AVT4_YEAST - dbPTM
AVT4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AVT4_YEAST
UniProt AC P50944
Protein Name Vacuolar amino acid transporter 4
Gene Name AVT4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 713
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Involved in amino acid efflux from the vacuole to the cytoplasm. Capable of transporting large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine..
Protein Sequence MVTNNGDGEHLGIRRNGNLRHPSNNMKIPRRAQSTVLNSNPFYSRKYSMSTLTPRDICRSVDSRVFVDMSSPNFQTLEDPHRDEIINSVRLNYLNSSKRSSVSHGNEAIPRVNPTKNSSASTIAAANVDSDDDETNLSSAGGDITHDIYKLVKAEDPKRLRRPRSMENVTPKIEHHTKLSSASGLNVPGGFRREFIVNKKRQEHQLNDSASSDFTSHESDSINQSSPSSNQDIDKVPFLTRNFLEFLYVFGHFAGESFEDDFIPDSSNMMIRGEDERSALLSRPDHMKVLPSAKGTTSTKKVFLILLKSFIGTGVLFLPNAFHNGGLFFSVSMLAFFGIYSYWCYYILVQAKSSCGVSSFGDIGLKLYGPWMRIIILFSLVITQVGFSGAYMIFTAKNLQAFLDNVFHVGVLPLSYLMVFQTIIFIPLSFIRNISKLSLPSLLANFFIMAGLVIVIIFTAKRLFFDLMGTPAMGVVYGLNADRWTLFIGTAIFAFEGIGLIIPVQDSMRNPEKFPLVLALVILTATILFISIATLGYLAYGSNVQTVILLNLPQSNIFVNLIQLFYSIAIMLSTPLQLFPAIKIIENKFFPKFTKIYVKHDDLTTRVELRPNSGKLNWKIKWLKNFIRSIIVIIVVSIAYFGSDNLDKFVSVIGSLACIPLVYIYPSMLHLRGNSLPETKGEFWRFKPMLDTILIFFGIASMLYTSYQSIFGV
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
34PhosphorylationKIPRRAQSTVLNSNP
CCCCHHHHHHHCCCC		21.3525533186
35PhosphorylationIPRRAQSTVLNSNPF
CCCHHHHHHHCCCCC		19.5528152593
39PhosphorylationAQSTVLNSNPFYSRK
HHHHHHCCCCCCCCC		41.5423749301
43PhosphorylationVLNSNPFYSRKYSMS
HHCCCCCCCCCCCCC		14.6026447709
44PhosphorylationLNSNPFYSRKYSMST
HCCCCCCCCCCCCCC		23.7526447709
47PhosphorylationNPFYSRKYSMSTLTP
CCCCCCCCCCCCCCH		14.4319684113
48PhosphorylationPFYSRKYSMSTLTPR
CCCCCCCCCCCCCHH		14.8628152593
50PhosphorylationYSRKYSMSTLTPRDI
CCCCCCCCCCCHHHH		17.8322369663
51PhosphorylationSRKYSMSTLTPRDIC
CCCCCCCCCCHHHHH		26.4722369663
53PhosphorylationKYSMSTLTPRDICRS
CCCCCCCCHHHHHHC		19.1622369663
60PhosphorylationTPRDICRSVDSRVFV
CHHHHHHCCCCCEEE		26.3523749301
70PhosphorylationSRVFVDMSSPNFQTL
CCEEEECCCCCCCCC		37.8722369663
71PhosphorylationRVFVDMSSPNFQTLE
CEEEECCCCCCCCCC		19.7522369663
76PhosphorylationMSSPNFQTLEDPHRD
CCCCCCCCCCCCCHH		28.1622369663
88PhosphorylationHRDEIINSVRLNYLN
CHHHHHHHHHHHHCC		9.7522369663
93PhosphorylationINSVRLNYLNSSKRS
HHHHHHHHCCCCCCC		16.3222369663
96PhosphorylationVRLNYLNSSKRSSVS
HHHHHCCCCCCCCCC		34.3422369663
97PhosphorylationRLNYLNSSKRSSVSH
HHHHCCCCCCCCCCC		30.8922369663
100PhosphorylationYLNSSKRSSVSHGNE
HCCCCCCCCCCCCCC		38.5419823750
101PhosphorylationLNSSKRSSVSHGNEA
CCCCCCCCCCCCCCC		31.5017330950
103PhosphorylationSSKRSSVSHGNEAIP
CCCCCCCCCCCCCCC		27.8529136822
115PhosphorylationAIPRVNPTKNSSAST
CCCCCCCCCCCCCCE		37.3428889911
118PhosphorylationRVNPTKNSSASTIAA
CCCCCCCCCCCEEEE		28.9222369663
119PhosphorylationVNPTKNSSASTIAAA
CCCCCCCCCCEEEEE		35.3222369663
121PhosphorylationPTKNSSASTIAAANV
CCCCCCCCEEEEECC		23.4622369663
122PhosphorylationTKNSSASTIAAANVD
CCCCCCCEEEEECCC		17.8522369663
130PhosphorylationIAAANVDSDDDETNL
EEEECCCCCCCCCCH		38.3622369663
135PhosphorylationVDSDDDETNLSSAGG
CCCCCCCCCHHHCCC		48.7522369663
138PhosphorylationDDDETNLSSAGGDIT
CCCCCCHHHCCCCCH		21.8822369663
139PhosphorylationDDETNLSSAGGDITH
CCCCCHHHCCCCCHH		33.8122369663
145PhosphorylationSSAGGDITHDIYKLV
HHCCCCCHHHHHHHH		20.4522369663
149PhosphorylationGDITHDIYKLVKAED
CCCHHHHHHHHHCCC		12.3422369663
165PhosphorylationKRLRRPRSMENVTPK
HHCCCCCCCCCCCCC		32.8822369663
170PhosphorylationPRSMENVTPKIEHHT
CCCCCCCCCCCHHHH		30.3722369663
177PhosphorylationTPKIEHHTKLSSASG
CCCCHHHHHCCCCCC		35.2724961812
180PhosphorylationIEHHTKLSSASGLNV
CHHHHHCCCCCCCCC		25.9724961812
181PhosphorylationEHHTKLSSASGLNVP
HHHHHCCCCCCCCCC		36.5725752575
183PhosphorylationHTKLSSASGLNVPGG
HHHCCCCCCCCCCCC		45.8428152593
215PhosphorylationDSASSDFTSHESDSI
CCCCCCCCCCCCCCC		33.8824961812
216PhosphorylationSASSDFTSHESDSIN
CCCCCCCCCCCCCCC		25.8324961812
219PhosphorylationSDFTSHESDSINQSS
CCCCCCCCCCCCCCC		31.1024961812
221PhosphorylationFTSHESDSINQSSPS
CCCCCCCCCCCCCCC		32.4924961812
292PhosphorylationDHMKVLPSAKGTTST
CCCCCCCCCCCCCCH		38.1519779198
297PhosphorylationLPSAKGTTSTKKVFL
CCCCCCCCCHHHHHH		42.9619779198
298PhosphorylationPSAKGTTSTKKVFLI
CCCCCCCCHHHHHHH		37.7619779198
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 AVT4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AVT4_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 AVT4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHO88_YEASTPHO88physical
16093310
MKAR_YEASTIFA38physical
16093310
YPC1_YEASTYPC1physical
16093310
ELO2_YEASTELO2physical
16093310
TECR_YEASTTSC13physical
16093310
SHR3_YEASTSHR3physical
16093310
STE14_YEASTSTE14physical
16093310
PSS_YEASTCHO1physical
16093310
SHO1_YEASTSHO1physical
16093310
MST27_YEASTMST27physical
16093310
MSMO_YEASTERG25physical
16093310
ERV29_YEASTERV29physical
16093310
LAG1_YEASTLAG1physical
16093310
CP51_YEASTERG11physical
16093310
YHU0_YEASTYHR140Wphysical
16093310
SNL1_YEASTSNL1physical
16093310
PHO86_YEASTPHO86physical
16093310
ELO1_YEASTELO1physical
16093310
STE24_YEASTSTE24physical
16093310
YET1_YEASTYET1physical
16093310
SRPB_YEASTSRP102physical
16093310
ELO3_YEASTELO3physical
16093310
GSF2_YEASTGSF2physical
16093310
SEC63_YEASTSEC63physical
16093310
GPI2_YEASTGPI2physical
16093310
YOP1_YEASTYOP1physical
16093310
AQY1_YEASTAQY1physical
16093310
AVT1_YEASTAVT1genetic
25747199
SMD1_YEASTSMD1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AVT4_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-71; SER-165; SER-181 ANDSER-183, 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-101; SER-165 ANDTHR-170, AND MASS SPECTROMETRY.

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