PKH1_YEAST - dbPTM
PKH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKH1_YEAST
UniProt AC Q03407
Protein Name Serine/threonine-protein kinase PKH1
Gene Name PKH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 766
Subcellular Localization
Protein Description Activates YPK1 by phosphorylating of a threonine residue..
Protein Sequence MGNRSLTEADHALLSKPLVPTSAEHTQTQEYPRPFVDGSNSQSGSELQASPQGQFGEKALTSTNRFIPLANDDPGMQHEMGLDPSMRRRREEWAERGAAKIVKDVVDPATGELTKHVVKMGIKDFKFGEQLGDGSYSSVVLATARDSGKKYAVKVLSKEYLIRQKKVKYVTVEKLALQKLNGTKGIFKLFFTFQDEASLYFLLEYAPHGDFLGLIKKYGSLNETCARYYASQIIDAVDSLHNIGIIHRDIKPENILLDKNMKVKLTDFGTAKILPEEPSNTADGKPYFDLYAKSKSFVGTAEYVSPELLNDNYTDSRCDIWAFGCILYQMLAGKPPFKAANEYLTFQKVMKIQYAFTAGFPQIVKDLVKKLLVRDPNDRLTIKQIKAHLFFHEVNFEDGSVWDDNPPEIQPYKINAEAMKPLQKVSESDTTVKMANLQLAGNGHADTPLQAPAATSQEHSVISMTAATAAFNKDYTSQPKLGSKSSTSVRSASNNTDREVIQKKVSKNRASVSSPSISTTSRGKDNRSRSSDAFWSRYLQNMDERVLLMKEVALSTRNLEDSPVGLENVALDYKNPLDIEPPTDSAGKFYKKMFLITNLGRALVFVKRRSLSMWEEQEFELQFELELNDVEKIRFISDQVLEIDGSRTIFIGCKERAVLMKLWKLIHNGMTAKPKVVSPKSDHKMFDKFILQKRQNTKKKNQAPPVPQSNRLINGLPDRCILKTPEEGALHTKRPTSLQTRSSSNYSKLLARSTQMRKNMTRTDEK
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
5Phosphorylation---MGNRSLTEADHA
---CCCCCCCHHHHH		43.5822369663
7Phosphorylation-MGNRSLTEADHALL
-CCCCCCCHHHHHHH		30.3022369663
15PhosphorylationEADHALLSKPLVPTS
HHHHHHHHCCCCCCC		32.8319795423
21PhosphorylationLSKPLVPTSAEHTQT
HHCCCCCCCCCCCCC		32.8419823750
22PhosphorylationSKPLVPTSAEHTQTQ
HCCCCCCCCCCCCCC		26.1119823750
26PhosphorylationVPTSAEHTQTQEYPR
CCCCCCCCCCCCCCC		25.4719823750
28PhosphorylationTSAEHTQTQEYPRPF
CCCCCCCCCCCCCCC		25.2319823750
31PhosphorylationEHTQTQEYPRPFVDG
CCCCCCCCCCCCCCC		8.5019823750
39PhosphorylationPRPFVDGSNSQSGSE
CCCCCCCCCCCCCCC		28.9219823750
41PhosphorylationPFVDGSNSQSGSELQ
CCCCCCCCCCCCCCC		27.6719823750
43PhosphorylationVDGSNSQSGSELQAS
CCCCCCCCCCCCCCC		44.0721551504
45PhosphorylationGSNSQSGSELQASPQ
CCCCCCCCCCCCCCC		40.1420377248
50PhosphorylationSGSELQASPQGQFGE
CCCCCCCCCCCCCCC		12.5620377248
61PhosphorylationQFGEKALTSTNRFIP
CCCCCCCCCCCCCEE		38.0623749301
85PhosphorylationHEMGLDPSMRRRREE
CCCCCCHHHHHHHHH		25.2923749301
115AcetylationPATGELTKHVVKMGI
CCCCHHHHHHHHCCC		47.2124489116
251UbiquitinationGIIHRDIKPENILLD
CEECCCCCHHHEEEC		51.0423749301
259AcetylationPENILLDKNMKVKLT
HHHEEECCCCCEEEC		59.9324489116
294PhosphorylationYFDLYAKSKSFVGTA
CCEEEECCCCCCCCC		25.9222369663
296PhosphorylationDLYAKSKSFVGTAEY
EEEECCCCCCCCCCC		32.0522369663
300PhosphorylationKSKSFVGTAEYVSPE
CCCCCCCCCCCCCHH		15.8322369663
303PhosphorylationSFVGTAEYVSPELLN
CCCCCCCCCCHHHHC		12.0822369663
305PhosphorylationVGTAEYVSPELLNDN
CCCCCCCCHHHHCCC		16.2629136822
485PhosphorylationQPKLGSKSSTSVRSA
CCCCCCCCCCCCCCC		40.3123749301
486PhosphorylationPKLGSKSSTSVRSAS
CCCCCCCCCCCCCCC		28.5621551504
487PhosphorylationKLGSKSSTSVRSASN
CCCCCCCCCCCCCCC		38.0321551504
488PhosphorylationLGSKSSTSVRSASNN
CCCCCCCCCCCCCCC		19.9219823750
491PhosphorylationKSSTSVRSASNNTDR
CCCCCCCCCCCCCCH		33.6222369663
493PhosphorylationSTSVRSASNNTDREV
CCCCCCCCCCCCHHH		31.6822369663
496PhosphorylationVRSASNNTDREVIQK
CCCCCCCCCHHHHHH		40.4622369663
511PhosphorylationKVSKNRASVSSPSIS
HHHCCCCCCCCCCCC		21.2122369663
513PhosphorylationSKNRASVSSPSISTT
HCCCCCCCCCCCCCC		33.7522369663
514PhosphorylationKNRASVSSPSISTTS
CCCCCCCCCCCCCCC		22.1022369663
516PhosphorylationRASVSSPSISTTSRG
CCCCCCCCCCCCCCC		30.9920377248
518PhosphorylationSVSSPSISTTSRGKD
CCCCCCCCCCCCCCC		29.9419823750
519PhosphorylationVSSPSISTTSRGKDN
CCCCCCCCCCCCCCC		27.4119823750
520PhosphorylationSSPSISTTSRGKDNR
CCCCCCCCCCCCCCC		15.0528889911
521PhosphorylationSPSISTTSRGKDNRS
CCCCCCCCCCCCCCC		38.8421440633
530PhosphorylationGKDNRSRSSDAFWSR
CCCCCCCCCHHHHHH		33.5421440633
531PhosphorylationKDNRSRSSDAFWSRY
CCCCCCCCHHHHHHH		31.6719779198
538PhosphorylationSDAFWSRYLQNMDER
CHHHHHHHHCCCCHH		13.7128889911
724PhosphorylationPDRCILKTPEEGALH
CCCCEEECCCCCCCC		32.2728889911
737PhosphorylationLHTKRPTSLQTRSSS
CCCCCCCCCCCCCCC		22.5927214570
742PhosphorylationPTSLQTRSSSNYSKL
CCCCCCCCCCCHHHH		41.3222369663
743PhosphorylationTSLQTRSSSNYSKLL
CCCCCCCCCCHHHHH		21.2222369663
744PhosphorylationSLQTRSSSNYSKLLA
CCCCCCCCCHHHHHH		40.8221440633
746PhosphorylationQTRSSSNYSKLLARS
CCCCCCCHHHHHHHH		14.7722369663
747PhosphorylationTRSSSNYSKLLARST
CCCCCCHHHHHHHHH		22.5222369663
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 PKH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKH1_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 PKH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LSP1_YEASTLSP1physical
11805837
PIL1_YEASTPIL1physical
11805837
KAPC_YEASTTPK3physical
11805837
SET5_YEASTSET5physical
10688190
YRF14_YEASTYRF1-4physical
10688190
LSP1_YEASTLSP1physical
15016821
PIL1_YEASTPIL1physical
15016821
YPK1_YEASTYPK1physical
10074427
YPK2_YEASTYPK2physical
15840588
YPK1_YEASTYPK1physical
15840588
SCH9_YEASTSCH9physical
15840588
PKH2_YEASTPKH2genetic
10074427
PKH2_YEASTPKH2genetic
10567559
REB1_YEASTREB1physical
16554755
BMH2_YEASTBMH2physical
16554755
PIL1_YEASTPIL1physical
16554755
LSP1_YEASTLSP1physical
16554755
AEP3_YEASTAEP3physical
16554755
PIL1_YEASTPIL1physical
11283351
SLM1_YEASTSLM1genetic
17101780
SIP1_YEASTSIP1genetic
19269370
RAS2_YEASTRAS2genetic
19269370
SSB1_YEASTSSB1physical
19536198
CSK22_YEASTCKA2physical
20489023
FKBP3_YEASTFPR3physical
20489023
PKH2_YEASTPKH2genetic
21163942
PIL1_YEASTPIL1physical
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
PKH2_YEASTPKH2genetic
20526336
SCH9_YEASTSCH9physical
21531713
KAPA_YEASTTPK1physical
21531713
PKH2_YEASTPKH2genetic
22319457
IF2G_YEASTGCD11physical
22326914
IF2A_YEASTSUI2physical
22326914
IF2B_YEASTSUI3physical
22326914
GCN2_YEASTGCN2physical
22326914
PKH2_YEASTPKH2genetic
22918958
UBR2_YEASTUBR2genetic
23891562
DAN1_YEASTDAN1genetic
23891562
GET2_YEASTGET2genetic
23891562
TPM1_YEASTTPM1genetic
23891562
PFD4_YEASTGIM3genetic
23891562
RS21A_YEASTRPS21Agenetic
22282571
HAL9_YEASTHAL9genetic
22282571
IRC18_YEASTIRC18genetic
22282571
RPA2_YEASTRPA135genetic
22282571
PMS1_YEASTPMS1genetic
22282571
UGO1_YEASTUGO1genetic
22282571
RRP46_YEASTRRP46genetic
22282571
ATG1_YEASTATG1genetic
22282571
YGZ2_YEASTYGL242Cgenetic
22282571
GYP1_YEASTGYP1genetic
22282571
MED5_YEASTNUT1genetic
22282571
YL032_YEASTYLL032Cgenetic
22282571
BUD21_YEASTBUD21genetic
22282571
SOK2_YEASTSOK2genetic
22282571
MSN1_YEASTMSN1genetic
22282571
ATG8_YEASTATG8genetic
22282571
NCBP2_YEASTCBC2genetic
22282571
YFF2_YEASTYFL052Wgenetic
22282571
ATC1_YEASTPMR1genetic
22282571
BMT5_YEASTBMT5genetic
22282571
ECM25_YEASTECM25genetic
22282571
CHO2_YEASTCHO2genetic
27708008
ATG8_YEASTATG8genetic
27708008
ETR1_YEASTETR1genetic
27708008
SLX5_YEASTSLX5genetic
27708008
VAM6_YEASTVAM6genetic
27708008
VPS41_YEASTVPS41genetic
27708008
MSH4_YEASTMSH4genetic
27708008
LSB3_YEASTLSB3genetic
27708008
MON1_YEASTMON1genetic
27708008
MED5_YEASTNUT1genetic
27708008
ATC1_YEASTPMR1genetic
27708008
ATG1_YEASTATG1genetic
27708008
TAN1_YEASTTAN1genetic
27708008
YGZ2_YEASTYGL242Cgenetic
27708008
OCA5_YEASTOCA5genetic
27708008
HTD2_YEASTHTD2genetic
27708008
THIK_YEASTPOT1genetic
27708008
IF4A_YEASTTIF2genetic
27708008
NNK1_YEASTNNK1genetic
27708008
MMM1_YEASTMMM1genetic
27708008
PFD6_YEASTYKE2genetic
27708008
YPT7_YEASTYPT7genetic
27708008
SOK2_YEASTSOK2genetic
27708008
COX7_YEASTCOX7genetic
27708008
RL9B_YEASTRPL9Bgenetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
ATG3_YEASTATG3genetic
27708008
MSN1_YEASTMSN1genetic
27708008
GYP1_YEASTGYP1genetic
27708008
PMA2_YEASTPMA2genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
BRR1_YEASTBRR1genetic
27708008
ATG13_YEASTATG13genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PKH1_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-5; SER-296; THR-300 ANDSER-513, 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-294 AND SER-296, 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 SER-5, AND MASSSPECTROMETRY.
"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-296, AND MASSSPECTROMETRY.

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