OSBP1_HUMAN - dbPTM
OSBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSBP1_HUMAN
UniProt AC P22059
Protein Name Oxysterol-binding protein 1 {ECO:0000305}
Gene Name OSBP {ECO:0000312|HGNC:HGNC:8503}
Organism Homo sapiens (Human).
Sequence Length 807
Subcellular Localization Cytoplasm, cytosol . Cytoplasm, perinuclear region . Golgi apparatus membrane
Peripheral membrane protein . Endoplasmic reticulum membrane
Peripheral membrane protein . Predominantly cytosolic.
Protein Description Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. [PubMed: 24209621 Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol]
Protein Sequence MAATELRGVVGPGPAAIAALGGGGAGPPVVGGGGGRGDAGPGSGAASGTVVAAAAGGPGPGAGGVAAAGPAPAPPTGGSGGSGAGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYHLKASSEVERQRWVTALELAKAKAVKMLAESDESGDEESVSQTDKTELQNTLRTLSSKVEDLSTCNDLIAKHGTALQRSLSELESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLMLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHLERAFRGATVLPANTPGNVGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLGHKRTGSNISGASSDISLDEQYKHQLEETKKEKRTRIPYKPNYSLNLWSIMKNCIGKELSKIPMPVNFNEPLSMLQRLTEDLEYHELLDRAAKCENSLEQLCYVAAFTVSSYSTTVFRTSKPFNPLLGETFELDRLEENGYRSLCEQVSHHPPAAAHHAESKNGWTLRQEIKITSKFRGKYLSIMPLGTIHCIFHATGHHYTWKKVTTTVHNIIVGKLWIDQSGEIDIVNHKTGDKCNLKFVPYSYFSRDVARKVTGEVTDPSGKVHFALLGTWDEKMECFKVQPVIGENGGDARQRGHEAEESRVMLWKRNPLPKNAENMYYFSELALTLNAWESGTAPTDSRLRPDQRLMENGRWDEANAEKQRLEEKQRLSRKKREAEAMKATEDGTPYDPYKALWFERKKDPVTKELTHIYRGEYWECKEKQDWSSCPDIF
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
2Acetylation------MAATELRGV
------CCCCCCCCC		24.0825944712
4Phosphorylation----MAATELRGVVG
----CCCCCCCCCCC		26.4720068231
7Methylation-MAATELRGVVGPGP
-CCCCCCCCCCCCCH		29.63115486053
43PhosphorylationRGDAGPGSGAASGTV
CCCCCCCCCCCCCEE		28.5222210691
79PhosphorylationPAPPTGGSGGSGAGG
CCCCCCCCCCCCCCC		41.1325627689
82PhosphorylationPTGGSGGSGAGGSGS
CCCCCCCCCCCCCCC		29.0622210691
97UbiquitinationAREGWLFKWTNYIKG
CCCCEEEEEECCCCC		51.4429967540
99PhosphorylationEGWLFKWTNYIKGYQ
CCEEEEEECCCCCCC		20.8027174698
101PhosphorylationWLFKWTNYIKGYQRR
EEEEEECCCCCCCCE		9.1627174698
103AcetylationFKWTNYIKGYQRRWF
EEEECCCCCCCCEEE		41.0019608861
105PhosphorylationWTNYIKGYQRRWFVL
EECCCCCCCCEEEEE		8.2124719451
113PhosphorylationQRRWFVLSNGLLSYY
CCEEEEEHHHHHHHH		24.4527174698
118PhosphorylationVLSNGLLSYYRSKAE
EEHHHHHHHHHCHHH		25.7627174698
119PhosphorylationLSNGLLSYYRSKAEM
EHHHHHHHHHCHHHH		11.6727174698
120PhosphorylationSNGLLSYYRSKAEMR
HHHHHHHHHCHHHHH		12.6827174698
129PhosphorylationSKAEMRHTCRGTINL
CHHHHHHHHCCEEEE		8.11-
174PhosphorylationVERQRWVTALELAKA
HHHHHHHHHHHHHHH		20.6821406692
190PhosphorylationAVKMLAESDESGDEE
HHHHHHHCCCCCCHH		40.8629255136
193PhosphorylationMLAESDESGDEESVS
HHHHCCCCCCHHHCC		57.4429255136
198PhosphorylationDESGDEESVSQTDKT
CCCCCHHHCCCCCHH		25.6422167270
200PhosphorylationSGDEESVSQTDKTEL
CCCHHHCCCCCHHHH		36.3230266825
202PhosphorylationDEESVSQTDKTELQN
CHHHCCCCCHHHHHH		31.7730266825
205PhosphorylationSVSQTDKTELQNTLR
HCCCCCHHHHHHHHH		44.7530266825
210PhosphorylationDKTELQNTLRTLSSK
CHHHHHHHHHHHHHH		12.4923927012
213PhosphorylationELQNTLRTLSSKVED
HHHHHHHHHHHHCCC		33.82-
215PhosphorylationQNTLRTLSSKVEDLS
HHHHHHHHHHCCCHH		27.7423898821
216PhosphorylationNTLRTLSSKVEDLST
HHHHHHHHHCCCHHH		43.7827251275
217UbiquitinationTLRTLSSKVEDLSTC
HHHHHHHHCCCHHHH		46.3929967540
222PhosphorylationSSKVEDLSTCNDLIA
HHHCCCHHHHHHHHH		43.1427251275
223PhosphorylationSKVEDLSTCNDLIAK
HHCCCHHHHHHHHHH		23.7227251275
230UbiquitinationTCNDLIAKHGTALQR
HHHHHHHHHHHHHHH		35.2632015554
230AcetylationTCNDLIAKHGTALQR
HHHHHHHHHHHHHHH		35.2625953088
230MalonylationTCNDLIAKHGTALQR
HHHHHHHHHHHHHHH		35.2626320211
233PhosphorylationDLIAKHGTALQRSLS
HHHHHHHHHHHHHHH		24.7429514088
238PhosphorylationHGTALQRSLSELESL
HHHHHHHHHHHHHHC		24.2429255136
240PhosphorylationTALQRSLSELESLKL
HHHHHHHHHHHHCCC		41.1919664994
244PhosphorylationRSLSELESLKLPAES
HHHHHHHHCCCCCCC		43.3530266825
246UbiquitinationLSELESLKLPAESNE
HHHHHHCCCCCCCCH		62.8029901268
251PhosphorylationSLKLPAESNEKIKQV
HCCCCCCCCHHHHHH		53.0123927012
269PhosphorylationATLFRITSNAMINAC
HHHHHHHHHHHHHHH		21.8823917254
285PhosphorylationDFLMLAQTHSKKWQK
HHHHHHHHCCHHHHH		23.6228348404
287PhosphorylationLMLAQTHSKKWQKSL
HHHHHHCCHHHHHHH		39.0428857561
292UbiquitinationTHSKKWQKSLQYERD
HCCHHHHHHHHHHHH		52.6029967540
296PhosphorylationKWQKSLQYERDQRIR
HHHHHHHHHHHHHHC		20.44-
313MalonylationETLEQLAKQHNHLER
HHHHHHHHHCCHHHH		61.7626320211
323MethylationNHLERAFRGATVLPA
CHHHHHHCCCEEECC		32.62115486063
326PhosphorylationERAFRGATVLPANTP
HHHHCCCEEECCCCC		25.9628464451
332PhosphorylationATVLPANTPGNVGSG
CEEECCCCCCCCCCC		34.3829255136
338PhosphorylationNTPGNVGSGKDQCCS
CCCCCCCCCCCCCCC		38.0823401153
340AcetylationPGNVGSGKDQCCSGK
CCCCCCCCCCCCCCC		46.4526051181
340UbiquitinationPGNVGSGKDQCCSGK
CCCCCCCCCCCCCCC		46.4529967540
345PhosphorylationSGKDQCCSGKGDMSD
CCCCCCCCCCCCCCC		51.6823927012
351PhosphorylationCSGKGDMSDEDDENE
CCCCCCCCCCCCCCC		42.4619664994
367PhosphorylationFDAPEIITMPENLGH
CCCCCEEECCHHHCC		32.1323927012
377PhosphorylationENLGHKRTGSNISGA
HHHCCCCCCCCCCCC		50.1722167270
379PhosphorylationLGHKRTGSNISGASS
HCCCCCCCCCCCCCC		30.3122167270
382PhosphorylationKRTGSNISGASSDIS
CCCCCCCCCCCCCCC		32.3422167270
385PhosphorylationGSNISGASSDISLDE
CCCCCCCCCCCCCCH		31.8822167270
386PhosphorylationSNISGASSDISLDEQ
CCCCCCCCCCCCCHH		38.1323927012
389PhosphorylationSGASSDISLDEQYKH
CCCCCCCCCCHHHHH		34.4623927012
394PhosphorylationDISLDEQYKHQLEET
CCCCCHHHHHHHHHH		14.3723927012
395UbiquitinationISLDEQYKHQLEETK
CCCCHHHHHHHHHHH		25.2729967540
401PhosphorylationYKHQLEETKKEKRTR
HHHHHHHHHHHHCCC		37.7325219547
4022-HydroxyisobutyrylationKHQLEETKKEKRTRI
HHHHHHHHHHHCCCC		63.31-
424UbiquitinationLNLWSIMKNCIGKEL
CHHHHHHHHHHCHHH		47.1723000965
429UbiquitinationIMKNCIGKELSKIPM
HHHHHHCHHHHCCCC		35.2523000965
429AcetylationIMKNCIGKELSKIPM
HHHHHHCHHHHCCCC		35.2526051181
433 (in isoform 1)Ubiquitination-64.5521906983
433UbiquitinationCIGKELSKIPMPVNF
HHCHHHHCCCCCCCC		64.5523000965
436SulfoxidationKELSKIPMPVNFNEP
HHHHCCCCCCCCCCC		7.0628465586
456PhosphorylationRLTEDLEYHELLDRA
HHHHHHHHHHHHHHH		14.11-
462MethylationEYHELLDRAAKCENS
HHHHHHHHHHHCCCH		36.09115486073
469PhosphorylationRAAKCENSLEQLCYV
HHHHCCCHHHHHHHH		15.81-
493UbiquitinationTTVFRTSKPFNPLLG
EEEEECCCCCCCCCC		53.6822817900
493 (in isoform 1)Ubiquitination-53.6821906983
544UbiquitinationWTLRQEIKITSKFRG
EEEEEEEEEEECCCC		38.9033845483
544AcetylationWTLRQEIKITSKFRG
EEEEEEEEEEECCCC		38.9025953088
547PhosphorylationRQEIKITSKFRGKYL
EEEEEEEECCCCEEE		33.0228634120
553PhosphorylationTSKFRGKYLSIMPLG
EECCCCEEEEEEECC		14.43-
573PhosphorylationFHATGHHYTWKKVTT
EECCCCCCCCEEEEC		14.50-
577AcetylationGHHYTWKKVTTTVHN
CCCCCCEEEECEEEH		36.0525953088
604UbiquitinationEIDIVNHKTGDKCNL
CEEEECCCCCCCCCE		49.3429967540
628PhosphorylationRDVARKVTGEVTDPS
HHHHHHHCCEEECCC		30.5721406692
632PhosphorylationRKVTGEVTDPSGKVH
HHHCCEEECCCCCEE		37.5821406692
635PhosphorylationTGEVTDPSGKVHFAL
CCEEECCCCCEEEEE		54.8021406692
645PhosphorylationVHFALLGTWDEKMEC
EEEEEEECCCCCCCE		29.70-
758PhosphorylationEAEAMKATEDGTPYD
HHHHHHHCCCCCCCC		29.14-
762PhosphorylationMKATEDGTPYDPYKA
HHHCCCCCCCCHHHH		30.8828152594
764PhosphorylationATEDGTPYDPYKALW
HCCCCCCCCHHHHHH		29.4128152594
767PhosphorylationDGTPYDPYKALWFER
CCCCCCHHHHHHEEE		13.1428152594
768UbiquitinationGTPYDPYKALWFERK
CCCCCHHHHHHEEEC		42.2529967540
780PhosphorylationERKKDPVTKELTHIY
EECCCCCCHHCCEEC		24.9624719451
787PhosphorylationTKELTHIYRGEYWEC
CHHCCEECCCCCCCC		12.6424719451
801PhosphorylationCKEKQDWSSCPDIF-
CCCCCCHHHCCCCC-		30.2824719451
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
240SPhosphorylationKinasePRKD1Q15139
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSBP1_HUMAN !!
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 OSBP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAPA_HUMANVAPAphysical
12023275
CAND1_HUMANCAND1physical
22863883
COR1B_HUMANCORO1Bphysical
22863883
CTNA1_HUMANCTNNA1physical
22863883
IF4B_HUMANEIF4Bphysical
22863883
GARS_HUMANGARSphysical
22863883
GFPT1_HUMANGFPT1physical
22863883
KCD12_HUMANKCTD12physical
22863883
NP1L1_HUMANNAP1L1physical
22863883
SYNC_HUMANNARSphysical
22863883
NPM_HUMANNPM1physical
22863883
PARVA_HUMANPARVAphysical
22863883
ANM3_HUMANPRMT3physical
22863883
SAMH1_HUMANSAMHD1physical
22863883
SC23A_HUMANSEC23Aphysical
22863883
SF01_HUMANSF1physical
22863883
SWP70_HUMANSWAP70physical
22863883
TBC17_HUMANTBC1D17physical
22863883
TTC1_HUMANTTC1physical
22863883
UBP11_HUMANUSP11physical
22863883
XPO7_HUMANXPO7physical
22863883
ZRAB2_HUMANZRANB2physical
22863883
LIPA1_HUMANPPFIA1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OSBP1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351AND SER-382, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351;THR-377; SER-379; SER-382; SER-385; SER-386 AND SER-389, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 ANDSER-351, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-198;SER-351; SER-379; SER-382 AND SER-385, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351;SER-379; SER-382; SER-385; SER-386 AND SER-389, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 ANDSER-351, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190 AND SER-193, ANDMASS SPECTROMETRY.

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