OSBL5_HUMAN - dbPTM
OSBL5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSBL5_HUMAN
UniProt AC Q9H0X9
Protein Name Oxysterol-binding protein-related protein 5
Gene Name OSBPL5
Organism Homo sapiens (Human).
Sequence Length 879
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Localizes to the cortical endoplasmic reticulum at the endoplasmic reticulum-plasma membrane contact sites.
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: 23934110]
Protein Sequence MKEEAFLRRRFSLCPPSSTPQKVDPRKLTRNLLLSGDNELYPLSPGKDMEPNGPSLPRDEGPPTPSSATKVPPAEYRLCNGSDKECVSPTARVTKKETLKAQKENYRQEKKRATRQLLSALTDPSVVIMADSLKIRGTLKSWTKLWCVLKPGVLLIYKTPKVGQWVGTVLLHCCELIERPSKKDGFCFKLFHPLDQSVWAVKGPKGESVGSITQPLPSSYLIFRAASESDGRCWLDALELALRCSSLLRLGTCKPGRDGEPGTSPDASPSSLCGLPASATVHPDQDLFPLNGSSLENDAFSDKSERENPEESDTETQDHSRKTESGSDQSETPGAPVRRGTTYVEQVQEELGELGEASQVETVSEENKSLMWTLLKQLRPGMDLSRVVLPTFVLEPRSFLNKLSDYYYHADLLSRAAVEEDAYSRMKLVLRWYLSGFYKKPKGIKKPYNPILGETFRCCWFHPQTDSRTFYIAEQVSHHPPVSAFHVSNRKDGFCISGSITAKSRFYGNSLSALLDGKATLTFLNRAEDYTLTMPYAHCKGILYGTMTLELGGKVTIECAKNNFQAQLEFKLKPFFGGSTSINQISGKITSGEEVLASLSGHWDRDVFIKEEGSGSSALFWTPSGEVRRQRLRQHTVPLEEQTELESERLWQHVTRAISKGDQHRATQEKFALEEAQRQRARERQESLMPWKPQLFHLDPITQEWHYRYEDHSPWDPLKDIAQFEQDGILRTLQQEAVARQTTFLGSPGPRHERSGPDQRLRKASDQPSGHSQATESSGSTPESCPELSDEEQDGDFVPGGESPCPRCRKEARRLQALHEAILSIREAQQELHRHLSAMLSSTARAAQAPTPGLLQSPRSWFLLCVFLACQLFINHILK
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
12PhosphorylationAFLRRRFSLCPPSST
HHHHHHHCCCCCCCC		27.5325849741
17PhosphorylationRFSLCPPSSTPQKVD
HHCCCCCCCCCCCCC		31.8028450419
18PhosphorylationFSLCPPSSTPQKVDP
HCCCCCCCCCCCCCH		50.2928450419
19PhosphorylationSLCPPSSTPQKVDPR
CCCCCCCCCCCCCHH		33.7923882029
35PhosphorylationLTRNLLLSGDNELYP
HHHHEEECCCCCEEE		44.0328450419
41PhosphorylationLSGDNELYPLSPGKD
ECCCCCEEECCCCCC		8.9228450419
44PhosphorylationDNELYPLSPGKDMEP
CCCEEECCCCCCCCC		27.4021815630
47UbiquitinationLYPLSPGKDMEPNGP
EEECCCCCCCCCCCC		58.23-
55PhosphorylationDMEPNGPSLPRDEGP
CCCCCCCCCCCCCCC		53.0223403867
64PhosphorylationPRDEGPPTPSSATKV
CCCCCCCCCCCCCCC		38.6530266825
66PhosphorylationDEGPPTPSSATKVPP
CCCCCCCCCCCCCCH		34.7730266825
67PhosphorylationEGPPTPSSATKVPPA
CCCCCCCCCCCCCHH		40.9530266825
69PhosphorylationPPTPSSATKVPPAEY
CCCCCCCCCCCHHHE		34.2330266825
70UbiquitinationPTPSSATKVPPAEYR
CCCCCCCCCCHHHEE		53.08-
82PhosphorylationEYRLCNGSDKECVSP
HEEECCCCCCCCCCC		31.3625849741
84UbiquitinationRLCNGSDKECVSPTA
EECCCCCCCCCCCCC		55.50-
88PhosphorylationGSDKECVSPTARVTK
CCCCCCCCCCCCCCH		28.3521815630
90PhosphorylationDKECVSPTARVTKKE
CCCCCCCCCCCCHHH		21.4223927012
100AcetylationVTKKETLKAQKENYR
CCHHHHHHHHHHHHH		57.087709857
103UbiquitinationKETLKAQKENYRQEK
HHHHHHHHHHHHHHH		53.43-
132PhosphorylationSVVIMADSLKIRGTL
CEEEECCCCCCCCCC		23.25-
140UbiquitinationLKIRGTLKSWTKLWC
CCCCCCCHHHHHEEE		43.73-
157PhosphorylationKPGVLLIYKTPKVGQ
CCCEEEEEECCCCCH		14.58-
183UbiquitinationLIERPSKKDGFCFKL
HHHCCCCCCCCEEEE		68.38-
202UbiquitinationDQSVWAVKGPKGESV
CCEEEEEECCCCCCC		62.84-
205UbiquitinationVWAVKGPKGESVGSI
EEEEECCCCCCCCCC		81.58-
246PhosphorylationELALRCSSLLRLGTC
HHHHHHHHHHHCCCC		34.7424719451
254UbiquitinationLLRLGTCKPGRDGEP
HHHCCCCCCCCCCCC		50.79-
293PhosphorylationDLFPLNGSSLENDAF
CCCCCCCCCCCCCCC		30.58-
301PhosphorylationSLENDAFSDKSEREN
CCCCCCCCCCCCCCC		45.94-
304PhosphorylationNDAFSDKSERENPEE
CCCCCCCCCCCCCCC		47.0421955146
312PhosphorylationERENPEESDTETQDH
CCCCCCCCCCCCCCC		48.4423401153
313UbiquitinationRENPEESDTETQDHS
CCCCCCCCCCCCCCC		52.41-
314PhosphorylationENPEESDTETQDHSR
CCCCCCCCCCCCCCC		50.6529255136
316PhosphorylationPEESDTETQDHSRKT
CCCCCCCCCCCCCCC		41.1922167270
320PhosphorylationDTETQDHSRKTESGS
CCCCCCCCCCCCCCC		43.7023927012
323PhosphorylationTQDHSRKTESGSDQS
CCCCCCCCCCCCCCC		33.9823663014
325PhosphorylationDHSRKTESGSDQSET
CCCCCCCCCCCCCCC		49.1529255136
327PhosphorylationSRKTESGSDQSETPG
CCCCCCCCCCCCCCC		41.5823663014
330PhosphorylationTESGSDQSETPGAPV
CCCCCCCCCCCCCCC		48.7223663014
332PhosphorylationSGSDQSETPGAPVRR
CCCCCCCCCCCCCCC		32.0623663014
334UbiquitinationSDQSETPGAPVRRGT
CCCCCCCCCCCCCCC		50.3521890473
334UbiquitinationSDQSETPGAPVRRGT
CCCCCCCCCCCCCCC		50.3521890473
379MethylationWTLLKQLRPGMDLSR
HHHHHHHCCCCCHHH		24.1930760571
402UbiquitinationEPRSFLNKLSDYYYH
CCHHHHHHHHHHHHH		52.0621890473
507PhosphorylationITAKSRFYGNSLSAL
EEECCCCCCCCHHHH		17.8122817900
591PhosphorylationQISGKITSGEEVLAS
HEECEECCCHHHHHH		47.91-
622PhosphorylationGSSALFWTPSGEVRR
CCCEEEECCCHHHHH		10.55-
624PhosphorylationSALFWTPSGEVRRQR
CEEEECCCHHHHHHH		39.96-
636PhosphorylationRQRLRQHTVPLEEQT
HHHHHHCCCCHHHHC		18.5827732954
655PhosphorylationERLWQHVTRAISKGD
HHHHHHHHHHHHHHH		16.5624719451
670UbiquitinationQHRATQEKFALEEAQ
HHHHHHHHHHHHHHH		26.56-
709PhosphorylationTQEWHYRYEDHSPWD
CCEEHHHCCCCCCCC		20.67-
742PhosphorylationQEAVARQTTFLGSPG
HHHHHHHCCCCCCCC		17.6023403867
743PhosphorylationEAVARQTTFLGSPGP
HHHHHHCCCCCCCCC		14.4423927012
747PhosphorylationRQTTFLGSPGPRHER
HHCCCCCCCCCCCCC		28.9123401153
755PhosphorylationPGPRHERSGPDQRLR
CCCCCCCCCCCHHHH		52.25-
765PhosphorylationDQRLRKASDQPSGHS
CHHHHHHHCCCCCCC		39.55-
769PhosphorylationRKASDQPSGHSQATE
HHHHCCCCCCCCCCC		43.4318767875
775PhosphorylationPSGHSQATESSGSTP
CCCCCCCCCCCCCCC		28.8518767875
777PhosphorylationGHSQATESSGSTPES
CCCCCCCCCCCCCCC		35.33-
778PhosphorylationHSQATESSGSTPESC
CCCCCCCCCCCCCCC		30.45-
780PhosphorylationQATESSGSTPESCPE
CCCCCCCCCCCCCCC		42.61-
781PhosphorylationATESSGSTPESCPEL
CCCCCCCCCCCCCCC		34.3028348404
784PhosphorylationSSGSTPESCPELSDE
CCCCCCCCCCCCCCC		35.8528348404
789PhosphorylationPESCPELSDEEQDGD
CCCCCCCCCCCCCCC		41.1228348404
824PhosphorylationALHEAILSIREAQQE
HHHHHHHHHHHHHHH		17.3127535140
837PhosphorylationQELHRHLSAMLSSTA
HHHHHHHHHHHHHHH		12.9018767875
841PhosphorylationRHLSAMLSSTARAAQ
HHHHHHHHHHHHHHH		16.7418767875
842PhosphorylationHLSAMLSSTARAAQA
HHHHHHHHHHHHHHC		23.3318767875
843PhosphorylationLSAMLSSTARAAQAP
HHHHHHHHHHHHHCC		19.4518767875
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 OSBL5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSBL5_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 OSBL5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPC1_HUMANNPC1physical
21220512
A4_HUMANAPPphysical
21832049
PRR11_HUMANPRR11physical
28514442
OSBL8_HUMANOSBPL8physical
28514442
ANAG_HUMANNAGLUphysical
28514442
PLD1_HUMANPLD1physical
28514442
KLH23_HUMANKLHL23physical
28514442
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 OSBL5_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-747, AND MASSSPECTROMETRY.
"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-747, 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-747, AND MASSSPECTROMETRY.

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