HRK1_YEAST - dbPTM
HRK1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HRK1_YEAST
UniProt AC Q08732
Protein Name Serine/threonine-protein kinase HRK1
Gene Name HRK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 759
Subcellular Localization Cytoplasm .
Protein Description Involved in regulating the activity of the plasma membrane proton pump PMA1..
Protein Sequence MPNLLSRNPFHGHHNDHHHDRENSSNNPPQLIRSSKSFLNFIGRKQSNDSLRSEKSTDSMKSTTTTTNYTTTNLNNNTHSHSNATSISTNNYNNNYETNHHHNISHGLHDYTSPASPKQTHSMAELKRFFRPSVNKKLSMSQLRSKKHSTHSPPPSKSTSTVNLNNHYRAQHPHGFTDHYAHTQSAIPPSTDSILSLSNNINIYHDDCILAQKYGKLGKLLGSGAGGSVKVLVRPTDGATFAVKEFRPRKPNESVKEYAKKCTAEFCIGSTLHHPNVIETVDVFSDSKQNKYYEVMEYCPIDFFAVVMTGKMSRGEINCCLKQLTEGVKYLHSMGLAHRDLKLDNCVMTSQGILKLIDFGSAVVFRYPFEDGVTMAHGIVGSDPYLAPEVITSTKSYDPQCVDIWSIGIIYCCMVLKRFPWKAPRDSDDNFRLYCMPDDIEHDYVESARHHEELLKERKEKRQRFLNHSDCSAINQQQPAHESNLKTVQNQVPNTPASIQGKSDNKPDIVEEETEENKEDDSNNDKESTPDNDKESTIDIKISKNENKSTVVSANPKKVDADADADCDANGDSNGRVDCKANSDCNDKTDCNANNDCSNESDCNAKVDTNVNTAANANPDMVPQNNPQQQQQQQQQQQQQQQQQQQQHHHHQHQNQDKAHSIASDNKSSQQHRGPHHKKIIHGPYRLLRLLPHASRPIMSRILQVDPKKRATLDDIFNDEWFAAIAACTMDSKNKVIRAPGHHHTLVREENAHLETYKV
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
24PhosphorylationHHHDRENSSNNPPQL
CCCCCCCCCCCCHHH
29.6822369663
25PhosphorylationHHDRENSSNNPPQLI
CCCCCCCCCCCHHHH
52.8122369663
34PhosphorylationNPPQLIRSSKSFLNF
CCHHHHHCCHHHHHH
34.8117563356
35PhosphorylationPPQLIRSSKSFLNFI
CHHHHHCCHHHHHHH
23.5917563356
36UbiquitinationPQLIRSSKSFLNFIG
HHHHHCCHHHHHHHC
46.6117644757
37PhosphorylationQLIRSSKSFLNFIGR
HHHHCCHHHHHHHCC
36.5922369663
45UbiquitinationFLNFIGRKQSNDSLR
HHHHHCCCCCCCCHH
53.5217644757
47PhosphorylationNFIGRKQSNDSLRSE
HHHCCCCCCCCHHCC
45.7119823750
50PhosphorylationGRKQSNDSLRSEKST
CCCCCCCCHHCCCCC
29.9019684113
53PhosphorylationQSNDSLRSEKSTDSM
CCCCCHHCCCCCCCC
55.4519795423
56PhosphorylationDSLRSEKSTDSMKST
CCHHCCCCCCCCCCC
33.1419795423
57PhosphorylationSLRSEKSTDSMKSTT
CHHCCCCCCCCCCCE
43.0619795423
59PhosphorylationRSEKSTDSMKSTTTT
HCCCCCCCCCCCEEE
28.3519795423
113PhosphorylationHGLHDYTSPASPKQT
CCCCCCCCCCCHHHC
16.5528889911
116PhosphorylationHDYTSPASPKQTHSM
CCCCCCCCHHHCCCH
35.6928889911
120PhosphorylationSPASPKQTHSMAELK
CCCCHHHCCCHHHHH
23.2622369663
122PhosphorylationASPKQTHSMAELKRF
CCHHHCCCHHHHHHH
24.0722369663
133PhosphorylationLKRFFRPSVNKKLSM
HHHHHCHHHCCCCCH
33.7823749301
136UbiquitinationFFRPSVNKKLSMSQL
HHCHHHCCCCCHHHH
53.5917644757
137UbiquitinationFRPSVNKKLSMSQLR
HCHHHCCCCCHHHHH
40.3617644757
139PhosphorylationPSVNKKLSMSQLRSK
HHHCCCCCHHHHHCC
25.8522369663
141PhosphorylationVNKKLSMSQLRSKKH
HCCCCCHHHHHCCCC
23.7622890988
145PhosphorylationLSMSQLRSKKHSTHS
CCHHHHHCCCCCCCC
55.4321440633
149PhosphorylationQLRSKKHSTHSPPPS
HHHCCCCCCCCCCCC
36.3722890988
150PhosphorylationLRSKKHSTHSPPPSK
HHCCCCCCCCCCCCC
26.5422890988
152PhosphorylationSKKHSTHSPPPSKST
CCCCCCCCCCCCCCC
38.9122890988
156PhosphorylationSTHSPPPSKSTSTVN
CCCCCCCCCCCCCEE
45.0422890988
157UbiquitinationTHSPPPSKSTSTVNL
CCCCCCCCCCCCEEC
64.6217644757
158PhosphorylationHSPPPSKSTSTVNLN
CCCCCCCCCCCEECC
31.7422369663
159PhosphorylationSPPPSKSTSTVNLNN
CCCCCCCCCCEECCC
31.9622369663
160PhosphorylationPPPSKSTSTVNLNNH
CCCCCCCCCEECCCC
37.1322369663
161PhosphorylationPPSKSTSTVNLNNHY
CCCCCCCCEECCCCC
17.3222369663
168PhosphorylationTVNLNNHYRAQHPHG
CEECCCCCCCCCCCC
15.1223749301
219UbiquitinationQKYGKLGKLLGSGAG
HHHHHHHHHHCCCCC
51.4823749301
223PhosphorylationKLGKLLGSGAGGSVK
HHHHHHCCCCCCCEE
25.9923749301
228PhosphorylationLGSGAGGSVKVLVRP
HCCCCCCCEEEEECC
20.1825752575
230UbiquitinationSGAGGSVKVLVRPTD
CCCCCCEEEEECCCC
31.3917644757
240PhosphorylationVRPTDGATFAVKEFR
ECCCCCCEEEEEECC
20.0430377154
244UbiquitinationDGATFAVKEFRPRKP
CCCEEEEEECCCCCC
47.9417644757
250UbiquitinationVKEFRPRKPNESVKE
EEECCCCCCCHHHHH
55.6817644757
256UbiquitinationRKPNESVKEYAKKCT
CCCCHHHHHHHHHCC
55.0423749301
260UbiquitinationESVKEYAKKCTAEFC
HHHHHHHHHCCCEEE
47.6917644757
261UbiquitinationSVKEYAKKCTAEFCI
HHHHHHHHCCCEEEC
28.7517644757
311UbiquitinationFAVVMTGKMSRGEIN
EEEEECCCCCHHHHH
25.2417644757
322UbiquitinationGEINCCLKQLTEGVK
HHHHHHHHHHHHHHH
29.3717644757
329UbiquitinationKQLTEGVKYLHSMGL
HHHHHHHHHHHHCCC
53.6117644757
342UbiquitinationGLAHRDLKLDNCVMT
CCCCCCCCCCCCEEE
59.0715699485
355UbiquitinationMTSQGILKLIDFGSA
EECCHHHHHHHCCCE
41.2817644757
382PhosphorylationMAHGIVGSDPYLAPE
EEECCCCCCCCCCCC
25.2323749301
396PhosphorylationEVITSTKSYDPQCVD
CHHHCCCCCCCCHHH
34.5528889911
397PhosphorylationVITSTKSYDPQCVDI
HHHCCCCCCCCHHHH
32.9528889911
406PhosphorylationPQCVDIWSIGIIYCC
CCHHHHHHHHHHHHH
15.9828889911
411PhosphorylationIWSIGIIYCCMVLKR
HHHHHHHHHHHHHHH
4.2528889911
427PhosphorylationPWKAPRDSDDNFRLY
CCCCCCCCCCCEEEE
48.4123749301
456UbiquitinationRHHEELLKERKEKRQ
HHHHHHHHHHHHHHH
69.0117644757
459UbiquitinationEELLKERKEKRQRFL
HHHHHHHHHHHHHHH
69.5417644757
469PhosphorylationRQRFLNHSDCSAINQ
HHHHHCHHHHHHHHH
38.9629136822
472PhosphorylationFLNHSDCSAINQQQP
HHCHHHHHHHHHCCC
36.8517330950
486UbiquitinationPAHESNLKTVQNQVP
CCCHHCHHHHHHHCC
51.4017644757
487PhosphorylationAHESNLKTVQNQVPN
CCHHCHHHHHHHCCC
30.4121126336
495PhosphorylationVQNQVPNTPASIQGK
HHHHCCCCCHHHCCC
17.7317330950
498PhosphorylationQVPNTPASIQGKSDN
HCCCCCHHHCCCCCC
19.3517330950
502UbiquitinationTPASIQGKSDNKPDI
CCHHHCCCCCCCCCC
37.9617644757
503PhosphorylationPASIQGKSDNKPDIV
CHHHCCCCCCCCCCH
53.9229136822
514PhosphorylationPDIVEEETEENKEDD
CCCHHHHCHHCCCCC
52.4529136822
522PhosphorylationEENKEDDSNNDKEST
HHCCCCCCCCCCCCC
50.2629136822
528PhosphorylationDSNNDKESTPDNDKE
CCCCCCCCCCCCCCC
51.4822369663
529PhosphorylationSNNDKESTPDNDKES
CCCCCCCCCCCCCCC
35.4322369663
536PhosphorylationTPDNDKESTIDIKIS
CCCCCCCCCEEEEEE
36.0822369663
537PhosphorylationPDNDKESTIDIKISK
CCCCCCCCEEEEEEC
24.6222369663
