GP108_HUMAN - dbPTM
GP108_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GP108_HUMAN
UniProt AC Q9NPR9
Protein Name Protein GPR108
Gene Name GPR108
Organism Homo sapiens (Human).
Sequence Length 543
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MAVSERRGLGRGSPAEWGQRLLLVLLLGGCSGRIHQLALTGEKRADIQLNSFGFYTNGSLEVELSVLRLGLREAEEKSLLVGFSLSRVRSGRVRSYSTRDFQDCPLQKNSSSFLVLFLINTKDLQVQVRKYGEQKTLFIFPGLLPEAPSKPGLPKPQATVPRKVDGGGTSAASKPKSTPAVIQGPSGKDKDLVLGLSHLNNSYNFSFHVVIGSQAEEGQYSLNFHNCNNSVPGKEHPFDITVMIREKNPDGFLSAAEMPLFKLYMVMSACFLAAGIFWVSILCRNTYSVFKIHWLMAALAFTKSISLLFHSINYYFINSQGHPIEGLAVMYYIAHLLKGALLFITIALIGSGWAFIKYVLSDKEKKVFGIVIPMQVLANVAYIIIESREEGASDYVLWKEILFLVDLICCGAILFPVVWSIRHLQDASGTDGKVAVNLAKLKLFRHYYVMVICYVYFTRIIAILLQVAVPFQWQWLYQLLVEGSTLAFFVLTGYKFQPTGNNPYLQLPQEDEEDVQMEQVMTDSGFREGLSKVNKTASGRELL
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
57N-linked_GlycosylationNSFGFYTNGSLEVEL
EEEEEECCCCEEEEE
27.03UniProtKB CARBOHYD
65PhosphorylationGSLEVELSVLRLGLR
CCEEEEEEHHHHCCC
12.9524719451
109N-linked_GlycosylationQDCPLQKNSSSFLVL
CCCCCCCCCCCEEEE
33.88UniProtKB CARBOHYD
159PhosphorylationGLPKPQATVPRKVDG
CCCCCCCCCCEEECC
26.2924719451
169PhosphorylationRKVDGGGTSAASKPK
EEECCCCCCCCCCCC
20.6124114839
169O-linked_GlycosylationRKVDGGGTSAASKPK
EEECCCCCCCCCCCC
20.61OGP
170O-linked_GlycosylationKVDGGGTSAASKPKS
EECCCCCCCCCCCCC
25.7230620550
173PhosphorylationGGGTSAASKPKSTPA
CCCCCCCCCCCCCCC
49.5624114839
173O-linked_GlycosylationGGGTSAASKPKSTPA
CCCCCCCCCCCCCCC
49.5630620550
177O-linked_GlycosylationSAASKPKSTPAVIQG
CCCCCCCCCCCEEEC
48.4255833219
178O-linked_GlycosylationAASKPKSTPAVIQGP
CCCCCCCCCCEEECC
22.7655833223
200N-linked_GlycosylationVLGLSHLNNSYNFSF
EEEEECCCCCCEEEE
29.94UniProtKB CARBOHYD
204N-linked_GlycosylationSHLNNSYNFSFHVVI
ECCCCCCEEEEEEEE
26.38UniProtKB CARBOHYD
228N-linked_GlycosylationSLNFHNCNNSVPGKE
EEEEECCCCCCCCCC
49.48UniProtKB CARBOHYD
241PhosphorylationKEHPFDITVMIREKN
CCCCCEEEEEEEECC
13.0827251275
302PhosphorylationLMAALAFTKSISLLF
HHHHHHHHHHHHHHH
20.48-
433UbiquitinationDASGTDGKVAVNLAK
HCCCCCCHHHHHHHH
29.812190698
532UbiquitinationGFREGLSKVNKTASG
HHHHHHHHCCCCCCC
55.67-
534N-linked_GlycosylationREGLSKVNKTASGRE
HHHHHHCCCCCCCCC
39.43UniProtKB CARBOHYD
535UbiquitinationEGLSKVNKTASGREL
HHHHHCCCCCCCCCC
48.75-
536PhosphorylationGLSKVNKTASGRELL
HHHHCCCCCCCCCCC
22.3523186163
538PhosphorylationSKVNKTASGRELL--
HHCCCCCCCCCCC--
43.5528857561

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 GP108_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GP108_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 GP108_HUMAN !!

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

Oops, there are no PPI records of GP108_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 GP108_HUMAN

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Related Literatures of Post-Translational Modification

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