OSBL6_HUMAN - dbPTM
OSBL6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSBL6_HUMAN
UniProt AC Q9BZF3
Protein Name Oxysterol-binding protein-related protein 6
Gene Name OSBPL6
Organism Homo sapiens (Human).
Sequence Length 934
Subcellular Localization Cytoplasm, cytosol . Endoplasmic reticulum membrane
Peripheral membrane protein . Nucleus envelope . Cell membrane
Peripheral membrane protein .
Protein Description Weakly binds 25-hydroxycholesterol..
Protein Sequence MSSDEKGISPAHKTSTPTHRSASSSTSSQRDSRQSIHILERTASSSTEPSVSRQLLEPEPVPLSKEADSWEIIEGLKIGQTNVQKPDKHEGFMLKKRKWPLKGWHKRFFVLDNGMLKYSKAPLDIQKGKVHGSIDVGLSVMSIKKKARRIDLDTEEHIYHLKVKSQDWFDAWVSKLRHHRLYRQNEIVRSPRDASFHIFPSTSTAESSPAANVSVMDGKMQPNSFPWQSPLPCSNSLPATCTTGQSKVAAWLQDSEEMDRCAEDLAHCQSNLVELSKLLQNLEILQRTQSAPNFTDMQANCVDISKKDKRVTRRWRTKSVSKDTKIQLQVPFSATMSPVRLHSSNPNLCADIEFQTPPSHLTDPLESSTDYTKLQEEFCLIAQKVHSLLKSAFNSIAIEKEKLKQMVSEQDHSKGHSTQMARLRQSLSQALNQNAELRSRLNRIHSESIICDQVVSVNIIPSPDEAGEQIHVSLPLSQQVANESRLSMSESVSEFFDAQEVLLSASSSENEASDDESYISDVSDNISEDNTSVADNISRQILNGELTGGAFRNGRRACLPAPCPDTSNINLWNILRNNIGKDLSKVSMPVELNEPLNTLQHLCEEMEYSELLDKASETDDPYERMVLVAAFAVSGYCSTYFRAGSKPFNPVLGETYECIREDKGFRFFSEQVSHHPPISACHCESKNFVFWQDIRWKNKFWGKSMEILPVGTLNVMLPKYGDYYVWNKVTTCIHNILSGRRWIEHYGEVTIRNTKSSVCICKLTFVKVNYWNSNMNEVQGVVIDQEGKAVYRLFGKWHEGLYCGVAPSAKCIWRPGSMPTNYELYYGFTRFAIELNELDPVLKDLLPPTDARFRPDQRFLEEGNLEAAASEKQRVEELQRSRRRYMEENNLEHIPKFFKKVIDANQREAWVSNDTYWELRKDPGFSKVDSPVLW
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------MSSDEKGIS
------CCCCCCCCC		46.6319369195
2Phosphorylation------MSSDEKGIS
------CCCCCCCCC		46.6319369195
3Phosphorylation-----MSSDEKGISP
-----CCCCCCCCCC		48.7929083192
5 (in isoform 3)Phosphorylation-55.95-
9PhosphorylationSSDEKGISPAHKTST
CCCCCCCCCCCCCCC		25.3830266825
14PhosphorylationGISPAHKTSTPTHRS
CCCCCCCCCCCCCCC		28.1524719451
14 (in isoform 3)Phosphorylation-28.15-
15PhosphorylationISPAHKTSTPTHRSA
CCCCCCCCCCCCCCC		36.8725159151
16PhosphorylationSPAHKTSTPTHRSAS
CCCCCCCCCCCCCCC		37.1225159151
18PhosphorylationAHKTSTPTHRSASSS
CCCCCCCCCCCCCCC		29.9725002506
23PhosphorylationTPTHRSASSSTSSQR
CCCCCCCCCCCCCCH		26.5218669648
23 (in isoform 3)Phosphorylation-26.5218669648
32PhosphorylationSTSSQRDSRQSIHIL
CCCCCHHHHHHHEEH		34.1130266825
35PhosphorylationSQRDSRQSIHILERT
CCHHHHHHHEEHHHH		18.2830266825
42PhosphorylationSIHILERTASSSTEP
HHEEHHHHCCCCCCC		22.8630266825
44PhosphorylationHILERTASSSTEPSV
EEHHHHCCCCCCCCH		24.9825159151
45PhosphorylationILERTASSSTEPSVS
EHHHHCCCCCCCCHH		38.5230266825
46PhosphorylationLERTASSSTEPSVSR
HHHHCCCCCCCCHHH		34.0030266825
47PhosphorylationERTASSSTEPSVSRQ
HHHCCCCCCCCHHHH		54.5930266825
50PhosphorylationASSSTEPSVSRQLLE
CCCCCCCCHHHHHCC		26.8826853621
52PhosphorylationSSTEPSVSRQLLEPE
CCCCCCHHHHHCCCC		20.7427251275
69PhosphorylationPLSKEADSWEIIEGL
CCCCCCCCCHHHCCC		33.3922199227
133PhosphorylationQKGKVHGSIDVGLSV
CCCCCCEECCCCCEE		10.75-
190PhosphorylationRQNEIVRSPRDASFH
CCCCCCCCCCCCCEE		17.2530266825
195PhosphorylationVRSPRDASFHIFPST
CCCCCCCCEEEECCC		22.9622199227
201PhosphorylationASFHIFPSTSTAESS
CCEEEECCCCCCCCC		25.0022199227
202PhosphorylationSFHIFPSTSTAESSP
CEEEECCCCCCCCCC		30.2722199227
203PhosphorylationFHIFPSTSTAESSPA
EEEECCCCCCCCCCC		29.9222199227
204PhosphorylationHIFPSTSTAESSPAA
EEECCCCCCCCCCCC		34.2422199227
207PhosphorylationPSTSTAESSPAANVS
CCCCCCCCCCCCCEE		38.8722199227
208PhosphorylationSTSTAESSPAANVSV
CCCCCCCCCCCCEEE		15.2922199227
214PhosphorylationSSPAANVSVMDGKMQ
CCCCCCEEEECCCCC		16.1322199227
229PhosphorylationPNSFPWQSPLPCSNS
CCCCCCCCCCCCCCC		25.2425159151
288PhosphorylationNLEILQRTQSAPNFT
HHHHHHHHCCCCCCC		17.5730377224
288 (in isoform 4)Phosphorylation-17.5729523821
288 (in isoform 6)Phosphorylation-17.5729523821
290PhosphorylationEILQRTQSAPNFTDM
HHHHHHCCCCCCCCC		45.1130576142
290 (in isoform 4)Phosphorylation-45.1122199227
290 (in isoform 6)Phosphorylation-45.1122199227
295 (in isoform 4)Phosphorylation-36.8829523821
295 (in isoform 6)Phosphorylation-36.8829523821
302 (in isoform 4)Phosphorylation-8.0028348404
302 (in isoform 6)Phosphorylation-8.0028348404
304 (in isoform 4)Phosphorylation-3.0321712546
304 (in isoform 6)Phosphorylation-3.0321712546
306 (in isoform 4)Phosphorylation-66.3821712546
306 (in isoform 6)Phosphorylation-66.3821712546
312PhosphorylationSKKDKRVTRRWRTKS
CHHCHHHHHHEECCC		20.6732142685
313PhosphorylationKKDKRVTRRWRTKSV
HHCHHHHHHEECCCC		33.0532142685
333PhosphorylationIQLQVPFSATMSPVR
EEEECCCCEEECCEE		19.4325159151
333 (in isoform 3)Phosphorylation-19.4328348404
335PhosphorylationLQVPFSATMSPVRLH
EECCCCEEECCEEEC		19.5825159151
337PhosphorylationVPFSATMSPVRLHSS
CCCCEEECCEEECCC		18.8525159151
337 (in isoform 3)Phosphorylation-18.8524719451
339 (in isoform 3)Phosphorylation-8.7926270265
341 (in isoform 3)Phosphorylation-4.7126270265
343PhosphorylationMSPVRLHSSNPNLCA
ECCEEECCCCCCCCE		36.0823401153
344PhosphorylationSPVRLHSSNPNLCAD
CCEEECCCCCCCCEE		45.6330266825
347PhosphorylationRLHSSNPNLCADIEF
EECCCCCCCCEEEEE		52.5932142685
348PhosphorylationLHSSNPNLCADIEFQ
ECCCCCCCCEEEEEC		2.4132142685
354 (in isoform 5)Phosphorylation-11.3628348404
356PhosphorylationCADIEFQTPPSHLTD
CEEEEECCCCHHCCC		42.3525159151
358 (in isoform 5)Phosphorylation-37.4624719451
359PhosphorylationIEFQTPPSHLTDPLE
EEECCCCHHCCCCCC		32.1229978859
360 (in isoform 5)Phosphorylation-38.2226270265
362PhosphorylationQTPPSHLTDPLESST
CCCCHHCCCCCCCCC		30.1029978859
362 (in isoform 5)Phosphorylation-30.1026270265
368PhosphorylationLTDPLESSTDYTKLQ
CCCCCCCCCCCHHHH		18.8732142685
369PhosphorylationTDPLESSTDYTKLQE
CCCCCCCCCCHHHHH		42.1632142685
386 (in isoform 6)Phosphorylation-21.5522210691
387PhosphorylationLIAQKVHSLLKSAFN
HHHHHHHHHHHHHHH		38.0824719451
387 (in isoform 6)Phosphorylation-38.0822210691
395 (in isoform 6)Phosphorylation-13.6222210691
397 (in isoform 6)Phosphorylation-12.0526437602
406 (in isoform 6)Phosphorylation-3.2422210691
413PhosphorylationMVSEQDHSKGHSTQM
HHCCCCCCCCHHHHH		48.93-
417 (in isoform 2)Phosphorylation-29.0622210691
418 (in isoform 2)Phosphorylation-19.3822210691
426PhosphorylationQMARLRQSLSQALNQ
HHHHHHHHHHHHHHH		24.4528555341
426 (in isoform 2)Phosphorylation-24.4522210691
428PhosphorylationARLRQSLSQALNQNA
HHHHHHHHHHHHHCH		20.7517525332
428 (in isoform 2)Phosphorylation-20.7526437602
437 (in isoform 2)Phosphorylation-5.8322210691
484PhosphorylationSQQVANESRLSMSES
HHHHHHHHHCCCCHH		38.03-
547PhosphorylationQILNGELTGGAFRNG
HHHCCCCCCCCCCCC		29.3024961811
581UbiquitinationILRNNIGKDLSKVSM
HHHCCCCCCHHHCCC		52.26-
616PhosphorylationSELLDKASETDDPYE
HHHHHHHCCCCCHHH		46.9330576142
638PhosphorylationFAVSGYCSTYFRAGS
HHHHCCHHHHHCCCC		20.0522210691
639PhosphorylationAVSGYCSTYFRAGSK
HHHCCHHHHHCCCCC		24.1030576142
640PhosphorylationVSGYCSTYFRAGSKP
HHCCHHHHHCCCCCC		3.7722210691
655PhosphorylationFNPVLGETYECIRED
CCCCCCCHHHHHHHC		23.8722210691
704PhosphorylationKNKFWGKSMEILPVG
CCCCCCCCEEEEECE		20.0824043423
712PhosphorylationMEILPVGTLNVMLPK
EEEEECEEEEEEECC		18.5224043423
746PhosphorylationGRRWIEHYGEVTIRN
CCCHHHHHCEEEEEC		11.37-
802PhosphorylationGKWHEGLYCGVAPSA
CCCCCCCCCCCCCCC		9.67-
836UbiquitinationTRFAIELNELDPVLK
EHHEEEHHHCCHHHH		34.6929967540
841UbiquitinationELNELDPVLKDLLPP
EHHHCCHHHHHHCCC		11.7929967540
872UbiquitinationLEAAASEKQRVEELQ
HHHHHHHHHHHHHHH		40.6929967540
876UbiquitinationASEKQRVEELQRSRR
HHHHHHHHHHHHHHH		56.0029967540
897UbiquitinationNLEHIPKFFKKVIDA
CHHHHHHHHHHHHCC		10.2229967540
926PhosphorylationLRKDPGFSKVDSPVL
HHCCCCCCCCCCCCC		37.37-
930PhosphorylationPGFSKVDSPVLW---
CCCCCCCCCCCC---		21.6428348404
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 OSBL6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSBL6_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 OSBL6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
CING_HUMANCGNphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
MAST3_HUMANMAST3physical
27173435
RGPS2_HUMANRALGPS2physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
MPIP3_HUMANCDC25Cphysical
27173435
GGYF2_HUMANGIGYF2physical
27173435
NF1_HUMANNF1physical
27173435
LPIN3_HUMANLPIN3physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
CBY1_HUMANCBY1physical
27173435
HDAC4_HUMANHDAC4physical
27173435
CAMP2_HUMANCAMSAP2physical
27173435
LIMA1_HUMANLIMA1physical
27173435
INP5E_HUMANINPP5Ephysical
27173435
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 OSBL6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-44 AND SER-343,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-229, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND MASSSPECTROMETRY.

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