543PhosphorylationSTIDIKISKNENKST
CCEEEEEECCCCCCE
25.1522369663
548UbiquitinationKISKNENKSTVVSAN
EEECCCCCCEEEECC
41.1315699485
549PhosphorylationISKNENKSTVVSANP
EECCCCCCEEEECCC
37.7122369663
550PhosphorylationSKNENKSTVVSANPK
ECCCCCCEEEECCCC
26.9122369663
553PhosphorylationENKSTVVSANPKKVD
CCCCEEEECCCCCCC
20.2822369663
557UbiquitinationTVVSANPKKVDADAD
EEEECCCCCCCCCCC
66.3015699485
558UbiquitinationVVSANPKKVDADADA
EEECCCCCCCCCCCC
46.7515699485
573PhosphorylationDCDANGDSNGRVDCK
CCCCCCCCCCCEEEC
42.4528889911
583PhosphorylationRVDCKANSDCNDKTD
CEEECCCCCCCCCCC
48.6921440633
588UbiquitinationANSDCNDKTDCNANN
CCCCCCCCCCCCCCC
32.0723749301
589PhosphorylationNSDCNDKTDCNANND
CCCCCCCCCCCCCCC
48.9625371407
598PhosphorylationCNANNDCSNESDCNA
CCCCCCCCCHHHHCC
46.6323749301
601PhosphorylationNNDCSNESDCNAKVD
CCCCCCHHHHCCCCC
52.2825521595
661PhosphorylationQNQDKAHSIASDNKS
HCHHHHHHHHCCCCC
25.3927214570
664PhosphorylationDKAHSIASDNKSSQQ
HHHHHHHCCCCCCCC
39.7923749301
668PhosphorylationSIASDNKSSQQHRGP
HHHCCCCCCCCCCCC
39.3723749301
669PhosphorylationIASDNKSSQQHRGPH
HHCCCCCCCCCCCCC
35.1523749301
708UbiquitinationRILQVDPKKRATLDD
HHCCCCHHHCCCHHH
50.8821427232
729PhosphorylationFAAIAACTMDSKNKV
HHHHHHHHHCCCCCE
21.2028889911

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 HRK1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HRK1_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 HRK1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SA185_YEASTSAP185physical
16429126
EF3A_YEASTYEF3physical
16429126
SEC2_YEASTSEC2physical
16319894
SYSC_YEASTSES1physical
16319894
HSP26_YEASTHSP26physical
16319894
CDC15_YEASTCDC15physical
16319894
UBP9_YEASTUBP9physical
16319894
ARE2_YEASTARE2physical
16319894
SRO7_YEASTSRO7physical
16319894
GPT1_YEASTSCT1physical
16319894
PHSG_YEASTGPH1physical
16319894
ASND1_YEASTYML096Wphysical
16319894
IST2_YEASTIST2physical
16319894
MST27_YEASTMST27physical
16319894
HPH2_YEASTFRT2physical
16319894
REXO1_YEASTRNH70physical
16319894
SAS10_YEASTSAS10physical
16319894
DUN1_YEASTDUN1genetic
19269370
KCS1_YEASTKCS1genetic
19269370
SNF1_YEASTSNF1genetic
19269370
CUL8_YEASTRTT101genetic
19269370
TBA3_YEASTTUB3genetic
19269370
ARK1_YEASTARK1genetic
19269370
HER1_YEASTHER1genetic
19269370
ECM33_YEASTECM33genetic
20093466
SSD1_YEASTSSD1genetic
20093466
CHO2_YEASTCHO2genetic
20093466
RPE_YEASTRPE1genetic
20093466
GSH1_YEASTGSH1genetic
20093466
SAC1_YEASTSAC1genetic
20093466
IMDH3_YEASTIMD3genetic
20093466
CBF5_YEASTCBF5physical
20489023
CIC1_YEASTCIC1physical
20489023
CSK22_YEASTCKA2physical
20489023
CSK2B_YEASTCKB1physical
20489023
DRS1_YEASTDRS1physical
20489023
EBP2_YEASTEBP2physical
20489023
ERB1_YEASTERB1physical
20489023
FKBP3_YEASTFPR3physical
20489023
FKBP4_YEASTFPR4physical
20489023
GIS4_YEASTGIS4physical
20489023
HAS1_YEASTHAS1physical
20489023
LOC1_YEASTLOC1physical
20489023
MAK16_YEASTMAK16physical
20489023
MRT4_YEASTMRT4physical
20489023
NOC2_YEASTNOC2physical
20489023
NOC3_YEASTNOC3physical
20489023
NOG1_YEASTNOG1physical
20489023
FBRL_YEASTNOP1physical
20489023
NOP2_YEASTNOP2physical
20489023
PESC_YEASTNOP7physical
20489023
NOP3_YEASTNPL3physical
20489023
NSA1_YEASTNSA1physical
20489023
NSA2_YEASTNSA2physical
20489023
NUG1_YEASTNUG1physical
20489023
PWP1_YEASTPWP1physical
20489023
REG1_YEASTREG1physical
20489023
RLP7_YEASTRLP7physical
20489023
RPF1_YEASTRPF1physical
20489023
RPF2_YEASTRPF2physical
20489023
RRP1_YEASTRRP1physical
20489023
RRP15_YEASTRRP15physical
20489023
RRS1_YEASTRRS1physical
20489023
SNF1_YEASTSNF1physical
20489023
AAKG_YEASTSNF4physical
20489023
SPB1_YEASTSPB1physical
20489023
SRP40_YEASTSRP40physical
20489023
IF6_YEASTTIF6physical
20489023
YP260_YEASTYPL260Wphysical
20489023
YRA1_YEASTYRA1physical
20489023
YTM1_YEASTYTM1physical
20489023
KAPC_YEASTTPK3genetic
21127252
REI1_YEASTREI1genetic
21127252
KCS1_YEASTKCS1genetic
21127252
MET18_YEASTMET18genetic
21127252
RPD3_YEASTRPD3genetic
21127252
CG11_YEASTCLN1genetic
21127252
GAL80_YEASTGAL80genetic
21127252
HEL2_YEASTHEL2genetic
21127252
MET32_YEASTMET32genetic
21127252
CBF1_YEASTCBF1genetic
21127252
SWI5_YEASTSWI5genetic
21127252
WTM2_YEASTWTM2genetic
21127252
DOT6_YEASTDOT6genetic
21127252
PP4C_YEASTPPH3genetic
21127252
WTM1_YEASTWTM1genetic
21127252
HAC1_YEASTHAC1genetic
21127252
GCR2_YEASTGCR2genetic
21127252
AP1_YEASTYAP1genetic
21127252
BCK1_YEASTBCK1genetic
21127252
PHO23_YEASTPHO23genetic
21127252
RIX7_YEASTRIX7genetic
22282571
HAL9_YEASTHAL9genetic
22282571
CCR4_YEASTCCR4genetic
22282571
YN12B_YEASTYNL054W-Bgenetic
22282571
SAC1_YEASTSAC1genetic
22282571
RPE_YEASTRPE1genetic
22282571
CHO2_YEASTCHO2genetic
22282571
UPS2_YEASTUPS2genetic
27708008
MED8_YEASTMED8genetic
27708008
CDC37_YEASTCDC37genetic
27708008
CDC4_YEASTCDC4genetic
27708008
SEC22_YEASTSEC22genetic
27708008
THIL_YEASTERG10genetic
27708008
CSM1_YEASTCSM1genetic
27708008
SWI5_YEASTSWI5genetic
27708008
H2A1_YEASTHTA1genetic
27708008
RPE_YEASTRPE1genetic
27708008
SMF3_YEASTSMF3genetic
27708008
TRX1_YEASTTRX1genetic
27708008
RNH2C_YEASTRNH203genetic
27708008
SHH4_YEASTSHH4genetic
27708008
ATG26_YEASTATG26genetic
27708008
YL271_YEASTYLR271Wgenetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HRK1_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-35; SER-37; SER-47;SER-113; SER-116; SER-139; SER-158; SER-160; SER-228; SER-382; SER-472AND SER-498, 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-34; SER-35; SER-37 ANDSER-47, 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-122 AND SER-139, 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-37; THR-495 AND SER-498,AND MASS SPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-522, AND MASSSPECTROMETRY.

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