PKH2_YEAST - dbPTM
PKH2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKH2_YEAST
UniProt AC Q12236
Protein Name Serine/threonine-protein kinase PKH2
Gene Name PKH2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1081
Subcellular Localization Nucleus. Cytoplasm, cell cortex. Localizes at eisosomes, large, immobile complexes that mark sites of endocytosis near the plasma membrane.
Protein Description Serine/threonine-protein kinase which is part sphingolipid-mediated signaling pathway that is required for the internalization step of endocytosis by regulating eisosome assembly and organization, and modulating the organization of the plasma membrane. Phosphorylates and activates PKC1. Activates YPK1 and YPK2, 2 components of signaling cascade required for maintenance of cell wall integrity. Required for stress-induced P-body assembly and regulates global mRNA decay at the deadenylation step..
Protein Sequence MYFDKDNSMSPRPLLPSDEQKLNINLLTKKEKFSHLDPHYDAKATPQRSTSNRNVGDLLLEKRTAKPMIQKALTNTDNFIEMYHNQQRKNLDDDTIKEVMINDENGKTVASTNDGRYDNDYDNNDINDQKTLDNIAGSPHMEKNRNKVKIEHDSSSQKPIAKESSKAQKNIIKKGIKDFKFGSVIGDGAYSTVMLATSIDTKKRYAAKVLNKEYLIRQKKVKYVSIEKTALQKLNNSPSVVRLFSTFQDESSLYFLLEYAPNGDFLSLMKKYGSLDETCARYYAAQIIDAIDYLHSNGIIHRDIKPENILLDGEMKIKLTDFGTAKLLNPTNNSVSKPEYDLSTRSKSFVGTAEYVSPELLNDSFTDYRCDIWAFGCILFQMIAGKPPFKATNEYLTFQKVMKVQYAFTPGFPLIIRDLVKKILVKNLDRRLTISQIKEHHFFKDLNFKDGSVWSKTPPEIKPYKINAKSMQAMPSGSDRKLVKKSVNTLGKSHLVTQRSASSPSVEETTHSTLYNNNTHASTESEISIKKRPTDERTAQILENARKGINNRKNQPGKRTPSGAASAALAASAALTKKTMQSYPTSSSKSSRSSSPATTSRPGTYKRTSSTESKPFAKSPPLSASVLSSKVPMPPYTPPMSPPMTPYDTYQMTPPYTTKQQDYSDTAIAAPKPCISKQNVKNSTDSPLMNKQDIQWSFYLKNINEHVLRTEKLDFVTTNYDILEKKMLKLNGSLLDPQLFGKPRHTFLSQVARSGGEVTGFRNDPTMTAYSKTEDTYYSKNIIDLQLLEDDYRIEGGDLSELLTNRSGEGYKCNQNSSPMKDDDKSESNNKGSSVFSGKIKKLFHPTSAAETLSSSDEKTKYYKRTIVMTSFGRFLVFAKRRQPNPVTNLKYELEYDINLRQQGTKIKELIIPLEMGTNHIVVIQTPYKSFLLSTDKKTTSKLFTVLKKILNSNTNKIEKELLQRNQKVIERRTSSSGRAIPKDLPTSKSPSPKPRTHSQSPSISKHNSFSESINSAKSNRSSRIFETFINAKEQNSKKHAAPVPLTSKLVNGLPKRQVTVGLGLNTGTNFKNSSAKSKRS
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
8PhosphorylationMYFDKDNSMSPRPLL
CCCCCCCCCCCCCCC		30.6720377248
10PhosphorylationFDKDNSMSPRPLLPS
CCCCCCCCCCCCCCC		19.9920377248
49PhosphorylationAKATPQRSTSNRNVG
CCCCCCCCCCCCCHH		30.8222369663
50PhosphorylationKATPQRSTSNRNVGD
CCCCCCCCCCCCHHH		32.0122369663
51PhosphorylationATPQRSTSNRNVGDL
CCCCCCCCCCCHHHH		34.7322369663
74PhosphorylationPMIQKALTNTDNFIE
HHHHHHHHCCHHHHH		40.7222369663
76PhosphorylationIQKALTNTDNFIEMY
HHHHHHCCHHHHHHH		27.3825521595
95PhosphorylationRKNLDDDTIKEVMIN
CCCCCCCCCEEEEEE		40.7324961812
