OSB11_HUMAN - dbPTM
OSB11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSB11_HUMAN
UniProt AC Q9BXB4
Protein Name Oxysterol-binding protein-related protein 11
Gene Name OSBPL11
Organism Homo sapiens (Human).
Sequence Length 747
Subcellular Localization Late endosome membrane . Golgi apparatus, trans-Golgi network membrane . Localizes at the Golgi-late endosome interface.
Protein Description Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage. [PubMed: 23028956 Weakly binds 25-hydroxycholesterol]
Protein Sequence MQGGEPVSTMKVSESEGKLEGQATAVTPNKNSSCGGGISSSSSSRGGSAKGWQYSDHMENVYGYLMKYTNLVTGWQYRFFVLNNEAGLLEYFVNEQSRNQKPRGTLQLAGAVISPSDEDSHTFTVNAASGEQYKLRATDAKERQHWVSRLQICTQHHTEAIGKNNPPLKSRSFSLASSSNSPISQRRPSQNAISFFNVGHSKLQSLSKRTNLPPDHLVEVREMMSHAEGQQRDLIRRIECLPTSGHLSSLDQDLLMLKATSMATMNCLNDCFHILQLQHASHQKGSLPSGTTIEWLEPKISLSNHYKNGADQPFATDQSKPVAVPEEQPVAESGLLAREPEEINADDEIEDTCDHKEDDLGAVEEQRSVILHLLSQLKLGMDLTRVVLPTFILEKRSLLEMYADFMSHPDLFIAITNGATAEDRMIRFVEYYLTSFHEGRKGAIAKKPYNPIIGETFHCSWKMPKSEVASSVFSSSSTQGVTNHAPLSGESLTQVGSDCYTVRFVAEQVSHHPPVSGFYAECTERKMCVNAHVWTKSKFLGMSIGVTMVGEGILSLLEHGEEYTFSLPCAYARSILTVPWVELGGKVSVNCAKTGYSASITFHTKPFYGGKLHRVTAEVKHNITNTVVCRVQGEWNSVLEFTYSNGETKYVDLTKLAVTKKRVRPLEKQDPFESRRLWKNVTDSLRESEIDKATEHKHTLEERQRTEERHRTETGTPWKTKYFIKEGDGWVYHKPLWKIIPTTQPAE
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
1Acetylation-------MQGGEPVS
-------CCCCCCCC		8.2419413330
8PhosphorylationMQGGEPVSTMKVSES
CCCCCCCCEEEEECC		33.2423403867
9PhosphorylationQGGEPVSTMKVSESE
CCCCCCCEEEEECCC		22.6530576142
13PhosphorylationPVSTMKVSESEGKLE
CCCEEEEECCCCCEE		29.8623401153
15PhosphorylationSTMKVSESEGKLEGQ
CEEEEECCCCCEEEE		44.1123911959
24PhosphorylationGKLEGQATAVTPNKN
CCEEEEEEEECCCCC		17.4821955146
27PhosphorylationEGQATAVTPNKNSSC
EEEEEEECCCCCCCC		20.7629255136
32PhosphorylationAVTPNKNSSCGGGIS
EECCCCCCCCCCCCC		28.7229978859
33PhosphorylationVTPNKNSSCGGGISS
ECCCCCCCCCCCCCC		26.6128857561
39PhosphorylationSSCGGGISSSSSSRG
CCCCCCCCCCCCCCC		27.6929978859
40PhosphorylationSCGGGISSSSSSRGG
CCCCCCCCCCCCCCC		32.1125627689
41PhosphorylationCGGGISSSSSSRGGS
CCCCCCCCCCCCCCC		27.7025262027
42PhosphorylationGGGISSSSSSRGGSA
CCCCCCCCCCCCCCC		33.9921815630
43PhosphorylationGGISSSSSSRGGSAK
CCCCCCCCCCCCCCC		26.4625627689
44PhosphorylationGISSSSSSRGGSAKG
CCCCCCCCCCCCCCC		36.5725262027
48PhosphorylationSSSSRGGSAKGWQYS
CCCCCCCCCCCCCHH		29.6325627689
62PhosphorylationSDHMENVYGYLMKYT
HHHHHHHHHHHHHHH		16.1925147952
170PhosphorylationKNNPPLKSRSFSLAS
CCCCCCCCCCEEECC		40.6222617229
172PhosphorylationNPPLKSRSFSLASSS
CCCCCCCCEEECCCC		26.6923927012
174PhosphorylationPLKSRSFSLASSSNS
CCCCCCEEECCCCCC		25.0325159151
177PhosphorylationSRSFSLASSSNSPIS
CCCEEECCCCCCCCC		39.3222167270
178PhosphorylationRSFSLASSSNSPISQ
CCEEECCCCCCCCCC		28.1222167270
179PhosphorylationSFSLASSSNSPISQR
CEEECCCCCCCCCCC		38.5422167270
181PhosphorylationSLASSSNSPISQRRP
EECCCCCCCCCCCCC		26.0919664994
184PhosphorylationSSSNSPISQRRPSQN
CCCCCCCCCCCCCCC		22.4830266825
189PhosphorylationPISQRRPSQNAISFF
CCCCCCCCCCCEEEE		33.9729255136
194PhosphorylationRPSQNAISFFNVGHS
CCCCCCEEEEECCHH		22.7523927012
201PhosphorylationSFFNVGHSKLQSLSK
EEEECCHHHHHHHHH		29.1823927012
205PhosphorylationVGHSKLQSLSKRTNL
CCHHHHHHHHHHCCC		45.0821815630
207PhosphorylationHSKLQSLSKRTNLPP
HHHHHHHHHHCCCCH		25.9123401153
208UbiquitinationSKLQSLSKRTNLPPD
HHHHHHHHHCCCCHH		69.41-
286PhosphorylationHASHQKGSLPSGTTI
HHHCCCCCCCCCCEE		44.1128355574
289PhosphorylationHQKGSLPSGTTIEWL
CCCCCCCCCCEEEEE		54.8126657352
291PhosphorylationKGSLPSGTTIEWLEP
CCCCCCCCEEEEECC		29.0130576142
292PhosphorylationGSLPSGTTIEWLEPK
CCCCCCCEEEEECCE		22.0322199227
301PhosphorylationEWLEPKISLSNHYKN
EEECCEECCCHHCCC		31.6925159151
303PhosphorylationLEPKISLSNHYKNGA
ECCEECCCHHCCCCC		18.1228555341
306PhosphorylationKISLSNHYKNGADQP
EECCCHHCCCCCCCC		15.4827642862
356AcetylationIEDTCDHKEDDLGAV
HCCCCCCCCCCCCHH		49.9726051181
356UbiquitinationIEDTCDHKEDDLGAV
HCCCCCCCCCCCCHH		49.97-
375PhosphorylationSVILHLLSQLKLGMD
HHHHHHHHHHHHCCC		39.5724719451
395AcetylationLPTFILEKRSLLEMY
HHHHHHHHHHHHHHH		43.797709827
395UbiquitinationLPTFILEKRSLLEMY
HHHHHHHHHHHHHHH		43.7921890473
447AcetylationRKGAIAKKPYNPIIG
CCCEECCCCCCCCCC		43.6526051181
460PhosphorylationIGETFHCSWKMPKSE
CCCEEEEEEECCHHH		22.5928857561
543PhosphorylationKSKFLGMSIGVTMVG
CCHHCCCCCCEEEEC		17.8822210691
563PhosphorylationLLEHGEEYTFSLPCA
HHHCCCEEEEECCCC		14.5822210691
564PhosphorylationLEHGEEYTFSLPCAY
HHCCCEEEEECCCCC		15.2722210691
574PhosphorylationLPCAYARSILTVPWV
CCCCCCCCEEEEEEE		17.4924719451
594PhosphorylationVSVNCAKTGYSASIT
EEEEECCCCCEEEEE		23.8721406692
596PhosphorylationVNCAKTGYSASITFH
EEECCCCCEEEEEEE		13.2921406692
597PhosphorylationNCAKTGYSASITFHT
EECCCCCEEEEEEEC		19.5121406692
599PhosphorylationAKTGYSASITFHTKP
CCCCCEEEEEEECCC		19.0721406692
601PhosphorylationTGYSASITFHTKPFY
CCCEEEEEEECCCCC		13.5821406692
604PhosphorylationSASITFHTKPFYGGK
EEEEEEECCCCCCCE		35.9021406692
655UbiquitinationTKYVDLTKLAVTKKR
EEEEEEEEEEEECCC		41.57-
668UbiquitinationKRVRPLEKQDPFESR
CCCCCCHHCCCHHHH		68.62-
674PhosphorylationEKQDPFESRRLWKNV
HHCCCHHHHHHHHHH		24.0723403867
738MethylationVYHKPLWKIIPTTQP
EEECCEEEEECCCCC		38.14116253681
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
189SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSB11_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 OSB11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 OSB11_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-27; SER-172; SER-181 AND SER-184, AND MASSSPECTROMETRY.
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 THR-27; TYR-62; SER-172;SER-174; SER-181 AND SER-189, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-27; SER-172; SER-181 AND SER-184, AND MASSSPECTROMETRY.
"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 THR-27; SER-181 AND SER-189,AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27 AND SER-181, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-181, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27 AND SER-181, AND MASSSPECTROMETRY.
"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-189, AND MASSSPECTROMETRY.
"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-181, AND MASSSPECTROMETRY.

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