PTP3_YEAST - dbPTM
PTP3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTP3_YEAST
UniProt AC P40048
Protein Name Tyrosine-protein phosphatase 3
Gene Name PTP3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 928
Subcellular Localization Cytoplasm .
Protein Description Major phosphatase responsible for tyrosine dephosphorylation of MAP kinases FUS3 and HOG1 to inactivate their activity; it also has important roles, along with MSG5, in the inactivation of FUS3 following pheromone stimulation..
Protein Sequence MKDSVDCPSILPTDRTSVLSETSTLVGSSSHVYSRHAPMNSYHNSMNSNIYHSPKASSPLVSYKTSSPVLLKRATAPVLPSFKPKEQRYNKPQGCSLITAVELGKIIETLPDEKVLLLDVRPFTEHAKSIITNSIHVCLPSTLLRRKNFTFSKLLDNLTPSEQSVLKSKLAIDNLRIIIYDSTANQTESSVSLPCYGIASKLIEFDTNVKKTVSILMCGFPQFKILFPDHINTNTFNSDCISSAEPKSPKTNLMNSLHNTAPHMTATTPLSSPQMNLKLKVPDDSRSDHSNFSSSPSPRNVLSDSPMSSSSPISALFKFQLPAPQTNINQMFKFSQNEEIMGLETYLSAVNIKEEHERWYNNDSAKKSLQNFQFPKNQNSLEKDTNKDKLGFQIRYENLSKNYEKEVIDSVIPEWFQHLMSIPKIELVSQFQKLDFLEKRRLNHSVSFRKKENSFILEKPSSYPEQLTSTSSSTIMPPKFPDVNKVQKRSHSQPIFTQYSKYKSMLSLESDSDSESDDVIISSGVELGAKNRYKDIFPYEHSRVILKKGLQSSKGIKHSHSTSDGGILDNYINANYLSLPRFSVEQNSSFQTTTTTTRRVRYIATQAPMPSTVHDFYTCILNNGVPLVLSLTNDFENGIEKCYRYWQEGNYNGIHVKLLEKKILKMPSTTSMRKNTMGTQNSSLYSAGVQGNSSNYSTDNDNDNDNNNNNNNNSNIAVTAAACDDDDDDDDDAILIRKILLTYHDQEKPYELLQIQVKNWPDLGTLLNPISILQAINVKNHIIDTLFARNYYQNDQLPTILVHCSAGCGRTGTLCTIDSILSNFEMFEMLQKEFVKLKYPAKLFDPISWTINIFRKQRISMVQNINQFIFIYDCLLFYFRLRLDDITERTDGDGSNKDNISLSALIEQIEKLEILQTFVDDKLKELPQ
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
45PhosphorylationPMNSYHNSMNSNIYH
CCCHHCCCCCCCCCC		13.1627017623
51PhosphorylationNSMNSNIYHSPKASS
CCCCCCCCCCCCCCC		10.6527017623
53PhosphorylationMNSNIYHSPKASSPL
CCCCCCCCCCCCCCC		15.8919779198
58PhosphorylationYHSPKASSPLVSYKT
CCCCCCCCCCEEEEC		27.4121440633
65PhosphorylationSPLVSYKTSSPVLLK
CCCEEEECCCCCCHH		26.6319795423
66PhosphorylationPLVSYKTSSPVLLKR
CCEEEECCCCCCHHH		28.6119795423
67PhosphorylationLVSYKTSSPVLLKRA
CEEEECCCCCCHHHC		25.0221440633
75PhosphorylationPVLLKRATAPVLPSF
CCCHHHCCCCCCCCC		35.2117330950
150PhosphorylationLLRRKNFTFSKLLDN
HHHCCCCCHHHHHHC		36.0721440633
243PhosphorylationFNSDCISSAEPKSPK
CCCCCCCCCCCCCCC		19.4220377248
248PhosphorylationISSAEPKSPKTNLMN
CCCCCCCCCCCCHHH		42.2020377248
256PhosphorylationPKTNLMNSLHNTAPH
CCCCHHHHHHCCCCC		19.6221440633
267PhosphorylationTAPHMTATTPLSSPQ
CCCCCCCCCCCCCCC		21.5628889911
268PhosphorylationAPHMTATTPLSSPQM
CCCCCCCCCCCCCCC		21.5521440633
271PhosphorylationMTATTPLSSPQMNLK
CCCCCCCCCCCCCEE		40.9728889911
272PhosphorylationTATTPLSSPQMNLKL
CCCCCCCCCCCCEEE		27.1721440633
293PhosphorylationRSDHSNFSSSPSPRN
CCCCCCCCCCCCCCC		33.8723749301
294PhosphorylationSDHSNFSSSPSPRNV
CCCCCCCCCCCCCCC		41.9721440633
295PhosphorylationDHSNFSSSPSPRNVL
CCCCCCCCCCCCCCC		28.3517563356
297PhosphorylationSNFSSSPSPRNVLSD
CCCCCCCCCCCCCCC		38.1417563356
303PhosphorylationPSPRNVLSDSPMSSS
CCCCCCCCCCCCCCC		31.5928152593
305PhosphorylationPRNVLSDSPMSSSSP
CCCCCCCCCCCCCCC		21.0821440633
308PhosphorylationVLSDSPMSSSSPISA
CCCCCCCCCCCCCHH		30.3823749301
309PhosphorylationLSDSPMSSSSPISAL
CCCCCCCCCCCCHHH		28.6919779198
310PhosphorylationSDSPMSSSSPISALF
CCCCCCCCCCCHHHH		32.5921551504
311PhosphorylationDSPMSSSSPISALFK
CCCCCCCCCCHHHHE		28.3521440633
314PhosphorylationMSSSSPISALFKFQL
CCCCCCCHHHHEECC		23.4628889911
368PhosphorylationNNDSAKKSLQNFQFP
CCHHHHHHHHHCCCC		34.1822369663
445PhosphorylationEKRRLNHSVSFRKKE
HHCCCCCCCCEECCC		20.5528889911
447PhosphorylationRRLNHSVSFRKKENS
CCCCCCCCEECCCCC		23.5028889911
454PhosphorylationSFRKKENSFILEKPS
CEECCCCCEEEECCC		18.1121551504
461PhosphorylationSFILEKPSSYPEQLT
CEEEECCCCCCHHCC		54.2825533186
462PhosphorylationFILEKPSSYPEQLTS
EEEECCCCCCHHCCC		53.9120377248
468PhosphorylationSSYPEQLTSTSSSTI
CCCCHHCCCCCCCCC		29.6521440633
490PhosphorylationVNKVQKRSHSQPIFT
CCCCCCCCCCCCCHH		34.2319823750
492PhosphorylationKVQKRSHSQPIFTQY
CCCCCCCCCCCHHHH		38.6119823750
497PhosphorylationSHSQPIFTQYSKYKS
CCCCCCHHHHHHHHH		27.5819823750
499PhosphorylationSQPIFTQYSKYKSML
CCCCHHHHHHHHHHH		12.2219823750
500PhosphorylationQPIFTQYSKYKSMLS
CCCHHHHHHHHHHHC		21.4919823750
502PhosphorylationIFTQYSKYKSMLSLE
CHHHHHHHHHHHCCC		11.4527017623
507PhosphorylationSKYKSMLSLESDSDS
HHHHHHHCCCCCCCC		22.8127017623
523PhosphorylationSDDVIISSGVELGAK
CCCEEECCCCCCCCC		36.1327017623
559PhosphorylationSSKGIKHSHSTSDGG
CCCCCCCCCCCCCCC		17.7128889911
561PhosphorylationKGIKHSHSTSDGGIL
CCCCCCCCCCCCCCC		32.4028889911
850PhosphorylationLFDPISWTINIFRKQ
HCCCCHHHHHHHHHH		9.4328889911
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 PTP3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTP3_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 PTP3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FET4_YEASTFET4physical
11805837
RRP5_YEASTRRP5physical
11805837
H4_YEASTHHF1physical
11805837
FUS3_YEASTFUS3physical
10557209
SLT2_YEASTSLT2physical
10523653
HOG1_YEASTHOG1physical
9211927
HOG1_YEASTHOG1physical
10817757
SLT2_YEASTSLT2physical
11923319
CDK1_YEASTCDC28physical
10580002
FUS3_YEASTFUS3physical
9224718
PTP2_YEASTPTP2genetic
9224718
GEM1_YEASTGEM1genetic
20093466
VPS8_YEASTVPS8genetic
20093466
SKT5_YEASTSKT5genetic
20093466
BEM1_YEASTBEM1genetic
20093466
BSD2_YEASTBSD2genetic
20093466
RV161_YEASTRVS161genetic
20093466
BUD31_YEASTBUD31genetic
20093466
TPS2_YEASTTPS2genetic
20093466
BLM10_YEASTBLM10genetic
20093466
HUR1_YEASTHUR1genetic
20093466
YG036_YEASTYGL036Wgenetic
20093466
ASK10_YEASTASK10genetic
20093466
RL24B_YEASTRPL24Bgenetic
20093466
PEX21_YEASTPEX21genetic
20093466
YG5B_YEASTYGR250Cgenetic
20093466
MAL12_YEASTMAL12genetic
20093466
SLT2_YEASTSLT2genetic
20093466
COX23_YEASTCOX23genetic
20093466
AIM18_YEASTAIM18genetic
20093466
CBT1_YEASTCBT1genetic
20093466
COXM1_YEASTCMC1genetic
20093466
VPS24_YEASTVPS24genetic
20093466
