dbPTM

OSBL8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	OSBL8_HUMAN
UniProt AC	Q9BZF1
Protein Name	Oxysterol-binding protein-related protein 8
Gene Name	OSBPL8
Organism	Homo sapiens (Human).
Sequence Length	889
Subcellular Localization	Isoform 1: Endoplasmic reticulum membrane Single-pass membrane protein . Nucleus membrane . The presence of the N-terminus extension contains an overall negative charge that may explain the weak localization to the cortical endoplasmic reticulum (P
Protein Description	Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner. [PubMed: 26206935 Binds oxysterol, 25-hydroxycholesterol and cholesterol]
Protein Sequence	MEGGLADGEPDRTSLLGDSKDVLGPSTVVANSDESQLLTPGKMSQRQGKEAYPTPTKDLHQPSLSPASPHSQGFERGKEDISQNKDESSLSMSKSKSESKLYNGSEKDSSTSSKLTKKESLKVQKKNYREEKKRATKELLSTITDPSVIVMADWLKIRGTLKSWTKLWCVLKPGVLLIYKTQKNGQWVGTVLLNACEIIERPSKKDGFCFKLFHPLEQSIWAVKGPKGEAVGSITQPLPSSYLIIRATSESDGRCWMDALELALKCSSLLKRTMIREGKEHDLSVSSDSTHVTFYGLLRANNLHSGDNFQLNDSEIERQHFKDQDMYSDKSDKENDQEHDESDNEVMGKSEESDTDTSERQDDSYIEPEPVEPLKETTYTEQSHEELGEAGEASQTETVSEENKSLIWTLLKQVRPGMDLSKVVLPTFILEPRSFLDKLSDYYYHADFLSEAALEENPYFRLKKVVKWYLSGFYKKPKGLKKPYNPILGETFRCLWIHPRTNSKTFYIAEQVSHHPPISAFYVSNRKDGFCLSGSILAKSKFYGNSLSAILEGEARLTFLNRGEDYVMTMPYAHCKGILYGTMTLELGGTVNITCQKTGYSAILEFKLKPFLGSSDCVNQISGKLKLGKEVLATLEGHWDSEVFITDKKTDNSEVFWNPTPDIKQWRLIRHTVKFEEQGDFESEKLWQRVTRAINAKDQTEATQEKYVLEEAQRQAARDRKTKNEEWSCKLFELDPLTGEWHYKFADTRPWDPLNDMIQFEKDGVIQTKVKHRTPMVSVPKMKHKPTRQQKKVAKGYSSPEPDIQDSSGSEAQSVKPSTRRKKGIELGDIQSSIESIKQTQEEIKRNIMALRNHLVSSTPATDYFLQQKDYFIIFLLILLQVIINFMFK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEGGLADG -------CCCCCCCC	11.02	22814378
10 (in isoform 3)	Phosphorylation	-	41.74	17924679
13	Phosphorylation	ADGEPDRTSLLGDSK CCCCCCCCCCCCCCC	30.98	29255136
14	Phosphorylation	DGEPDRTSLLGDSKD CCCCCCCCCCCCCCC	23.61	29255136
14 (in isoform 3)	Phosphorylation	-	23.61	-
19	Phosphorylation	RTSLLGDSKDVLGPS CCCCCCCCCCCCCCC	29.02	30108239
21 (in isoform 3)	Phosphorylation	-	44.84	-
23 (in isoform 3)	Phosphorylation	-	13.81	-
26	Phosphorylation	SKDVLGPSTVVANSD CCCCCCCCEEEECCC	31.84	22199227
26 (in isoform 3)	Phosphorylation	-	31.84	-
27	Phosphorylation	KDVLGPSTVVANSDE CCCCCCCEEEECCCH	23.33	22199227
32	Phosphorylation	PSTVVANSDESQLLT CCEEEECCCHHHCCC	32.77	22199227
35	Phosphorylation	VVANSDESQLLTPGK EEECCCHHHCCCCCC	30.99	29255136
39	Phosphorylation	SDESQLLTPGKMSQR CCHHHCCCCCCCCCC	38.29	29255136
