YPK1_YEAST - dbPTM
YPK1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YPK1_YEAST
UniProt AC P12688
Protein Name Serine/threonine-protein kinase YPK1
Gene Name YPK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 680
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Intracellular localization is regulated by the intracellular sphingolipid levels. During the yeast cell cycle, distributed both on the plasma membrane and in the cytosol. Gr
Protein Description Plays an essential role in the proliferation of yeast cells. Involved in a signaling pathway, required for optimal cell wall integrity, that acts in parallel with the PKC1-SLT2-dependent pathway. Downstream kinase in the sphingolipid-mediated signaling pathway. Its phosphorylation is regulated by the intracellular sphingolipid concentration. Cooperates with SLI1 in mediating resistance to the sphingolipid biosynthesis inhibitor drug myriocin (ISP-1). Its kinase activity is essential for the resistance. Required for both receptor-mediated and fluid-phase endocytosis, but is not necessary for receptor phosphorylation or ubiquitination. Necessary for the internalization of plasma membrane proteins carrying different types of internalization signals. Acts downstream of the PKH kinases to control endocytosis by phosphorylating components of the endocytic machinery. Phosphorylation of residue Thr-504 in the activation loop is essential for activity. phosphorylates and down-regulates flippase activator FPK1..
Protein Sequence MYSWKSKFKFGKSKEEKEAKHSGFFHSSKKEEQQNNQATAGEHDASITRSSLDRKGTINPSNSSVVPVRVSYDASSSTSTVRDSNGGNSENTNSSQNLDETANIGSTGTPNDATSSSGMMTIKVYNGDDFILPFPITSSEQILNKLLASGVPPPHKEISKEVDALIAQLSRVQIKNQGPADEDLISSESAAKFIPSTIMLPGSSTLNPLLYFTIEFDNTVATIEAEYGTIAKPGFNKISTFDVTRKLPYLKIDVFARIPSILLPSKTWQQEMGLQDEKLQTIFDKINSNQDIHLDSFHLPINLSFDSAASIRLYNHHWITLDNGLGKINISIDYKPSRNKPLSIDDFDLLKVIGKGSFGKVMQVRKKDTQKVYALKAIRKSYIVSKSEVTHTLAERTVLARVDCPFIVPLKFSFQSPEKLYFVLAFINGGELFYHLQKEGRFDLSRARFYTAELLCALDNLHKLDVVYRDLKPENILLDYQGHIALCDFGLCKLNMKDDDKTDTFCGTPEYLAPELLLGLGYTKAVDWWTLGVLLYEMLTGLPPYYDEDVPKMYKKILQEPLVFPDGFDRDAKDLLIGLLSRDPTRRLGYNGADEIRNHPFFSQLSWKRLLMKGYIPPYKPAVSNSMDTSNFDEEFTREKPIDSVVDEYLSESVQKQFGGWTYVGNEQLGSSMVQGRSIR
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
13PhosphorylationSKFKFGKSKEEKEAK
CCCCCCCCHHHHHHH		45.7530377154
22PhosphorylationEEKEAKHSGFFHSSK
HHHHHHHCCCCCCCH		36.2728889911
39PhosphorylationEQQNNQATAGEHDAS
HHHHHCCCCCCCCHH		25.9819823750
46PhosphorylationTAGEHDASITRSSLD
CCCCCCHHCCHHHCC		30.4620377248
48PhosphorylationGEHDASITRSSLDRK
CCCCHHCCHHHCCCC		23.2317330950
50PhosphorylationHDASITRSSLDRKGT
CCHHCCHHHCCCCCC		26.9717330950
51PhosphorylationDASITRSSLDRKGTI
CHHCCHHHCCCCCCC		30.8817330950
55UbiquitinationTRSSLDRKGTINPSN
CHHHCCCCCCCCCCC		61.1323749301
57PhosphorylationSSLDRKGTINPSNSS
HHCCCCCCCCCCCCC		22.1822369663
61PhosphorylationRKGTINPSNSSVVPV
