OSBL2_HUMAN - dbPTM
OSBL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSBL2_HUMAN
UniProt AC Q9H1P3
Protein Name Oxysterol-binding protein-related protein 2
Gene Name OSBPL2
Organism Homo sapiens (Human).
Sequence Length 480
Subcellular Localization
Protein Description Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate. [PubMed: 11279184 Binds 25-hydroxycholesterol]
Protein Sequence MNGEEEFFDAVTGFDSDNSSGEFSEANQKVTGMIDLDTSKNNRIGKTGERPSQENGIQKHRTSLPAPMFSRSDFSVWTILKKCVGLELSKITMPIAFNEPLSFLQRITEYMEHVYLIHRASCQPQPLERMQSVAAFAVSAVASQWERTGKPFNPLLGETYELIREDLGFRFISEQVSHHPPISAFHSEGLNHDFLFHGSIYPKLKFWGKSVEAEPRGTITLELLKHNEAYTWTNPTCCVHNVIIGKLWIEQYGTVEILNHRTGHKCVLHFKPCGLFGKELHKVEGHIQDKNKKKLFMIYGKWTECLWGIDPVSYESFKKQERRGDHLRKAKLDEDSGKADSDVADDVPVAQETVQVIPGSKLLWRINTRPPNSAQMYNFTSFTVSLNELETGMEKTLPPTDCRLRPDIRGMENGNMDLASQEKERLEEKQREARRERAKEEAEWQTRWFYPGNNPYTGTPDWLYAGDYFERNFSDCPDIY
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
12PhosphorylationEEFFDAVTGFDSDNS
HHHHHHHCCCCCCCC
33.5727251275
16PhosphorylationDAVTGFDSDNSSGEF
HHHCCCCCCCCCCCC
36.1127251275
19PhosphorylationTGFDSDNSSGEFSEA
CCCCCCCCCCCCCHH
44.7227251275
20PhosphorylationGFDSDNSSGEFSEAN
CCCCCCCCCCCCHHH
48.9011735225
38PhosphorylationTGMIDLDTSKNNRIG
ECEEECCCCCCCCCC
49.2322199227
39PhosphorylationGMIDLDTSKNNRIGK
CEEECCCCCCCCCCC
32.8121815630
47PhosphorylationKNNRIGKTGERPSQE
CCCCCCCCCCCCCHH
38.78-
52PhosphorylationGKTGERPSQENGIQK
CCCCCCCCHHCCCCC
57.2425159151
59UbiquitinationSQENGIQKHRTSLPA
CHHCCCCCCCCCCCC
32.88-
62PhosphorylationNGIQKHRTSLPAPMF
CCCCCCCCCCCCCCC
34.0428348404
63PhosphorylationGIQKHRTSLPAPMFS
CCCCCCCCCCCCCCC
32.1024719451
81UbiquitinationFSVWTILKKCVGLEL
HHHHHHHHHHHCCCH
40.03-
138 (in isoform 2)Ubiquitination-2.8121890473
150 (in isoform 1)Ubiquitination-45.9121890473
150UbiquitinationSQWERTGKPFNPLLG
HHHHHHCCCCCHHHH
45.9121906983
160PhosphorylationNPLLGETYELIREDL
CHHHHHHHHHHHHHC
12.3927642862
197 (in isoform 2)Ubiquitination-31.1021890473
209UbiquitinationPKLKFWGKSVEAEPR
CCCCCCEECCEECCC
41.7621890473
209 (in isoform 1)Ubiquitination-41.7621890473
282UbiquitinationLFGKELHKVEGHIQD
CCCHHHHHEECEEEC
55.39-
349 (in isoform 2)Ubiquitination-9.6121890473
361UbiquitinationVQVIPGSKLLWRINT
EEECCCCEEEEEEEC
54.222190698
361 (in isoform 1)Ubiquitination-54.2221890473
411 (in isoform 2)Ubiquitination-2.31-
423UbiquitinationMDLASQEKERLEEKQ
CCHHHHHHHHHHHHH
40.26-
439UbiquitinationEARRERAKEEAEWQT
HHHHHHHHHHHHHCC
63.41-
474PhosphorylationDYFERNFSDCPDIY-
CHHHHCCCCCCCCC-
41.6827251275

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 OSBL2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSBL2_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 OSBL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZFPL1_HUMANZFPL1physical
28514442
BIRC6_HUMANBIRC6physical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
616340Deafness, autosomal dominant, 67 (DFNA67)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OSBL2_HUMAN

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Related Literatures of Post-Translational Modification

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