CMGA_HUMAN - dbPTM
CMGA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CMGA_HUMAN
UniProt AC P10645
Protein Name Chromogranin-A
Gene Name CHGA
Organism Homo sapiens (Human).
Sequence Length 457
Subcellular Localization Cytoplasmic vesicle, secretory vesicle lumen. Cytoplasmic vesicle, secretory vesicle membrane. Secreted. Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intra
Protein Description Pancreastatin: Strongly inhibits glucose induced insulin release from the pancreas.; Catestatin: Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist. [PubMed: 15326220 Displays antibacterial activity against Gram-positive bacteria S.aureus and M.luteus, and Gram-negative bacteria E.coli and P.aeruginosa]
Protein Sequence MRSAAVLALLLCAGQVTALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAHQQKKHSGFEDELSEVLENQSSQAELKEAVEEPSSKDVMEKREDSKEAEKSGEATDGARPQALPEPMQESKAEGNNQAPGEEEEEEEEATNTHPPASLPSQKYPGPQAEGDSEGLSQGLVDREKGLSAEPGWQAKREEEEEEEEEAEAGEEAVPEEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGAGKPGAEEAQDPEGKGEQEHSQQKEEEEEMAVVPQGLFRGGKSGELEQEEERLSKEWEDSKRWSKMDQLAKELTAEKRLEGQEEEEDNRDSSMKLSFRARAYGFRGPGPQLRRGWRPSSREDSLEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLQALRRG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
48O-linked_GlycosylationSDTLSKPSPMPVSQE
HHHCCCCCCCCCCHH		37.25OGP
53PhosphorylationKPSPMPVSQECFETL
CCCCCCCCHHHHHHH		17.8726657352
59PhosphorylationVSQECFETLRGDERI
CCHHHHHHHCCCHHH		11.0829691806
88UbiquitinationDLALQGAKERAHQQK
HHHHHHHHHHHHHHH		55.33-
98PhosphorylationAHQQKKHSGFEDELS
HHHHHCCCCHHHHHH		54.8026657352
105PhosphorylationSGFEDELSEVLENQS
CCHHHHHHHHHHCCC		24.5026657352
112PhosphorylationSEVLENQSSQAELKE
HHHHHCCCCHHHHHH		35.6826657352
113PhosphorylationEVLENQSSQAELKEA
HHHHCCCCHHHHHHH		24.5226657352
125PhosphorylationKEAVEEPSSKDVMEK
HHHHHCCCHHHHHHH		53.9829691806
126PhosphorylationEAVEEPSSKDVMEKR
HHHHCCCHHHHHHHH		43.5226657352
136PhosphorylationVMEKREDSKEAEKSG
HHHHHHHHHHHHHHC		27.8726657352
142PhosphorylationDSKEAEKSGEATDGA
HHHHHHHHCCCCCCC		33.1126657352
146PhosphorylationAEKSGEATDGARPQA
HHHHCCCCCCCCCCC		30.5726657352
161PhosphorylationLPEPMQESKAEGNNQ
CCCCHHHHHCCCCCC		21.9227732954
181O-linked_GlycosylationEEEEEEATNTHPPAS
HHHHHHHHCCCCCCC		43.889852066
181PhosphorylationEEEEEEATNTHPPAS
HHHHHHHHCCCCCCC		43.8823312004
181O-linked_GlycosylationEEEEEEATNTHPPAS
HHHHHHHHCCCCCCC		43.889852066
183PhosphorylationEEEEATNTHPPASLP
HHHHHHCCCCCCCCC		31.2523312004
183O-linked_GlycosylationEEEEATNTHPPASLP
HHHHHHCCCCCCCCC		31.259852066
183O-linked_GlycosylationEEEEATNTHPPASLP
HHHHHHCCCCCCCCC		31.259852066
188PhosphorylationTNTHPPASLPSQKYP
HCCCCCCCCCCCCCC		46.7326657352
191O-linked_GlycosylationHPPASLPSQKYPGPQ
CCCCCCCCCCCCCCC		44.60OGP
191PhosphorylationHPPASLPSQKYPGPQ
CCCCCCCCCCCCCCC		44.6023312004
194PhosphorylationASLPSQKYPGPQAEG
CCCCCCCCCCCCCCC		13.048910482
203PhosphorylationGPQAEGDSEGLSQGL
CCCCCCCCCCHHHCC		44.4126657352
207PhosphorylationEGDSEGLSQGLVDRE
CCCCCCHHHCCCCHH		32.8126657352
207O-linked_GlycosylationEGDSEGLSQGLVDRE
CCCCCCHHHCCCCHH		32.81-
207O-linked_GlycosylationEGDSEGLSQGLVDRE
CCCCCCHHHCCCCHH		32.819115255
218PhosphorylationVDREKGLSAEPGWQA
CCHHHCCCCCCCHHH		38.9726657352
251O-linked_GlycosylationVPEEEGPTVVLNPHP
CCCCCCCEEEECCCC		33.829115255
251O-linked_GlycosylationVPEEEGPTVVLNPHP
CCCCCCCEEEECCCC		33.829115255
270PhosphorylationKEIRKGESRSEALAV
CHHHCCCCHHHHHCC		50.1822817900
272PhosphorylationIRKGESRSEALAVDG
HHCCCCHHHHHCCCC		36.1823312004
300PhosphorylationGKGEQEHSQQKEEEE
CCCHHHHHHHHHHHH		33.2926657352
319AmidationVPQGLFRGGKSGELE
CCCCHHCCCCCCCHH		40.312830133
319Glycine amideVPQGLFRGGKSGELE
CCCCHHCCCCCCCHH		40.31-
322PhosphorylationGLFRGGKSGELEQEE
CHHCCCCCCCHHHHH		40.5514997482
333PhosphorylationEQEEERLSKEWEDSK
HHHHHHHHHHHHHHH		34.4514997482
339PhosphorylationLSKEWEDSKRWSKMD
HHHHHHHHHHHHHHH		16.7727732954
370PhosphorylationEEEDNRDSSMKLSFR
CCCCCCCCHHHHHHH		29.1524719451
371PhosphorylationEEDNRDSSMKLSFRA
CCCCCCCHHHHHHHH		24.9923312004
372OxidationEDNRDSSMKLSFRAR
CCCCCCHHHHHHHHH		6.1517991725
372Methionine sulfoxideEDNRDSSMKLSFRAR
CCCCCCHHHHHHHHH		6.15-
373UbiquitinationDNRDSSMKLSFRARA
CCCCCHHHHHHHHHH		42.82-
375PhosphorylationRDSSMKLSFRARAYG
CCCHHHHHHHHHHHC		13.7325554490
381PhosphorylationLSFRARAYGFRGPGP
HHHHHHHHCCCCCCH		15.9624043423
397PhosphorylationLRRGWRPSSREDSLE
CCCCCCCCCHHHHHH		33.1926657352
398PhosphorylationRRGWRPSSREDSLEA
CCCCCCCCHHHHHHC		42.2326657352
402PhosphorylationRPSSREDSLEAGLPL
CCCCHHHHHHCCCCC		24.2921082442
424PhosphorylationEKKEEEGSANRRPED
HHCCCCCCCCCCHHH		26.17-
432Pyrrolidone_carboxylic_acidANRRPEDQELESLSA
CCCCHHHHHHHHHHH		56.35-
436PhosphorylationPEDQELESLSAIEAE
HHHHHHHHHHHHHHH		40.0026657352
438PhosphorylationDQELESLSAIEAELE
HHHHHHHHHHHHHHH		36.1626657352
456AmidationHQLQALRRG------
HHHHHHHCC------		56.9012442257
456Arginine amideHQLQALRRG------
HHHHHHHCC------		56.90-
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

