HXT2_YEAST - dbPTM
HXT2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HXT2_YEAST
UniProt AC P23585
Protein Name High-affinity glucose transporter HXT2
Gene Name HXT2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 541
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description High-affinity glucose transporter. Is only indispensable for growth on low glucose-containing media, because S.cerevisiae possesses other sugar transporters..
Protein Sequence MSEFATSRVESGSQQTSIHSTPIVQKLETDESPIQTKSEYTNAELPAKPIAAYWTVICLCLMIAFGGFVFGWDTGTISGFVNQTDFKRRFGQMKSDGTYYLSDVRTGLIVGIFNIGCAFGGLTLGRLGDMYGRRIGLMCVVLVYIVGIVIQIASSDKWYQYFIGRIISGMGVGGIAVLSPTLISETAPKHIRGTCVSFYQLMITLGIFLGYCTNYGTKDYSNSVQWRVPLGLNFAFAIFMIAGMLMVPESPRFLVEKGRYEDAKRSLAKSNKVTIEDPSIVAEMDTIMANVETERLAGNASWGELFSNKGAILPRVIMGIMIQSLQQLTGNNYFFYYGTTIFNAVGMKDSFQTSIVLGIVNFASTFVALYTVDKFGRRKCLLGGSASMAICFVIFSTVGVTSLYPNGKDQPSSKAAGNVMIVFTCLFIFFFAISWAPIAYVIVAESYPLRVKNRAMAIAVGANWIWGFLIGFFTPFITSAIGFSYGYVFMGCLVFSFFYVFFFVCETKGLTLEEVNEMYVEGVKPWKSGSWISKEKRVSEE
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------MSEFATSRV
------CCCCCCCCC		41.2328132839
2Acetylation------MSEFATSRV
------CCCCCCCCC		41.2322814378
6Phosphorylation--MSEFATSRVESGS
--CCCCCCCCCCCCC		23.5319823750
7Phosphorylation-MSEFATSRVESGSQ
-CCCCCCCCCCCCCC		30.7928889911
11PhosphorylationFATSRVESGSQQTSI
CCCCCCCCCCCCCEE		40.6722369663
13PhosphorylationTSRVESGSQQTSIHS
CCCCCCCCCCCEECC		28.5222369663
16PhosphorylationVESGSQQTSIHSTPI
CCCCCCCCEECCCCC		23.2422369663
17PhosphorylationESGSQQTSIHSTPIV
CCCCCCCEECCCCCE		17.6122369663
20PhosphorylationSQQTSIHSTPIVQKL
CCCCEECCCCCEEEC		33.9222369663
21PhosphorylationQQTSIHSTPIVQKLE
CCCEECCCCCEEECC		11.6722369663
26UbiquitinationHSTPIVQKLETDESP
CCCCCEEECCCCCCC		37.0823749301
29PhosphorylationPIVQKLETDESPIQT
CCEEECCCCCCCCCC		56.3422369663
32PhosphorylationQKLETDESPIQTKSE
EECCCCCCCCCCCCC		30.0722369663
36PhosphorylationTDESPIQTKSEYTNA
CCCCCCCCCCCCCCC		36.9422890988
82N-linked_GlycosylationGTISGFVNQTDFKRR
CCCHHCCCHHHHHHH		36.45-
94UbiquitinationKRRFGQMKSDGTYYL
HHHHCCCCCCCEEEE		37.1923749301
266PhosphorylationRYEDAKRSLAKSNKV
CHHHHHHHHHHHCCC		31.78-
286PhosphorylationSIVAEMDTIMANVET
HHHHHHHHHHHHHHH		16.0226447709
293PhosphorylationTIMANVETERLAGNA
HHHHHHHHHHHCCCC		23.3226447709
309UbiquitinationWGELFSNKGAILPRV
HHHHHCCCCCHHHHH		48.8223749301
530PhosphorylationVKPWKSGSWISKEKR
CCCCCCCCCCCCCCC		28.4730377154
539PhosphorylationISKEKRVSEE-----
CCCCCCCCCC-----		39.79-
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
266SPhosphorylationKinasePKA-Uniprot
539SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HXT2_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 HXT2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HXT3_YEASTHXT3genetic
9151960
