CAB3_YEAST - dbPTM
CAB3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAB3_YEAST
UniProt AC P36076
Protein Name Coenzyme A biosynthesis protein 3
Gene Name CAB3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 571
Subcellular Localization Cytoplasm .
Protein Description Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis..
Protein Sequence MTDEKVNSDQNMNGKQGVNLISSLPTTQVPVSILTNKERRKSIHDESNFERSDSHEDQSKSNSNRRNIYKNDYSTNLRDFSFANLKQNSERNKDGHEIQINTSMPANTNGQQKRFSPSLPSAVSFTVPEVERLPYHRYSISNKPGKQQQQQEQLQQNQQQEEQQKAQLQEQNQRAKQQEEVKQIQEQVQKKQTERQQLIDEKERIANAIFKENTTNDGTDIRKHSVSSGTSNSEDEVDSPSMEKNSIVHMPGDFIYFNPKSNASKPITAKAAPLSANNSTHKNKEVITAPTGPRVPFTEFFQKEDDKKFHILIGATGSVATIKVPLIIDKLFKIYGPEKISIQLIVTKPAEHFLKGLKMSTHVKIWREEDAWVFDAVNKNDTSLSLNLILHHELRKWADIFLIAPLSANTLAKLANGICNNLLTSVMRDWSPLTPVLIAPAMNTFMYINPMTKKHLTSLVQDYPFIQVLKPVEKVLICGDIGMGGMREWTDIVEIVRRRINEIRKARDEETGDKEQEQEEQEGADNEDDDDEDDEEDEEDEEEEEALNETASDESNDEEDEEDEEDVKTEV
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
8PhosphorylationMTDEKVNSDQNMNGK
CCCCCCCCCCCCCCC		43.4919823750
22PhosphorylationKQGVNLISSLPTTQV
CCCCCHHHCCCCCCC		29.0524909858
23PhosphorylationQGVNLISSLPTTQVP
CCCCHHHCCCCCCCC		31.2319823750
26PhosphorylationNLISSLPTTQVPVSI
CHHHCCCCCCCCEEE		34.8419823750
27PhosphorylationLISSLPTTQVPVSIL
HHHCCCCCCCCEEEC		26.1519823750
32PhosphorylationPTTQVPVSILTNKER
CCCCCCEEECCCHHH		13.0524909858
35PhosphorylationQVPVSILTNKERRKS
CCCEEECCCHHHHHC		42.4419823750
42PhosphorylationTNKERRKSIHDESNF
CCHHHHHCCCCCCCC		24.2822369663
47PhosphorylationRKSIHDESNFERSDS
HHCCCCCCCCCCCCC		53.5322369663
52PhosphorylationDESNFERSDSHEDQS
CCCCCCCCCCCCCHH		35.9522369663
54PhosphorylationSNFERSDSHEDQSKS
CCCCCCCCCCCHHCC		29.9822369663
59PhosphorylationSDSHEDQSKSNSNRR
CCCCCCHHCCCCCCC		50.8322369663
70AcetylationSNRRNIYKNDYSTNL
CCCCHHHHCCCCCCH		39.2724489116
74PhosphorylationNIYKNDYSTNLRDFS
HHHHCCCCCCHHHCC		17.4319823750
75PhosphorylationIYKNDYSTNLRDFSF
HHHCCCCCCHHHCCC		31.8523749301
81PhosphorylationSTNLRDFSFANLKQN
CCCHHHCCCCCCCCC		27.9520377248
116PhosphorylationNGQQKRFSPSLPSAV
CCCCCCCCCCCCCCE		20.0122369663
118PhosphorylationQQKRFSPSLPSAVSF
CCCCCCCCCCCCEEE		52.2822369663
121PhosphorylationRFSPSLPSAVSFTVP
CCCCCCCCCEEEECC		46.7422369663
124PhosphorylationPSLPSAVSFTVPEVE
CCCCCCEEEECCCCC		18.2122369663
126PhosphorylationLPSAVSFTVPEVERL
CCCCEEEECCCCCCC		27.8722890988
135PhosphorylationPEVERLPYHRYSISN
CCCCCCCCCCCCCCC		11.9722369663
138PhosphorylationERLPYHRYSISNKPG
CCCCCCCCCCCCCCC		9.3128889911
139PhosphorylationRLPYHRYSISNKPGK
CCCCCCCCCCCCCCH		21.3523749301
141PhosphorylationPYHRYSISNKPGKQQ
CCCCCCCCCCCCHHH		32.6219779198
214PhosphorylationNAIFKENTTNDGTDI