Oops, there are no upstream regulatory protein records of CMGA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CMGA_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 CMGA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAPC2_HUMANSAPCD2physical
28514442
SGF29_HUMANCCDC101physical
28514442
DENR_HUMANDENRphysical
28514442
Drug and Disease Associations
Kegg Disease
H00034 Carcinoid
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 CMGA_HUMAN

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Related Literatures of Post-Translational Modification
Amidation
ReferencePubMed
"Isolation of human pancreastatin fragment containing the activesequence from a glucagonoma.";
Sekiya K., Ghatei M.A., Minamino N., Bretherton-Watt D., Matsuo H.,Bloom S.R.;
FEBS Lett. 228:153-156(1988).
Cited for: PROTEIN SEQUENCE OF 291-319.
O-linked Glycosylation
ReferencePubMed
"Phosphorylation and O-glycosylation sites of human chromogranin A(CGA79-439) from urine of patients with carcinoid tumors.";
Gadroy P., Stridsberg M., Capon C., Michalski J.-C., Strub J.-M.,van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.;
J. Biol. Chem. 273:34087-34097(1998).
Cited for: GLYCOSYLATION AT THR-181; THR-183 AND THR-251, AND PHOSPHORYLATION ATSER-218; SER-270 AND SER-333.
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-113; SER-136;SER-142; SER-203; SER-300; SER-322; SER-333 AND SER-402, AND MASSSPECTROMETRY.
"Identification and characterization of phosphorylated proteins in thehuman pituitary.";
Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.;
Proteomics 4:587-598(2004).
Cited for: PHOSPHORYLATION AT SER-322.
"Phosphorylation and O-glycosylation sites of human chromogranin A(CGA79-439) from urine of patients with carcinoid tumors.";
Gadroy P., Stridsberg M., Capon C., Michalski J.-C., Strub J.-M.,van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.;
J. Biol. Chem. 273:34087-34097(1998).
Cited for: GLYCOSYLATION AT THR-181; THR-183 AND THR-251, AND PHOSPHORYLATION ATSER-218; SER-270 AND SER-333.

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