HXKA_YEAST - dbPTM
HXKA_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HXKA_YEAST
UniProt AC P04806
Protein Name Hexokinase-1
Gene Name HXK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 485
Subcellular Localization
Protein Description
Protein Sequence MVHLGPKKPQARKGSMADVPKELMDEIHQLEDMFTVDSETLRKVVKHFIDELNKGLTKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKLPHDMRTTKHQEELWSFIADSLKDFMVEQELLNTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQNEISKRELPIEIVALINDTVGTLIASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKLADDIPSNSPMAINCEYGSFDNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIEDDPFENLEDTDDIFQKDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTGHIAADGSVYNKYPGFKEAAAKGLRDIYGWTGDASKDPITIVPAEDGSGAGAAVIAALSEKRIAEGKSLGIIGA
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
40PhosphorylationMFTVDSETLRKVVKH
HHCCCHHHHHHHHHH		35.5027017623
46AcetylationETLRKVVKHFIDELN
HHHHHHHHHHHHHHH		35.4724489116
54AcetylationHFIDELNKGLTKKGG
HHHHHHHHCCCCCCC		68.8424489116
90PhosphorylationLAIDLGGTNLRVVLV
EEEECCCCEEEEEEE		29.3128889911
98UbiquitinationNLRVVLVKLSGNHTF
EEEEEEEECCCCCCE		32.5417644757
98AcetylationNLRVVLVKLSGNHTF
EEEEEEEECCCCCCE		32.5424489116
100PhosphorylationRVVLVKLSGNHTFDT
EEEEEECCCCCCEEC		31.6530377154
104PhosphorylationVKLSGNHTFDTTQSK
EECCCCCCEECCCCC		27.4922369663
107PhosphorylationSGNHTFDTTQSKYKL
CCCCCEECCCCCCCC		23.6523749301
110PhosphorylationHTFDTTQSKYKLPHD
CCEECCCCCCCCCCC		35.5428889911
111AcetylationTFDTTQSKYKLPHDM
CEECCCCCCCCCCCC		36.2724489116
111UbiquitinationTFDTTQSKYKLPHDM
CEECCCCCCCCCCCC		36.2723749301
112PhosphorylationFDTTQSKYKLPHDMR
EECCCCCCCCCCCCC		24.0128889911
113AcetylationDTTQSKYKLPHDMRT
ECCCCCCCCCCCCCC		60.3124489116
120PhosphorylationKLPHDMRTTKHQEEL
CCCCCCCCCHHHHHH		33.2928889911
121PhosphorylationLPHDMRTTKHQEELW
CCCCCCCCHHHHHHH		19.0328889911
150PhosphorylationELLNTKDTLPLGFTF
HHHCCCCCCCCCEEE		31.6529136822
156PhosphorylationDTLPLGFTFSYPASQ
CCCCCCEEEECCHHH		15.1822369663
158PhosphorylationLPLGFTFSYPASQNK
CCCCEEEECCHHHCC		27.4422369663
159PhosphorylationPLGFTFSYPASQNKI
CCCEEEECCHHHCCC		9.9129136822
162PhosphorylationFTFSYPASQNKINEG
EEEECCHHHCCCCHH		29.7622369663
165UbiquitinationSYPASQNKINEGILQ
ECCHHHCCCCHHHHH		38.9923749301
175PhosphorylationEGILQRWTKGFDIPN
HHHHHHHHCCCCCCC		24.3921440633
197PhosphorylationPLLQNEISKRELPIE
HHCCCCCCCCCCCHH		21.3422369663
198AcetylationLLQNEISKRELPIEI
HCCCCCCCCCCCHHH		56.4024489116
245PhosphorylationGAFYDVVSDIEKLEG
CHHHHHHHHHHHHCC		32.4922369663
260PhosphorylationKLADDIPSNSPMAIN
CCCCCCCCCCCCEEE		50.7222369663
262PhosphorylationADDIPSNSPMAINCE
CCCCCCCCCCEEEEE		22.0122369663
270PhosphorylationPMAINCEYGSFDNEH
CCEEEEECCCCCCCC		21.9222369663
272PhosphorylationAINCEYGSFDNEHLV
EEEEECCCCCCCCEE		28.6422369663
284UbiquitinationHLVLPRTKYDVAVDE
CEEECCCEEEEECCC		40.5123749301
284AcetylationHLVLPRTKYDVAVDE
CEEECCCEEEEECCC		40.5124489116
293PhosphorylationDVAVDEQSPRPGQQA
EEECCCCCCCCCHHH		22.3422369663
308NitrationFEKMTSGYYLGELLR
HHHHHCCHHHHHHHH		8.69-
309NitrationEKMTSGYYLGELLRL
HHHHCCHHHHHHHHH		16.26-
324AcetylationVLLELNEKGLMLKDQ
HHHHHHHCCCCCCCC		57.1624489116
329AcetylationNEKGLMLKDQDLSKL
HHCCCCCCCCCHHHC		39.1024489116
340NitrationLSKLKQPYIMDTSYP
HHHCCCCEECCCCCC		13.34-
346NitrationPYIMDTSYPARIEDD
CEECCCCCCCCCCCC		11.73-
361PhosphorylationPFENLEDTDDIFQKD
CCCCCCCCCCHHHHH		26.6228889911
367UbiquitinationDTDDIFQKDFGVKTT
CCCCHHHHHCCCCCC		44.2523749301
372UbiquitinationFQKDFGVKTTLPERK
HHHHCCCCCCCCHHH		35.8523749301
406AcetylationGIAAICQKRGYKTGH
HHHHHHHHCCCCCCE		43.3025381059
410AcetylationICQKRGYKTGHIAAD
HHHHCCCCCCEEECC		51.3522865919
410UbiquitinationICQKRGYKTGHIAAD
HHHHCCCCCCEEECC		51.3517644757
419PhosphorylationGHIAADGSVYNKYPG
CEEECCCCHHHCCCC		23.2122369663
423AcetylationADGSVYNKYPGFKEA
CCCCHHHCCCCHHHH		34.8324489116
423UbiquitinationADGSVYNKYPGFKEA
CCCCHHHCCCCHHHH		34.8323749301
428AcetylationYNKYPGFKEAAAKGL
HHCCCCHHHHHHHCC		52.9724489116
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 HXKA_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HXKA_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 HXKA_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HXKB_YEASTHXK2genetic
3540605
HXKB_YEASTHXK2genetic
10633097
HXKB_YEASTHXK2genetic
10217505
HXKB_YEASTHXK2genetic
15358789
HXKG_YEASTGLK1genetic
15358789
KPYK1_YEASTCDC19genetic
147195
HXKB_YEASTHXK2genetic
17248750
TPS1_YEASTTPS1genetic
19269370
HXKB_YEASTHXK2genetic
19269370
PLC1_YEASTPLC1genetic
19269370
HXKB_YEASTHXK2genetic
19525230
HXKG_YEASTGLK1genetic
19525230
HXKB_YEASTHXK2genetic
16941010
TPS1_YEASTTPS1genetic
20093466
NDH2_YEASTNDE2genetic
20093466
HXKB_YEASTHXK2genetic
20093466
XRN1_YEASTXRN1genetic
20093466
TFS2_YEASTDST1genetic
20093466
YOR1_YEASTYOR1genetic
20093466
EF1G2_YEASTTEF4genetic
20093466
FRMSR_YEASTYKL069Wgenetic
20093466
RL14A_YEASTRPL14Agenetic
20093466
FPS1_YEASTFPS1genetic
20093466
YM24_YEASTYMR147Wgenetic
20093466
TMA23_YEASTTMA23genetic
20093466
ADE_YEASTAAH1genetic
20093466
LCB4_YEASTLCB4genetic
20093466
TCO89_YEASTTCO89genetic
20093466
HSP7F_YEASTSSE1genetic
20093466
MTNA_YEASTMRI1genetic
20093466
HXKB_YEASTHXK2genetic
20815814
TPS1_YEASTTPS1genetic
21623372
HXKB_YEASTHXK2genetic
21623372
THDH_YEASTILV1genetic
21623372
KCS1_YEASTKCS1genetic
21623372
CSG2_YEASTCSG2genetic
21623372
KTR5_YEASTKTR5genetic
21623372
HXKA_YEASTHXK1physical
10877063
TPS1_YEASTTPS1genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
BRE1_YEASTBRE1genetic
27708008
PEX5_YEASTPEX5genetic
27708008
UBP3_YEASTUBP3genetic
27708008
XRN1_YEASTXRN1genetic
27708008
HXKB_YEASTHXK2genetic
27708008
YOR1_YEASTYOR1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
EF1G2_YEASTTEF4genetic
27708008
RS21A_YEASTRPS21Agenetic
27708008
FPS1_YEASTFPS1genetic
27708008
SWI6_YEASTSWI6genetic
27708008
PEX13_YEASTPEX13genetic
27708008
PEX12_YEASTPEX12genetic
27708008
PKR1_YEASTPKR1genetic
27708008
YM24_YEASTYMR147Wgenetic
27708008
TMA23_YEASTTMA23genetic
27708008
EOS1_YEASTEOS1genetic
27708008
RRP6_YEASTRRP6genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
MED1_YEASTMED1genetic
27708008
HXKB_YEASTHXK2genetic
26865637
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HXKA_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-15; SER-158; SER-245;SER-262; SER-272 AND SER-293, 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-15, AND MASSSPECTROMETRY.
"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-15, 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 SER-15, 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.

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