SRN2_YEASTSRN2genetic
20093466
YPT6_YEASTYPT6genetic
20093466
RSC2_YEASTRSC2genetic
20093466
IMP2_YEASTIMP2genetic
20093466
TOM70_YEASTTOM70genetic
20093466
CTU2_YEASTNCS2genetic
20093466
NST1_YEASTNST1genetic
20093466
SWS2_YEASTSWS2genetic
20093466
MKS1_YEASTMKS1genetic
20093466
IDH1_YEASTIDH1genetic
20093466
VPS27_YEASTVPS27genetic
20093466
COQ2_YEASTCOQ2genetic
20093466
EXO1_YEASTEXO1genetic
20093466
WHI5_YEASTWHI5genetic
20093466
PTP2_YEASTPTP2genetic
20093466
NEW1_YEASTNEW1genetic
20093466
COX10_YEASTCOX10genetic
20093466
TKT1_YEASTTKL1genetic
20093466
HOG1_YEASTHOG1genetic
12455951
PTP2_YEASTPTP2genetic
20430884
HKR1_YEASTHKR1genetic
20932477
MSB2_YEASTMSB2genetic
20932477
HOG1_YEASTHOG1genetic
20932477
PBS2_YEASTPBS2genetic
20932477
STE11_YEASTSTE11genetic
20932477
STE50_YEASTSTE50genetic
20932477
OPY2_YEASTOPY2genetic
20932477
STE20_YEASTSTE20genetic
20932477
MSG5_YEASTMSG5genetic
20932477
GAS1_YEASTGAS1genetic
27708008
SGT2_YEASTSGT2genetic
27708008
QCR2_YEASTQCR2genetic
27708008
GEM1_YEASTGEM1genetic
27708008
BSD2_YEASTBSD2genetic
27708008
RV161_YEASTRVS161genetic
27708008
BUD31_YEASTBUD31genetic
27708008
TPS2_YEASTTPS2genetic
27708008
RV167_YEASTRVS167genetic
27708008
BLM10_YEASTBLM10genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
MRM2_YEASTMRM2genetic
27708008
HUR1_YEASTHUR1genetic
27708008
PEX21_YEASTPEX21genetic
27708008
YG5B_YEASTYGR250Cgenetic
27708008
NPR3_YEASTNPR3genetic
27708008
COX23_YEASTCOX23genetic
27708008
FKH1_YEASTFKH1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
CBT1_YEASTCBT1genetic
27708008
SRN2_YEASTSRN2genetic
27708008
VPS9_YEASTVPS9genetic
27708008
IMP2_YEASTIMP2genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
MKS1_YEASTMKS1genetic
27708008
SWS2_YEASTSWS2genetic
27708008
CTU2_YEASTNCS2genetic
27708008
VPS27_YEASTVPS27genetic
27708008
HMI1_YEASTHMI1genetic
27708008
EXO1_YEASTEXO1genetic
27708008
WHI5_YEASTWHI5genetic
27708008
COQ7_YEASTCAT5genetic
27708008
PTP2_YEASTPTP2genetic
27708008
ELOC_YEASTELC1genetic
27708008
COX10_YEASTCOX10genetic
27708008
JID1_YEASTJID1genetic
27708008
VPS4_YEASTVPS4genetic
27708008
KPC1_YEASTPKC1genetic
29674565
FCF1_YEASTFCF1genetic
29674565
MAD1_YEASTMAD1genetic
29674565
CTF8_YEASTCTF8genetic
29674565
EXO70_YEASTEXO70genetic
29674565
VPS24_YEASTVPS24genetic
29674565
ELM1_YEASTELM1genetic
29674565
PFD6_YEASTYKE2genetic
29674565
SUB1_YEASTSUB1genetic
29674565
PFD4_YEASTGIM3genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTP3_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-67; SER-311; SER-368;SER-492 AND THR-850, 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-295 AND SER-297, ANDMASS 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 THR-75 AND SER-492, 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 THR-75, AND MASSSPECTROMETRY.

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