OSH1_YEAST - dbPTM
OSH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSH1_YEAST
UniProt AC P35845
Protein Name Oxysterol-binding protein homolog 1
Gene Name SWH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1188
Subcellular Localization Cytoplasm. Golgi apparatus membrane. Nucleus outer membrane. Soluble protein that accumulates on the surface of late Golgi membranes and at nucleus-vacuole (NV) junctions, interorganelle interfaces between the nuclear envelope and the vacuole membran
Protein Description Lipid-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides. May be involved in formation of PMN vesicles by altering the membrane lipid composition..
Protein Sequence MEQPDLSSVAISKPLLKLKLLDALRQGSFPNLQDLLKKQFQPLDDPNVQQVLHLMLHYAVQVAPMAVIKEIVHHWVSTTNTTFLNIHLDLNERDSNGNTPLHIAAYQSRGDIVAFLLDQPTINDCVLNNSHLQAIEMCKNLNIAQMMQVKRSTYVAETAQEFRTAFNNRDFGHLESILSSPRNAELLDINGMDPETGDTVLHEFVKKRDVIMCRWLLEHGADPFKRDRKGKLPIELVRKVNENDTATNTKIAIDIELKKLLERATREQSVIDVTNNNLHEAPTYKGYLKKWTNFAQGYKLRWFILSSDGKLSYYIDQADTKNACRGSLNMSSCSLHLDSSEKLKFEIIGGNNGVIRWHLKGNHPIETNRWVWAIQGAIRYAKDREILLHNGPYSPSLALSHGLSSKVSNKENLHATSKRLTKSPHLSKSTLTQNDHDNDDDSTNNNNNKSNNDYDDNNNNNNNDDDDYDDDDESRPLIEPLPLISSRSQSLSEITPGPHSRKSTVSSTRAADIPSDDEGYSEDDSDDDGNSSYTMENGGENDGDEDLNAIYGPYIQKLHMLQRSISIELASLNELLQDKQQHDEYWNTVNTSIETVSEFFDKLNRLTSQREKRMIAQMTKQRDVNNVWIQSVKDLEMELVDKDEKLVALDKERKNLKKMLQKKLNNQPQVETEANEESDDANSMIKGSQESTNTLEEIVKFIEATKESDEDSDADEFFDAEEAASDKKANDSEDLTTNKETPANAKPQEEAPEDESLIVISSPQVEKKNQLLKEGSFVGYEDPVRTKLALDEDNRPKIGLWSVLKSMVGQDLTKLTLPVSFNEPTSLLQRVSEDIEYSHILDQAATFEDSSLRMLYVAAFTASMYASTTNRVSKPFNPLLGETFEYARTDGQYRFFTEQVSHHPPISATWTESPKWDFYGECNVDSSFNGRTFAVQHLGLWYITIRPDHNISVPEETYSWKKPNNTVIGILMGKPQVDNSGDVKVTNHTTGDYCMLHYKAHGWTSAGAYEVRGEVFNKDDKKLWVLGGHWNDSIYGKKVTARGGELTLDRIKTANSATGGPKLDGSKFLIWKANERPSVPFNLTSFALTLNALPPHLIPYLAPTDSRLRPDQRAMENGEYDKAAAEKHRVEVKQRAAKKEREQKGEEYRPKWFVQEEHPVTKSLYWKFNGEYWNKRKNHDFKDCADIF
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-MEQPDLSSVAISKP
-CCCCCHHHHHCCHH		30.1019795423
8PhosphorylationMEQPDLSSVAISKPL
CCCCCHHHHHCCHHH		23.9019795423
12PhosphorylationDLSSVAISKPLLKLK
CHHHHHCCHHHHHHH		20.6219823750
19AcetylationSKPLLKLKLLDALRQ
CHHHHHHHHHHHHHC		45.4724489116
245PhosphorylationRKVNENDTATNTKIA
EECCCCCCCCCCEEE		47.1424909858
247PhosphorylationVNENDTATNTKIAID
CCCCCCCCCCEEEEE		45.5824909858
249PhosphorylationENDTATNTKIAIDIE
CCCCCCCCEEEEEHH		21.3324909858
269PhosphorylationERATREQSVIDVTNN
HHHHHHCCEEECCCC		19.1128889911
299AcetylationTNFAQGYKLRWFILS
CCCCCCCEEEEEEEC		38.1024489116
393PhosphorylationILLHNGPYSPSLALS
EEEECCCCCHHHHHH		34.3128889911
394PhosphorylationLLHNGPYSPSLALSH
EEECCCCCHHHHHHC		15.9017330950
396PhosphorylationHNGPYSPSLALSHGL
ECCCCCHHHHHHCCC		21.9720377248
400PhosphorylationYSPSLALSHGLSSKV
CCHHHHHHCCCCCCC		15.2021440633
404PhosphorylationLALSHGLSSKVSNKE
HHHHCCCCCCCCCCC		32.4824961812
405PhosphorylationALSHGLSSKVSNKEN
HHHCCCCCCCCCCCH		41.9624961812
408PhosphorylationHGLSSKVSNKENLHA
CCCCCCCCCCCHHHH		46.0121440633
423PhosphorylationTSKRLTKSPHLSKST
HHHHHHCCCCCCCCC		16.5929136822
429PhosphorylationKSPHLSKSTLTQNDH
CCCCCCCCCCCCCCC		25.8519795423
430PhosphorylationSPHLSKSTLTQNDHD
CCCCCCCCCCCCCCC		37.2529136822
432PhosphorylationHLSKSTLTQNDHDND
CCCCCCCCCCCCCCC		25.9729136822
442PhosphorylationDHDNDDDSTNNNNNK
CCCCCCCCCCCCCCC		39.7825521595
443PhosphorylationHDNDDDSTNNNNNKS
CCCCCCCCCCCCCCC		49.3022369663
450PhosphorylationTNNNNNKSNNDYDDN
CCCCCCCCCCCCCCC		42.8822369663
454PhosphorylationNNKSNNDYDDNNNNN
CCCCCCCCCCCCCCC		27.5922369663
468PhosphorylationNNNDDDDYDDDDESR
CCCCCCCCCCCCCCC		28.4122369663
474PhosphorylationDYDDDDESRPLIEPL
CCCCCCCCCCCCCCC		46.3122369663
485PhosphorylationIEPLPLISSRSQSLS
CCCCCCCCCCCCCHH		27.6422369663
486PhosphorylationEPLPLISSRSQSLSE
CCCCCCCCCCCCHHH		29.0223749301
488PhosphorylationLPLISSRSQSLSEIT
CCCCCCCCCCHHHCC		26.5222369663
490PhosphorylationLISSRSQSLSEITPG
CCCCCCCCHHHCCCC		34.8022369663
492PhosphorylationSSRSQSLSEITPGPH
CCCCCCHHHCCCCCC		32.0022890988
495PhosphorylationSQSLSEITPGPHSRK
CCCHHHCCCCCCCCC		20.3822890988
500PhosphorylationEITPGPHSRKSTVSS
HCCCCCCCCCCCCCC		44.5322369663
503PhosphorylationPGPHSRKSTVSSTRA
CCCCCCCCCCCCCCC		32.6928889911
508PhosphorylationRKSTVSSTRAADIPS
CCCCCCCCCCCCCCC		19.4725752575
564PhosphorylationKLHMLQRSISIELAS
HHHHHHHHHHHHHHH		14.0224961812
566PhosphorylationHMLQRSISIELASLN
HHHHHHHHHHHHHHH		15.9728889911
672PhosphorylationNNQPQVETEANEESD
CCCCCCCHHHCCCCC		41.3522369663
678PhosphorylationETEANEESDDANSMI
CHHHCCCCCCHHHHH		34.3122369663
683PhosphorylationEESDDANSMIKGSQE
CCCCCHHHHHCCCHH		24.4922369663
688PhosphorylationANSMIKGSQESTNTL
HHHHHCCCHHHCCHH		26.2722890988
691PhosphorylationMIKGSQESTNTLEEI
HHCCCHHHCCHHHHH		21.2222369663
692PhosphorylationIKGSQESTNTLEEIV
HCCCHHHCCHHHHHH		31.3222369663
694PhosphorylationGSQESTNTLEEIVKF
CCHHHCCHHHHHHHH		35.3222369663
705PhosphorylationIVKFIEATKESDEDS
HHHHHHHHCCCCCCC		23.6628152593
708PhosphorylationFIEATKESDEDSDAD
HHHHHCCCCCCCCHH		48.1022369663
712PhosphorylationTKESDEDSDADEFFD
HCCCCCCCCHHHHCC		32.4322369663
725PhosphorylationFDAEEAASDKKANDS
CCHHHHHHCCCCCCC		57.9419823750
732PhosphorylationSDKKANDSEDLTTNK
HCCCCCCCCCCCCCC		32.5828889911
741PhosphorylationDLTTNKETPANAKPQ
CCCCCCCCCCCCCCC		29.3429734811
756PhosphorylationEEAPEDESLIVISSP
CCCCCCCCEEEECCC		35.4024961812
761PhosphorylationDESLIVISSPQVEKK
CCCEEEECCCCHHHH		25.6824961812
762PhosphorylationESLIVISSPQVEKKN
CCEEEECCCCHHHHH		14.2923749301
773AcetylationEKKNQLLKEGSFVGY
HHHHHHHHCCCCCCC		69.4924489116
776PhosphorylationNQLLKEGSFVGYEDP
HHHHHCCCCCCCCCC		20.1828889911
825PhosphorylationPVSFNEPTSLLQRVS
CCCCCCCCHHHHHHH		26.3123749301
826PhosphorylationVSFNEPTSLLQRVSE
CCCCCCCHHHHHHHC		37.4923749301
966PhosphorylationSWKKPNNTVIGILMG
CCCCCCCEEEEEEEC		21.8219795423
1047PhosphorylationTARGGELTLDRIKTA
EECCCEEEHHHHHCC		23.4722369663
1053PhosphorylationLTLDRIKTANSATGG
EEHHHHHCCCCCCCC		28.8022369663
1056PhosphorylationDRIKTANSATGGPKL
HHHHCCCCCCCCCCC		25.4122369663
1058PhosphorylationIKTANSATGGPKLDG
HHCCCCCCCCCCCCC		42.3622369663
1067AcetylationGPKLDGSKFLIWKAN
CCCCCCCEEEEEECC		50.1224489116
1120PhosphorylationRAMENGEYDKAAAEK
HHHHCCCCCHHHHHH		24.9228132839
1172PhosphorylationYWKFNGEYWNKRKNH
EEEECCCCCCCCCCC		18.7119779198
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 OSH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSH1_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 OSH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AFG2_YEASTAFG2physical
11805826
G3P3_YEASTTDH3physical
11805826
NVJ1_YEASTNVJ1physical
15367582
OSH1_YEASTSWH1physical
16554755
EIF3A_YEASTRPG1physical
16554755
NAT1_YEASTNAT1physical
16554755
POB3_YEASTPOB3physical
16554755
EIF3B_YEASTPRT1physical
16554755
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RS7A_YEASTRPS7Aphysical
16429126
SER33_YEASTSER33physical
16429126
ERF1_YEASTSUP45physical
16429126
GOSR1_YEASTGOS1genetic
16269340
SAC1_YEASTSAC1genetic
16269340
ATC3_YEASTDRS2genetic
16269340
ACO1_YEASTOLE1genetic
16269340
SEC65_YEASTSEC65genetic
16269340
ERG2_YEASTERG2genetic
16269340
PGA3_YEASTPGA3genetic
16269340
OSTD_YEASTSWP1genetic
16269340
LCB2_YEASTLCB2genetic
16269340
AGE2_YEASTAGE2genetic
16269340
CWH43_YEASTCWH43genetic
16269340
RGP1_YEASTRGP1genetic
16269340
TVP15_YEASTTVP15physical
18467557
VAC8_YEASTVAC8physical
18467557
OSH1_YEASTSWH1physical
18467557
OSH2_YEASTOSH2genetic
11238399
KES1_YEASTKES1genetic
21819498
SSB1_YEASTSSB1physical
22940862
GOSR1_YEASTGOS1genetic
23891562
ERG3_YEASTERG3genetic
23891562
YPT31_YEASTYPT31genetic
23891562
AGE2_YEASTAGE2genetic
23891562
CSG2_YEASTCSG2genetic
23891562
SCS2_YEASTSCS2physical
24366873
SLX5_YEASTSLX5genetic
27708008
UBX6_YEASTUBX6genetic
27708008
YCY0_YEASTYCR090Cgenetic
27708008
MTU1_YEASTSLM3genetic
27708008
GPR1_YEASTGPR1genetic
27708008
RS16A_YEASTRPS16Bgenetic
27708008
RS16B_YEASTRPS16Bgenetic
27708008
YD061_YEASTYDR061Wgenetic
27708008
AIM7_YEASTAIM7genetic
27708008
VPS41_YEASTVPS41genetic
27708008
RPA14_YEASTRPA14genetic
27708008
SWA2_YEASTSWA2genetic
27708008
RAD4_YEASTRAD4genetic
27708008
UBP6_YEASTUBP6genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
THI4_YEASTTHI4genetic
27708008
MAL12_YEASTMAL12genetic
27708008
AIM17_YEASTAIM17genetic
27708008
GOSR1_YEASTGOS1genetic
27708008
SMF2_YEASTSMF2genetic
27708008
AGE2_YEASTAGE2genetic
27708008
YIF5_YEASTYIL055Cgenetic
27708008
GPI7_YEASTLAS21genetic
27708008
GSH1_YEASTGSH1genetic
27708008
MOG1_YEASTMOG1genetic
27708008
SAC1_YEASTSAC1genetic
27708008
DNM1_YEASTDNM1genetic
27708008
FRA1_YEASTFRA1genetic
27708008
ERG3_YEASTERG3genetic
27708008
COQ11_YEASTYLR290Cgenetic
27708008
VPS9_YEASTVPS9genetic
27708008
FMS1_YEASTFMS1genetic
27708008
RAD14_YEASTRAD14genetic
27708008
DIA1_YEASTDIA1genetic
27708008
HDA1_YEASTHDA1genetic
27708008
FAR11_YEASTFAR11genetic
27708008
LSM7_YEASTLSM7genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
MSO1_YEASTMSO1genetic
27708008
RLA2_YEASTRPP2Agenetic
27708008
INO4_YEASTINO4genetic
27708008
HIR2_YEASTHIR2genetic
27708008
PUS7_YEASTPUS7genetic
27708008
MTHR1_YEASTMET12genetic
27708008
AIM44_YEASTAIM44genetic
27708008
YPR71_YEASTYPR071Wgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OSH1_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-442; SER-490; SER-492;SER-500; SER-678; SER-683; SER-691; THR-692; THR-694; SER-708;SER-712; SER-762; THR-1053 AND SER-1056, 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-442; SER-488; SER-490;SER-678; SER-712; THR-1053 AND SER-1056, AND MASS SPECTROMETRY.
"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-396, 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-394; SER-490; SER-678;SER-708 AND SER-712, AND MASS SPECTROMETRY.
"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-490, AND MASSSPECTROMETRY.

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