108PhosphorylationINDENGKTVASTNDG
EECCCCCEEEECCCC		23.7828889911
111PhosphorylationENGKTVASTNDGRYD
CCCCEEEECCCCCCC		24.3329136822
112PhosphorylationNGKTVASTNDGRYDN
CCCEEEECCCCCCCC		27.8224961812
117PhosphorylationASTNDGRYDNDYDNN
EECCCCCCCCCCCCC		25.3224961812
121PhosphorylationDGRYDNDYDNNDIND
CCCCCCCCCCCCCCC		27.1624961812
131PhosphorylationNDINDQKTLDNIAGS
CCCCCCHHHHHHCCC		33.4422369663
138PhosphorylationTLDNIAGSPHMEKNR
HHHHHCCCCCHHHCC		11.5622369663
239PhosphorylationQKLNNSPSVVRLFST
HHHCCCCCHHEEEEE		32.8228889911
334PhosphorylationLLNPTNNSVSKPEYD
ECCCCCCCCCCCCCC		29.8230377154
346PhosphorylationEYDLSTRSKSFVGTA
CCCCCCCCCCCCCCE		32.5117563356
348PhosphorylationDLSTRSKSFVGTAEY
CCCCCCCCCCCCEEC		26.8127214570
352PhosphorylationRSKSFVGTAEYVSPE
CCCCCCCCEECCCHH		15.8328889911
355PhosphorylationSFVGTAEYVSPELLN
CCCCCEECCCHHHHC		12.0828889911
560PhosphorylationKNQPGKRTPSGAASA
CCCCCCCCCCHHHHH		25.8717563356
562PhosphorylationQPGKRTPSGAASAAL
CCCCCCCCHHHHHHH		40.2121440633
576PhosphorylationLAASAALTKKTMQSY
HHHHHHHCHHHHHHC		26.2617563356
588PhosphorylationQSYPTSSSKSSRSSS
HHCCCCCCCCCCCCC		36.0021440633
590PhosphorylationYPTSSSKSSRSSSPA
CCCCCCCCCCCCCCC		32.6921440633
591PhosphorylationPTSSSKSSRSSSPAT
CCCCCCCCCCCCCCC		39.6621440633
593PhosphorylationSSSKSSRSSSPATTS
CCCCCCCCCCCCCCC		36.8022369663
594PhosphorylationSSKSSRSSSPATTSR
CCCCCCCCCCCCCCC		38.9522369663
595PhosphorylationSKSSRSSSPATTSRP
CCCCCCCCCCCCCCC		21.5722369663
598PhosphorylationSRSSSPATTSRPGTY
CCCCCCCCCCCCCCC		28.7822369663
599PhosphorylationRSSSPATTSRPGTYK
CCCCCCCCCCCCCCC		25.5022369663
600PhosphorylationSSSPATTSRPGTYKR
CCCCCCCCCCCCCCC		31.9322369663
608PhosphorylationRPGTYKRTSSTESKP
CCCCCCCCCCCCCCC		23.9123749301
609PhosphorylationPGTYKRTSSTESKPF
CCCCCCCCCCCCCCC		39.0230377154
610PhosphorylationGTYKRTSSTESKPFA
CCCCCCCCCCCCCCC		35.2629136822
611PhosphorylationTYKRTSSTESKPFAK
CCCCCCCCCCCCCCC		44.0125752575
613PhosphorylationKRTSSTESKPFAKSP
CCCCCCCCCCCCCCC		45.8021082442
619PhosphorylationESKPFAKSPPLSASV
CCCCCCCCCCCCHHH		28.4625521595
623PhosphorylationFAKSPPLSASVLSSK
CCCCCCCCHHHHHCC		25.0328889911
636PhosphorylationSKVPMPPYTPPMSPP
CCCCCCCCCCCCCCC		26.4721440633
637PhosphorylationKVPMPPYTPPMSPPM
CCCCCCCCCCCCCCC		27.0419779198
641PhosphorylationPPYTPPMSPPMTPYD
CCCCCCCCCCCCCCC		31.4628889911
647PhosphorylationMSPPMTPYDTYQMTP
CCCCCCCCCCCCCCC		16.2619779198
650PhosphorylationPMTPYDTYQMTPPYT
CCCCCCCCCCCCCCC		8.0628132839
653PhosphorylationPYDTYQMTPPYTTKQ
CCCCCCCCCCCCCCC		12.9421440633
664PhosphorylationTTKQQDYSDTAIAAP
CCCCCCCCCCCCCCC		36.4527214570
666PhosphorylationKQQDYSDTAIAAPKP
