BPT1_YEAST - dbPTM
BPT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BPT1_YEAST
UniProt AC P14772
Protein Name Bile pigment transporter 1
Gene Name BPT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1559
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Cooperates for the ATP-dependent vacuolar transport of bilirubin and glutathione conjugates..
Protein Sequence MSSLEVVDGCPYGYRPYPDSGTNALNPCFISVISAWQAVFFLLIGSYQLWKLYKNNKVPPRFKNFPTLPSKINSRHLTHLTNVCFQSTLIICELALVSQSSDRVYPFILKKALYLNLLFNLGISLPTQYLAYFKSTFSMGNQLFYYMFQILLQLFLILQRYYHGSSNERLTVISGQTAMILEVLLLFNSVAIFIYDLCIFEPINELSEYYKKNGWYPPVHVLSYITFIWMNKLIVETYRNKKIKDPNQLPLPPVDLNIKSISKEFKANWELEKWLNRNSLWRAIWKSFGRTISVAMLYETTSDLLSVVQPQFLRIFIDGLNPETSSKYPPLNGVFIALTLFVISVVSVFLTNQFYIGIFEAGLGIRGSLASLVYQKSLRLTLAERNEKSTGDILNLMSVDVLRIQRFFENAQTIIGAPIQIIVVLTSLYWLLGKAVIGGLVTMAIMMPINAFLSRKVKKLSKTQMKYKDMRIKTITELLNAIKSIKLYAWEEPMMARLNHVRNDMELKNFRKIGIVSNLIYFAWNCVPLMVTCSTFGLFSLFSDSPLSPAIVFPSLSLFNILNSAIYSVPSMINTIIETSVSMERLKSFLLSDEIDDSFIERIDPSADERALPAIEMNNITFLWKSKEVLTSSQSGDNLRTDEESIIGSSQIALKNIDHFEAKRGDLVCVVGRVGAGKSTFLKAILGQLPCMSGSRDSIPPKLIIRSSSVAYCSQESWIMNASVRENILFGHKFDQDYYDLTIKACQLLPDLKILPDGDETLVGEKGISLSGGQKARLSLARAVYSRADIYLLDDILSAVDAEVSKNIIEYVLIGKTALLKNKTIILTTNTVSILKHSQMIYALENGEIVEQGNYEDVMNRKNNTSKLKKLLEEFDSPIDNGNESDVQTEHRSESEVDEPLQLKVTESETEDEVVTESELELIKANSRRASLATLRPRPFVGAQLDSVKKTAQKAEKTEVGRVKTKIYLAYIKACGVLGVVLFFLFMILTRVFDLAENFWLKYWSESNEKNGSNERVWMFVGVYSLIGVASAAFNNLRSIMMLLYCSIRGSKKLHESMAKSVIRSPMTFFETTPVGRIINRFSSDMDAVDSNLQYIFSFFFKSILTYLVTVILVGYNMPWFLVFNMFLVVIYIYYQTFYIVLSRELKRLISISYSPIMSLMSESLNGYSIIDAYDHFERFIYLNYEKIQYNVDFVFNFRSTNRWLSVRLQTIGATIVLATAILALATMNTKRQLSSGMVGLLMSYSLEVTGSLTWIVRTTVTIETNIVSVERIVEYCELPPEAQSINPEKRPDENWPSKGGIEFKNYSTKYRENLDPVLNNINVKIEPCEKVGIVGRTGAGKSTLSLALFRILEPTEGKIIIDGIDISDIGLFDLRSHLAIIPQDAQAFEGTVKTNLDPFNRYSEDELKRAVEQAHLKPHLEKMLHSKPRGDDSNEEDGNVNDILDVKINENGSNLSVGQRQLLCLARALLNRSKILVLDEATASVDMETDKIIQDTIRREFKDRTILTIAHRIDTVLDSDKIIVLDQGSVREFDSPSKLLSDKTSIFYSLCEKGGYLK
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
631PhosphorylationWKSKEVLTSSQSGDN
EECHHHHHCCCCCCC		31.3522369663
632PhosphorylationKSKEVLTSSQSGDNL
ECHHHHHCCCCCCCC		23.4022369663
633PhosphorylationSKEVLTSSQSGDNLR
CHHHHHCCCCCCCCC		24.1122369663
635PhosphorylationEVLTSSQSGDNLRTD
HHHHCCCCCCCCCCC		50.4922369663
641PhosphorylationQSGDNLRTDEESIIG
CCCCCCCCCHHHHHC		51.4322369663
645PhosphorylationNLRTDEESIIGSSQI
CCCCCHHHHHCCHHH		19.9122369663
649PhosphorylationDEESIIGSSQIALKN
CHHHHHCCHHHHHHC		14.5222369663
650PhosphorylationEESIIGSSQIALKNI
HHHHHCCHHHHHHCC		22.0122369663
663UbiquitinationNIDHFEAKRGDLVCV
CCCHHCHHCCCEEEE		50.1117644757
753UbiquitinationCQLLPDLKILPDGDE
HHCCCCCEECCCCCC		49.9623749301
877PhosphorylationKLLEEFDSPIDNGNE
HHHHHCCCCCCCCCC		29.1319795423
885PhosphorylationPIDNGNESDVQTEHR
CCCCCCCCHHCCCCC		47.2721551504
889PhosphorylationGNESDVQTEHRSESE
CCCCHHCCCCCCHHC		33.3420377248
893PhosphorylationDVQTEHRSESEVDEP
HHCCCCCCHHCCCCC		47.5920377248
895PhosphorylationQTEHRSESEVDEPLQ
CCCCCCHHCCCCCEE		44.1322369663
906PhosphorylationEPLQLKVTESETEDE
CCEEEEEECCCCCCC		32.0122369663
908PhosphorylationLQLKVTESETEDEVV
EEEEEECCCCCCCEE		40.2222369663
910PhosphorylationLKVTESETEDEVVTE
EEEECCCCCCCEECH		59.0020377248
916PhosphorylationETEDEVVTESELELI
CCCCCEECHHHHHHH		38.6822369663
918PhosphorylationEDEVVTESELELIKA
CCCEECHHHHHHHHH		37.8122369663
927PhosphorylationLELIKANSRRASLAT
HHHHHHCCCCCCCCC		28.1820377248
931PhosphorylationKANSRRASLATLRPR
HHCCCCCCCCCCCCC		19.4119823750
934PhosphorylationSRRASLATLRPRPFV
CCCCCCCCCCCCCCC		28.7019823750
947PhosphorylationFVGAQLDSVKKTAQK
CCCHHHHHHHHHHHH		44.4119823750
1011N-linked_GlycosylationWSESNEKNGSNERVW
HCCCCCCCCCCCCEE		53.61-
1024PhosphorylationVWMFVGVYSLIGVAS
EEEEEHHHHHHHHHH		7.5728132839
1045PhosphorylationRSIMMLLYCSIRGSK
HHHHHHHHHHHHCCH		4.7228132839
1047PhosphorylationIMMLLYCSIRGSKKL
HHHHHHHHHHCCHHH		11.1928889911
1154PhosphorylationKRLISISYSPIMSLM
HHHHHCCCHHHHHHH		19.4530377154
1168PhosphorylationMSESLNGYSIIDAYD
HCHHHCCCCHHHHHH		8.8130377154
1169PhosphorylationSESLNGYSIIDAYDH
CHHHCCCCHHHHHHH		17.9230377154
1211PhosphorylationWLSVRLQTIGATIVL
EEEEEHHHHHHHHHH		26.4330377154
1220PhosphorylationGATIVLATAILALAT
HHHHHHHHHHHHHHH		15.2930377154
1227PhosphorylationTAILALATMNTKRQL
HHHHHHHHCCCCCHH		16.2930377154
1230PhosphorylationLALATMNTKRQLSSG
HHHHHCCCCCHHHCC		19.4430377154
1310UbiquitinationEFKNYSTKYRENLDP
EECCCCCHHHHCCCH		36.0517644757
1325UbiquitinationVLNNINVKIEPCEKV
HHHHCCEEEEECCEE		36.5417644757
1342AcetylationVGRTGAGKSTLSLAL
ECCCCCCHHHHHHHH		39.4724489116
1394UbiquitinationQAFEGTVKTNLDPFN
HHCCCCCCCCCCCCC		31.3717644757
1418UbiquitinationAVEQAHLKPHLEKML
HHHHHHCHHHHHHHH		22.1122106047
1434PhosphorylationSKPRGDDSNEEDGNV
CCCCCCCCCCCCCCC		51.3723749301
1448UbiquitinationVNDILDVKINENGSN
CCHHEEEEECCCCCC		39.2117644757
1539UbiquitinationREFDSPSKLLSDKTS
EECCCHHHHCCCCHH		57.7518433149
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 BPT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BPT1_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 BPT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YCFI_YEASTYCF1genetic
15632430
HSP72_YEASTSSA2physical
22940862
HSP71_YEASTSSA1physical
22940862
YD85C_YEASTYDL085C-Aphysical
23831759
PROF_YEASTPFY1physical
23831759
COFI_YEASTCOF1physical
23831759
SYNC_YEASTDED81physical
23831759
XRN1_YEASTXRN1physical
23831759
TPIS_YEASTTPI1physical
23831759
INO4_YEASTINO4genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
SNF5_YEASTSNF5genetic
27708008
ODO2_YEASTKGD2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
TBP7_YEASTYTA7genetic
27708008
SNF6_YEASTSNF6genetic
27708008
VPS53_YEASTVPS53genetic
27708008
YJ9J_YEASTYJR142Wgenetic
27708008
AP1_YEASTYAP1genetic
27708008
ERG6_YEASTERG6genetic
27708008
MLH1_YEASTMLH1genetic
27708008
ADE_YEASTAAH1genetic
27708008
RRP6_YEASTRRP6genetic
27708008
ROX1_YEASTROX1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BPT1_YEAST

loading...

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 THR-641; SER-645; SER-895;THR-906; SER-908 AND THR-916, AND MASS SPECTROMETRY.
"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-885, AND MASSSPECTROMETRY.
"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-927; SER-931 ANDTHR-934, 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-645, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory