OSBL3_MOUSE - dbPTM
OSBL3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSBL3_MOUSE
UniProt AC Q9DBS9
Protein Name Oxysterol-binding protein-related protein 3
Gene Name Osbpl3
Organism Mus musculus (Mouse).
Sequence Length 855
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein . Cytoplasm, cytosol . Cell membrane
Peripheral membrane protein . Cell projection, filopodium tip . Nucleus membrane
Peripheral membrane protein .
Protein Description Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes. Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With VAPA, may regulate ER morphology. Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion. Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3. Also binds 25-hydroxycholesterol and cholesterol..
Protein Sequence MSDEKNLGVSQKLVSPSRSTSSCSSKQGSRQDSWEVVEGLRGEMTYTQEPPVQKGFLLKKRKWPLKGWHKRFFCLEKGILKYAKSQADIEREKLHGCIDVGLSVMSVKKSSKCIDLDTEEHIYHLKVKSEELFDEWVSKLRHHRMYRQNEIAMFPRDVNHFFSGSSVTDSAPGVFESVSSRKRSSLSKQNSFPPGSNLSFSCGGDTRVPFWLQSSEDMEKCSKDMAHCHAYLLEMSQLLESMDVLHRTYSAPAINAIQVPKPFSGPVRLHSSNPNLSTLDFGEEKSYSDGSEASSEFSKMQEDLCHVAHKVYFALRSAFNSISVEREKLKQLMELDTSPSPSAQVVGLKHALSSALAQNTDLKERLRRIHAESLLLDPPAVPKPGDNLAEENSRDEGRALVHQLSNESRLSITDSLSEFFDAQEVLLSPSSSENEISDDDSYVSDISDNLSLDNLSNDLDNERQTLGPVLESSGEARSKRRTSLPAPGPNTSSVSLWSILRNNIGKDLSKVAMPVELNEPLNTLQRLCEELEYSELLDKASRIPSPLERMVYVAAFAISAYASSYFRAGSKPFNPVLGETYECIRQDKGFQFFAEQVSHHPPISACHAESGNFVFWQDVRWKNKFWGKSMEIVPIGTTHVTLPAFGDHFEWNKVTSCIHNILSGQRWIEHYGEIDIKNLNDDSCHCKVNFIKAKYWSTNAHEIEGTVFDRSGKAVHRLFGKWHESIYCGGASSSTCVWRANPMPKGYEQYYGFTQFALELNEMDPLSRSLLPPTDTRFRPDQRLLEEGNIEEAEVQKQRIEKLQRERRRVLEENGVEHQPRFFRKSSDDAWVSNGTYLELRKDLGFSKLDHPVLW
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------MSDEKNLGV
------CCCCCCCCC		55.2524719451
10PhosphorylationDEKNLGVSQKLVSPS
CCCCCCCCCCCCCCC		21.5729514104
15PhosphorylationGVSQKLVSPSRSTSS
CCCCCCCCCCCCCCC		27.8226745281
17PhosphorylationSQKLVSPSRSTSSCS
CCCCCCCCCCCCCCC		31.2125367039
19PhosphorylationKLVSPSRSTSSCSSK
CCCCCCCCCCCCCCC		36.6629550500
20PhosphorylationLVSPSRSTSSCSSKQ
CCCCCCCCCCCCCCC		24.4529550500
21PhosphorylationVSPSRSTSSCSSKQG
CCCCCCCCCCCCCCC		30.5129550500
22PhosphorylationSPSRSTSSCSSKQGS
CCCCCCCCCCCCCCC		20.3629550500
24PhosphorylationSRSTSSCSSKQGSRQ
CCCCCCCCCCCCCCC		42.3829550500
25PhosphorylationRSTSSCSSKQGSRQD
CCCCCCCCCCCCCCC		33.0729550500
29PhosphorylationSCSSKQGSRQDSWEV
CCCCCCCCCCCCHHH		25.0326239621
33PhosphorylationKQGSRQDSWEVVEGL
CCCCCCCCHHHHHHH		19.4627742792
165PhosphorylationVNHFFSGSSVTDSAP
CCHHCCCCCCCCCCC		22.0423684622
166PhosphorylationNHFFSGSSVTDSAPG
CHHCCCCCCCCCCCC		32.3429514104
168PhosphorylationFFSGSSVTDSAPGVF
HCCCCCCCCCCCCCH		26.6125338131
170PhosphorylationSGSSVTDSAPGVFES
CCCCCCCCCCCCHHC		27.3121082442
179PhosphorylationPGVFESVSSRKRSSL
CCCHHCCCHHCCCCC		33.4325338131
180PhosphorylationGVFESVSSRKRSSLS
CCHHCCCHHCCCCCC		39.4029514104
185PhosphorylationVSSRKRSSLSKQNSF
CCHHCCCCCCCCCCC		40.4727149854
191PhosphorylationSSLSKQNSFPPGSNL
CCCCCCCCCCCCCCC		36.3126745281
196PhosphorylationQNSFPPGSNLSFSCG
CCCCCCCCCCEEECC		40.1325777480
199PhosphorylationFPPGSNLSFSCGGDT
CCCCCCCEEECCCCC		21.2625777480
201PhosphorylationPGSNLSFSCGGDTRV
CCCCCEEECCCCCCC		14.4225777480
206PhosphorylationSFSCGGDTRVPFWLQ
EEECCCCCCCCEEEC		36.5225777480
248PhosphorylationSMDVLHRTYSAPAIN
HHCHHHHHCCCCCEE		15.8726745281
249PhosphorylationMDVLHRTYSAPAINA
HCHHHHHCCCCCEEE		11.6425777480
