OSB10_HUMAN - dbPTM
OSB10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSB10_HUMAN
UniProt AC Q9BXB5
Protein Name Oxysterol-binding protein-related protein 10
Gene Name OSBPL10
Organism Homo sapiens (Human).
Sequence Length 764
Subcellular Localization Cytoplasm, cytoskeleton . Associates with microtubules.
Protein Description Probable lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane. Its ability to bind phosphatidylserine, suggests that it specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P. [PubMed: 23934110) (Probable Plays a role in negative regulation of lipid biosynthesis]
Protein Sequence MERAVQGTDGGGGSNSSSRSSSRATSAGSSPSCSLAGRGVSSRSAAAGLGGGGSRSSPGSVAASPSGGGGRRREPALEGVLSKYTNLLQGWQNRYFVLDFEAGILQYFVNEQSKHQKPRGVLSLSGAIVSLSDEAPHMLVVYSANGEMFKLRAADAKEKQFWVTQLRACAKYHMEMNSKSAPSSRSRSLTLLPHGTPNSASPCSQRHLSVGAPGVVTITHHKSPAAARRAKSQYSGQLHEVREMMNQVEGQQKNLVHAIESLPGSGPLTALDQDLLLLKATSAATLSCLGECLNLLQQSVHQAGQPSQKPGASENILGWHGSKSHSTEQLKNGTLGSLPSASANITWAILPNSAEDEQTSQPEPEPNSGSELVLSEDEKSDNEDKEETELGVMEDQRSIILHLISQLKLGMDLTKVVLPTFILEKRSLLEMYADFMAHPDLLLAITAGATPEERVICFVEYYLTAFHEGRKGALAKKPYNPIIGETFHCSWEVPKDRVKPKRTASRSPASCHEHPMADDPSKSYKLRFVAEQVSHHPPISCFYCECEEKRLCVNTHVWTKSKFMGMSVGVSMIGEGVLRLLEHGEEYVFTLPSAYARSILTIPWVELGGKVSINCAKTGYSATVIFHTKPFYGGKVHRVTAEVKHNPTNTIVCKAHGEWNGTLEFTYNNGETKVIDTTTLPVYPKKIRPLEKQGPMESRNLWREVTRYLRLGDIDAATEQKRHLEEKQRVEERKRENLRTPWKPKYFIQEGDGWVYFNPLWKAH
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
8PhosphorylationMERAVQGTDGGGGSN
CCCCCCCCCCCCCCC		17.8728102081
14PhosphorylationGTDGGGGSNSSSRSS
CCCCCCCCCCCCCCC		36.4922210691
16PhosphorylationDGGGGSNSSSRSSSR
CCCCCCCCCCCCCCC		31.2430576142
17PhosphorylationGGGGSNSSSRSSSRA
CCCCCCCCCCCCCCC		33.7428102081
18PhosphorylationGGGSNSSSRSSSRAT
CCCCCCCCCCCCCCC		35.6828102081
20PhosphorylationGSNSSSRSSSRATSA
CCCCCCCCCCCCCCC		34.3128258704
21PhosphorylationSNSSSRSSSRATSAG
CCCCCCCCCCCCCCC		23.8030576142
25PhosphorylationSRSSSRATSAGSSPS
CCCCCCCCCCCCCCC		20.2823927012
26PhosphorylationRSSSRATSAGSSPSC
CCCCCCCCCCCCCCC		29.6429255136
29PhosphorylationSRATSAGSSPSCSLA
CCCCCCCCCCCCCCC		38.5029255136
30PhosphorylationRATSAGSSPSCSLAG
CCCCCCCCCCCCCCC		21.6629255136
32PhosphorylationTSAGSSPSCSLAGRG
CCCCCCCCCCCCCCC		20.4829255136
34PhosphorylationAGSSPSCSLAGRGVS
CCCCCCCCCCCCCCC		26.1229255136
38MethylationPSCSLAGRGVSSRSA
CCCCCCCCCCCCCHH		36.4124129315
44PhosphorylationGRGVSSRSAAAGLGG
CCCCCCCHHCCCCCC		24.9828857561
54PhosphorylationAGLGGGGSRSSPGSV
CCCCCCCCCCCCCCC		32.0622199227
56PhosphorylationLGGGGSRSSPGSVAA
CCCCCCCCCCCCCCC		42.4530266825
57PhosphorylationGGGGSRSSPGSVAAS
CCCCCCCCCCCCCCC		31.9730266825
60PhosphorylationGSRSSPGSVAASPSG
CCCCCCCCCCCCCCC		16.3926055452
64PhosphorylationSPGSVAASPSGGGGR
CCCCCCCCCCCCCCC		15.1725159151
66PhosphorylationGSVAASPSGGGGRRR
CCCCCCCCCCCCCCC		47.8027794612
159UbiquitinationRAADAKEKQFWVTQL
EECCCCCCHHHHHHH		50.52-
186PhosphorylationKSAPSSRSRSLTLLP
CCCCCCCCCCEEECC		28.3328152594
188PhosphorylationAPSSRSRSLTLLPHG
CCCCCCCCEEECCCC		27.2723927012
190PhosphorylationSSRSRSLTLLPHGTP
CCCCCCEEECCCCCC		27.7425159151
196PhosphorylationLTLLPHGTPNSASPC
EEECCCCCCCCCCCC		19.1022167270
199PhosphorylationLPHGTPNSASPCSQR
CCCCCCCCCCCCCCC		31.1822167270
201PhosphorylationHGTPNSASPCSQRHL
CCCCCCCCCCCCCCC		26.6822167270
204PhosphorylationPNSASPCSQRHLSVG
CCCCCCCCCCCCCCC		33.3622167270
209PhosphorylationPCSQRHLSVGAPGVV
CCCCCCCCCCCCCEE		16.6329255136
217PhosphorylationVGAPGVVTITHHKSP
CCCCCEEEEEECCCH		20.1123927012
219PhosphorylationAPGVVTITHHKSPAA
CCCEEEEEECCCHHH		14.4629255136
223PhosphorylationVTITHHKSPAAARRA
EEEEECCCHHHHHHH		18.5329255136
231MethylationPAAARRAKSQYSGQL
HHHHHHHHHHHHCHH		35.96115974477
231UbiquitinationPAAARRAKSQYSGQL
HHHHHHHHHHHHCHH		35.96-
232PhosphorylationAAARRAKSQYSGQLH
HHHHHHHHHHHCHHH		33.1122496350
234PhosphorylationARRAKSQYSGQLHEV
HHHHHHHHHCHHHHH		23.1223312004
235PhosphorylationRRAKSQYSGQLHEVR
HHHHHHHHCHHHHHH		16.6625159151
265PhosphorylationAIESLPGSGPLTALD
HHHCCCCCCCCCCCC		34.9925159151
322PhosphorylationNILGWHGSKSHSTEQ
CCCCCCCCCCCCCHH		20.3525159151
324PhosphorylationLGWHGSKSHSTEQLK
CCCCCCCCCCCHHHH		25.1124719451
326PhosphorylationWHGSKSHSTEQLKNG
CCCCCCCCCHHHHCC		40.5025849741
361UbiquitinationAEDEQTSQPEPEPNS
CCCCCCCCCCCCCCC		50.1721890473
375PhosphorylationSGSELVLSEDEKSDN
CCCEEEECCCCCCCC		35.2127362937
380PhosphorylationVLSEDEKSDNEDKEE
EECCCCCCCCCCHHH		43.5525159151
388PhosphorylationDNEDKEETELGVMED
CCCCHHHHHHHHHHH		37.2922496350
398PhosphorylationGVMEDQRSIILHLIS
HHHHHHHHHHHHHHH		14.3520873877
405PhosphorylationSIILHLISQLKLGMD
HHHHHHHHHHHHCCC		35.5024719451
425UbiquitinationLPTFILEKRSLLEMY
HHHHHHHHHHHHHHH		43.7921890473
425AcetylationLPTFILEKRSLLEMY
HHHHHHHHHHHHHHH		43.797709839
479PhosphorylationGALAKKPYNPIIGET
CHHCCCCCCCCCCCE		42.31-
503PhosphorylationDRVKPKRTASRSPAS
HHCCCCCCCCCCCCC		34.8028857561
505PhosphorylationVKPKRTASRSPASCH
CCCCCCCCCCCCCCC		32.4520201521
507PhosphorylationPKRTASRSPASCHEH
CCCCCCCCCCCCCCC		23.4830266825
510PhosphorylationTASRSPASCHEHPMA
CCCCCCCCCCCCCCC		21.2830266825
521PhosphorylationHPMADDPSKSYKLRF
CCCCCCCCCCCCHHH		41.0324702127
561PhosphorylationNTHVWTKSKFMGMSV
EEEEEECHHHCCCCC		24.6122115753
595PhosphorylationVFTLPSAYARSILTI
EEECCHHHHHHCEEE		13.5926074081
598PhosphorylationLPSAYARSILTIPWV
CCHHHHHHCEEEEEE		17.4926074081
685UbiquitinationTTLPVYPKKIRPLEK
CCCCCCCCCCCCCHH		43.05-
721UbiquitinationIDAATEQKRHLEEKQ
CCHHHHHHHHHHHHH		35.242190698
762UbiquitinationVYFNPLWKAH-----
EEECCCCCCC-----		44.24-
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 OSB10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSB10_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 OSB10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2B1_HUMANAP2B1physical
19615732
ALDOA_HUMANALDOAphysical
19615732
BBS1_HUMANBBS1physical
19615732
NIPS2_HUMANGBASphysical
19615732
MMP2_HUMANMMP2physical
19615732
CUL1_HUMANCUL1physical
19615732
EPN4_HUMANCLINT1physical
19615732
KEAP1_HUMANKEAP1physical
19615732
SAP18_HUMANSAP18physical
19615732
SRRM2_HUMANSRRM2physical
19615732
WRIP1_HUMANWRNIP1physical
19615732
CLPB_HUMANCLPBphysical
19615732
ZCH18_HUMANZC3H18physical
19615732
PGAM5_HUMANPGAM5physical
19615732
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 OSB10_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-56; SER-57; SER-60;SER-64; SER-66; THR-196; SER-201 AND SER-223, 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 SER-30, AND MASSSPECTROMETRY.

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