YBT1_YEAST - dbPTM
YBT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YBT1_YEAST
UniProt AC P32386
Protein Name ATP-dependent bile acid permease
Gene Name YBT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1661
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Vacuolar class C ABC transporter which regulates the translocation of phosphatidylcholine to the vacuole lumen, the release of lumenal calcium stores, and acts as a negative regulator of vacuole fusion. Exhibits ATP-dependent bile acid transport..
Protein Sequence MHHVLNSTRPDHRFWFYDDVTQYGRTKYLNYYTPLVLLIFTVLFITYNIWKHYYYYDVLHLKQKNPIDELLYSSTDEDEQSPLINNNTITTNYVDNNCTKDALKNRHFSLEKLKSVKVNGEPHGTPEIVRRGFIEKSRIILEFFLVLSQVIIHSFILLHYVNKNPEFTQQGTITGLVEWCALFIIVSLRLANVNQNFKFINKYPGNLWSVSFINYLALFISMILPFRSIFIHHINSPISRKYYISQISINLALFLLLFFARIRNNFAIIYKTDSWITPSPEPVTSIAGFICWAWLDSFVWKAHKVSIKVKDIWGLMMQDYSFFVVKKFRYFVDHKVKRKRIFSLNLFFFFSNYLVLQCFWAFLGSVLSFIPTVLLKRILEYVEDQSSAPSNLAWFYVTVMFVGRILVAICQAQALFFGRRVCIRMKSIIISEIYTKALRRKISTNKTKPSNEDPQEINDQKSINGDEESTSSANLGAIINLMAIDAFKVSEICGYLHSFLEAFVMTVVALALLYRLLGFAAIVGVLIIVAMLPLNYKLAKYIGDLQKKNLAVTDNRIQKLNEAFQAIRIIKYFSWEENFEKDINTIRENELSLLLMRSIVWSISSFLWFVTPTIVTAASFAYYIYVQGEVLTTPVAFTALSLFTLLRDPLDRLSDMLSFVVQSKVSLDRVQDFLNENDTKKYDQLTIDPNGNRFAFENSTISWDKDNQDFKLKDLNIEFKTGKLNVVIGPTGSGKTSLLMALLGEMYLLNGKVVVPALEPRQELIVDANGTTNSIAYCSQAAWLLNDTVKNNILFNSPFNEARYKAVVEACGLKRDFEILKAGDLTEIGEKGITLSGGQKQRVSLARALYSNARHVLLDDCLSAVDSHTASWIYDNCITGPLMEDRTCILVSHNIALTLRNAELVVLLEDGRVKDQGDPIDMLQKGLFGEDELVKSSILSRANSSANLAAKSSTSLSNLPAVKEQQVSVNNNSSHFEAKKLQKSLRTEAERTEDGKLIKEETKEEGVVGLDVYKWYLKIFGGWKIVSFLASLFLIAQLLYIGQSWWVRAWASHNVIAKIIPRAQRAIAFISKKASHLIDWRGSSQISMASAENQPSSGHSTMYYLVLYLIIGFAQALLGAGKTILNFVAGINASRKIFNMILNKVLHSKIRFFDATPTGRIMNRFSKDIEAIDQELTPYIQGAFYSLIECLSTVILITFITPQFLSVAIVVSILYYFVGYFYMAGSRELKRFESISRSPIYQHFSETLVGVTTIRAFGDEGRFMQENLHKIDENNKPFFYLWVANRWLAFRIDMIGSLVIFGAGLFILFNINNLDSGMAGISLTYAISFTEGALWLVRLYSEVEMNMNSVERVKEYMEIEQEPYNEHKEIPPPQWPQDGKIEVNDLSLRYAPNLPRVIKNVSFSVDAQSKIGIVGRTGAGKSTIITALFRFLEPETGHIKIDNIDISGVDLQRLRRSITIIPQDPTLFSGTIKTNLDPYDEFSDRQIFEALKRVNLISEEQLQQGATRETSNEASSTNSENVNKFLDLSSEISEGGSNLSQGQRQLMCLARSLLRSPKIILLDEATASIDYSSDAKIQETIRKEFQGSTILTIAHRLRSVIDYDKILVMDAGEVKEYDHPYSLLLNKQSAFYSMCEHSGELDILIELAKKAFVEKLNSKKD
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
6N-linked_Glycosylation--MHHVLNSTRPDHR
--CCCCCCCCCCCCC		40.00-
72PhosphorylationNPIDELLYSSTDEDE
CCHHHHHCCCCCCCC		17.1321440633
73PhosphorylationPIDELLYSSTDEDEQ
CHHHHHCCCCCCCCC		27.0821551504
74PhosphorylationIDELLYSSTDEDEQS
HHHHHCCCCCCCCCC		26.7319779198
75PhosphorylationDELLYSSTDEDEQSP
HHHHCCCCCCCCCCC		37.1519779198
81PhosphorylationSTDEDEQSPLINNNT
CCCCCCCCCCCCCCC		21.4528889911
97N-linked_GlycosylationTTNYVDNNCTKDALK
CCCEECCCCCHHHHH		30.30-
109PhosphorylationALKNRHFSLEKLKSV
HHHCCCCCHHHHHCC		29.5028747907
112AcetylationNRHFSLEKLKSVKVN
CCCCCHHHHHCCEEC		67.5222865919
431PhosphorylationRMKSIIISEIYTKAL
HHHHHHHHHHHHHHH		13.9228889911
434PhosphorylationSIIISEIYTKALRRK
HHHHHHHHHHHHHHH		9.7228889911
443PhosphorylationKALRRKISTNKTKPS
HHHHHHHCCCCCCCC		29.0324930733
444PhosphorylationALRRKISTNKTKPSN
HHHHHHCCCCCCCCC		44.1824930733
448UbiquitinationKISTNKTKPSNEDPQ
HHCCCCCCCCCCCHH		48.3223749301
471PhosphorylationNGDEESTSSANLGAI
CCCCCCCCCCHHHHH		36.4128747907
559AcetylationVTDNRIQKLNEAFQA
CCCHHHHHHHHHHHH		51.4024489116
705AcetylationNSTISWDKDNQDFKL
CCEEEECCCCCCEEE		52.9324489116
711AcetylationDKDNQDFKLKDLNIE
CCCCCCEEECEEEEE		64.0224489116
713UbiquitinationDNQDFKLKDLNIEFK
CCCCEEECEEEEEEE		61.8424961812
721PhosphorylationDLNIEFKTGKLNVVI
EEEEEEECCCEEEEE		44.8921551504
736PhosphorylationGPTGSGKTSLLMALL
CCCCCCHHHHHHHHH		28.2927017623
737PhosphorylationPTGSGKTSLLMALLG
CCCCCHHHHHHHHHH		24.0027017623
747PhosphorylationMALLGEMYLLNGKVV
HHHHHCHHHHCCEEE		12.0727017623
790UbiquitinationWLLNDTVKNNILFNS
HHHCCCHHCCCCCCC		46.5017644757
831AcetylationDLTEIGEKGITLSGG
CCCEECCCCEECCCC		50.8524489116
831UbiquitinationDLTEIGEKGITLSGG
CCCEECCCCEECCCC		50.8523749301
850PhosphorylationVSLARALYSNARHVL
HHHHHHHHHCCCCHH		10.0119779198
851PhosphorylationSLARALYSNARHVLL
HHHHHHHHCCCCHHH		25.5119779198
867PhosphorylationDCLSAVDSHTASWIY
HHHHHHHHCCHHHHH		19.0119779198
935AcetylationFGEDELVKSSILSRA
CCCHHHHHHHHHHHC		51.6224489116
935UbiquitinationFGEDELVKSSILSRA
CCCHHHHHHHHHHHC		51.6223749301
936PhosphorylationGEDELVKSSILSRAN
CCHHHHHHHHHHHCC		18.3522369663
937PhosphorylationEDELVKSSILSRANS
CHHHHHHHHHHHCCC		23.1022369663
940PhosphorylationLVKSSILSRANSSAN
HHHHHHHHHCCCCCC		27.9022369663
944PhosphorylationSILSRANSSANLAAK
HHHHHCCCCCCHHHH		29.8222369663
945PhosphorylationILSRANSSANLAAKS
HHHHCCCCCCHHHHC		22.4525521595
951UbiquitinationSSANLAAKSSTSLSN
CCCCHHHHCCCCHHC		39.0523749301
952PhosphorylationSANLAAKSSTSLSNL
CCCHHHHCCCCHHCC		33.8422369663
953PhosphorylationANLAAKSSTSLSNLP
CCHHHHCCCCHHCCC		22.7025521595
954PhosphorylationNLAAKSSTSLSNLPA
CHHHHCCCCHHCCCC		40.5522369663
955PhosphorylationLAAKSSTSLSNLPAV
HHHHCCCCHHCCCCC		31.5722369663
957PhosphorylationAKSSTSLSNLPAVKE
HHCCCCHHCCCCCEE		35.7725521595
963UbiquitinationLSNLPAVKEQQVSVN
HHCCCCCEEEEEECC		52.4924961812
968PhosphorylationAVKEQQVSVNNNSSH
CCEEEEEECCCCCCH		18.1321440633
973PhosphorylationQVSVNNNSSHFEAKK
EEECCCCCCHHHHHH		27.5821440633
974PhosphorylationVSVNNNSSHFEAKKL
EECCCCCCHHHHHHH		34.0321440633
979AcetylationNSSHFEAKKLQKSLR
CCCHHHHHHHHHHHH		46.9824489116
979UbiquitinationNSSHFEAKKLQKSLR
CCCHHHHHHHHHHHH		46.9823749301
1052PhosphorylationWWVRAWASHNVIAKI
HHHHHHHCCCHHHHH		12.6119684113
1156PhosphorylationKIRFFDATPTGRIMN
CCCCCCCCCCCHHHH		24.1921551504
1457PhosphorylationDLQRLRRSITIIPQD
CHHHHHHCEEEECCC		20.0427017623
1492UbiquitinationRQIFEALKRVNLISE
HHHHHHHHHCCCCCH		62.4417644757
1498PhosphorylationLKRVNLISEEQLQQG
HHHCCCCCHHHHHCC		37.9421551504
1507PhosphorylationEQLQQGATRETSNEA
HHHHCCCCCCCCCCC		35.5421551504
1510PhosphorylationQQGATRETSNEASST
HCCCCCCCCCCCCCC		33.3022890988
1511PhosphorylationQGATRETSNEASSTN
CCCCCCCCCCCCCCC		28.1122890988
1515PhosphorylationRETSNEASSTNSENV
CCCCCCCCCCCCCHH		31.3622890988
1516PhosphorylationETSNEASSTNSENVN
CCCCCCCCCCCCHHH		38.3625521595
1517PhosphorylationTSNEASSTNSENVNK
CCCCCCCCCCCHHHH		40.0222369663
1519PhosphorylationNEASSTNSENVNKFL
CCCCCCCCCHHHHHH		30.5422369663
1529PhosphorylationVNKFLDLSSEISEGG
HHHHHHHHHHHCCCC		26.1221440633
1530PhosphorylationNKFLDLSSEISEGGS
HHHHHHHHHHCCCCC		46.3721440633
1572PhosphorylationATASIDYSSDAKIQE
CCCCCCCCCCHHHHH		20.2819779198
1573PhosphorylationTASIDYSSDAKIQET
CCCCCCCCCHHHHHH		35.0419779198
1655UbiquitinationAKKAFVEKLNSKKD-
HHHHHHHHHHCCCC-		47.9023749301
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 YBT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YBT1_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 YBT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHO1_YEASTSHO1physical
16093310
PXA1_YEASTPXA1physical
16093310
SSB1_YEASTSSB1physical
22940862
HSP72_YEASTSSA2physical
22940862
HSP71_YEASTSSA1physical
22940862
YEV1_YEASTYER121Wphysical
23831759
GYL1_YEASTGYL1physical
23831759
COFI_YEASTCOF1physical
23831759
GRP78_YEASTKAR2physical
23831759
FBRL_YEASTNOP1physical
23831759
SSB1_YEASTSSB1physical
23831759
AGP1_YEASTAGP1genetic
27708008
THRC_YEASTTHR4genetic
27708008
RRP8_YEASTRRP8genetic
27708008
YHK5_YEASTYHR045Wgenetic
27708008
ALY1_YEASTALY1genetic
27708008
CYSD_YEASTMET17genetic
27708008
RIM13_YEASTRIM13genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YBT1_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 SER-81; SER-936; SER-937;SER-940; SER-944; SER-952; SER-953; THR-954; SER-955; SER-1516;THR-1517 AND SER-1519, 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-936, AND MASSSPECTROMETRY.
"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-936, 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-940; SER-944 ANDTHR-954, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940; SER-944; SER-1516AND THR-1517, AND MASS SPECTROMETRY.

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