HXT4_YEASTHXT4genetic
9151960
HXT5_YEASTHXT5genetic
9151960
HXT6_YEASTHXT6genetic
9151960
HXT7_YEASTHXT7genetic
9151960
SWD1_YEASTSWD1genetic
20093466
CSG2_YEASTCSG2genetic
20093466
SWD3_YEASTSWD3genetic
20093466
SGF29_YEASTSGF29genetic
20093466
PTP1_YEASTPTP1genetic
20093466
PP4C_YEASTPPH3genetic
20093466
YD131_YEASTYDR131Cgenetic
20093466
CTH1_YEASTCTH1genetic
20093466
MSN5_YEASTMSN5genetic
20093466
EAF1_YEASTEAF1genetic
20093466
MRB1_YEASTPHO92genetic
20093466
SPT3_YEASTSPT3genetic
20093466
UBP3_YEASTUBP3genetic
20093466
RPOM_YEASTRPO41genetic
20093466
MMS2_YEASTMMS2genetic
20093466
PALF_YEASTRIM8genetic
20093466
ART5_YEASTART5genetic
20093466
VMA21_YEASTVMA21genetic
20093466
COPE_YEASTSEC28genetic
20093466
FIS1_YEASTFIS1genetic
20093466
APQ12_YEASTAPQ12genetic
20093466
MRX5_YEASTYJL147Cgenetic
20093466
VPS55_YEASTVPS55genetic
20093466
CBT1_YEASTCBT1genetic
20093466
HAP4_YEASTHAP4genetic
20093466
IXR1_YEASTIXR1genetic
20093466
RL14A_YEASTRPL14Agenetic
20093466
DBP7_YEASTDBP7genetic
20093466
SKG1_YEASTSKG1genetic
20093466
MMM1_YEASTMMM1genetic
20093466
PSR2_YEASTPSR2genetic
20093466
LIPB_YEASTLIP2genetic
20093466
VRP1_YEASTVRP1genetic
20093466
FKS1_YEASTFKS1genetic
20093466
COX8_YEASTCOX8genetic
20093466
YM79_YEASTYMR244Wgenetic
20093466
COX7_YEASTCOX7genetic
20093466
GAS1_YEASTGAS1genetic
20093466
FAR11_YEASTFAR11genetic
20093466
CTU2_YEASTNCS2genetic
20093466
SWS2_YEASTSWS2genetic
20093466
MKS1_YEASTMKS1genetic
20093466
TOM7_YEASTTOM7genetic
20093466
COX5A_YEASTCOX5Agenetic
20093466
MED9_YEASTCSE2genetic
20093466
HPH1_YEASTFRT1genetic
20093466
RAD17_YEASTRAD17genetic
20093466
MRN1_YEASTMRN1genetic
20093466
HSP7F_YEASTSSE1genetic
20093466
GGPPS_YEASTBTS1genetic
20093466
SNF3_YEASTSNF3genetic
9559544
AIM3_YEASTAIM3genetic
21035341
TOR2_YEASTTOR2genetic
20526336
GGPPS_YEASTBTS1genetic
21623372
ATPF_YEASTATP4genetic
21623372
FOLE_YEASTMET7genetic
21623372
ATPA_YEASTATP1genetic
21623372
ARO1_YEASTARO1genetic
21623372
INP53_YEASTINP53genetic
21623372
GSH1_YEASTGSH1genetic
21623372
ETR1_YEASTETR1genetic
21623372
TPS2_YEASTTPS2genetic
21623372
THRC_YEASTTHR4genetic
21623372
PPT2_YEASTPPT2genetic
21623372
6PGD1_YEASTGND1genetic
21623372
KCS1_YEASTKCS1genetic
21623372
COX6_YEASTCOX6genetic
21623372
KTR3_YEASTKTR3genetic
21623372
CYS3_YEASTCYS3genetic
21623372
GLRX3_YEASTGRX3genetic
21623372
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HXT2_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-29 AND SER-32, 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-11; SER-13; SER-17;SER-20; THR-29 AND SER-32, AND MASS SPECTROMETRY.
"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-13; SER-17; SER-20;THR-29 AND SER-32, AND MASS SPECTROMETRY.

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