OMGP_HUMAN - dbPTM
OMGP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OMGP_HUMAN
UniProt AC P23515
Protein Name Oligodendrocyte-myelin glycoprotein
Gene Name OMG
Organism Homo sapiens (Human).
Sequence Length 440
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor.
Protein Description Cell adhesion molecule contributing to the interactive process required for myelination in the central nervous system..
Protein Sequence MEYQILKMSLCLFILLFLTPGILCICPLQCICTERHRHVDCSGRNLSTLPSGLQENIIHLNLSYNHFTDLHNQLTQYTNLRTLDISNNRLESLPAHLPRSLWNMSAANNNIKLLDKSDTAYQWNLKYLDVSKNMLEKVVLIKNTLRSLEVLNLSSNKLWTVPTNMPSKLHIVDLSNNSLTQILPGTLINLTNLTHLYLHNNKFTFIPDQSFDQLFQLQEITLYNNRWSCDHKQNITYLLKWMMETKAHVIGTPCSTQISSLKEHNMYPTPSGFTSSLFTVSGMQTVDTINSLSVVTQPKVTKIPKQYRTKETTFGATLSKDTTFTSTDKAFVPYPEDTSTETINSHEAAAATLTIHLQDGMVTNTSLTSSTKSSPTPMTLSITSGMPNNFSEMPQQSTTLNLWREETTTNVKTPLPSVANAWKVNASFLLLLNVVVMLAV
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
45N-linked_GlycosylationHVDCSGRNLSTLPSG
CCCCCCCCHHCCCCC
41.70UniProtKB CARBOHYD
61N-linked_GlycosylationQENIIHLNLSYNHFT
HHCEEEEEECCCCHH
16.87UniProtKB CARBOHYD
103N-linked_GlycosylationHLPRSLWNMSAANNN
CCCHHHHCHHHCCCC
21.59UniProtKB CARBOHYD
112UbiquitinationSAANNNIKLLDKSDT
HHCCCCEEEECCCCC
45.1630230243
132AcetylationLKYLDVSKNMLEKVV
CEEEECCHHHHHHHH
46.3419413330
152N-linked_GlycosylationLRSLEVLNLSSNKLW
HHCCEEEECCCCCCE
42.95UniProtKB CARBOHYD
154O-linked_GlycosylationSLEVLNLSSNKLWTV
CCEEEECCCCCCEEE
30.6928657654
167PhosphorylationTVPTNMPSKLHIVDL
EECCCCCCCEEEEEC
36.7629116813
176N-linked_GlycosylationLHIVDLSNNSLTQIL
EEEEECCCCCCCCCC
49.78UniProtKB CARBOHYD
189N-linked_GlycosylationILPGTLINLTNLTHL
CCCCCEEECCCCEEE
43.88UniProtKB CARBOHYD
192N-linked_GlycosylationGTLINLTNLTHLYLH
CCEEECCCCEEEEEE
46.22UniProtKB CARBOHYD
234N-linked_GlycosylationWSCDHKQNITYLLKW
CCCCHHHHHHHHHHH
33.11UniProtKB CARBOHYD
236PhosphorylationCDHKQNITYLLKWMM
CCHHHHHHHHHHHHH
18.7024114839
237PhosphorylationDHKQNITYLLKWMME
CHHHHHHHHHHHHHH
13.2624114839
259PhosphorylationTPCSTQISSLKEHNM
CCCHHHHHHHHHCCC
21.5724719451
285PhosphorylationFTVSGMQTVDTINSL
EEECCCCEEEECCEE
16.08-
301PhosphorylationVVTQPKVTKIPKQYR
EEECCCCCCCCCCCC
29.40-
312PhosphorylationKQYRTKETTFGATLS
CCCCCCCCCCCCEEC
29.05-
313PhosphorylationQYRTKETTFGATLSK
CCCCCCCCCCCEECC
22.59-
317PhosphorylationKETTFGATLSKDTTF
CCCCCCCEECCCCCC
31.76-
364N-linked_GlycosylationLQDGMVTNTSLTSST
ECCCCEEECCCCCCC
19.09UniProtKB CARBOHYD
389N-linked_GlycosylationITSGMPNNFSEMPQQ
EECCCCCCHHCCCCC
35.63UniProtKB CARBOHYD
417GPI-anchorNVKTPLPSVANAWKV
CCCCCCCCHHHHHHC
41.36-
425N-linked_GlycosylationVANAWKVNASFLLLL
HHHHHHCCHHHHHHH
26.58UniProtKB CARBOHYD

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 OMGP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OMGP_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 OMGP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of OMGP_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 OMGP_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP