
706	Phosphorylation	RENPMRFSCQRRTRF CCCCCCCCCCCCCCC	10.04	26091039
730	Nitration	VFLDCCNYITELRRQ HHHHHHHHHHHHHHH	8.70	-
742	Phosphorylation	RRQHARASHLGLARS HHHHHHHHHHHHHHC	17.43	26657352
798	Phosphorylation	MNIFLKDSITTWEIL HHHHHCCCCCHHHEE	21.90	26552605
800	Phosphorylation	IFLKDSITTWEILAV HHHCCCCCHHHEEEE	29.79	26552605
801	Phosphorylation	FLKDSITTWEILAVS HHCCCCCHHHEEEEE	21.30	26552605
808	Phosphorylation	TWEILAVSMSDKKGI HHHEEEEECCCCCCE	13.63	26552605
810	Phosphorylation	EILAVSMSDKKGICV HEEEEECCCCCCEEE	38.48	26552605
879	2-Hydroxyisobutyrylation	FCSLATTKRRHQQTV CCCHHCCCCCCCCCE	42.98	-
885	Phosphorylation	TKRRHQQTVTIPPKS CCCCCCCCEEECCCC	17.04	29978859
887	O-linked_Glycosylation	RRHQQTVTIPPKSSL CCCCCCEEECCCCCC	31.02	OGP
887	Phosphorylation	RRHQQTVTIPPKSSL CCCCCCEEECCCCCC	31.02	29978859
922	Phosphorylation	AVYHHFISDGVRKSL HHHHHHHCHHHHHHC	27.63	-
928	Phosphorylation	ISDGVRKSLKVVPEG HCHHHHHHCEECCCC	23.90	-
939	N-linked_Glycosylation	VPEGIRMNKTVAVRT CCCCCCCCCEEEEEE	27.31	17051150
939	N-linked_Glycosylation	VPEGIRMNKTVAVRT CCCCCCCCCEEEEEE	27.31	16335952
968	Phosphorylation	DIPPADLSDQVPDTE CCCCCCCCCCCCCCC	26.92	28270605
985	O-linked_Glycosylation	TRILLQGTPVAQMTE CEEEECCCCCEECCC	11.13	OGP
1031	Phosphorylation	AVHYLDETEQWEKFG EEEEECCHHHHHHHC	32.89	22817900
1036	Acetylation	DETEQWEKFGLEKRQ CCHHHHHHHCHHHHH	41.60	18293486
1041	Acetylation	WEKFGLEKRQGALEL HHHHCHHHHHCHHHH	55.88	18293486
1063	Phosphorylation	QLAFRQPSSAFAAFV HHHHCCCCHHHHHHH	26.43	30087585
1071	Acetylation	SAFAAFVKRAPSTWL HHHHHHHHHCCCHHH	36.07	18293486
1105	Acetylation	QVLCGAVKWLILEKQ HHHHHHHHHHHEECC	35.43	18293486
1111	Acetylation	VKWLILEKQKPDGVF HHHHHEECCCCCCCC	61.24	18293486
1113	Acetylation	WLILEKQKPDGVFQE HHHEECCCCCCCCCC	57.03	18293486
1139	Acetylation	GLRNNNEKDMALTAF CCCCCCHHHHHHHHH	55.73	18293486
1155	Acetylation	LISLQEAKDICEEQV HHHHHHHHHHHHHHH	47.04	18293486
1171	Acetylation	SLPGSITKAGDFLEA CCCCCCCCCHHHHHH	49.02	18293486
1181	Sulfoxidation	DFLEANYMNLQRSYT HHHHHHHCCCCHHHH	3.96	27929071
1194	Phosphorylation	YTVAIAGYALAQMGR HHHHHHHHHHHHCCC	6.87	-
1215	Acetylation	NKFLTTAKDKNRWED HHHHHCCCCCCCCCC	68.12	18293486
1217	Acetylation	FLTTAKDKNRWEDPG HHHCCCCCCCCCCCC	47.94	18293486
1225	Acetylation	NRWEDPGKQLYNVEA CCCCCCCCCCCCHHH	42.38	18293486
1284	Acetylation	QALAQYQKDAPDHQE HHHHHHHCCCCCCCE	51.42	18293486
1315	O-linked_Glycosylation	THRIHWESASLLRSE EEEEEHHHHHHHCCC	20.26	OGP
1315	Phosphorylation	THRIHWESASLLRSE EEEEEHHHHHHHCCC	20.26	27130503
1317	Phosphorylation	RIHWESASLLRSEET EEEHHHHHHHCCCCC	36.90	27130503
1321	Phosphorylation	ESASLLRSEETKENE HHHHHHCCCCCCCCC	39.49	26657352
1324	Phosphorylation	SLLRSEETKENEGFT HHHCCCCCCCCCCEE	39.34	27130503
1331	O-linked_Glycosylation	TKENEGFTVTAEGKG CCCCCCEEEEEECCC	28.01	OGP
1331	Phosphorylation	TKENEGFTVTAEGKG CCCCCCEEEEEECCC	28.01	23312004
1333	O-linked_Glycosylation	ENEGFTVTAEGKGQG CCCCEEEEEECCCCC	18.88	OGP
1341	O-linked_Glycosylation	AEGKGQGTLSVVTMY EECCCCCEEEEEEEE	14.15	OGP
1341	Phosphorylation	AEGKGQGTLSVVTMY EECCCCCEEEEEEEE	14.15	24275569
1343	Phosphorylation	GKGQGTLSVVTMYHA CCCCCEEEEEEEEEC	17.87	-
1346	O-linked_Glycosylation	QGTLSVVTMYHAKAK CCEEEEEEEEECCCC	15.17	OGP
1360	Acetylation	KDQLTCNKFDLKVTI CCCEECCEEEEEEEE	42.26	27178108
1364	Acetylation	TCNKFDLKVTIKPAP ECCEEEEEEEEECCC	38.89	27178108
1390	Phosphorylation	TMILEICTRYRGDQD CCHHHHHHHCCCCCC	36.07	27732954
1392	Phosphorylation	ILEICTRYRGDQDAT HHHHHHHCCCCCCCE	10.78	27732954
1436	Acetylation	ISKYELDKAFSDRNT HHHHHHHHHHCCCCE	65.05	27178108
1466	Phosphorylation	LAFKVHQYFNVELIQ EEEEEEEEECEEEEC	5.13	24043423
1480	Phosphorylation	QPGAVKVYAYYNLEE CCCCEEEEEEEECHH	5.33	24043423
1482	Phosphorylation	GAVKVYAYYNLEESC CCEEEEEEEECHHHH	3.84	24043423
1483	Phosphorylation	AVKVYAYYNLEESCT CEEEEEEEECHHHHH	12.71	24043423
1488	Phosphorylation	AYYNLEESCTRFYHP EEEECHHHHHCCCCC	16.06	24043423
1490	Phosphorylation	YNLEESCTRFYHPEK EECHHHHHCCCCCCC	32.85	24043423
1526	Acetylation	FIQKSDDKVTLEERL EEEECCCCCCHHHHH	41.95	27178108
1571	Phosphorylation	AIEQTIKSGSDEVQV HHHHHHHCCCCCEEE	39.41	27130503
1573	Phosphorylation	EQTIKSGSDEVQVGQ HHHHHCCCCCEEECC	37.37	20951140
1586	Phosphorylation	GQQRTFISPIKCREA CCEEEEECCCCHHHH	19.17	20068231
1617	N-linked_Glycosylation	DFWGEKPNLSYIIGK CCCCCCCCCEEEEEC	53.33	16335952
1626	Phosphorylation	SYIIGKDTWVEHWPE EEEEECCCCCCCCCC	34.59	28060719

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
38	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
70	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
297	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
303	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
672	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
968	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
1321	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
1573	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CO3_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 CO3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PROP_HUMAN	CFP	physical	11513971
PROP_HUMAN	CFP	physical	3421908
FHR5_HUMAN	CFHR5	physical	11058592
ITAX_HUMAN	ITGAX	physical	4062888
CO5_HUMAN	C5	physical	11367533
CFAH_HUMAN	CFH	physical	11367533
CFAB_HUMAN	CFB	physical	11367533
TGM2_HUMAN	TGM2	physical	21988832
ITB2_HUMAN	ITGB2	physical	4062888
TRFE_HUMAN	TF	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613779	Complement component 3 deficiency (C3D)
611378	Macular degeneration, age-related, 9 (ARMD9)
612925	Hemolytic uremic syndrome atypical 5 (AHUS5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CO3_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structure of compstatin in complex with complement component C3creveals a new mechanism of complement inhibition."; Janssen B.J., Halff E.F., Lambris J.D., Gros P.; J. Biol. Chem. 282:29241-29247(2007). Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-936 AND 1321-1663 INCOMPLEX WITH INHIBITOR COMPSTATIN, DISULFIDE BONDS, AND GLYCOSYLATIONAT ASN-85.	17684013 [Abstract]
"Structure of C3b in complex with CRIg gives insights into regulationof complement activation."; Wiesmann C., Katschke K.J., Yin J., Helmy K.Y., Steffek M.,Fairbrother W.J., McCallum S.A., Embuscado L., DeForge L., Hass P.E.,van Lookeren Campagne M.; Nature 444:217-220(2006). Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF C3C IN COMPLEX WITH VSIG4,X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF C3B IN COMPLEX WITH VSIG4,AND GLYCOSYLATION AT ASN-85 AND ASN-939.	17051150 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85, AND MASS SPECTROMETRY.	19159218 [Abstract]
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85, AND MASS SPECTROMETRY.	16263699 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85; ASN-939 AND ASN-1617,AND MASS SPECTROMETRY.	16335952 [Abstract]
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry."; Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; Proteomics 4:454-465(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-939, AND MASSSPECTROMETRY.	14760718 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-85.	12754519 [Abstract]
"Human complement component C3: cDNA coding sequence and derivedprimary structure."; de Bruijn M.H.L., Fey G.H.; Proc. Natl. Acad. Sci. U.S.A. 82:708-712(1985). Cited for: NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-314.	2579379 [Abstract]
Phosphorylation
Reference	PubMed
"An initial characterization of the serum phosphoproteome."; Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III; J. Proteome Res. 8:5523-5531(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-1571 ANDSER-1573, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.	19824718 [Abstract]