AVT1_YEAST - dbPTM
AVT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AVT1_YEAST
UniProt AC P47082
Protein Name Vacuolar amino acid transporter 1
Gene Name AVT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 602
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Required for the vacuolar uptake of large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine. Requires ATP for function..
Protein Sequence MPEQEPLSPNGRKRSEVHYISIPLNRGSAFSPDDSVSQFQSDGFMTRRQSILDHPVGSFKGVNSLSRFATSLRRANSFRNIELNADNERSFFKESNDETYDPDTLAPALDGRRLSVTLNNAGRPRITNLANNDRVSTASMAIHDDDYGSIQNSTIGDSGSILRPTASLTEMMSGGAGRRFTNNDMDSIVVKRVEGVDGKVVTLLAGQSTAPQTIFNSINVLIGIGLLALPLGLKYAGWVIGLTMLAIFALATFCTAELLSRCLDTDPTLISYADLGYAAFGTKGRALISALFTLDLLGSGVSLVILFGDSLNALFPQYSTTFFKIVSFFIVTPPVFIPLSVLSNISLLGILSTTGTVLVICCCGLYKSSSPGSLVNPMETSMWPIDLKHLCLSIGLLSACWGGHAVFPNLKTDMRHPDKFKDCLKTTYKITSVTDIGTAVIGFLMFGNLVKDEITKNVLLTEGYPKFVYGLISALMTIIPIAKTPLNARPIVSVLDVLMNVQHIDEAASAIKRRAAKGLQVFNRIFINVVFVLIAINFPEFDKIIAFLGAGLCFTICLILPCWFYLRLCKTTIKPWERVACHVTICISVVLSTLGVGAAIIS
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
8PhosphorylationMPEQEPLSPNGRKRS
CCCCCCCCCCCCCCC		27.3422369663
15PhosphorylationSPNGRKRSEVHYISI
CCCCCCCCEEEEEEE		47.1817330950
19PhosphorylationRKRSEVHYISIPLNR
CCCCEEEEEEEECCC		11.0919779198
21PhosphorylationRSEVHYISIPLNRGS
CCEEEEEEEECCCCC		15.8128889911
28PhosphorylationSIPLNRGSAFSPDDS
EEECCCCCCCCCCCC		23.9323749301
31PhosphorylationLNRGSAFSPDDSVSQ
CCCCCCCCCCCCHHH		27.4325752575
35PhosphorylationSAFSPDDSVSQFQSD
CCCCCCCCHHHHHCC		30.9222369663
37PhosphorylationFSPDDSVSQFQSDGF
CCCCCCHHHHHCCCC		29.2722369663
41PhosphorylationDSVSQFQSDGFMTRR
CCHHHHHCCCCCCCC		40.7822369663
46PhosphorylationFQSDGFMTRRQSILD
HHCCCCCCCCHHHHH		22.0519779198
50PhosphorylationGFMTRRQSILDHPVG
CCCCCCHHHHHCCCC		24.2529136822
58PhosphorylationILDHPVGSFKGVNSL
HHHCCCCCCCCHHHH		24.8221082442
60AcetylationDHPVGSFKGVNSLSR
HCCCCCCCCHHHHHH		64.7424489116
60UbiquitinationDHPVGSFKGVNSLSR
HCCCCCCCCHHHHHH		64.7417644757
64PhosphorylationGSFKGVNSLSRFATS
CCCCCHHHHHHHHHH		25.8928152593
66PhosphorylationFKGVNSLSRFATSLR
CCCHHHHHHHHHHHH		25.7719684113
70PhosphorylationNSLSRFATSLRRANS
HHHHHHHHHHHHHHC		26.1124961812
71PhosphorylationSLSRFATSLRRANSF
HHHHHHHHHHHHHCC		19.2224961812
77PhosphorylationTSLRRANSFRNIELN
HHHHHHHCCCCEECC		25.2928152593
90PhosphorylationLNADNERSFFKESND
CCCCCCHHHCCCCCC		28.9328889911
93UbiquitinationDNERSFFKESNDETY
CCCHHHCCCCCCCCC		59.2223749301
93AcetylationDNERSFFKESNDETY
CCCHHHCCCCCCCCC		59.2224489116
95PhosphorylationERSFFKESNDETYDP
CHHHCCCCCCCCCCC		50.6128152593
99PhosphorylationFKESNDETYDPDTLA
CCCCCCCCCCCCCCC		35.7719795423
100PhosphorylationKESNDETYDPDTLAP
CCCCCCCCCCCCCCH		24.3523749301
115PhosphorylationALDGRRLSVTLNNAG
HCCCCEEEEEECCCC		15.9624909858
117PhosphorylationDGRRLSVTLNNAGRP
CCCEEEEEECCCCCC		22.0125005228
136PhosphorylationLANNDRVSTASMAIH
CCCCCCCCCCHHEEC		21.1028889911
137PhosphorylationANNDRVSTASMAIHD
CCCCCCCCCHHEECC		21.6428889911
181PhosphorylationGGAGRRFTNNDMDSI
CCCCCCCCCCCCCCE		31.1617330950
187PhosphorylationFTNNDMDSIVVKRVE
CCCCCCCCEEEEEEE		15.6222369663
191UbiquitinationDMDSIVVKRVEGVDG
CCCCEEEEEEECCCC		39.5723749301
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 AVT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AVT1_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 AVT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FABD_YEASTMCT1genetic
21623372
FOLE_YEASTMET7genetic
21623372
CSG2_YEASTCSG2genetic
21623372
GPP1_YEASTGPP1genetic
21623372
COX7_YEASTCOX7genetic
21623372
THRC_YEASTTHR4genetic
21623372
GDE1_YEASTGDE1genetic
21623372
COQ2_YEASTCOQ2genetic
21623372
CKS1_YEASTCKS1genetic
27708008
FAD1_YEASTFAD1genetic
27708008
SNU23_YEASTSNU23genetic
27708008
TEL2_YEASTTEL2genetic
27708008
MED6_YEASTMED6genetic
27708008
ORC6_YEASTORC6genetic
27708008
FNTA_YEASTRAM2genetic
27708008
SED5_YEASTSED5genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
DBP6_YEASTDBP6genetic
27708008
CLP1_YEASTCLP1genetic
27708008
BUR1_YEASTSGV1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AVT1_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-8; SER-35; SER-37;SER-95; SER-136 AND THR-137, 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 THR-181 AND SER-187, ANDMASS SPECTROMETRY.

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