250PhosphorylationDVLHRTYSAPAINAI
CHHHHHCCCCCEEEE		27.4526824392
264PhosphorylationIQVPKPFSGPVRLHS
EECCCCCCCCEEECC		51.1923984901
271PhosphorylationSGPVRLHSSNPNLST
CCCEEECCCCCCCCC		36.0827742792
272PhosphorylationGPVRLHSSNPNLSTL
CCEEECCCCCCCCCC		45.6327087446
277PhosphorylationHSSNPNLSTLDFGEE
CCCCCCCCCCCCCCC		33.3027742792
278PhosphorylationSSNPNLSTLDFGEEK
CCCCCCCCCCCCCCC		33.2525619855
286PhosphorylationLDFGEEKSYSDGSEA
CCCCCCCCCCCCCHH		32.9023984901
287PhosphorylationDFGEEKSYSDGSEAS
CCCCCCCCCCCCHHH		23.1129899451
288PhosphorylationFGEEKSYSDGSEASS
CCCCCCCCCCCHHHH		42.4627742792
291PhosphorylationEKSYSDGSEASSEFS
CCCCCCCCHHHHHHH		34.6723684622
294PhosphorylationYSDGSEASSEFSKMQ
CCCCCHHHHHHHHHH		26.7523684622
295PhosphorylationSDGSEASSEFSKMQE
CCCCHHHHHHHHHHH		50.1130635358
298PhosphorylationSEASSEFSKMQEDLC
CHHHHHHHHHHHHHH		24.1430635358
337PhosphorylationKQLMELDTSPSPSAQ
HHHHHCCCCCCCCHH		55.9826745281
338PhosphorylationQLMELDTSPSPSAQV
HHHHCCCCCCCCHHH		24.0528507225
340PhosphorylationMELDTSPSPSAQVVG
HHCCCCCCCCHHHHH		31.1122942356
342PhosphorylationLDTSPSPSAQVVGLK
CCCCCCCCHHHHHHH		35.3525266776
353PhosphorylationVGLKHALSSALAQNT
HHHHHHHHHHHHCCC		17.8524719451
393PhosphorylationDNLAEENSRDEGRAL
CCCCHHCCHHHHHHH		44.37-
405PhosphorylationRALVHQLSNESRLSI
HHHHHHHCCCCCCCC		31.7927742792
408PhosphorylationVHQLSNESRLSITDS
HHHHCCCCCCCCCHH		42.6527742792
447PhosphorylationDSYVSDISDNLSLDN
CCCCCCCCCCCCCCC		25.9924719451
472PhosphorylationTLGPVLESSGEARSK
CHHHHHHCCCCCCCC		39.2130635358
473PhosphorylationLGPVLESSGEARSKR
HHHHHHCCCCCCCCC		31.1430635358
478PhosphorylationESSGEARSKRRTSLP
HCCCCCCCCCCCCCC		37.2528059163
482PhosphorylationEARSKRRTSLPAPGP
CCCCCCCCCCCCCCC		38.3526239621
483PhosphorylationARSKRRTSLPAPGPN
CCCCCCCCCCCCCCC		30.4621082442
491PhosphorylationLPAPGPNTSSVSLWS
CCCCCCCCHHHHHHH		26.0519060867
492PhosphorylationPAPGPNTSSVSLWSI
CCCCCCCHHHHHHHH		35.0725777480
493PhosphorylationAPGPNTSSVSLWSIL
CCCCCCHHHHHHHHH		17.4325777480
495PhosphorylationGPNTSSVSLWSILRN
CCCCHHHHHHHHHHC		26.5225777480
498PhosphorylationTSSVSLWSILRNNIG
CHHHHHHHHHHCCCC		19.6225777480
510UbiquitinationNIGKDLSKVAMPVEL
CCCCCHHHHCCCCCC		41.11-
725PhosphorylationLFGKWHESIYCGGAS
HHCCCCCCEECCCCC		13.1325777480
727PhosphorylationGKWHESIYCGGASSS
CCCCCCEECCCCCCC		8.3625777480
732PhosphorylationSIYCGGASSSTCVWR
CEECCCCCCCCEEEE		28.2626239621
733PhosphorylationIYCGGASSSTCVWRA
EECCCCCCCCEEEEC		29.1826239621
734PhosphorylationYCGGASSSTCVWRAN
ECCCCCCCCEEEECC		24.2726239621
735PhosphorylationCGGASSSTCVWRANP
CCCCCCCCEEEECCC		17.0226239621
747PhosphorylationANPMPKGYEQYYGFT
CCCCCCCHHHHCCHH		13.1430635358
750PhosphorylationMPKGYEQYYGFTQFA
CCCCHHHHCCHHHHH		8.1330635358
751PhosphorylationPKGYEQYYGFTQFAL
CCCHHHHCCHHHHHH		12.8830635358
754PhosphorylationYEQYYGFTQFALELN
HHHHCCHHHHHHHHH		20.5830635358
767PhosphorylationLNEMDPLSRSLLPPT
HHCCCCCHHCCCCCC		25.8030635358
827PhosphorylationPRFFRKSSDDAWVSN
CCCEECCCCCCCCCC		42.4121659604
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 OSBL3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSBL3_MOUSE !!
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 OSBL3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of OSBL3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OSBL3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASSSPECTROMETRY.

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