HHHHHHCCCCCCCCC		28.2421440633
215PhosphorylationAIFKENTTNDGTDIR
HHHHHCCCCCCCCCC		42.7821440633
219PhosphorylationENTTNDGTDIRKHSV
HCCCCCCCCCCHHCC		30.9920377248
225PhosphorylationGTDIRKHSVSSGTSN
CCCCCHHCCCCCCCC		27.0820377248
227PhosphorylationDIRKHSVSSGTSNSE
CCCHHCCCCCCCCCC		26.5122369663
228PhosphorylationIRKHSVSSGTSNSED
CCHHCCCCCCCCCCC		43.8922369663
230PhosphorylationKHSVSSGTSNSEDEV
HHCCCCCCCCCCCCC		27.0422369663
231PhosphorylationHSVSSGTSNSEDEVD
HCCCCCCCCCCCCCC		41.7122369663
233PhosphorylationVSSGTSNSEDEVDSP
CCCCCCCCCCCCCCC		46.3122369663
239PhosphorylationNSEDEVDSPSMEKNS
CCCCCCCCCCCCCCC		24.8522369663
241PhosphorylationEDEVDSPSMEKNSIV
CCCCCCCCCCCCCEE		43.4522369663
246PhosphorylationSPSMEKNSIVHMPGD
CCCCCCCCEEECCCC		36.7421440633
264PhosphorylationFNPKSNASKPITAKA
ECCCCCCCCCCCCCC		43.1219915539
279PhosphorylationAPLSANNSTHKNKEV
CCCCCCCCCCCCCCC		31.5328889911
330AcetylationKVPLIIDKLFKIYGP
CHHHHHHHHHHHHCC		45.4724489116
333AcetylationLIIDKLFKIYGPEKI
HHHHHHHHHHCCCCE		45.5124489116
511PhosphorylationRKARDEETGDKEQEQ
HHHHHCCCCCHHHHH		48.9424909858
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 CAB3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAB3_YEAST !!
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 CAB3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIS2_YEASTSIS2physical
14690591
VHS3_YEASTVHS3physical
14690591
CSK21_YEASTCKA1physical
14759368
CSK22_YEASTCKA2physical
14759368
UTP22_YEASTUTP22physical
14759368
SIS2_YEASTSIS2physical
14759368
CAB3_YEASTCAB3physical
14759368
VHS3_YEASTVHS3physical
14759368
SIS2_YEASTSIS2physical
16554755
VHS3_YEASTVHS3physical
16554755
CSK2B_YEASTCKB1physical
16554755
CSK21_YEASTCKA1physical
16429126
CSK22_YEASTCKA2physical
16429126
CSK2C_YEASTCKB2physical
16429126
PPZ1_YEASTPPZ1physical
16429126
HSP73_YEASTSSA3physical
16429126
SCS7_YEASTSCS7physical
18467557
VHS3_YEASTVHS3physical
18467557
OSTD_YEASTSWP1physical
18467557
PIS_YEASTPIS1physical
18467557
SIS2_YEASTSIS2physical
18467557
PPZ1_YEASTPPZ1physical
18467557
VHS3_YEASTVHS3physical
20826334
CAB5_YEASTCAB5physical
23789928
PPCS_YEASTCAB2physical
23789928
COAD_YEASTCAB4physical
23789928
CAB3_YEASTCAB3physical
23789928
SIS2_YEASTSIS2physical
23789928
VHS3_YEASTVHS3physical
23789928
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAB3_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-116; SER-118;SER-233 AND SER-264, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; THR-230;SER-231 AND SER-239, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-116; SER-121 ANDSER-124, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory