VBA4_YEAST - dbPTM
VBA4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VBA4_YEAST
UniProt AC Q04602
Protein Name Vacuolar basic amino acid transporter 4
Gene Name VBA4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 768
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Transporter required for vacuolar uptake of basic amino acids..
Protein Sequence MGKKDRQRKKLREFAKLKNRQRNLRKSVQTLKNEVQREAKVPRTSNQIALGNDKIEEINENSPLLSAPSKQEEVSIPKAVDIDTIDAQPLHEGPKIDDSPQDEVNSIKGKPADKANEDDLKPPSQHEACGNSALQSSITDFSDRSVSPLQSITSCNTPMSEHELPVSSSNSFERADDMPVVQADNQTSSSKSLHIVAPSPEVPVSGDEITSYGYGSIPQSIGDVENGLNPPYVENTSSDELVHDLTRRRIFSSCMCTYLFFIAMDSSIILVIASKIASEFHELWRLSLVISAYLLSNAIGQLVFLKLSLISSVKLLLCIAQFSFILGGYLSWSSAHFWTFIFARCVTGFGGGSLIALKSTIMNRFSQKNDSRYSLSASMITFAMGVVIGPFMMNLFDSSHGSGWRNAFLIPVPFCLVNASIMLADMYSVKSTLYGRPTPTLWKRFKNTLLSPDLYEILTLTLFLLCFVQVTSLDLTGLKNNTMIQALLFSVIIVCGILFFLIETSDTYMNSVISMSLQGDKRLIWTMIGISFCFAALMCIIPFGTTYFIIVLNLSTLQLAERLSPFFFSIVLGYFSVSYFWKSKGQNFLLKFVLSGATLLLYVALMGVSLNLPVWKQYICLSLPFLGSSMILTLLSNLYHEYHEQRKSPISGSIVYCFGAVGGTVGISLGGYVFHKTLIKLMHEKVMPFSKQGYLKKDLLKIIKHATESSDWVHESAPKFVFQTLIECYLQACRNVFKLSTLFFTITVVAIFIFNRIHCRSQNCLSLS
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
16AcetylationKKLREFAKLKNRQRN
HHHHHHHHHHHHHHH		66.3725381059
26AcetylationNRQRNLRKSVQTLKN
HHHHHHHHHHHHHHH		59.1325381059
27PhosphorylationRQRNLRKSVQTLKNE
HHHHHHHHHHHHHHH		17.0224961812
30PhosphorylationNLRKSVQTLKNEVQR
HHHHHHHHHHHHHHH		37.2324961812
32UbiquitinationRKSVQTLKNEVQREA
HHHHHHHHHHHHHHC		55.2223749301
44PhosphorylationREAKVPRTSNQIALG
HHCCCCCCCCCEECC		26.4222369663
45PhosphorylationEAKVPRTSNQIALGN
HCCCCCCCCCEECCC		28.1922369663
54UbiquitinationQIALGNDKIEEINEN
CEECCCHHHHHHHCC		56.8923749301
62PhosphorylationIEEINENSPLLSAPS
HHHHHCCCCCCCCCC		15.6722369663
66PhosphorylationNENSPLLSAPSKQEE
HCCCCCCCCCCCCCC		45.9022369663
69PhosphorylationSPLLSAPSKQEEVSI
CCCCCCCCCCCCCCC		46.8422369663
70UbiquitinationPLLSAPSKQEEVSIP
CCCCCCCCCCCCCCC		61.7524961812
75PhosphorylationPSKQEEVSIPKAVDI
CCCCCCCCCCCCCCC		36.1321440633
78UbiquitinationQEEVSIPKAVDIDTI
CCCCCCCCCCCCCCC		60.4124961812
84PhosphorylationPKAVDIDTIDAQPLH
CCCCCCCCCCCCCCC		22.5322369663
95UbiquitinationQPLHEGPKIDDSPQD
CCCCCCCCCCCCCHH		70.4017644757
99PhosphorylationEGPKIDDSPQDEVNS
CCCCCCCCCHHHHHH		22.2522369663
106PhosphorylationSPQDEVNSIKGKPAD
CCHHHHHHCCCCCCC		30.7422369663
108UbiquitinationQDEVNSIKGKPADKA
HHHHHHCCCCCCCCC		61.7817644757
124PhosphorylationEDDLKPPSQHEACGN
CCCCCCCCHHHHCCC		53.3428889911
136PhosphorylationCGNSALQSSITDFSD
CCCHHHHHHHCCCCC		25.2619779198
137PhosphorylationGNSALQSSITDFSDR
CCHHHHHHHCCCCCC		19.2928889911
139PhosphorylationSALQSSITDFSDRSV
HHHHHHHCCCCCCCC		32.7019779198
142PhosphorylationQSSITDFSDRSVSPL
HHHHCCCCCCCCCCC		34.6225704821
145PhosphorylationITDFSDRSVSPLQSI
HCCCCCCCCCCCHHH		31.7519779198
147PhosphorylationDFSDRSVSPLQSITS
CCCCCCCCCCHHHHC		22.5728889911
153PhosphorylationVSPLQSITSCNTPMS
CCCCHHHHCCCCCCC		32.2628889911
154PhosphorylationSPLQSITSCNTPMSE
CCCHHHHCCCCCCCC		12.0519779198
157PhosphorylationQSITSCNTPMSEHEL
HHHHCCCCCCCCCCC		25.3723749301
160PhosphorylationTSCNTPMSEHELPVS
HCCCCCCCCCCCCCC		36.6823749301
167PhosphorylationSEHELPVSSSNSFER
CCCCCCCCCCCCCCC		26.5528889911
168PhosphorylationEHELPVSSSNSFERA
CCCCCCCCCCCCCCC		33.5028889911
169PhosphorylationHELPVSSSNSFERAD
CCCCCCCCCCCCCCC		29.0523749301
171PhosphorylationLPVSSSNSFERADDM
CCCCCCCCCCCCCCC		30.3628889911
187PhosphorylationVVQADNQTSSSKSLH
EEECCCCCCCCCEEE		36.5122890988
188PhosphorylationVQADNQTSSSKSLHI
EECCCCCCCCCEEEE		23.8922890988
189PhosphorylationQADNQTSSSKSLHIV
ECCCCCCCCCEEEEE		45.2122369663
190PhosphorylationADNQTSSSKSLHIVA
CCCCCCCCCEEEEEC		26.4822369663
191UbiquitinationDNQTSSSKSLHIVAP
CCCCCCCCEEEEECC		60.0117644757
192PhosphorylationNQTSSSKSLHIVAPS
CCCCCCCEEEEECCC		27.4228747907
373PhosphorylationSQKNDSRYSLSASMI
HCCCCCCCCCHHHHH		20.2227017623
376PhosphorylationNDSRYSLSASMITFA
CCCCCCCHHHHHHHH		16.6227017623
378PhosphorylationSRYSLSASMITFAMG
CCCCCHHHHHHHHHH		13.8227017623
398PhosphorylationFMMNLFDSSHGSGWR
HHHHHHCCCCCCCCC		19.5227017623
399PhosphorylationMMNLFDSSHGSGWRN
HHHHHCCCCCCCCCC		33.4427017623
402PhosphorylationLFDSSHGSGWRNAFL
HHCCCCCCCCCCCEE		29.7427017623
443AcetylationRPTPTLWKRFKNTLL
CCCHHHHHHHHCCCC		51.5824489116
480N-linked_GlycosylationLDLTGLKNNTMIQAL
CCCCCCCCCHHHHHH		55.00-
553N-linked_GlycosylationTYFIIVLNLSTLQLA
EEEEEEEEHHHHHHH		22.50-
690PhosphorylationHEKVMPFSKQGYLKK
HHHHCCCCCCCCCHH		20.4221551504
701AcetylationYLKKDLLKIIKHATE
CCHHHHHHHHHHHHH		50.0824489116
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 VBA4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VBA4_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 VBA4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATC2_YEASTPMC1physical
18467557
ATG27_YEASTATG27physical
18467557
BUD9_YEASTBUD9physical
16093310
YHN8_YEASTYHR078Wphysical
16093310
YMC1_YEASTYMC1physical
16093310
NOP56_YEASTNOP56genetic
27708008
ALG14_YEASTALG14genetic
27708008
NHP2_YEASTNHP2genetic
27708008
GPI19_YEASTGPI19genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ORC6_YEASTORC6genetic
27708008
CDC23_YEASTCDC23genetic
27708008
RRN7_YEASTRRN7genetic
27708008
NU192_YEASTNUP192genetic
27708008
KTHY_YEASTCDC8genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
RPF2_YEASTRPF2genetic
27708008
DIM1_YEASTDIM1genetic
27708008
CUL3_YEASTCUL3genetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
OPI1_YEASTOPI1genetic
27708008
MPCP_YEASTMIR1genetic
27708008
YL032_YEASTYLL032Cgenetic
27708008
YL278_YEASTYLR278Cgenetic
27708008
MAC1_YEASTMAC1genetic
27708008
HAT1_YEASTHAT1genetic
27708008
YP264_YEASTYPL264Cgenetic
27708008
ISR1_YEASTISR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VBA4_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-62; THR-84; SER-99;SER-106; SER-137; THR-153; SER-190 AND SER-192, 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-106, 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 SER-62, 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 THR-84, AND MASSSPECTROMETRY.

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