HXT1_YEAST - dbPTM
HXT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HXT1_YEAST
UniProt AC P32465
Protein Name Low-affinity glucose transporter HXT1
Gene Name HXT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 570
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Low-affinity glucose transporter. HXT1 is as well involved in the transport of mannose..
Protein Sequence MNSTPDLISPQKSNSSNSYELESGRSKAMNTPEGKNESFHDNLSESQVQPAVAPPNTGKGVYVTVSICCVMVAFGGFIFGWDTGTISGFVAQTDFLRRFGMKHHDGSHYLSKVRTGLIVSIFNIGCAIGGIVLAKLGDMYGRRIGLIVVVVIYTIGIIIQIASINKWYQYFIGRIISGLGVGGITVLSPMLISEVAPSEMRGTLVSCYQVMITLGIFLGYCTNFGTKNYSNSVQWRVPLGLCFAWALFMIGGMMFVPESPRYLVEAGRIDEARASLAKVNKCPPDHPYIQYELETIEASVEEMRAAGTASWGELFTGKPAMFQRTMMGIMIQSLQQLTGDNYFFYYGTIVFQAVGLSDSFETSIVFGVVNFFSTCCSLYTVDRFGRRNCLMWGAVGMVCCYVVYASVGVTRLWPNGQDQPSSKGAGNCMIVFACFYIFCFATTWAPIAYVVISECFPLRVKSKCMSIASAANWIWGFLISFFTPFITGAINFYYGYVFMGCMVFAYFYVFFFVPETKGLSLEEVNDMYAEGVLPWKSASWVPVSKRGADYNADDLMHDDQPFYKSLFSRK
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
1Oxidation-------MNSTPDLI
-------CCCCCCCC		8.9115665377
3Phosphorylation-----MNSTPDLISP
-----CCCCCCCCCC		39.7622369663
4Phosphorylation----MNSTPDLISPQ
----CCCCCCCCCCC		18.8022369663
9PhosphorylationNSTPDLISPQKSNSS
CCCCCCCCCCCCCCC		28.6828132839
13PhosphorylationDLISPQKSNSSNSYE
CCCCCCCCCCCCCEE		36.3822369663
15PhosphorylationISPQKSNSSNSYELE
CCCCCCCCCCCEEEC		37.6822369663
16PhosphorylationSPQKSNSSNSYELES
CCCCCCCCCCEEECC		33.7622369663
18PhosphorylationQKSNSSNSYELESGR
CCCCCCCCEEECCCC		23.1825521595
19PhosphorylationKSNSSNSYELESGRS
CCCCCCCEEECCCCC		28.8725521595
23PhosphorylationSNSYELESGRSKAMN
CCCEEECCCCCCCCC		52.7325521595
26PhosphorylationYELESGRSKAMNTPE
EEECCCCCCCCCCCC		28.4320377248
27UbiquitinationELESGRSKAMNTPEG
EECCCCCCCCCCCCC		50.7423749301
31PhosphorylationGRSKAMNTPEGKNES
CCCCCCCCCCCCCCC		15.0519823750
35UbiquitinationAMNTPEGKNESFHDN
CCCCCCCCCCCCCCC		56.7423749301
38PhosphorylationTPEGKNESFHDNLSE
CCCCCCCCCCCCCCH		36.9622369663
44PhosphorylationESFHDNLSESQVQPA
CCCCCCCCHHHCCCC		41.2622369663
46PhosphorylationFHDNLSESQVQPAVA
CCCCCCHHHCCCCCC		32.0725521595
57PhosphorylationPAVAPPNTGKGVYVT
CCCCCCCCCCCCEEE		46.1522890988
228N-linked_GlycosylationCTNFGTKNYSNSVQW
HHCCCCCCCCCCCCC		45.35-
229PhosphorylationTNFGTKNYSNSVQWR
HCCCCCCCCCCCCCC		15.7028889911
318UbiquitinationWGELFTGKPAMFQRT
HHHHHCCCCHHHHHH		26.9217644757
318AcetylationWGELFTGKPAMFQRT
HHHHHCCCCHHHHHH		26.9224489116
401PhosphorylationAVGMVCCYVVYASVG
CHHHHHHHHHHHCCC		6.4530377154
404PhosphorylationMVCCYVVYASVGVTR
HHHHHHHHHCCCCEE		5.3230377154
406PhosphorylationCCYVVYASVGVTRLW
HHHHHHHCCCCEEEC		11.1728889911
410PhosphorylationVYASVGVTRLWPNGQ
HHHCCCCEEECCCCC		17.7030377154
528PhosphorylationLEEVNDMYAEGVLPW
HHHHHHHHHCCCCCC		12.3628889911
564AcetylationHDDQPFYKSLFSRK-
CCCCHHHHHHHCCC-		40.8524489116
564UbiquitinationHDDQPFYKSLFSRK-
CCCCHHHHHHHCCC-		40.8517644757
568PhosphorylationPFYKSLFSRK-----
HHHHHHHCCC-----		44.4421440633
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 HXT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HXT1_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 HXT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GPA2_YEASTGPA2genetic
11577163
HXT2_YEASTHXT2genetic
