OSBL1_HUMAN - dbPTM
OSBL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSBL1_HUMAN
UniProt AC Q9BXW6
Protein Name Oxysterol-binding protein-related protein 1
Gene Name OSBPL1A
Organism Homo sapiens (Human).
Sequence Length 950
Subcellular Localization Late endosome . Colocalizes with RAB7A, RAB9A and LAMP1 in late endosomes.
Protein Description Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate (By similarity). Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and alters functional properties of late endocytic compartments via its interaction with RAB7A. [PubMed: 16176980 Binds 25-hydroxycholesterol and cholesterol]
Protein Sequence MNTEAEQQLLHHARNGNAEEVRQLLETMARNEVIADINCKGRSKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTAKEVTHAEEIRSMLEAVERTQQRKLEELLLAAAREGKTTELTALLNRPNPPDVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLAQGAEMKHILVGNKVIYKALKRYEGPLWKSSRFFGWRLFWVVLEHGVLSWYRKQPDAVHNIYRQGCKHLTQAVCTVKSTDSCLFFIKCFDDTIHGFRVPKNSLQQSREDWLEAIEEHSAYSTHYCSQDQLTDEEEEDTVSAADLKKSLEKAQSCQQRLDREISNFLKMIKECDMAKEMLPSFLQKVEVVSEASRETCVALTDCLNLFTKQEGVRNFKLEQEQEKNKILSEALETLATEHHELEQSLVKGSPPASILSEDEFYDALSDSESERSLSRLEAVTARSFEEEGEHLGSRKHRMSEEKDCGGGDALSNGIKKHRTSLPSPMFSRNDFSIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKPFNPLLGETYELVRDDLGFRLISEQVSHHPPISAFHAEGLNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLEHNEAYTWTNPTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFGKELHKVEGYIQDKSKKKLCALYGKWTECLYSVDPATFDAYKKNDKKNTEEKKNSKQMSTSEELDEMPVPDSESVFIIPGSVLLWRIAPRPPNSAQMYNFTSFAMVLNEVDKDMESVIPKTDCRLRPDIRAMENGEIDQASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQGPNPYNGAQDWIYSGSYWDRNYFNLPDIY
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
40UbiquitinationVIADINCKGRSKSNL
EEEECCCCCCCCCCC		53.52-
43PhosphorylationDINCKGRSKSNLGWT
ECCCCCCCCCCCCCC		49.4524719451
45PhosphorylationNCKGRSKSNLGWTPL
CCCCCCCCCCCCCHH		38.2322617229
110 (in isoform 2)Ubiquitination-6.6121906983
169 (in isoform 2)Ubiquitination-10.8321906983
238PhosphorylationIYKALKRYEGPLWKS
HHHHHHHCCCCCCCC		24.53-
315UbiquitinationIHGFRVPKNSLQQSR
CCCCCCCCHHHHHCH		57.20-
317PhosphorylationGFRVPKNSLQQSRED
CCCCCCHHHHHCHHH		33.41-
321PhosphorylationPKNSLQQSREDWLEA
CCHHHHHCHHHHHHH		25.36-
333PhosphorylationLEAIEEHSAYSTHYC
HHHHHHHCCCCCCCC		31.9826471730
335PhosphorylationAIEEHSAYSTHYCSQ
HHHHHCCCCCCCCCH		19.6726471730
336PhosphorylationIEEHSAYSTHYCSQD
HHHHCCCCCCCCCHH		14.3926471730
337PhosphorylationEEHSAYSTHYCSQDQ
HHHCCCCCCCCCHHH		12.2826471730
339PhosphorylationHSAYSTHYCSQDQLT
HCCCCCCCCCHHHCC		8.2226471730
341PhosphorylationAYSTHYCSQDQLTDE
CCCCCCCCHHHCCCH		29.6226471730
346PhosphorylationYCSQDQLTDEEEEDT
CCCHHHCCCHHHHCC		35.4127422710
365UbiquitinationDLKKSLEKAQSCQQR
HHHHHHHHHHHHHHH		57.95-
378PhosphorylationQRLDREISNFLKMIK
HHHHHHHHHHHHHHH		19.44-
382MethylationREISNFLKMIKECDM
HHHHHHHHHHHHCHH		34.15-
396PhosphorylationMAKEMLPSFLQKVEV
HHHHHHHHHHHHHHH		34.3321406692
424UbiquitinationDCLNLFTKQEGVRNF
HHHHHHCCHHHHHCC		38.73-
441UbiquitinationEQEQEKNKILSEALE
CHHHHHHHHHHHHHH		56.97-
452PhosphorylationEALETLATEHHELEQ
HHHHHHHHHCHHHHH		38.6827732954
460PhosphorylationEHHELEQSLVKGSPP
HCHHHHHHHHCCCCC		26.2525849741
465PhosphorylationEQSLVKGSPPASILS
HHHHHCCCCCHHHCC		23.2226657352
469PhosphorylationVKGSPPASILSEDEF
HCCCCCHHHCCHHHH		29.8126657352
472PhosphorylationSPPASILSEDEFYDA
CCCHHHCCHHHHHHH		41.1327732954
477PhosphorylationILSEDEFYDALSDSE
HCCHHHHHHHCCCCH		9.7727732954
481PhosphorylationDEFYDALSDSESERS
HHHHHHCCCCHHHHH		40.5927732954
483PhosphorylationFYDALSDSESERSLS
HHHHCCCCHHHHHHH		39.3822617229
485PhosphorylationDALSDSESERSLSRL
HHCCCCHHHHHHHHH		42.1122115753
488PhosphorylationSDSESERSLSRLEAV
CCCHHHHHHHHHHHH		27.0120068231
490PhosphorylationSESERSLSRLEAVTA
CHHHHHHHHHHHHHC		35.7520068231
496PhosphorylationLSRLEAVTARSFEEE
HHHHHHHHCCCHHHH		24.3322617229
499PhosphorylationLEAVTARSFEEEGEH
HHHHHCCCHHHHHCC		34.2529255136
509PhosphorylationEEGEHLGSRKHRMSE
HHHCCCCCCCCCCCC		44.5123401153
515PhosphorylationGSRKHRMSEEKDCGG
CCCCCCCCCCCCCCC		42.4329255136
535PhosphorylationNGIKKHRTSLPSPMF
HHHHHCCCCCCCCCC		34.0428857561
536PhosphorylationGIKKHRTSLPSPMFS
HHHHCCCCCCCCCCC		37.9326657352
539PhosphorylationKHRTSLPSPMFSRND
HCCCCCCCCCCCCCC		34.0029214152
543PhosphorylationSLPSPMFSRNDFSIW
CCCCCCCCCCCHHHH		24.7523312004
551PhosphorylationRNDFSIWSILRKCIG
CCCHHHHHHHHHHHC		15.2924719451
565PhosphorylationGMELSKITMPVIFNE
CCCHHHCCCCHHCCC		21.11-
623UbiquitinationSQWERTGKPFNPLLG
HHHHHHCCCCCHHCC		45.9121906983
623 (in isoform 1)Ubiquitination-45.9121906983
637MethylationGETYELVRDDLGFRL
CCHHHHHHHCCCHHH		44.33115368603
682UbiquitinationPKLKFWGKSVEAEPK
CCCCCCEECEEECCC		41.762190698
682 (in isoform 1)Ubiquitination-41.7621906983
755UbiquitinationLFGKELHKVEGYIQD
CCCHHHHCCCCEECC		55.39-
763UbiquitinationVEGYIQDKSKKKLCA
CCCEECCCCHHHHHH		48.04-
764O-linked_GlycosylationEGYIQDKSKKKLCAL
CCEECCCCHHHHHHH		58.9830379171
780PhosphorylationGKWTECLYSVDPATF
CCHHHHHHCCCHHHH		20.5029759185
791UbiquitinationPATFDAYKKNDKKNT
HHHHHHHHHCCCCCH		46.98-
808PhosphorylationKKNSKQMSTSEELDE
HHHHHCCCCCHHHHC		26.7028348404
809PhosphorylationKNSKQMSTSEELDEM
HHHHCCCCCHHHHCC		34.5128348404
810PhosphorylationNSKQMSTSEELDEMP
HHHCCCCCHHHHCCC		23.0527251275
890PhosphorylationNGEIDQASEEKKRLE
CCCCCHHHHHHHHHH		40.4327794612
908PhosphorylationRAARKNRSKSEEDWK
HHHHHHCCCCHHHHH		50.3430108239
910PhosphorylationARKNRSKSEEDWKTR
HHHHCCCCHHHHHHC		47.6830108239
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 OSBL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSBL1_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 OSBL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of OSBL1_HUMAN !!
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 OSBL1_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-499, 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-499, AND MASSSPECTROMETRY.

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