44	Phosphorylation	LLTPGKMSQRQGKEA CCCCCCCCCCCCCCC	26.20	26074081
52	Phosphorylation	QRQGKEAYPTPTKDL CCCCCCCCCCCCCCC	14.55	26657352
54	Phosphorylation	QGKEAYPTPTKDLHQ CCCCCCCCCCCCCCC	30.80	26055452
56	Phosphorylation	KEAYPTPTKDLHQPS CCCCCCCCCCCCCCC	39.40	17924679
63	Phosphorylation	TKDLHQPSLSPASPH CCCCCCCCCCCCCCC	34.60	25159151
65	Phosphorylation	DLHQPSLSPASPHSQ CCCCCCCCCCCCCCC	23.82	25159151
68	Phosphorylation	QPSLSPASPHSQGFE CCCCCCCCCCCCCCC	26.91	25159151
71	Phosphorylation	LSPASPHSQGFERGK CCCCCCCCCCCCCCC	35.07	30266825
82	Phosphorylation	ERGKEDISQNKDESS CCCCHHHHCCCCCCC	39.77	30108239
88	Phosphorylation	ISQNKDESSLSMSKS HHCCCCCCCCCCCCC	46.87	30108239
89	Phosphorylation	SQNKDESSLSMSKSK HCCCCCCCCCCCCCC	23.55	30108239
91	Phosphorylation	NKDESSLSMSKSKSE CCCCCCCCCCCCCCC	23.98	25849741
93	Phosphorylation	DESSLSMSKSKSESK CCCCCCCCCCCCCHH	30.33	21815630
95	Phosphorylation	SSLSMSKSKSESKLY CCCCCCCCCCCHHCC	33.82	24719451
97	Phosphorylation	LSMSKSKSESKLYNG CCCCCCCCCHHCCCC	54.94	26074081
99	Phosphorylation	MSKSKSESKLYNGSE CCCCCCCHHCCCCCC	34.74	26074081
102	Phosphorylation	SKSESKLYNGSEKDS CCCCHHCCCCCCCCC	22.63	25002506
105	Phosphorylation	ESKLYNGSEKDSSTS CHHCCCCCCCCCCCC	37.52	24719451
107	Acetylation	KLYNGSEKDSSTSSK HCCCCCCCCCCCCCC	65.69	19813555
109	Phosphorylation	YNGSEKDSSTSSKLT CCCCCCCCCCCCCCC	46.73	25002506
110	Phosphorylation	NGSEKDSSTSSKLTK CCCCCCCCCCCCCCH	42.30	25002506
111	Phosphorylation	GSEKDSSTSSKLTKK CCCCCCCCCCCCCHH	40.76	25002506
112	Phosphorylation	SEKDSSTSSKLTKKE CCCCCCCCCCCCHHH	27.68	25002506
113	Phosphorylation	EKDSSTSSKLTKKES CCCCCCCCCCCHHHH	31.60	25002506
114	Acetylation	KDSSTSSKLTKKESL CCCCCCCCCCHHHHH	61.00	25953088
117	Acetylation	STSSKLTKKESLKVQ CCCCCCCHHHHHHHH	66.05	15605841
117	Ubiquitination	STSSKLTKKESLKVQ CCCCCCCHHHHHHHH	66.05	-
118	Acetylation	TSSKLTKKESLKVQK CCCCCCHHHHHHHHH	47.50	15605849
120	Phosphorylation	SKLTKKESLKVQKKN CCCCHHHHHHHHHHH	42.23	27422710
122	Acetylation	LTKKESLKVQKKNYR CCHHHHHHHHHHHHH	52.48	15605857
122	Ubiquitination	LTKKESLKVQKKNYR CCHHHHHHHHHHHHH	52.48	-
136	Phosphorylation	REEKKRATKELLSTI HHHHHHHHHHHHHHC	29.14	26503514
141	Phosphorylation	RATKELLSTITDPSV HHHHHHHHHCCCHHH	30.32	25072903
142	Phosphorylation	ATKELLSTITDPSVI HHHHHHHHCCCHHHE	28.06	25072903
144	Phosphorylation	KELLSTITDPSVIVM HHHHHHCCCHHHEEE	41.78	25072903
147	Phosphorylation	LSTITDPSVIVMADW HHHCCCHHHEEEECH	27.56	25072903
162	Ubiquitination	LKIRGTLKSWTKLWC HHHHCCCHHHHHEEE	43.73	-
179	Phosphorylation	KPGVLLIYKTQKNGQ CCEEEEEEEECCCCC	14.14	-
183	Acetylation	LLIYKTQKNGQWVGT EEEEEECCCCCEEEE	69.17	20167786
205	Ubiquitination	IIERPSKKDGFCFKL HHCCCCCCCCCCHHH	68.38	-
209	Ubiquitination	PSKKDGFCFKLFHPL CCCCCCCCHHHCCCH	3.43	21890473
209 (in isoform 2)	Ubiquitination	-	3.43	21890473
224	Acetylation	EQSIWAVKGPKGEAV HHEEEEEECCCCCCC	62.84	25953088
224	Ubiquitination	EQSIWAVKGPKGEAV HHEEEEEECCCCCCC	62.84	21890473
225 (in isoform 1)	Ubiquitination	-	23.66	21890473
227	Ubiquitination	IWAVKGPKGEAVGSI EEEEECCCCCCCEEC	77.41	-
240	Phosphorylation	SITQPLPSSYLIIRA ECCCCCCCCEEEEEE	39.02	-
248	Phosphorylation	SYLIIRATSESDGRC CEEEEEEECCCCCCH	24.15	-
268	Phosphorylation	ELALKCSSLLKRTMI HHHHHHHHHHHHHHH	47.38	24719451
271	Acetylation	LKCSSLLKRTMIREG HHHHHHHHHHHHHCC	51.63	25953088
271	Ubiquitination	LKCSSLLKRTMIREG HHHHHHHHHHHHHCC	51.63	-
272 (in isoform 3)	Phosphorylation	-	29.51	-
273	Phosphorylation	CSSLLKRTMIREGKE HHHHHHHHHHHCCCC	18.50	22210691
279	Ubiquitination	RTMIREGKEHDLSVS HHHHHCCCCCCEEEC	47.31	-
284	Phosphorylation	EGKEHDLSVSSDSTH CCCCCCEEECCCCCC	26.47	22496350
285 (in isoform 3)	Phosphorylation	-	9.14	-
286	Phosphorylation	KEHDLSVSSDSTHVT CCCCEEECCCCCCEE	25.67	19651622
286 (in isoform 3)	Phosphorylation	-	25.67	-
287	Phosphorylation	EHDLSVSSDSTHVTF CCCEEECCCCCCEEE	33.16	22496350
289	Phosphorylation	DLSVSSDSTHVTFYG CEEECCCCCCEEEEE	23.51	19651622
289 (in isoform 3)	Phosphorylation	-	23.51	-
293	Phosphorylation	SSDSTHVTFYGLLRA CCCCCCEEEEEEHHC	11.97	28796482
295	Phosphorylation	DSTHVTFYGLLRANN CCCCEEEEEEHHCCC	9.48	25884760
300 (in isoform 3)	Phosphorylation	-	14.83	-
305	Phosphorylation	LRANNLHSGDNFQLN HHCCCCCCCCCCCCC	51.51	30266825
308 (in isoform 3)	Phosphorylation	-	30.04	-
311 (in isoform 3)	Phosphorylation	-	7.23	-
313 (in isoform 3)	Phosphorylation	-	57.13	-
314	Phosphorylation	DNFQLNDSEIERQHF CCCCCCHHHHHHHHC	39.12	29255136
315 (in isoform 3)	Phosphorylation	-	52.30	-
316 (in isoform 3)	Phosphorylation	-	6.48	-
327	Phosphorylation	HFKDQDMYSDKSDKE HCCCCCCCCCCCCCC	23.23	23927012
328	Phosphorylation	FKDQDMYSDKSDKEN CCCCCCCCCCCCCCC	31.74	28355574
331	Phosphorylation	QDMYSDKSDKENDQE CCCCCCCCCCCCCCC	59.93	25159151
342	Phosphorylation	NDQEHDESDNEVMGK CCCCCCCHHHCCCCC	52.36	28355574
350	Phosphorylation	DNEVMGKSEESDTDT HHCCCCCCCCCCCCC	40.65	21082442
353	Phosphorylation	VMGKSEESDTDTSER CCCCCCCCCCCCCCC	41.58	21082442
355	Phosphorylation	GKSEESDTDTSERQD CCCCCCCCCCCCCCC	50.92	30631047
357	Phosphorylation	SEESDTDTSERQDDS CCCCCCCCCCCCCCC	34.28	30631047
358	Phosphorylation	EESDTDTSERQDDSY CCCCCCCCCCCCCCC	33.32	30631047
364	Phosphorylation	TSERQDDSYIEPEPV CCCCCCCCCCCCCCC	35.98	29255136
365	Phosphorylation	SERQDDSYIEPEPVE CCCCCCCCCCCCCCC	19.12	27251275
405	Phosphorylation	TVSEENKSLIWTLLK ECCHHHHHHHHHHHH	36.35	29396449
409	Phosphorylation	ENKSLIWTLLKQVRP HHHHHHHHHHHHHCC	18.41	29396449
412	Ubiquitination	SLIWTLLKQVRPGMD HHHHHHHHHHCCCCC	50.27	-
501	Phosphorylation	CLWIHPRTNSKTFYI EEEEECCCCCCEEEE	48.58	29052541
503	Phosphorylation	WIHPRTNSKTFYIAE EEECCCCCCEEEEEE	32.24	29052541
505	Phosphorylation	HPRTNSKTFYIAEQV ECCCCCCEEEEEEEE	22.84	29052541
507	Phosphorylation	RTNSKTFYIAEQVSH CCCCCEEEEEEEECC	12.40	29052541
513	Phosphorylation	FYIAEQVSHHPPISA EEEEEEECCCCCCEE	18.77	29052541
519	Phosphorylation	VSHHPPISAFYVSNR ECCCCCCEEEEEECC	20.35	29052541
522	Phosphorylation	HPPISAFYVSNRKDG CCCCEEEEEECCCCC	11.59	29052541
524	Phosphorylation	PISAFYVSNRKDGFC CCEEEEEECCCCCEE	21.38	29052541
540	Phosphorylation	SGSILAKSKFYGNSL CCHHHCCCCCCCCCH	23.53	28152594
543	Phosphorylation	ILAKSKFYGNSLSAI HHCCCCCCCCCHHHH	21.09	28152594
546	Phosphorylation	KSKFYGNSLSAILEG CCCCCCCCHHHHHHC	21.24	28152594
548	Phosphorylation	KFYGNSLSAILEGEA CCCCCCHHHHHHCEE	17.06	28152594
590	Phosphorylation	MTLELGGTVNITCQK EEEEECCEEEEEEEC	14.47	22210691
594	Phosphorylation	LGGTVNITCQKTGYS ECCEEEEEEECCCCE	12.04	22210691
598	Phosphorylation	VNITCQKTGYSAILE EEEEEECCCCEEEEE	18.57	28152594
600	Phosphorylation	ITCQKTGYSAILEFK EEEECCCCEEEEEEE	10.52	28152594
601	Phosphorylation	TCQKTGYSAILEFKL EEECCCCEEEEEEEE	15.35	28152594
609	Ubiquitination	AILEFKLKPFLGSSD EEEEEEECCCCCCHH	34.02	-
614	Phosphorylation	KLKPFLGSSDCVNQI EECCCCCCHHHHHHH	25.75	25627689
615	Phosphorylation	LKPFLGSSDCVNQIS ECCCCCCHHHHHHHC	32.98	25627689
624	Ubiquitination	CVNQISGKLKLGKEV HHHHHCCCCCCCHHH	35.34	-
649	Ubiquitination	EVFITDKKTDNSEVF EEEEEECCCCCCCCC	65.01	-
664	Ubiquitination	WNPTPDIKQWRLIRH CCCCCCHHHHHHHEE	51.71	-
685	Ubiquitination	QGDFESEKLWQRVTR HCCCCHHHHHHHHHH	65.39	-
697	Ubiquitination	VTRAINAKDQTEATQ HHHHHCCCCCCHHHH	45.97	-
706	Ubiquitination	QTEATQEKYVLEEAQ CCHHHHHHHHHHHHH	30.73	-
730	Ubiquitination	KNEEWSCKLFELDPL CCCHHEEEEEEECCC	51.17	-
732 (in isoform 3)	Phosphorylation	-	5.53	-
756 (in isoform 3)	Phosphorylation	-	43.15	-
762	Ubiquitination	NDMIQFEKDGVIQTK HHCEEECCCCEEEEE	62.16	-
765 (in isoform 3)	Phosphorylation	-	4.15	-
766 (in isoform 3)	Phosphorylation	-	5.42	-
768 (in isoform 3)	Phosphorylation	-	27.04	-
769	Acetylation	KDGVIQTKVKHRTPM CCCEEEEEECCCCCC	32.67	25953088
769	Ubiquitination	KDGVIQTKVKHRTPM CCCEEEEEECCCCCC	32.67	-
772 (in isoform 3)	Phosphorylation	-	41.66	-
774	Phosphorylation	QTKVKHRTPMVSVPK EEEECCCCCCCCCCC	18.56	25159151
778	Phosphorylation	KHRTPMVSVPKMKHK CCCCCCCCCCCCCCC	26.84	28555341
797	Phosphorylation	QKKVAKGYSSPEPDI HHHHHCCCCCCCCCC	12.79	23927012
798	Phosphorylation	KKVAKGYSSPEPDIQ HHHHCCCCCCCCCCC	48.35	23927012
799	Phosphorylation	KVAKGYSSPEPDIQD HHHCCCCCCCCCCCC	25.46	30278072
801 (in isoform 2)	Ubiquitination	-	58.51	21890473
807	Phosphorylation	PEPDIQDSSGSEAQS CCCCCCCCCCCCCCC	21.89	23927012
808	Phosphorylation	EPDIQDSSGSEAQSV CCCCCCCCCCCCCCC	55.41	25159151
810	Phosphorylation	DIQDSSGSEAQSVKP CCCCCCCCCCCCCCC	31.54	25159151
814	Phosphorylation	SSGSEAQSVKPSTRR CCCCCCCCCCCCCCC	38.87	30278072
816	Ubiquitination	GSEAQSVKPSTRRKK CCCCCCCCCCCCCCC	38.20	2190698
817 (in isoform 1)	Ubiquitination	-	38.48	21890473
818	Phosphorylation	EAQSVKPSTRRKKGI CCCCCCCCCCCCCCC	28.91	23927012
819	Phosphorylation	AQSVKPSTRRKKGIE CCCCCCCCCCCCCCC	42.91	23927012
823	Ubiquitination	KPSTRRKKGIELGDI CCCCCCCCCCCHHHH	64.41	-
832	Phosphorylation	IELGDIQSSIESIKQ CCHHHHHHHHHHHHH	33.35	26471730
833	Phosphorylation	ELGDIQSSIESIKQT CHHHHHHHHHHHHHH	17.63	26471730
836	Phosphorylation	DIQSSIESIKQTQEE HHHHHHHHHHHHHHH	33.16	26471730
838	Ubiquitination	QSSIESIKQTQEEIK HHHHHHHHHHHHHHH	57.48	-
840	Phosphorylation	SIESIKQTQEEIKRN HHHHHHHHHHHHHHH	32.71	-
864	Phosphorylation	SSTPATDYFLQQKDY CCCCCHHHHHHCHHH	11.22	-

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 OSBL8_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of OSBL8_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 OSBL8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of OSBL8_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 OSBL8_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-314; SER-807 ANDSER-808, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-65; SER-68; SER-314;SER-807; SER-808; SER-810 AND SER-814, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-65 AND SER-68, AND MASSSPECTROMETRY.	18220336 [Abstract]
"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-328; SER-342; SER-350;SER-353; THR-355; THR-357; SER-358; SER-798; SER-799; SER-807; SER-808AND SER-810, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52 AND THR-56, AND MASSSPECTROMETRY.	17924679 [Abstract]