TAT1_YEAST - dbPTM
TAT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAT1_YEAST
UniProt AC P38085
Protein Name Valine/tyrosine/tryptophan amino-acid permease 1
Gene Name TAT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 619
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description High-affinity transport of valine and tyrosine. Low-affinity transport of tryptophan. Can also transport L-cysteine..
Protein Sequence MDDSVSFIAKEASPAQYSHSLHERTHSEKQKRDFTITEKQDEVSGQTAEPRRTDSKSILQRKCKEFFDSFKRQLPPDRNSELESQEKNNLTKSIKSRHLVMISLGTGIGTGLLVGNGQVLGTAGPAGLVLGYGIASIMLYCIIQAAGELGLCYAGLTGNYTRYPSILVDPSLGFAVSVVYTIQWLTVLPLQLVTAAMTVKYWTSVNADIFVAVVFVFVIIINLFGSRGYAEAEFIFNSCKILMVIGFVILAIIINCGGAGDRRYIGAEYWHNPGPFAHGFKGVCTVFCYAAFSYGGIEVLLLSAAEQENPTKSIPNACKKVVYRILLIYMLTTILVCFLVPYNSDELLGSSDSSGSHASPFVIAVASHGVKVVPHFINAVILISVISVANSSLYSGPRLLLSLAEQGVLPKCLAYVDRNGRPLLCFFVSLVFGCIGFVATSDAEEQVFTWLLAISSLSQLFIWMSMSLSHIRFRDAMAKQGRSMNEVGYKAQTGYWGSWLAVLIAIFFLVCQFWVAIAPVNEHGKLNVKVFFQNYLAMPIVLFAYFGHKIYFKSWSFWIPAEKIDLDSHRNIFVSPSLTEIDKVDDNDDLKEYENSESSENPNSSRSRKFFKRMTNFWC
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-------MDDSVSFI
-------CCCCHHHH		13.4215665377
1Acetylation-------MDDSVSFI
-------CCCCHHHH		13.42-
4Phosphorylation----MDDSVSFIAKE
----CCCCHHHHHHC		18.5222369663
6Phosphorylation--MDDSVSFIAKEAS
--CCCCHHHHHHCCC		18.1922369663
13PhosphorylationSFIAKEASPAQYSHS
HHHHHCCCHHHHHHC		23.1219823750
17PhosphorylationKEASPAQYSHSLHER
HCCCHHHHHHCHHHC		15.5119823750
18PhosphorylationEASPAQYSHSLHERT
CCCHHHHHHCHHHCC		8.4319823750
20PhosphorylationSPAQYSHSLHERTHS
CHHHHHHCHHHCCCC		26.0219823750
25PhosphorylationSHSLHERTHSEKQKR
HHCHHHCCCCHHHHC		27.1119823750
27PhosphorylationSLHERTHSEKQKRDF
CHHHCCCCHHHHCCE		45.9720377248
35PhosphorylationEKQKRDFTITEKQDE
HHHHCCEEEECCCCC		31.1421551504
37PhosphorylationQKRDFTITEKQDEVS
HHCCEEEECCCCCCC		33.7923749301
39UbiquitinationRDFTITEKQDEVSGQ
CCEEEECCCCCCCCC		55.1623749301
39AcetylationRDFTITEKQDEVSGQ
CCEEEECCCCCCCCC		55.1624489116
44PhosphorylationTEKQDEVSGQTAEPR
ECCCCCCCCCCCCCC		24.1222369663
47PhosphorylationQDEVSGQTAEPRRTD
CCCCCCCCCCCCCCC		36.1919823750
53PhosphorylationQTAEPRRTDSKSILQ
CCCCCCCCCCHHHHH		46.0024961812
55PhosphorylationAEPRRTDSKSILQRK
CCCCCCCCHHHHHHH		27.9124961812
56UbiquitinationEPRRTDSKSILQRKC
CCCCCCCHHHHHHHH		44.3023749301
71SuccinylationKEFFDSFKRQLPPDR
HHHHHHHHHHCCCCC		43.0923954790
80PhosphorylationQLPPDRNSELESQEK
HCCCCCCHHHHHHHH		44.4419823750
84PhosphorylationDRNSELESQEKNNLT
CCCHHHHHHHHHCCC		57.1525521595
87UbiquitinationSELESQEKNNLTKSI
HHHHHHHHHCCCHHH		43.4223749301
91PhosphorylationSQEKNNLTKSIKSRH
HHHHHCCCHHHHHCC		25.5225005228
92UbiquitinationQEKNNLTKSIKSRHL
HHHHCCCHHHHHCCE		54.0423749301
568PhosphorylationAEKIDLDSHRNIFVS
HHHCCCCCCCCEEEC		31.4819823750
575PhosphorylationSHRNIFVSPSLTEID
CCCCEEECCCCCCCE		9.6822369663
577PhosphorylationRNIFVSPSLTEIDKV
CCEEECCCCCCCEEC		40.1822369663
579PhosphorylationIFVSPSLTEIDKVDD
EEECCCCCCCEECCC		34.9222369663
591UbiquitinationVDDNDDLKEYENSES
CCCCCCHHHHCCCCC		66.3023749301
593PhosphorylationDNDDLKEYENSESSE
CCCCHHHHCCCCCCC		20.8722890988
596PhosphorylationDLKEYENSESSENPN
CHHHHCCCCCCCCCC		27.2419823750
598PhosphorylationKEYENSESSENPNSS
HHHCCCCCCCCCCCH		42.6522890988
599PhosphorylationEYENSESSENPNSSR
HHCCCCCCCCCCCHH		37.0225521595
604PhosphorylationESSENPNSSRSRKFF
CCCCCCCCHHHHHHH		28.5221440633
605PhosphorylationSSENPNSSRSRKFFK
CCCCCCCHHHHHHHH		40.7019795423
607PhosphorylationENPNSSRSRKFFKRM
CCCCCHHHHHHHHHH		41.5924961812
619S-palmitoylationKRMTNFWC-------
HHHHCCCC-------		3.3216751107
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAT1_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 TAT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XPO1_YEASTCRM1physical
11805826
HSP42_YEASTHSP42physical
11805826
IMB4_YEASTKAP123physical
11805826
MPCP_YEASTMIR1physical
11805826
PDC1_YEASTPDC1physical
11805826
PRP11_YEASTPRP11physical
11805826
MAS5_YEASTYDJ1physical
11805826
YHI0_YEASTYHR020Wphysical
11805826
NSL1_YEASTNSL1physical
11805826
ARO1_YEASTARO1genetic
20093466
AROC_YEASTARO2genetic
20093466
TKT1_YEASTTKL1genetic
20093466
MPCP_YEASTMIR1physical
16093310
PRM9_YEASTPRM9physical
16093310
ELO2_YEASTELO2physical
16093310
TECR_YEASTTSC13physical
16093310
MST27_YEASTMST27physical
16093310
EMP24_YEASTEMP24physical
16093310
ERV29_YEASTERV29physical
16093310
ERP5_YEASTERP5physical
16093310
PHO86_YEASTPHO86physical
16093310
SPC1_YEASTSPC1physical
16093310
YET1_YEASTYET1physical
16093310
GAS2_YEASTGAS2physical
16093310
ELO3_YEASTELO3physical
16093310
GSF2_YEASTGSF2physical
16093310
ERP4_YEASTERP4physical
16093310
SGE1_YEASTSGE1physical
16093310
YPT31_YEASTYPT31genetic
20526336
END3_YEASTEND3physical
23666621
TAT1_YEASTTAT1physical
24875539
ARO1_YEASTARO1genetic
27708008
AROC_YEASTARO2genetic
27708008
ZEO1_YEASTZEO1genetic
27708008
CHMU_YEASTARO7genetic
27708008
TKT1_YEASTTKL1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAT1_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION AT SER-4AND SER-44, AND MASS SPECTROMETRY.
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-80 AND SER-84, AND MASSSPECTROMETRY.
"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-13; SER-18; SER-20 ANDSER-84, 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-13; SER-18; SER-20;SER-80; SER-84; SER-596 AND SER-599, AND MASS SPECTROMETRY.
"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-84, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION AT SER-4AND SER-44, 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-44 AND THR-47, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-39, AND MASSSPECTROMETRY.

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