HXT5_YEAST - dbPTM
HXT5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HXT5_YEAST
UniProt AC P38695
Protein Name Probable glucose transporter HXT5
Gene Name HXT5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 592
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Probable glucose transporter..
Protein Sequence MSELENAHQGPLEGSATVSTNSNSYNEKSGNSTAPGTAGYNDNLAQAKPVSSYISHEGPPKDELEELQKEVDKQLEKKSKSDLLFVSVCCLMVAFGGFVFGWDTGTISGFVRQTDFIRRFGSTRANGTTYLSDVRTGLMVSIFNIGCAIGGIVLSKLGDMYGRKIGLMTVVVIYSIGIIIQIASIDKWYQYFIGRIISGLGVGGITVLAPMLISEVSPKQLRGTLVSCYQLMITFGIFLGYCTNFGTKNYSNSVQWRVPLGLCFAWSIFMIVGMTFVPESPRYLVEVGKIEEAKRSLARANKTTEDSPLVTLEMENYQSSIEAERLAGSASWGELVTGKPQMFRRTLMGMMIQSLQQLTGDNYFFYYGTTIFQAVGLEDSFETAIVLGVVNFVSTFFSLYTVDRFGRRNCLLWGCVGMICCYVVYASVGVTRLWPNGQDQPSSKGAGNCMIVFACFYIFCFATTWAPVAYVLISESYPLRVRGKAMSIASACNWIWGFLISFFTPFITSAINFYYGYVFMGCMVFAYFYVFFFVPETKGLTLEEVNEMYEENVLPWKSTKWIPPSRRTTDYDLDATRNDPRPFYKRMFTKEK
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
2Phosphorylation------MSELENAHQ
------CCHHHCCCC		51.3829136822
15PhosphorylationHQGPLEGSATVSTNS
CCCCCCCCEEEECCC		16.0524961812
17PhosphorylationGPLEGSATVSTNSNS
CCCCCCEEEECCCCC		19.3822369663
19PhosphorylationLEGSATVSTNSNSYN
CCCCEEEECCCCCCC		19.9522369663
20PhosphorylationEGSATVSTNSNSYNE
CCCEEEECCCCCCCC		38.0322369663
22PhosphorylationSATVSTNSNSYNEKS
CEEEECCCCCCCCCC		27.5222369663
24PhosphorylationTVSTNSNSYNEKSGN
EEECCCCCCCCCCCC		29.2022369663
25PhosphorylationVSTNSNSYNEKSGNS
EECCCCCCCCCCCCC		31.4322369663
29PhosphorylationSNSYNEKSGNSTAPG
CCCCCCCCCCCCCCC		36.7127214570
32PhosphorylationYNEKSGNSTAPGTAG
CCCCCCCCCCCCCCC		29.4829136822
33PhosphorylationNEKSGNSTAPGTAGY
CCCCCCCCCCCCCCC		40.6529734811
37PhosphorylationGNSTAPGTAGYNDNL
CCCCCCCCCCCCCCH		18.8229136822
40PhosphorylationTAPGTAGYNDNLAQA
CCCCCCCCCCCHHHC		19.5129136822
51PhosphorylationLAQAKPVSSYISHEG
HHHCCCCHHHCCCCC		26.4229136822
52PhosphorylationAQAKPVSSYISHEGP
HHCCCCHHHCCCCCC		27.0717287358
53PhosphorylationQAKPVSSYISHEGPP
HCCCCHHHCCCCCCC		10.0329136822
55PhosphorylationKPVSSYISHEGPPKD
CCCHHHCCCCCCCHH		13.7825533186
61UbiquitinationISHEGPPKDELEELQ
CCCCCCCHHHHHHHH		67.9512872131
126N-linked_GlycosylationRFGSTRANGTTYLSD
HHCCCCCCCEEECHH		45.08-
155PhosphorylationAIGGIVLSKLGDMYG
HHHHHHHHHHHHHHH		18.2328889911
249N-linked_GlycosylationCTNFGTKNYSNSVQW
HHCCCCCCCCCCCCC		45.35-
250PhosphorylationTNFGTKNYSNSVQWR
HCCCCCCCCCCCCCC		15.7028889911
427PhosphorylationCCYVVYASVGVTRLW
HHHHHHHCCCCCEEC		11.1728889911
568PhosphorylationWIPPSRRTTDYDLDA
CCCCCCCCCCCCCCC		23.9427214570
569PhosphorylationIPPSRRTTDYDLDAT
CCCCCCCCCCCCCCC		30.6527214570
571PhosphorylationPSRRTTDYDLDATRN
CCCCCCCCCCCCCCC		19.1327214570
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 HXT5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HXT5_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 HXT5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HXT6_YEASTHXT6genetic
9151960
HXT7_YEASTHXT7genetic
9151960
PDR12_YEASTPDR12physical
18467557
TCB3_YEASTTCB3physical
18467557
DIP5_YEASTDIP5physical
18467557
TPO1_YEASTTPO1physical
18467557
SFK1_YEASTSFK1physical
18467557
MEP3_YEASTMEP3physical
18467557
PDR5_YEASTPDR5physical
18467557
QDR2_YEASTQDR2physical
18467557
HXT5_YEASTHXT5physical
18467557
TPO3_YEASTTPO3physical
18467557
GST1_YEASTGTT1physical
18719252
TXTP_YEASTCTP1physical
16093310
PMT1_YEASTPMT1physical
16093310
HXT15_YEASTHXT15physical
16093310
KRE2_YEASTKRE2physical
16093310
GSF2_YEASTGSF2physical
16093310
PFKA1_YEASTPFK1genetic
21623372
APC11_YEASTAPC11genetic
27708008
RPB1_YEASTRPO21genetic
27708008
PDC2_YEASTPDC2genetic
27708008
CDC37_YEASTCDC37genetic
27708008
GPI19_YEASTGPI19genetic
27708008
MCM10_YEASTMCM10genetic
27708008
TAD2_YEASTTAD2genetic
27708008
ARP4_YEASTARP4genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SSL1_YEASTSSL1genetic
27708008
DPOA_YEASTPOL1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
SEC12_YEASTSEC12genetic
27708008
PROF_YEASTPFY1genetic
27708008
DYR_YEASTDFR1genetic
27708008
CR3L1_HUMANCREB3L1physical
27107014
KASH5_HUMANCCDC155physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HXT5_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-155, 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-52 AND SER-55, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-61, AND MASSSPECTROMETRY.

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