CCCCCCCCCCCEEEE		44.8722369663
63PhosphorylationGTINPSNSSVVPVRV
CCCCCCCCCEEEEEE		28.9322890988
64PhosphorylationTINPSNSSVVPVRVS
CCCCCCCCEEEEEEE		31.2422369663
71PhosphorylationSVVPVRVSYDASSST
CEEEEEEEEECCCCC		13.5122369663
72PhosphorylationVVPVRVSYDASSSTS
EEEEEEEEECCCCCC		16.8122890988
75PhosphorylationVRVSYDASSSTSTVR
EEEEEECCCCCCEEE		23.1722369663
76PhosphorylationRVSYDASSSTSTVRD
EEEEECCCCCCEEEC		39.0822890988
77PhosphorylationVSYDASSSTSTVRDS
EEEECCCCCCEEECC		24.7122369663
78PhosphorylationSYDASSSTSTVRDSN
EEECCCCCCEEECCC		30.3022890988
79PhosphorylationYDASSSTSTVRDSNG
EECCCCCCEEECCCC		27.1822890988
80PhosphorylationDASSSTSTVRDSNGG
ECCCCCCEEECCCCC		21.4622890988
84PhosphorylationSTSTVRDSNGGNSEN
CCCEEECCCCCCCCC		27.1530377154
89PhosphorylationRDSNGGNSENTNSSQ
ECCCCCCCCCCCCCC		35.1819779198
159PhosphorylationPPPHKEISKEVDALI
CCCCHHHHHHHHHHH		24.6928889911
170PhosphorylationDALIAQLSRVQIKNQ
HHHHHHHHCCHHCCC		20.5128889911
175UbiquitinationQLSRVQIKNQGPADE
HHHCCHHCCCCCCCH		26.5723749301
192UbiquitinationISSESAAKFIPSTIM
CCCHHHHHHCCCEEE		43.4717644757
244PhosphorylationKISTFDVTRKLPYLK
CCCCCCCCCCCCCCE		24.7521440633
310PhosphorylationLSFDSAASIRLYNHH
EECCCCCEEEEEECC		14.1428889911
335AcetylationINISIDYKPSRNKPL
EEEEEEECCCCCCCC		32.5424489116
340AcetylationDYKPSRNKPLSIDDF
EECCCCCCCCCCCCC		46.3424489116
343PhosphorylationPSRNKPLSIDDFDLL
CCCCCCCCCCCCCHH		32.2817330950
360AcetylationIGKGSFGKVMQVRKK
CCCCCCCCEEEEECC		32.3024489116
376AcetylationTQKVYALKAIRKSYI
HHHHHHHHHHHHHHE		33.3324489116
376UbiquitinationTQKVYALKAIRKSYI
HHHHHHHHHHHHHHE		33.3323749301
381PhosphorylationALKAIRKSYIVSKSE
HHHHHHHHHEEEHHH		15.3921440633
382PhosphorylationLKAIRKSYIVSKSEV
HHHHHHHHEEEHHHH		14.3725752575
386UbiquitinationRKSYIVSKSEVTHTL
HHHHEEEHHHHHHCH		39.4822817900
386AcetylationRKSYIVSKSEVTHTL
HHHHEEEHHHHHHCH		39.4824489116
502PhosphorylationNMKDDDKTDTFCGTP
CCCCCCCCCCCCCCH		47.4622369663
504PhosphorylationKDDDKTDTFCGTPEY
CCCCCCCCCCCCHHH		26.5122369663
508PhosphorylationKTDTFCGTPEYLAPE
CCCCCCCCHHHHCHH		17.7125521595
511PhosphorylationTFCGTPEYLAPELLL
CCCCCHHHHCHHHHH		14.9022369663
522PhosphorylationELLLGLGYTKAVDWW
HHHHHCCCHHHHHHH		15.3122369663
523PhosphorylationLLLGLGYTKAVDWWT
HHHHCCCHHHHHHHH		15.6622369663
556UbiquitinationDVPKMYKKILQEPLV
CHHHHHHHHHCCCCC		31.0324961812
608AcetylationFFSQLSWKRLLMKGY
HHHHHCHHHHHHHCC		29.7724489116
615PhosphorylationKRLLMKGYIPPYKPA
HHHHHHCCCCCCCCC		12.5327017623
624PhosphorylationPPYKPAVSNSMDTSN
CCCCCCCCCCCCCCC		25.8727017623
629PhosphorylationAVSNSMDTSNFDEEF
CCCCCCCCCCCCHHH		19.5427017623
640AcetylationDEEFTREKPIDSVVD
CHHHHCCCCCHHHHH		43.9424489116
644PhosphorylationTREKPIDSVVDEYLS
HCCCCCHHHHHHHHC		25.4317330950
649PhosphorylationIDSVVDEYLSESVQK
CHHHHHHHHCHHHHH		15.8628889911
651PhosphorylationSVVDEYLSESVQKQF
HHHHHHHCHHHHHHH		27.2425005228
653PhosphorylationVDEYLSESVQKQFGG
HHHHHCHHHHHHHCC		26.8617330950
662PhosphorylationQKQFGGWTYVGNEQL
HHHHCCEEEECCCCC		16.1715470109
663PhosphorylationKQFGGWTYVGNEQLG
HHHCCEEEECCCCCC		10.3919779198
671PhosphorylationVGNEQLGSSMVQGRS
ECCCCCCCCCCCCCC		24.6915470109
672PhosphorylationGNEQLGSSMVQGRSI
CCCCCCCCCCCCCCC		22.6028152593
678PhosphorylationSSMVQGRSIR-----
CCCCCCCCCC-----		29.5521440633
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
504TPhosphorylationKinasePKH1Q03407
Uniprot
662TPhosphorylationKinasePKH1Q03407
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YPK1_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 YPK1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PKH2_YEASTPKH2genetic
12221112
YPK2_YEASTYPK2genetic
12196392
YPK2_YEASTYPK2genetic
8437590
PKH1_YEASTPKH1genetic
12221112
SAC7_YEASTSAC7genetic
14593073
KPC1_YEASTPKC1genetic
15470109
TEC1_YEASTTEC1physical
16554755
FIMB_YEASTSAC6physical
16554755
SLM1_YEASTSLM1physical
16554755
CORO_YEASTCRN1physical
16554755
YPK2_YEASTYPK2physical
16554755
INP52_YEASTINP52physical
16554755
YPK2_YEASTYPK2genetic
12221112
EXG1_YEASTEXG1genetic
12221112
SEA4_YEASTSEA4genetic
12221112
PLB1_YEASTPLB1genetic
12221112
HLJ1_YEASTHLJ1genetic
12221112
MED17_YEASTSRB4genetic
12221112
TDA1_YEASTTDA1genetic
12221112
GOT1_YEASTGOT1genetic
12221112
RS6A_YEASTRPS6Bgenetic
12221112
RS6B_YEASTRPS6Bgenetic
12221112
SMP1_YEASTSMP1genetic
12221112
YPC1_YEASTYPC1genetic
12221112
CHI2_YEASTCTS2genetic
12221112
VPS74_YEASTVPS74genetic
12221112
NCS1_YEASTFRQ1genetic
12221112
MRB1_YEASTPHO92genetic
12221112
FPK1_YEASTFPK1physical
19966303
FPK1_YEASTFPK1genetic
19966303
KIN82_YEASTKIN82genetic
19966303
SLI1_YEASTSLI1genetic
15025559
AVO1_YEASTAVO1physical
20489023
GIS4_YEASTGIS4physical
20489023
IF5_YEASTTIF5physical
20489023
TOR2_YEASTTOR2physical
20489023
TSC11_YEASTTSC11physical
20489023
ACO1_YEASTOLE1genetic
20516150
SGK1_HUMANSGK1genetic
20516150
YPK2_YEASTYPK2genetic
11839800
TUS1_YEASTTUS1genetic
11839800
ROM2_YEASTROM2genetic
11839800
RHO2_YEASTRHO2genetic
11839800
KPC1_YEASTPKC1genetic
11839800
BCK1_YEASTBCK1genetic
11839800
MKK1_YEASTMKK1genetic
11839800
FAS1_YEASTFAS1physical
21460040
GLRX1_YEASTGRX1physical
21460040
RAD53_YEASTRAD53physical
21460040
SPS1_YEASTSPS1physical
21460040
SWI5_YEASTSWI5genetic
21127252
ORM1_YEASTORM1physical
22080611
ORM2_YEASTORM2physical
22080611
YPK2_YEASTYPK2genetic
22307609
CANB_YEASTCNB1genetic
22307609
GPD1_YEASTGPD1physical
22988299
KAPC_YEASTTPK3genetic
24462291
PDE2_YEASTPDE2genetic
24462291
FPK1_YEASTFPK1genetic
24462291
ATC5_YEASTDNF1genetic
24462291
ATC4_YEASTDNF2genetic
24462291
ATC8_YEASTDNF3genetic
24462291
AP1_YEASTYAP1genetic
24462291
ORM1_YEASTORM1genetic
25279700
ORM2_YEASTORM2genetic
25279700
GPD1_YEASTGPD1genetic
25279700
FPK1_YEASTFPK1genetic
25279700
PAL1_YEASTPAL1genetic
25279700
YHP7_YEASTYHR097Cgenetic
25279700
SEG1_YEASTSEG1genetic
25279700
YN87_YEASTYNR014Wgenetic
25279700
PTK2_YEASTPTK2genetic
25279700
KIN1_YEASTKIN1genetic
25279700
NPR1_YEASTNPR1genetic
25279700
GPT2_YEASTGPT2genetic
25279700
LAC1_YEASTLAC1genetic
25279700
LAG1_YEASTLAG1genetic
25279700
FPS1_YEASTFPS1genetic
25279700
BRE5_YEASTBRE5genetic
25279700
MUK1_YEASTMUK1genetic
25279700
MDS3_YEASTMDS3genetic
25279700
ROD1_YEASTROD1genetic
25279700
YSP2_YEASTYSP2genetic
25279700
CYK3_YEASTCYK3genetic
25279700
PEX31_YEASTPEX31genetic
25279700
ATG21_YEASTATG21genetic
25279700
ORM1_YEASTORM1physical
25279700
GPD1_YEASTGPD1physical
25279700
FPK1_YEASTFPK1physical
25279700
ORM2_YEASTORM2physical
25279700
YHP7_YEASTYHR097Cphysical
25279700
YN87_YEASTYNR014Wphysical
25279700
SMP1_YEASTSMP1physical
25279700
CDC1_YEASTCDC1physical
25279700
GPT2_YEASTGPT2physical
25279700
LAC1_YEASTLAC1physical
25279700
LAG1_YEASTLAG1physical
25279700
DS1P1_YEASTLCB3physical
25279700
CCH1_YEASTCCH1physical
25279700
FPS1_YEASTFPS1physical
25279700
MUK1_YEASTMUK1physical
25279700
ROD1_YEASTROD1physical
25279700
HER1_YEASTHER1physical
25279700
YSP2_YEASTYSP2physical
25279700
PEX31_YEASTPEX31physical
25279700
ATG21_YEASTATG21physical
25279700
CALM_YEASTCMD1genetic
25002487
CANB_YEASTCNB1genetic
25002487
FPS1_YEASTFPS1physical
26274562
SWE1_YEASTSWE1genetic
26634277
ACT_YEASTACT1genetic
25253719
FPK1_YEASTFPK1genetic
25253719
ATC5_YEASTDNF1genetic
25253719
ATC4_YEASTDNF2genetic
25253719
ATC8_YEASTDNF3genetic
25253719
KAPC_YEASTTPK3genetic
25253719
KPC1_YEASTPKC1genetic
25253719
ROM2_YEASTROM2genetic
25253719
BCK1_YEASTBCK1genetic
25253719
SSN8_YEASTSSN8genetic
25253719
PMP1_YEASTPMP1physical
26404137
CBS1_YEASTCBS1genetic
27899413
MSS51_YEASTMSS51genetic
27899413
ATP10_YEASTATP10genetic
27899413
KAPC_YEASTTPK3genetic
27899413
MID1_YEASTMID1genetic
27899413
RHO1_YEASTRHO1genetic
28167678
LEM3_YEASTLEM3genetic
28167678
PLB1_YEASTPLB1genetic
25258318
CRZ1_YEASTCRZ1genetic
25258318
ORM1_YEASTORM1genetic
25258318
ORM2_YEASTORM2genetic
25258318
ROD1_YEASTROD1physical
26920760
RS5_YEASTRPS5physical
29352143
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YPK1_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 THR-57; SER-61; SER-71;TYR-72; SER-77; SER-159; SER-170; THR-502; SER-651 AND SER-653, ANDMASS 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-51; SER-71; SER-75;SER-343; SER-644 AND SER-653, 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-50 AND SER-51, 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-57; SER-644 AND SER-653,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 THR-504, AND MASSSPECTROMETRY.
"Functional counterparts of mammalian protein kinases PDK1 and SGK inbudding yeast.";
Casamayor A., Torrance P.D., Kobayashi T., Thorner J., Alessi D.R.;
Curr. Biol. 9:186-197(1999).
Cited for: PHOSPHORYLATION AT THR-504 BY PKH1.

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