CCCCCCCCCCCCCCC		17.6421440633
683PhosphorylationSKQNVKNSTDSPLMN
CCCCCCCCCCCCCCC		28.0729688323
684PhosphorylationKQNVKNSTDSPLMNK
CCCCCCCCCCCCCCH		50.3027214570
686PhosphorylationNVKNSTDSPLMNKQD
CCCCCCCCCCCCHHH		21.7425704821
974PhosphorylationQKVIERRTSSSGRAI
HHHHHHHHCCCCCCC		38.9019823750
975PhosphorylationKVIERRTSSSGRAIP
HHHHHHHCCCCCCCC		22.2417287358
976PhosphorylationVIERRTSSSGRAIPK
HHHHHHCCCCCCCCC		35.8821440633
977PhosphorylationIERRTSSSGRAIPKD
HHHHHCCCCCCCCCC		31.8719823750
987PhosphorylationAIPKDLPTSKSPSPK
CCCCCCCCCCCCCCC		56.9619684113
988PhosphorylationIPKDLPTSKSPSPKP
CCCCCCCCCCCCCCC		29.2421551504
990PhosphorylationKDLPTSKSPSPKPRT
CCCCCCCCCCCCCCC		30.3121551504
992PhosphorylationLPTSKSPSPKPRTHS
CCCCCCCCCCCCCCC		53.2821551504
997PhosphorylationSPSPKPRTHSQSPSI
CCCCCCCCCCCCCCH		34.1124961812
999PhosphorylationSPKPRTHSQSPSISK
CCCCCCCCCCCCHHH		31.5723749301
1001PhosphorylationKPRTHSQSPSISKHN
CCCCCCCCCCHHHCC		24.5121082442
1003PhosphorylationRTHSQSPSISKHNSF
CCCCCCCCHHHCCCH		44.7528889911
1005PhosphorylationHSQSPSISKHNSFSE
CCCCCCHHHCCCHHH		32.0028889911
1009PhosphorylationPSISKHNSFSESINS
CCHHHCCCHHHHHHH		29.8422369663
1011PhosphorylationISKHNSFSESINSAK
HHHCCCHHHHHHHHH		30.2022369663
1013PhosphorylationKHNSFSESINSAKSN
HCCCHHHHHHHHHCC		26.3522369663
1016PhosphorylationSFSESINSAKSNRSS
CHHHHHHHHHCCHHH		35.0922369663
1019PhosphorylationESINSAKSNRSSRIF
HHHHHHHCCHHHHHH		36.8719795423
1022PhosphorylationNSAKSNRSSRIFETF
HHHHCCHHHHHHHHH		28.3719795423
1023PhosphorylationSAKSNRSSRIFETFI
HHHCCHHHHHHHHHH		26.5924961812
1028PhosphorylationRSSRIFETFINAKEQ
HHHHHHHHHHHHHHH		21.0419823750
1039AcetylationAKEQNSKKHAAPVPL
HHHHCCCCCCCCCCC		37.9925381059
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 PKH2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKH2_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 PKH2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIM21_YEASTTIM21physical
11805837
HXT6_YEASTHXT6physical
11805837
LSP1_YEASTLSP1physical
11805837
HXT7_YEASTHXT7physical
11805837
PIL1_YEASTPIL1physical
11805837
LSP1_YEASTLSP1physical
15016821
PIL1_YEASTPIL1physical
15016821
KPC1_YEASTPKC1physical
10567559
PKH1_YEASTPKH1genetic
11807089
BRX1_YEASTBRX1physical
16319894
NKP1_YEASTNKP1physical
16319894
KCC2_YEASTCMK2physical
16319894
SLM1_YEASTSLM1genetic
17101780
PP11_YEASTSIT4genetic
19269370
PKH1_YEASTPKH1genetic
19269370
GET2_YEASTGET2genetic
19269370
SCH9_YEASTSCH9genetic
19269370
6P22_YEASTPFK27genetic
19269370
NOP12_YEASTNOP12physical
20489023
TOR1_YEASTTOR1physical
20489023
ORC6_YEASTORC6physical
21118957
PIL1_YEASTPIL1physical
21118957
PKH1_YEASTPKH1physical
21118957
PKH2_YEASTPKH2physical
21118957
RV161_YEASTRVS161physical
21118957
ROM2_YEASTROM2genetic
21163942
SLT2_YEASTSLT2genetic
21163942
SMI1_YEASTSMI1genetic
21163942
BCK1_YEASTBCK1genetic
21163942
FKS1_YEASTFKS1genetic
21163942
GAS1_YEASTGAS1genetic
21163942
GAS4_YEASTGAS4genetic
21163942
GAS5_YEASTGAS5genetic
21163942
GPI7_YEASTLAS21genetic
21163942
YUR1_YEASTYUR1genetic
21163942
PALH_YEASTRIM21genetic
21163942
OST6_YEASTOST6genetic
21163942
DHH1_YEASTDHH1genetic
21163942
XRN1_YEASTXRN1genetic
21163942
RTG3_YEASTRTG3genetic
20526336
ARA2_YEASTARA2physical
21460040
BUD4_YEASTBUD4physical
21460040
BUG1_YEASTBUG1physical
21460040
TCPZ_YEASTCCT6physical
21460040
CLC1_YEASTCLC1physical
21460040
CRZ1_YEASTCRZ1physical
21460040
CSM3_YEASTCSM3physical
21460040
ATG19_YEASTATG19physical
21460040
DID4_YEASTDID4physical
21460040
DRS1_YEASTDRS1physical
21460040
SYFB_YEASTFRS1physical
21460040
BUD27_YEASTBUD27physical
21460040
EI2BG_YEASTGCD1physical
21460040
GYS2_YEASTGSY2physical
21460040
DPOD2_YEASTPOL31physical
21460040
LSP1_YEASTLSP1physical
21460040
MDM36_YEASTMDM36physical
21460040
NNF1_YEASTNNF1physical
21460040
PFD3_YEASTPAC10physical
21460040
KPR1_YEASTPRS1physical
21460040
RDS2_YEASTRDS2physical
21460040
RIM4_YEASTRIM4physical
21460040
RLA4_YEASTRPP2Bphysical
21460040
PRS6A_YEASTRPT5physical
21460040
RSC6_YEASTRSC6physical
21460040
RTR1_YEASTRTR1physical
21460040
SCH9_YEASTSCH9physical
21460040
UBX1_YEASTSHP1physical
21460040
SHQ1_YEASTSHQ1physical
21460040
SRC1_YEASTSRC1physical
21460040
IF4A_YEASTTIF2physical
21460040
YAP3_YEASTYAP3physical
21460040
YG1D_YEASTYGR021Wphysical
21460040
DOHH_YEASTLIA1physical
21460040
DPH4_YEASTJJJ3physical
21460040
YP077_YEASTYPL077Cphysical
21460040
YPT7_YEASTYPT7physical
21460040
PLM2_YEASTPLM2genetic
21127252
KCS1_YEASTKCS1genetic
21127252
SUM1_YEASTSUM1genetic
21127252
VMS1_YEASTVMS1genetic
21127252
CSG2_YEASTCSG2genetic
21987634
PKH1_YEASTPKH1genetic
21987634
GET2_YEASTGET2genetic
21987634
VPS27_YEASTVPS27physical
22918958
PKH1_YEASTPKH1genetic
23891562
PKH1_YEASTPKH1genetic
24516402
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PKH2_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-74; SER-138; SER-346;THR-352; SER-1001 AND SER-1009, 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-346; THR-560 ANDTHR-576, 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-975; SER-1009; SER-1011AND SER-1016, AND MASS 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-1009, AND MASSSPECTROMETRY.

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