COASY_HUMAN - dbPTM
COASY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COASY_HUMAN
UniProt AC Q13057
Protein Name Bifunctional coenzyme A synthase
Gene Name COASY
Organism Homo sapiens (Human).
Sequence Length 564
Subcellular Localization Cytoplasm. Mitochondrion matrix . The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but is also present in cell lysate.
Protein Description Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation..
Protein Sequence MAVFRSGLLVLTTPLASLAPRLASILTSAARLVNHTLYVHLQPGMSLEGPAQPQSSPVQATFEVLDFITHLYAGADVHRHLDVRILLTNIRTKSTFLPPLPTSVQNLAHPPEVVLTDFQTLDGSQYNPVKQQLVRYATSCYSCCPRLASVLLYSDYGIGEVPVEPLDVPLPSTIRPASPVAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDLRHTENEEDKVSSSSFRQRMLGNLLRPPYERPELPTCLYVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQMSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALLQKRIPKTHQALD
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
13PhosphorylationSGLLVLTTPLASLAP
CCEEEECCHHHHHHH		16.49-
15 (in isoform 2)Phosphorylation-4.8023663014
17PhosphorylationVLTTPLASLAPRLAS
EECCHHHHHHHHHHH		32.5224719451
19 (in isoform 2)Phosphorylation-5.6723663014
24PhosphorylationSLAPRLASILTSAAR
HHHHHHHHHHHHHHH		23.7920393185
27PhosphorylationPRLASILTSAARLVN
HHHHHHHHHHHHHHC		18.0429449344
28PhosphorylationRLASILTSAARLVNH
HHHHHHHHHHHHHCC		19.2420393185
29 (in isoform 2)Phosphorylation-7.4323663014
35UbiquitinationSAARLVNHTLYVHLQ
HHHHHHCCEEEEEEC		15.1224816145
88PhosphorylationLDVRILLTNIRTKST
CCHHHHHCCCCCCCC		25.7520068231
136PhosphorylationVKQQLVRYATSCYSC
HHHHHHHHHHHHHHH		13.5223401153
138PhosphorylationQQLVRYATSCYSCCP
HHHHHHHHHHHHHCH		15.4723401153
139PhosphorylationQLVRYATSCYSCCPR
HHHHHHHHHHHHCHH		11.6823401153
141PhosphorylationVRYATSCYSCCPRLA
HHHHHHHHHHCHHHH		12.4323401153
142PhosphorylationRYATSCYSCCPRLAS
HHHHHHHHHCHHHHH		17.3623401153
149PhosphorylationSCCPRLASVLLYSDY
HHCHHHHHHHHHCCC		20.2120068231
153PhosphorylationRLASVLLYSDYGIGE
HHHHHHHHCCCCCCC		8.7120068231
154PhosphorylationLASVLLYSDYGIGEV
HHHHHHHCCCCCCCC		25.0720068231
156PhosphorylationSVLLYSDYGIGEVPV
HHHHHCCCCCCCCCC		12.5220068231
172PhosphorylationPLDVPLPSTIRPASP
CCCCCCCCCCCCCCC		44.1225159151
173PhosphorylationLDVPLPSTIRPASPV
CCCCCCCCCCCCCCC		21.0425159151
178PhosphorylationPSTIRPASPVAGSPK
CCCCCCCCCCCCCCC		23.6929255136
183PhosphorylationPASPVAGSPKQPVRG
CCCCCCCCCCCCCCC		21.1329255136
191PhosphorylationPKQPVRGYYRGAVGG
CCCCCCCCCCCCCCC		4.5726074081
192PhosphorylationKQPVRGYYRGAVGGT
CCCCCCCCCCCCCCH		12.8526074081
199PhosphorylationYRGAVGGTFDRLHNA
CCCCCCCHHHHHHHH		19.2126074081
201 (in isoform 2)Phosphorylation-52.6627251275
202 (in isoform 2)Phosphorylation-33.3927251275
207 (in isoform 2)Phosphorylation-26.5227251275
207PhosphorylationFDRLHNAHKVLLSVA
HHHHHHHHHHHHHHH		26.5232645325
212 (in isoform 2)Phosphorylation-11.9627251275
212PhosphorylationNAHKVLLSVACILAQ
HHHHHHHHHHHHHHH		11.9620068231
228 (in isoform 2)Phosphorylation-42.4627251275
235 (in isoform 1)Ubiquitination-53.0821890473
235UbiquitinationDKDLLKSKLLPELLQ
CHHHHHCCCHHHHHH		53.0821890473
259UbiquitinationSEFLVDIKPSLTFDV
HHHHHCCCCCCEEEE		24.8821890473
261PhosphorylationFLVDIKPSLTFDVIP
HHHCCCCCCEEEEEE		34.7322210691
264 (in isoform 2)Ubiquitination-9.5321890473
264UbiquitinationDIKPSLTFDVIPLLD
CCCCCCEEEEEECCC		9.5321890473
288PhosphorylationSLEFLVVSEETYRGG
CCEEEEEECCEECCC		23.4122210691
291PhosphorylationFLVVSEETYRGGMAI
EEEEECCEECCCCEE		17.9222210691
324PhosphorylationLLKDLRHTENEEDKV
HHHHHCCCCCCCCCC		33.7920068231
330UbiquitinationHTENEEDKVSSSSFR
CCCCCCCCCCCHHHH		47.5033845483
332PhosphorylationENEEDKVSSSSFRQR
CCCCCCCCCHHHHHH		30.1828857561
333PhosphorylationNEEDKVSSSSFRQRM
CCCCCCCCHHHHHHH		32.7528857561
334PhosphorylationEEDKVSSSSFRQRML
CCCCCCCHHHHHHHH		26.4528857561
335PhosphorylationEDKVSSSSFRQRMLG
CCCCCCHHHHHHHHH		26.7928857561
356PhosphorylationYERPELPTCLYVIGL
CCCCCCCCEEEEEEC		27.9730387612
359UbiquitinationPELPTCLYVIGLTGI
CCCCCEEEEEECCCC		7.6833845483
359 (in isoform 2)Ubiquitination-7.68-
367PhosphorylationVIGLTGISGSGKSSI
EEECCCCCCCCHHHH		28.4030387612
369PhosphorylationGLTGISGSGKSSIAQ
ECCCCCCCCHHHHHH		35.9430387612
379UbiquitinationSSIAQRLKGLGAFVI
HHHHHHHCCCCCEEE		55.04-
408 (in isoform 2)Ubiquitination-38.22-
417UbiquitinationFGTDILHKDGIINRK
HCCCCCCCCCCCCCH		54.9629967540
441PhosphorylationKKQLKILTDIMWPII
HHHHHHHHHHHHHHH		27.2720860994
446UbiquitinationILTDIMWPIIAKLAR
HHHHHHHHHHHHHHH		7.2529967540
450UbiquitinationIMWPIIAKLAREEMD
HHHHHHHHHHHHHHH		32.0733845483
469UbiquitinationEGKRVCVIDAAVLLE
CCCCEEEEEHHHHHH		2.2321890473
479UbiquitinationAVLLEAGWQNLVHEV
HHHHHHHHHHHHHHH		7.3133845483
507PhosphorylationIVERDGLSEAAAQSR
HHHHCCCCHHHHHHH		30.6233259812
513PhosphorylationLSEAAAQSRLQSQMS
CCHHHHHHHHHHHHC		30.1721406692
536PhosphorylationHVVLSTLWEPHITQR
HHHHHHCCCCCCCHH		19.7033259812
536 (in isoform 2)Phosphorylation-19.7024719451
554UbiquitinationKAWALLQKRIPKTHQ
HHHHHHHHHCCCHHH		52.8721890473
554AcetylationKAWALLQKRIPKTHQ
HHHHHHHHHCCCHHH		52.8725953088
554 (in isoform 1)Ubiquitination-52.8721890473
558UbiquitinationLLQKRIPKTHQALD-
HHHHHCCCHHHCCC-		57.1629967540
583Ubiquitination--------------------------
--------------------------		21890473
583 (in isoform 2)Ubiquitination-21890473
587Ubiquitination------------------------------
------------------------------		29967540
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 COASY_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COASY_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 COASY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KS6B1_HUMANRPS6KB1physical
15589845
A4_HUMANAPPphysical
21832049
EFHD2_HUMANEFHD2physical
22863883
ENOG_HUMANENO2physical
22863883
GLRX3_HUMANGLRX3physical
22863883
GUAA_HUMANGMPSphysical
22863883
PPME1_HUMANPPME1physical
22863883
FCL_HUMANTSTA3physical
22863883
CNTRB_HUMANCNTROBphysical
25416956
K1958_HUMANKIAA1958physical
25416956
HPHL1_HUMANHEPHL1physical
26186194
CALL3_HUMANCALML3physical
26186194
S10A3_HUMANS100A3physical
26186194
PKP1_HUMANPKP1physical
26186194
LRC15_HUMANLRRC15physical
26186194
LEG3_HUMANLGALS3physical
26186194
DUS14_HUMANDUSP14physical
26186194
DSG4_HUMANDSG4physical
26186194
PCY2_HUMANPCYT2physical
26344197
HPHL1_HUMANHEPHL1physical
28514442
DSG4_HUMANDSG4physical
28514442
S10A3_HUMANS100A3physical
28514442
LRC15_HUMANLRRC15physical
28514442
CALL3_HUMANCALML3physical
28514442
DUS14_HUMANDUSP14physical
28514442
LEG3_HUMANLGALS3physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615643Neurodegeneration with brain iron accumulation 6 (NBIA6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COASY_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-178, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASSSPECTROMETRY.
"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-178, AND MASSSPECTROMETRY.

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