AVT3_YEAST - dbPTM
AVT3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AVT3_YEAST
UniProt AC P36062
Protein Name Vacuolar amino acid transporter 3
Gene Name AVT3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 692
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 MNGKEVSSGSGRTQSNNNKKNNNGGSTGISHASGSPLTDGNGGNSNGNSRSRSRSRKSSGTTGGLLKKPPLLVNNEAVHASVPDASHTSCNNGTLEVSINNPEPHVVDAVARHLIRNPSNSLQLQGGDITRDLYKWTNDHPSSPSQYQYPSQPALSTSIPSQAPSFSNRKRSMSFSAASIASSSHLNNNSEANGNPLAAIGLAPAPMTHEEIRAPGGFRRSFIIQKRRKHNVDAPIPNFFTRNFIEFLTLYGHFAGEDLSEEEEEEEETEEEPEEEALETESTQLVSREHGRHPHKSSTVKAVLLLLKSFVGTGVLFLPKAFHNGGWGFSALCLLSCALISYGCFVSLITTKDKVGVDGYGDMGRILYGPKMKFAILSSIALSQIGFSAAYTVFTATNLQVFSENFFHLKPGSISLATYIFAQVLIFVPLSLTRNIAKLSGTALIADLFILLGLVYVYVYSIYYIAVNGVASDTMLMFNKADWSLFIGTAIFTFEGIGLLIPIQESMKHPKHFRPSLSAVMCIVAVIFISCGLLCYAAFGSDVKTVVLLNFPQDTSYTLTVQLLYALAILLSTPLQLFPAIRILENWTFPSNASGKYNPKVKWLKNYFRCAIVVLTSILAWVGANDLDKFVSLVGSFACIPLIYIYPPLLHYKASILSGTSRARLLLDLIVIVFGVAVMAYTSWQTIKMWSQ
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
7Phosphorylation-MNGKEVSSGSGRTQ
-CCCCCCCCCCCCCC		30.0319795423
8PhosphorylationMNGKEVSSGSGRTQS
CCCCCCCCCCCCCCC		42.0019823750
10PhosphorylationGKEVSSGSGRTQSNN
CCCCCCCCCCCCCCC		27.3519823750
13PhosphorylationVSSGSGRTQSNNNKK
CCCCCCCCCCCCCCC		39.6219823750
15PhosphorylationSGSGRTQSNNNKKNN
CCCCCCCCCCCCCCC		40.6919823750
26PhosphorylationKKNNNGGSTGISHAS
CCCCCCCCCCCCCCC		25.5130377154
27PhosphorylationKNNNGGSTGISHASG
CCCCCCCCCCCCCCC		41.6426447709
30PhosphorylationNGGSTGISHASGSPL
CCCCCCCCCCCCCCC		17.8526447709
33PhosphorylationSTGISHASGSPLTDG
CCCCCCCCCCCCCCC		34.0928889911
35PhosphorylationGISHASGSPLTDGNG
CCCCCCCCCCCCCCC		17.7823749301
38PhosphorylationHASGSPLTDGNGGNS
CCCCCCCCCCCCCCC		45.2921440633
45PhosphorylationTDGNGGNSNGNSRSR
CCCCCCCCCCCCCCC		49.7623749301
49PhosphorylationGGNSNGNSRSRSRSR
CCCCCCCCCCCCCCC		32.7923749301
51PhosphorylationNSNGNSRSRSRSRKS
CCCCCCCCCCCCCCC		34.1323749301
53PhosphorylationNGNSRSRSRSRKSSG
CCCCCCCCCCCCCCC		35.5421551504
55PhosphorylationNSRSRSRSRKSSGTT
CCCCCCCCCCCCCCC		45.3528889911
58PhosphorylationSRSRSRKSSGTTGGL
CCCCCCCCCCCCCCC		32.6522369663
59PhosphorylationRSRSRKSSGTTGGLL
CCCCCCCCCCCCCCC		43.1022369663
61PhosphorylationRSRKSSGTTGGLLKK
CCCCCCCCCCCCCCC		24.9822369663
62PhosphorylationSRKSSGTTGGLLKKP
CCCCCCCCCCCCCCC		32.5522369663
119PhosphorylationRHLIRNPSNSLQLQG
HHHHHCCCCCCEECC		42.4721082442
121PhosphorylationLIRNPSNSLQLQGGD
HHHCCCCCCEECCCC		23.1025533186
134PhosphorylationGDITRDLYKWTNDHP
CCHHHHHHHHHCCCC		14.5821440633
135UbiquitinationDITRDLYKWTNDHPS
CHHHHHHHHHCCCCC		55.6417644757
137PhosphorylationTRDLYKWTNDHPSSP
HHHHHHHHCCCCCCH		26.9821551504
142PhosphorylationKWTNDHPSSPSQYQY
HHHCCCCCCHHHCCC		52.0020377248
143PhosphorylationWTNDHPSSPSQYQYP
HHCCCCCCHHHCCCC		32.7820377248
145PhosphorylationNDHPSSPSQYQYPSQ
CCCCCCHHHCCCCCC		43.3920377248
147PhosphorylationHPSSPSQYQYPSQPA
CCCCHHHCCCCCCCC		17.8529136822
149PhosphorylationSSPSQYQYPSQPALS
CCHHHCCCCCCCCCC		10.4229136822
151PhosphorylationPSQYQYPSQPALSTS
HHHCCCCCCCCCCCC		43.8129136822
156PhosphorylationYPSQPALSTSIPSQA
CCCCCCCCCCCCCCC		23.3929136822
157PhosphorylationPSQPALSTSIPSQAP
CCCCCCCCCCCCCCC		31.3729136822
158PhosphorylationSQPALSTSIPSQAPS
CCCCCCCCCCCCCCC		29.1720377248
161PhosphorylationALSTSIPSQAPSFSN
CCCCCCCCCCCCCCC		36.9929136822
165PhosphorylationSIPSQAPSFSNRKRS
CCCCCCCCCCCCCCC		44.3029136822
167PhosphorylationPSQAPSFSNRKRSMS
CCCCCCCCCCCCCCC		39.8121440633
170UbiquitinationAPSFSNRKRSMSFSA
CCCCCCCCCCCCCCH		53.7417644757
172PhosphorylationSFSNRKRSMSFSAAS
CCCCCCCCCCCCHHH		23.0919779198
176PhosphorylationRKRSMSFSAASIASS
CCCCCCCCHHHHHCC		18.6719779198
183PhosphorylationSAASIASSSHLNNNS
CHHHHHCCHHHCCCC		16.8619779198
184PhosphorylationAASIASSSHLNNNSE
HHHHHCCHHHCCCCC		29.5119779198
190PhosphorylationSSHLNNNSEANGNPL
CHHHCCCCCCCCCCC		39.9619779198
221PhosphorylationAPGGFRRSFIIQKRR
CCCCCCHHHHHHHCH		19.2825533186
229UbiquitinationFIIQKRRKHNVDAPI
HHHHHCHHCCCCCCC		43.4924961812
283PhosphorylationEALETESTQLVSREH
HHHHCHHHHHHHCCC		21.4928889911
360PhosphorylationDKVGVDGYGDMGRIL
CCCCCCCCCCCHHHH		12.8928889911
596UbiquitinationFPSNASGKYNPKVKW
CCCCCCCCCCCCHHH		39.0824961812
658PhosphorylationHYKASILSGTSRARL
HHHHHHCCCCHHHHH		38.0523749301
660PhosphorylationKASILSGTSRARLLL
HHHHCCCCHHHHHHH		16.2123749301
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 AVT3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AVT3_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 AVT3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLX5_YEASTSLX5genetic
20093466
MNN10_YEASTMNN10genetic
20093466
STP1_YEASTSTP1genetic
20093466
YBT1_YEASTYBT1genetic
20093466
YL173_YEASTYLR173Wgenetic
20093466
VRP1_YEASTVRP1genetic
20093466
OCA1_YEASTOCA1genetic
20093466
PHO88_YEASTPHO88physical
16093310
MKAR_YEASTIFA38physical
16093310
MST27_YEASTMST27physical
16093310
GPI7_YEASTLAS21physical
16093310
LAC1_YEASTLAC1physical
16093310
ERFB_YEASTERF2physical
16093310
ADK_YEASTADO1genetic
21623372
COQ7_YEASTCAT5genetic
21623372
CY1_YEASTCYT1genetic
21623372
COX10_YEASTCOX10genetic
21623372
PDX3_YEASTPDX3genetic
21623372
GSH1_YEASTGSH1genetic
21623372
QCR2_YEASTQCR2genetic
21623372
ARGJ_YEASTARG7genetic
21623372
COX6_YEASTCOX6genetic
21623372
6PGD1_YEASTGND1genetic
21623372
TPS2_YEASTTPS2genetic
21623372
ATPF_YEASTATP4genetic
21623372
AVT4_YEASTAVT4genetic
25036121
AVT1_YEASTAVT1genetic
25747199
SLX5_YEASTSLX5genetic
27708008
PRY2_YEASTPRY2genetic
27708008
YBT1_YEASTYBT1genetic
27708008
VRP1_YEASTVRP1genetic
27708008
VPS38_YEASTVPS38genetic
27708008
ROM2_YEASTROM2genetic
27708008
TSA1_YEASTTSA1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AVT3_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-59; SER-119; SER-121;SER-143; SER-145; THR-157; SER-158; SER-165 AND THR-283, 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-58; SER-59 AND THR-61,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-59, AND MASSSPECTROMETRY.

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