9151960
HXT3_YEASTHXT3genetic
9151960
HXT4_YEASTHXT4genetic
9151960
HXT5_YEASTHXT5genetic
9151960
HXT6_YEASTHXT6genetic
9151960
HXT7_YEASTHXT7genetic
9151960
SNA3_YEASTSNA3physical
18467557
HXT2_YEASTHXT2physical
18467557
PDR12_YEASTPDR12physical
18467557
TCB3_YEASTTCB3physical
18467557
DIP5_YEASTDIP5physical
18467557
TPO1_YEASTTPO1physical
18467557
SFK1_YEASTSFK1physical
18467557
GST1_YEASTGTT1physical
18467557
COT1_YEASTCOT1physical
18467557
MID2_YEASTMID2physical
18467557
PDR5_YEASTPDR5physical
18467557
PVH1_YEASTYVH1physical
18467557
QDR2_YEASTQDR2physical
18467557
HXT1_YEASTHXT1physical
18467557
TPO3_YEASTTPO3physical
18467557
SNF3_YEASTSNF3genetic
20014043
GAL2_YEASTGAL2genetic
20014043
FUN30_YEASTFUN30genetic
20093466
ATG8_YEASTATG8genetic
20093466
APN2_YEASTAPN2genetic
20093466
PP2C4_YEASTPTC4genetic
20093466
REI1_YEASTREI1genetic
20093466
RAD61_YEASTRAD61genetic
20093466
URC2_YEASTURC2genetic
20093466
AIM24_YEASTAIM24genetic
20093466
PLB1_YEASTPLB1genetic
20093466
GBLP_YEASTASC1genetic
20093466
JLP2_YEASTJLP2genetic
20093466
AEP2_YEASTAEP2genetic
20093466
INO4_YEASTINO4genetic
20093466
COQ10_YEASTCOQ10genetic
20093466
SIN3_YEASTSIN3genetic
20093466
AXL1_YEASTAXL1genetic
20093466
PHO88_YEASTPHO88physical
16093310
ELO2_YEASTELO2physical
16093310
SHR3_YEASTSHR3physical
16093310
YET1_YEASTYET1physical
16093310
ELO3_YEASTELO3physical
16093310
GSF2_YEASTGSF2physical
16093310
TPS2_YEASTTPS2genetic
21623372
CSG2_YEASTCSG2genetic
21623372
PLB2_YEASTPLB2genetic
21623372
GAL2_YEASTGAL2genetic
21623372
COQ7_YEASTCAT5genetic
21623372
YM71_YEASTYMR226Cgenetic
21623372
THI7_YEASTTHI7genetic
21623372
METK2_YEASTSAM2genetic
21623372
COQ2_YEASTCOQ2genetic
21623372
TRX1_YEASTTRX1genetic
21623372
GSHR_YEASTGLR1genetic
21623372
ASNS2_YEASTASN2genetic
21623372
INP54_YEASTINP54genetic
21623372
ODPB_YEASTPDB1genetic
21623372
QCR1_YEASTCOR1genetic
21623372
LEU9_YEASTLEU9genetic
21623372
KPR5_YEASTPRS5genetic
21623372
DED1_YEASTDED1physical
22940862
SSB1_YEASTSSB1physical
22940862
HSP71_YEASTSSA1physical
22940862
HXT1_YEASTHXT1physical
24875539
INO4_YEASTINO4genetic
27708008
FUN30_YEASTFUN30genetic
27708008
ATG8_YEASTATG8genetic
27708008
NU170_YEASTNUP170genetic
27708008
REI1_YEASTREI1genetic
27708008
QRI7_YEASTQRI7genetic
27708008
ICE2_YEASTICE2genetic
27708008
YJS1_YEASTYJL181Wgenetic
27708008
AIM24_YEASTAIM24genetic
27708008
XDJ1_YEASTXDJ1genetic
27708008
SWI6_YEASTSWI6genetic
27708008
PLB1_YEASTPLB1genetic
27708008
JLP2_YEASTJLP2genetic
27708008
AEP2_YEASTAEP2genetic
27708008
EAF7_YEASTEAF7genetic
27708008
HUB1_YEASTHUB1genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
SIN3_YEASTSIN3genetic
27708008
TOP1_YEASTTOP1genetic
27708008
CY1_YEASTCYT1genetic
27708008
DIA2_YEASTDIA2genetic
27708008
YME1_YEASTYME1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HXT1_YEAST

loading...

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-16; SER-18; SER-23;SER-38; SER-44 AND SER-46, 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-16 AND SER-23, 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-38 AND SER-44, AND MASSSPECTROMETRY.
"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 TYR-528, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory