PIG2_YEAST - dbPTM
PIG2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIG2_YEAST
UniProt AC P40187
Protein Name GSY2-interacting protein PIG2
Gene Name PIG2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 538
Subcellular Localization
Protein Description Interacts with glycogen synthase 2 (GSY2); possibly also interacts with phosphatase 1 (GLC7)..
Protein Sequence MATTTQPQNILMDEPLNLPNNSAHNNNYGNINANIRTFAGMSMHMHPARLNSLEFLHKPRRLSNVKLHRLPQDELQRNTDMNKGMYFNGKQVHAHHPFINSGANFNAHHQDVSKLGEEEDEISPLSHDNFQYESEENGNPSPPIYKKSGELVKSSLKRRSKSLPITPKSIFNKTGSKSKHVNLDHVDTRLLQRSKSVHFDRVLPIKLFNENEKPIDVGKQMVQQDVLNFKHKPLTRLSALNGGSDSVPIEDLLSENNQNEYGDTWLQNPKGVFLFGTNSNNRRNKKKKFKLSDDDSDIENDNDSDDAINRLVRQQDKDQAHLAHGLKNLLINDDDDYLETRTNSAKSGANLFIGNSKRIVGLYNKNFPILSDRNRKSLKLNIFLNLSRGRPVFLQEITLLTGFHNMVIIGKVFVKNIYFDKKIIVRYTWDAWRTFHESECVYFSNANGILPGSNMDIFKFSIDDIHNPNDKDSNISQLEFCIQYLTWGVDRSRKEYWDNNDSANYKIDVVTNETRTGPTTDVNDNYEMKHSLFRNPFH
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
52PhosphorylationMHPARLNSLEFLHKP
CCHHHHHHHHHHCCC		33.5928889911
63PhosphorylationLHKPRRLSNVKLHRL
HCCCCCCCCCCCCCC		37.4519795423
123PhosphorylationGEEEDEISPLSHDNF
CCCCCCCCCCCCCCC		20.1022369663
126PhosphorylationEDEISPLSHDNFQYE
CCCCCCCCCCCCCCC		31.9822369663
132PhosphorylationLSHDNFQYESEENGN
CCCCCCCCCCCCCCC		19.7922369663
134PhosphorylationHDNFQYESEENGNPS
CCCCCCCCCCCCCCC		45.3221440633
141PhosphorylationSEENGNPSPPIYKKS
CCCCCCCCCCCCHHH		47.5122369663
145PhosphorylationGNPSPPIYKKSGELV
CCCCCCCCHHHHHHH		20.3822369663
160PhosphorylationKSSLKRRSKSLPITP
HHHHHHHHCCCCCCC		30.5422369663
162PhosphorylationSLKRRSKSLPITPKS
HHHHHHCCCCCCCHH		40.3922369663
166PhosphorylationRSKSLPITPKSIFNK
HHCCCCCCCHHHHCC		23.7922369663
194PhosphorylationDTRLLQRSKSVHFDR
CHHHHHHHCCCCCCC		19.1329136822
196PhosphorylationRLLQRSKSVHFDRVL
HHHHHHCCCCCCCEE		23.2825521595
292PhosphorylationKKKKFKLSDDDSDIE
CCCCCCCCCCCCCCC		39.3122369663
296PhosphorylationFKLSDDDSDIENDND
CCCCCCCCCCCCCCC		47.7022369663
304PhosphorylationDIENDNDSDDAINRL
CCCCCCCCHHHHHHH		43.5822369663
337PhosphorylationLINDDDDYLETRTNS
HCCCCCCHHHHHCCC		17.2722369663
340PhosphorylationDDDDYLETRTNSAKS
CCCCHHHHHCCCCCC		39.9522369663
342PhosphorylationDDYLETRTNSAKSGA
CCHHHHHCCCCCCCC		40.7322369663
344PhosphorylationYLETRTNSAKSGANL
HHHHHCCCCCCCCEE		36.1422369663
347PhosphorylationTRTNSAKSGANLFIG
HHCCCCCCCCEEEEC		42.7422369663
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 PIG2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIG2_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 PIG2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GPP2_YEASTGPP2physical
16554755
LSM12_YEASTLSM12physical
16554755
GAC1_YEASTGAC1physical
18719252
PHSG_YEASTGPH1physical
20489023
GYS1_YEASTGSY1physical
20489023
GYS2_YEASTGSY2physical
20489023
IMB1_YEASTKAP95physical
20489023
MAM33_YEASTMAM33physical
20489023
IMA1_YEASTSRP1physical
20489023
2ABA_YEASTCDC55genetic
22290422
RKM3_YEASTRKM3genetic
27708008
PFF1_YEASTPFF1genetic
27708008
RL41A_YEASTRPL41Agenetic
27708008
RL41B_YEASTRPL41Agenetic
27708008
FMP45_YEASTFMP45genetic
27708008
YD089_YEASTYDR089Wgenetic
27708008
RTN1_YEASTRTN1genetic
27708008
SWM1_YEASTSWM1genetic
27708008
PEA2_YEASTPEA2genetic
27708008
MED5_YEASTNUT1genetic
27708008
RIM4_YEASTRIM4genetic
27708008
ECM34_YEASTECM34genetic
27708008
PEX28_YEASTPEX28genetic
27708008
VPS53_YEASTVPS53genetic
27708008
ELM1_YEASTELM1genetic
27708008
TSA1_YEASTTSA1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIG2_YEAST

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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-162, AND MASSSPECTROMETRY.
"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-162 AND SER-196, ANDMASS SPECTROMETRY.
"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-162, AND MASSSPECTROMETRY.

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