OSH2_YEAST - dbPTM
OSH2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSH2_YEAST
UniProt AC Q12451
Protein Name Oxysterol-binding protein homolog 2
Gene Name OSH2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1283
Subcellular Localization Cell membrane
Peripheral membrane protein . Cell periphery, enriched in small buds of G1 phase cells and near the bud-neck region of S phase cells.
Protein Description Lipid-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides..
Protein Sequence MSREDLSIAEDLNQVSKPLLKVKLLEVLGQGDFKHLKALVDNEFQPKDDPSVQQVLNLILHYAVQVAPILLIKEIVAHWVDQVGDEKSSSKSDDGIHLDLNYQDENGNTPLHLAAAQSRSDVISFLLSQKSINDCVKNKAHQQPLDMCKDLNVAQMIQLKRDDYFLETVHSLRAAMNKRDFSKLDSIWKNPRNLNLLDINGIDPETGTTLLYEYSQKKDIEMCQWLLKHGAEATVKDGKGRSPLDLVKNIKLPAKPSNNVTPEIKLKNLLEKNLREQAIVHEDVASSKPPTYKGFLKKWTNFAHGYKLRWFILSGDGNLSYYKDQSHVDRPRGTLKVSTCRLHIDSSEKLNFELLGGITGTTRWRLKGNHPIETTRWVNAIQSAIRFAKDKEILNKKKAVPPSLALKNKSPALISHSKTQGSLPEASQYYQHTLHKEVIQPSSVSLYRRPSNNLSVVSSEIQLNDNLTESGKRFVSKMIENRLDGSKTPVGVHTGSALQRVRSSNTLKSNRSMQSGSGVASPIDKVPNGANLSQSNTTTGSTASLSDNNYIDNFEGDEANSDDEEEDLGINFDRDEEYIKAQYGPYKEKLDMYEQAISIELSSLIELIEQEEPSPEVWLTIKKSLINTSTIFGKLKDLTYKRDKRLVDMVSKQGDVNNVWVQSVKELEMELSNKTERLASIDKERRGLKKILHKKLLESHATAGNKESLENDKEQESDTTASTLGQIAKFISATKEEDEASDADEFYDAAELVDEVTELTEAHPEISTAAAPKHAPPPVPNETDNDSQYVQDEKSKIESNVEKTSQKFEKQNNLVTEDEPKTDQSLKNFKAEDKESQVKEKTKEIASSVIGEKTIVAVTTVQKRKEEYLLKEGSYLGYEDGIRKRLSMDKDDRPKISLWAVLKSMVGKDMTRMTLPVTFNEPTSLLQRVAEDLEYSELLDQAATFEDSTLRTLYVAAFTASSYASTTKRVAKPFNPLLGETFEYSRPDKQYRFFTEQVSHHPPISATWTESPRWDFWGESFVDTKFNGRSFNVKHLGLWHIKLRPNDNEKEELYTWKKPNNTVIGILIGNPQVDNHGEVNVVNHTTGDHCKLYFKARGWRSSGAYEITGEVYNKKKQKVWILGGHWNEAIFAKKVVKDGDLSLEKTRTAASAGNGPTDDGTKFLIWKANDRPEEPFNLTPFAITLNAPQPHLLPWLPPTDTRLRPDQRAMEDGRYDEAGDEKFRVEEKQRAARRKREENNLEYHPQWFVRDTHPITKAKYWRYTGKYWVKRRDHDLKDCGDIF
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
2Phosphorylation------MSREDLSIA
------CCHHHHHHH
56.5322369663
2Acetylation------MSREDLSIA
------CCHHHHHHH
56.5315665377
7Phosphorylation-MSREDLSIAEDLNQ
-CCHHHHHHHHHHHH
31.8822369663
16PhosphorylationAEDLNQVSKPLLKVK
HHHHHHCCHHHHHHH
20.8422369663
34AcetylationVLGQGDFKHLKALVD
HHCCCCHHHHHHHHC
53.4124489116
89PhosphorylationQVGDEKSSSKSDDGI
HHCCCCCCCCCCCCE
53.5019779198
90PhosphorylationVGDEKSSSKSDDGIH
HCCCCCCCCCCCCEE
43.1819779198
92PhosphorylationDEKSSSKSDDGIHLD
CCCCCCCCCCCEEEE
42.7728889911
183AcetylationMNKRDFSKLDSIWKN
HHHCCHHHHHHHHCC
57.2024489116
248AcetylationRSPLDLVKNIKLPAK
CCHHHHHHHCCCCCC
61.3224489116
255UbiquitinationKNIKLPAKPSNNVTP
HHCCCCCCCCCCCCH
47.2223749301
272AcetylationKLKNLLEKNLREQAI
HHHHHHHHHHHHHHC
62.3424489116
307AcetylationTNFAHGYKLRWFILS
CCCCCCCEEEEEEEC
35.8524489116
323AcetylationDGNLSYYKDQSHVDR
CCCCCEECCCCCCCC
40.8524489116
407AcetylationVPPSLALKNKSPALI
CCHHHHHCCCCCHHH
57.6425381059
409AcetylationPSLALKNKSPALISH
HHHHHCCCCCHHHCC
57.1225381059
410PhosphorylationSLALKNKSPALISHS
HHHHCCCCCHHHCCC
25.4629136822
415PhosphorylationNKSPALISHSKTQGS
CCCCHHHCCCCCCCC
23.6619779198
417PhosphorylationSPALISHSKTQGSLP
CCHHHCCCCCCCCCC
30.5219779198
419PhosphorylationALISHSKTQGSLPEA
HHHCCCCCCCCCCHH
40.9729136822
422PhosphorylationSHSKTQGSLPEASQY
CCCCCCCCCCHHHHH
30.8217330950
427PhosphorylationQGSLPEASQYYQHTL
CCCCCHHHHHHHHHC
19.6329136822
429PhosphorylationSLPEASQYYQHTLHK
CCCHHHHHHHHHCCC
11.5519779198
433PhosphorylationASQYYQHTLHKEVIQ
HHHHHHHHCCCCEEC
18.2919779198
442PhosphorylationHKEVIQPSSVSLYRR
CCCEECCCCCEEEEC
27.3122890988
443PhosphorylationKEVIQPSSVSLYRRP
CCEECCCCCEEEECC
23.5522890988
445PhosphorylationVIQPSSVSLYRRPSN
EECCCCCEEEECCCC
22.9525521595
447PhosphorylationQPSSVSLYRRPSNNL
CCCCCEEEECCCCCE
9.3222890988
451PhosphorylationVSLYRRPSNNLSVVS
CEEEECCCCCEEEEE
36.2222369663
455PhosphorylationRRPSNNLSVVSSEIQ
ECCCCCEEEEEEEEE
23.6925521595
458PhosphorylationSNNLSVVSSEIQLND
CCCEEEEEEEEECCC
21.7925521595
459PhosphorylationNNLSVVSSEIQLNDN
CCEEEEEEEEECCCC
27.4020377248
470PhosphorylationLNDNLTESGKRFVSK
CCCCCCHHHHHHHHH
44.3619779198
477AcetylationSGKRFVSKMIENRLD
HHHHHHHHHHHHCCC
38.3025381059
486PhosphorylationIENRLDGSKTPVGVH
HHHCCCCCCCCCCCC
32.7822369663
488PhosphorylationNRLDGSKTPVGVHTG
HCCCCCCCCCCCCCC
25.5522369663
494PhosphorylationKTPVGVHTGSALQRV
CCCCCCCCCHHHHHH
30.3522369663
496PhosphorylationPVGVHTGSALQRVRS
CCCCCCCHHHHHHHC
27.2822369663
503PhosphorylationSALQRVRSSNTLKSN
HHHHHHHCCCCCCCC
25.6919823750
504PhosphorylationALQRVRSSNTLKSNR
HHHHHHCCCCCCCCC
24.2220377248
506PhosphorylationQRVRSSNTLKSNRSM
HHHHCCCCCCCCCCC
37.1920377248
509PhosphorylationRSSNTLKSNRSMQSG
HCCCCCCCCCCCCCC
40.3622369663
512PhosphorylationNTLKSNRSMQSGSGV
CCCCCCCCCCCCCCC
25.9822369663
515PhosphorylationKSNRSMQSGSGVASP
CCCCCCCCCCCCCCC
26.7022369663
517PhosphorylationNRSMQSGSGVASPID
CCCCCCCCCCCCCCC
35.0322369663
521PhosphorylationQSGSGVASPIDKVPN
CCCCCCCCCCCCCCC
21.7120377248
587UbiquitinationKAQYGPYKEKLDMYE
HHHHCCHHHHHHHHH
52.0523749301
634AcetylationNTSTIFGKLKDLTYK
CCHHHHHHHHHCCCC
41.4324489116
652UbiquitinationRLVDMVSKQGDVNNV
HHHHHHHCCCCCCCE
47.0623749301
663PhosphorylationVNNVWVQSVKELEME
CCCEEHHHHHHHHHH
26.0721551504
699PhosphorylationLHKKLLESHATAGNK
HHHHHHHHHCCCCCH
20.5621440633
702PhosphorylationKLLESHATAGNKESL
HHHHHHCCCCCHHHH
29.6721440633
708PhosphorylationATAGNKESLENDKEQ
CCCCCHHHHHCCCHH
42.4620377248
717PhosphorylationENDKEQESDTTASTL
HCCCHHCCCCHHHHH
39.6922369663
719PhosphorylationDKEQESDTTASTLGQ
CCHHCCCCHHHHHHH
33.2820377248
720PhosphorylationKEQESDTTASTLGQI
CHHCCCCHHHHHHHH
24.4922369663
722PhosphorylationQESDTTASTLGQIAK
HCCCCHHHHHHHHHH
23.2825521595
723PhosphorylationESDTTASTLGQIAKF
CCCCHHHHHHHHHHH
32.2325521595
732PhosphorylationGQIAKFISATKEEDE
HHHHHHHHCCCCCCC
32.7723749301
734PhosphorylationIAKFISATKEEDEAS
HHHHHHCCCCCCCCC
32.0021551504
741PhosphorylationTKEEDEASDADEFYD
CCCCCCCCCHHHHHH
31.1422369663
747PhosphorylationASDADEFYDAAELVD
CCCHHHHHHHHHHHH
11.5622369663
757PhosphorylationAELVDEVTELTEAHP
HHHHHHHHHHHHHCC
24.1922369663
760PhosphorylationVDEVTELTEAHPEIS
HHHHHHHHHHCCCCC
25.5422369663
767PhosphorylationTEAHPEISTAAAPKH
HHHCCCCCCCCCCCC
15.4422369663
768PhosphorylationEAHPEISTAAAPKHA
HHCCCCCCCCCCCCC
26.4422369663
783PhosphorylationPPPVPNETDNDSQYV
CCCCCCCCCCCCHHC
46.9021551504
787PhosphorylationPNETDNDSQYVQDEK
CCCCCCCCHHCHHHH
29.6622369663
789PhosphorylationETDNDSQYVQDEKSK
CCCCCCHHCHHHHHH
12.2022369663
795PhosphorylationQYVQDEKSKIESNVE
HHCHHHHHHHHHHHH
36.5021440633
799PhosphorylationDEKSKIESNVEKTSQ
HHHHHHHHHHHHHHH
50.0426447709
804PhosphorylationIESNVEKTSQKFEKQ
HHHHHHHHHHHHHHH
23.9221440633
805PhosphorylationESNVEKTSQKFEKQN
HHHHHHHHHHHHHHC
42.3020377248
816PhosphorylationEKQNNLVTEDEPKTD
HHHCCCCCCCCCCCH
40.6722369663
821UbiquitinationLVTEDEPKTDQSLKN
CCCCCCCCCHHHHHC
63.7923749301
822PhosphorylationVTEDEPKTDQSLKNF
CCCCCCCCHHHHHCC
50.4122369663
825PhosphorylationDEPKTDQSLKNFKAE
CCCCCHHHHHCCCCC
44.0922369663
827UbiquitinationPKTDQSLKNFKAEDK
CCCHHHHHCCCCCCH
66.6323749301
834UbiquitinationKNFKAEDKESQVKEK
HCCCCCCHHHHHHHH
51.2623749301
836PhosphorylationFKAEDKESQVKEKTK
CCCCCHHHHHHHHHH
46.1228889911
847PhosphorylationEKTKEIASSVIGEKT
HHHHHHHHHHHCCCE
30.6928152593
848PhosphorylationKTKEIASSVIGEKTI
HHHHHHHHHHCCCEE
14.5620377248
952PhosphorylationFEDSTLRTLYVAAFT
CCHHHHHHHHHHHHH
26.0828889911
954PhosphorylationDSTLRTLYVAAFTAS
HHHHHHHHHHHHHHH
6.3428889911
959PhosphorylationTLYVAAFTASSYAST
HHHHHHHHHHHCHHC
22.3928889911
967PhosphorylationASSYASTTKRVAKPF
HHHCHHCCCCCCCCC
17.8528889911
1050AcetylationLRPNDNEKEELYTWK
ECCCCCCCCCCEEEE
63.8424489116
1142PhosphorylationVVKDGDLSLEKTRTA
EEECCCCCCEEEECH
38.9428889911
1146PhosphorylationGDLSLEKTRTAASAG
CCCCCEEEECHHHCC
24.7122369663
1148PhosphorylationLSLEKTRTAASAGNG
CCCEEEECHHHCCCC
31.6325521595
1151PhosphorylationEKTRTAASAGNGPTD
EEEECHHHCCCCCCC
33.9622369663
1157PhosphorylationASAGNGPTDDGTKFL
HHCCCCCCCCCCEEE
48.3922890988
1161PhosphorylationNGPTDDGTKFLIWKA
CCCCCCCCEEEEEEC
26.1422890988

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 OSH2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSH2_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 OSH2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATC3_YEASTDRS2physical
16554755
OSH1_YEASTSWH1physical
16554755
H2A2_YEASTHTA2physical
16554755
EIF3A_YEASTRPG1physical
16554755
YRA1_YEASTYRA1physical
16554755
COPB2_YEASTSEC27physical
16554755
LAA1_YEASTLAA1physical
16554755
SSO2_YEASTSSO2genetic
16269340
TSC3_YEASTTSC3genetic
16269340
PLSC_YEASTSLC1genetic
16269340
PST2_YEASTPST2genetic
16269340
MYO5_YEASTMYO5physical
18467557
UME1_YEASTUME1physical
18467557
HSP71_YEASTSSA1physical
19536198
OSH3_YEASTOSH3genetic
11238399
SYSC_YEASTSES1genetic
20526336
TOR2_YEASTTOR2genetic
20526336
KES1_YEASTKES1genetic
21819498
OSH2_YEASTOSH2physical
22940862
HSP71_YEASTSSA1physical
22940862
SCS2_YEASTSCS2physical
24366873
SCS22_YEASTSCS22physical
24366873
SEC22_YEASTSEC22physical
24705552
SSO1_YEASTSSO1physical
24705552
GPI19_YEASTGPI19genetic
27708008
COG2_YEASTCOG2genetic
27708008
UTP9_YEASTUTP9genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
SEC23_YEASTSEC23genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OSH2_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-422; SER-445; THR-488;SER-515; SER-722; SER-732; SER-787; SER-825; THR-1146; THR-1148 ANDSER-1151, 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-7; THR-783; SER-787;SER-825; THR-1146; THR-1148 AND SER-1151, 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-422 AND SER-503, ANDMASS SPECTROMETRY.

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