HXKB_YEAST - dbPTM
HXKB_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HXKB_YEAST
UniProt AC P04807
Protein Name Hexokinase-2
Gene Name HXK2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 486
Subcellular Localization
Protein Description Main glucose phosphorylating enzyme. May play a regulatory role in both induction and repression of gene expression by glucose..
Protein Sequence MVHLGPKKPQARKGSMADVPKELMQQIENFEKIFTVPTETLQAVTKHFISELEKGLSKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRTFDTTQSKYRLPDAMRTTQNPDELWEFIADSLKAFIDEQFPQGISEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKLSDDIPPSAPMAINCEYGSFDNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIEEDPFENLEDTDDLFQNEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTGHIAADGSVYNRYPGFKEKAANALKDIYGWTQTSLDDYPIKIVPAEDGSGAGAAVIAALAQKRIAEGKSVGIIGA
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
13UbiquitinationPKKPQARKGSMADVP
CCCCCCCCCCCCCCC		59.3523749301
15PhosphorylationKPQARKGSMADVPKE
CCCCCCCCCCCCCHH		17.5222369663
21AcetylationGSMADVPKELMQQIE
CCCCCCCHHHHHHHH		64.4324489116
35PhosphorylationENFEKIFTVPTETLQ
HCHHHHCCCCHHHHH		29.1128889911
38PhosphorylationEKIFTVPTETLQAVT
HHHCCCCHHHHHHHH		36.9525752575
40PhosphorylationIFTVPTETLQAVTKH
HCCCCHHHHHHHHHH		27.0124961812
46AcetylationETLQAVTKHFISELE
HHHHHHHHHHHHHHH		29.8924489116
50PhosphorylationAVTKHFISELEKGLS
HHHHHHHHHHHHHHH		34.8721440633
54AcetylationHFISELEKGLSKKGG
HHHHHHHHHHHHCCC		77.2024489116
90PhosphorylationLAIDLGGTNLRVVLV
EEEECCCCEEEEEEE		29.3128889911
98AcetylationNLRVVLVKLGGDRTF
EEEEEEEECCCCCCE		36.9324489116
982-HydroxyisobutyrylationNLRVVLVKLGGDRTF
EEEEEEEECCCCCCE		36.93-
104PhosphorylationVKLGGDRTFDTTQSK
EECCCCCCEECCCHH		30.5121440633
108PhosphorylationGDRTFDTTQSKYRLP
CCCCEECCCHHCCCC		32.4621440633
110PhosphorylationRTFDTTQSKYRLPDA
CCEECCCHHCCCCCH		29.5721440633
111AcetylationTFDTTQSKYRLPDAM
CEECCCHHCCCCCHH		25.2724489116
111UbiquitinationTFDTTQSKYRLPDAM
CEECCCHHCCCCCHH		25.2723749301
158PhosphorylationIPLGFTFSFPASQNK
CCCEEEEECCHHHCC		27.549047292
175PhosphorylationEGILQRWTKGFDIPN
HHHHHHHHCCCCCCC		24.3921440633
176AcetylationGILQRWTKGFDIPNI
HHHHHHHCCCCCCCC		51.0924489116
194AcetylationDVVPMLQKQITKRNI
CHHHHHHHHHHHCCC		39.4424489116
194SuccinylationDVVPMLQKQITKRNI
CHHHHHHHHHHHCCC		39.4423954790
240PhosphorylationGTGVNGAYYDVCSDI
ECCCCCHHHHHHHHH		11.1221440633
245PhosphorylationGAYYDVCSDIEKLQG
CHHHHHHHHHHHHCC		41.2822369663
249AcetylationDVCSDIEKLQGKLSD
HHHHHHHHHCCCCCC		46.5825381059
272PhosphorylationAINCEYGSFDNEHVV
EEEEEECCCCCCEEE		28.6421440633
284AcetylationHVVLPRTKYDITIDE
EEEECCCEEEEEECC		42.0524489116
285PhosphorylationVVLPRTKYDITIDEE
EEECCCEEEEEECCC		16.3820377248
288PhosphorylationPRTKYDITIDEESPR
CCCEEEEEECCCCCC		21.3422369663
293PhosphorylationDITIDEESPRPGQQT
EEEECCCCCCCCCHH		24.9422369663
300PhosphorylationSPRPGQQTFEKMSSG
CCCCCCHHHHHHHCC		26.3521440633
305PhosphorylationQQTFEKMSSGYYLGE
CHHHHHHHCCCHHHH		31.5121440633
306PhosphorylationQTFEKMSSGYYLGEI
HHHHHHHCCCHHHHH		27.5821440633
323AcetylationLALMDMYKQGFIFKN
HHHHHHHHCCCEECC		36.9924489116
329SuccinylationYKQGFIFKNQDLSKF
HHCCCEECCCCHHHC		49.2123954790
3292-HydroxyisobutyrylationYKQGFIFKNQDLSKF
HHCCCEECCCCHHHC		49.21-
329AcetylationYKQGFIFKNQDLSKF
HHCCCEECCCCHHHC		49.2124489116
335AcetylationFKNQDLSKFDKPFVM
ECCCCHHHCCCCEEC		65.9524489116
338UbiquitinationQDLSKFDKPFVMDTS
CCHHHCCCCEECCCC		43.4123749301
338AcetylationQDLSKFDKPFVMDTS
CCHHHCCCCEECCCC		43.4124489116
385PhosphorylationRKLIRRLSELIGARA
HHHHHHHHHHHHHHH		28.6629136822
396PhosphorylationGARAARLSVCGIAAI
HHHHHHHHHHHHHHH		15.1417287358
406UbiquitinationGIAAICQKRGYKTGH
HHHHHHHHCCCCCCE		43.3023749301
4102-HydroxyisobutyrylationICQKRGYKTGHIAAD
HHHHCCCCCCEEECC		51.35-
410AcetylationICQKRGYKTGHIAAD
HHHHCCCCCCEEECC		51.35-
419PhosphorylationGHIAADGSVYNRYPG
CEEECCCCHHHCCCC		23.2122369663
421PhosphorylationIAADGSVYNRYPGFK
EECCCCHHHCCCCHH		8.8120377248
424PhosphorylationDGSVYNRYPGFKEKA
CCCHHHCCCCHHHHH		12.2222369663
428AcetylationYNRYPGFKEKAANAL
HHCCCCHHHHHHHHH		65.3124489116
430UbiquitinationRYPGFKEKAANALKD
CCCCHHHHHHHHHHH		54.0823749301
436SuccinylationEKAANALKDIYGWTQ
HHHHHHHHHHHCCCC		39.4023954790
436AcetylationEKAANALKDIYGWTQ
HHHHHHHHHHHCCCC		39.4024489116
445PhosphorylationIYGWTQTSLDDYPIK
HHCCCCCCCCCCCEE		21.7130377154
473SuccinylationVIAALAQKRIAEGKS
HHHHHHHHHHHCCCC		39.9223954790
473AcetylationVIAALAQKRIAEGKS
HHHHHHHHHHHCCCC		39.9224489116
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 HXKB_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HXKB_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 HXKB_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED8_YEASTMED8physical
12054864
HXKB_YEASTHXK2physical
9566913
FOB1_YEASTFOB1genetic
15328540
SIR2_YEASTSIR2genetic
15328540
HXKA_YEASTHXK1physical
16554755
RGT1_YEASTRGT1physical
16528100
HXKA_YEASTHXK1genetic
17428308
HXKG_YEASTGLK1genetic
17428308
OCA4_YEASTOCA4genetic
19269370
SIP2_YEASTSIP2genetic
19269370
OCA5_YEASTOCA5genetic
19269370
ADK_YEASTADO1genetic
19269370
ATG17_YEASTATG17genetic
19269370
OCA1_YEASTOCA1genetic
19269370
HXKG_YEASTGLK1genetic
19525230
XPO1_YEASTCRM1physical
19525230
HXKA_YEASTHXK1genetic
18408719
DEP1_YEASTDEP1genetic
20093466
SEC66_YEASTSEC66genetic
20093466
DER1_YEASTDER1genetic
20093466
TRM3_YEASTTRM3genetic
20093466
INO2_YEASTINO2genetic
20093466
ARO1_YEASTARO1genetic
20093466
NBP2_YEASTNBP2genetic
20093466
SSD1_YEASTSSD1genetic
20093466
HPRT_YEASTHPT1genetic
20093466
HXKA_YEASTHXK1genetic
20093466
AAKG_YEASTSNF4genetic
20093466
PALF_YEASTRIM8genetic
20093466
PIB2_YEASTPIB2genetic
20093466
SMI1_YEASTSMI1genetic
20093466
YIT6_YEASTYIR016Wgenetic
20093466
RPE_YEASTRPE1genetic
20093466
UPS1_YEASTUPS1genetic
20093466
LIPB_YEASTLIP2genetic
20093466
YPT6_YEASTYPT6genetic
20093466
MSN2_YEASTMSN2genetic
20093466
FET3_YEASTFET3genetic
20093466
PALI_YEASTRIM9genetic
20093466
RIM11_YEASTRIM11genetic
20093466
RIM13_YEASTRIM13genetic
20093466
YM49_YEASTYMR187Cgenetic
20093466
ERG2_YEASTERG2genetic
20093466
IDH1_YEASTIDH1genetic
20093466
HDA1_YEASTHDA1genetic
20093466
INO4_YEASTINO4genetic
20093466
IRA2_YEASTIRA2genetic
20093466
DFG16_YEASTDFG16genetic
20093466
WHI2_YEASTWHI2genetic
20093466
VPS21_YEASTVPS21genetic
20093466
GCY1_YEASTGCY1genetic
20093466
PALA_YEASTRIM20genetic
20093466
PDE2_YEASTPDE2genetic
20093466
HDA3_YEASTHDA3genetic
20093466
PHO80_YEASTPHO80genetic
19325107
ALG5_YEASTALG5genetic
19325107
SSH1_YEASTSSH1genetic
19325107
MIG1_YEASTMIG1physical
20815814
HXKA_YEASTHXK1genetic
21623372
ERG2_YEASTERG2genetic
21623372
COQ4_YEASTCOQ4genetic
21623372
ARO1_YEASTARO1genetic
21623372
ACON2_YEASTACO2genetic
21623372
TPS1_YEASTTPS1genetic
21623372
INP53_YEASTINP53genetic
21623372
ADH3_YEASTADH3genetic
21623372
POS5_YEASTPOS5genetic
21623372
SIR2_YEASTSIR2genetic
21902802
SNF1_YEASTSNF1physical
23066030
RIM11_YEASTRIM11genetic
22282571
SNF1_YEASTSNF1genetic
25116136
AIF1_YEASTAIF1genetic
26895787
AIM44_YEASTAIM44genetic
27708008
MAK16_YEASTMAK16genetic
27708008
ORC2_YEASTORC2genetic
27708008
POP7_YEASTPOP7genetic
27708008
PRP9_YEASTPRP9genetic
27708008
TFB1_YEASTTFB1genetic
27708008
FCF1_YEASTFCF1genetic
27708008
ACT_YEASTACT1genetic
27708008
CP51_YEASTERG11genetic
27708008
EXO70_YEASTEXO70genetic
27708008
RRN3_YEASTRRN3genetic
27708008
GRC3_YEASTGRC3genetic
27708008
BOS1_YEASTBOS1genetic
27708008
CDC25_YEASTCDC25genetic
27708008
SEC65_YEASTSEC65genetic
27708008
TFC8_YEASTTFC8genetic
27708008
COPZ_YEASTRET3genetic
27708008
IF6_YEASTTIF6genetic
27708008
ORC4_YEASTORC4genetic
27708008
INO2_YEASTINO2genetic
27708008
SWF1_YEASTSWF1genetic
27708008
ARO1_YEASTARO1genetic
27708008
SNF1_YEASTSNF1genetic
27708008
IOC3_YEASTIOC3genetic
27708008
HXKA_YEASTHXK1genetic
27708008
YG1C_YEASTYGR018Cgenetic
27708008
RL26B_YEASTRPL26Bgenetic
27708008
NNF2_YEASTNNF2genetic
27708008
GOSR1_YEASTGOS1genetic
27708008
RPE_YEASTRPE1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
VPS51_YEASTVPS51genetic
27708008
BCH2_YEASTBCH2genetic
27708008
YPT6_YEASTYPT6genetic
27708008
FET3_YEASTFET3genetic
27708008
PALI_YEASTRIM9genetic
27708008
RIM11_YEASTRIM11genetic
27708008
ERG2_YEASTERG2genetic
27708008
VPS21_YEASTVPS21genetic
27708008
MIG2_YEASTMIG2physical
26865637
SNF1_YEASTSNF1physical
26865637
AAKG_YEASTSNF4physical
26865637
GAL83_YEASTGAL83physical
26865637
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HXKB_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-38; SER-158; SER-245;SER-272 AND SER-419, 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-396, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.
"Hexokinase 2 from Saccharomyces cerevisiae: regulation of oligomericstructure by in vivo phosphorylation at serine-14.";
Behlke J., Heidrich K., Naumann M., Mueller E.-C., Otto A., Reuter R.,Kriegel T.;
Biochemistry 37:11989-11995(1998).
Cited for: PROTEIN SEQUENCE OF 2-19, AND PHOSPHORYLATION AT SER-15.
"Autophosphorylation-inactivation site of hexokinase 2 inSaccharomyces cerevisiae.";
Heidrich K., Otto A., Behlke J., Rush J., Wenzel K.W., Kriegel T.;
Biochemistry 36:1960-1964(1997).
Cited for: PHOSPHORYLATION AT SER-158.
"In vivo phosphorylation site of hexokinase 2 in Saccharomycescerevisiae.";
Kriegel T.M., Rush J., Vojtek A.B., Clifton D., Fraenkel D.G.;
Biochemistry 33:148-152(1994).
Cited for: PHOSPHORYLATION AT SER-15.

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