GPNMB_HUMAN - dbPTM
GPNMB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPNMB_HUMAN
UniProt AC Q14956
Protein Name Transmembrane glycoprotein NMB
Gene Name GPNMB
Organism Homo sapiens (Human).
Sequence Length 572
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Detected at the cell surface in different types of cancers cells, including glioblastoma multiforme cell
Protein Description Could be a melanogenic enzyme..
Protein Sequence MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDANGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVSTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENSPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS
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
35PhosphorylationVLGNERPSAYMREHN
HHCCCCCCHHHHHHC		37.9525278378
37PhosphorylationGNERPSAYMREHNQL
CCCCCCHHHHHHCCC		10.8825278378
93N-linked_GlycosylationSPALVGSNITFAVNL
CCCCCCCCEEEEEEE		31.24UniProtKB CARBOHYD
134N-linked_GlycosylationSADPYVYNWTAWSED
CCCCCEEEEEECCCC		21.41UniProtKB CARBOHYD
146N-linked_GlycosylationSEDSDGENGTGQSHH
CCCCCCCCCCCCCCC		59.88UniProtKB CARBOHYD
195PhosphorylationGRCSVRVSVNTANVT
CCCEEEEEECCCCCE		10.0922210691
198PhosphorylationSVRVSVNTANVTLGP
EEEEEECCCCCEECC		19.9022210691
200N-linked_GlycosylationRVSVNTANVTLGPQL
EEEECCCCCEECCEE		25.8519159218
202PhosphorylationSVNTANVTLGPQLME
EECCCCCEECCEEEE		26.2922210691
211PhosphorylationGPQLMEVTVYRRHGR
CCEEEEEEEEEECCE		9.8622210691
213PhosphorylationQLMEVTVYRRHGRAY
EEEEEEEEEECCEEE		7.8022210691
220PhosphorylationYRRHGRAYVPIAQVK
EEECCEEEEEEEEEE		12.85-
230PhosphorylationIAQVKDVYVVTDQIP
EEEEEEEEEEECCCE		10.19-
249N-linked_GlycosylationMFQKNDRNSSDETFL
EEECCCCCCCCCHHH		49.0519159218
275N-linked_GlycosylationHDPSHFLNYSTINYK
CCHHHHCCCEEEEEE		27.9719159218
296N-linked_GlycosylationTGLFVSTNHTVNHTY
CEEEEECCCEECEEE		22.7119159218
300N-linked_GlycosylationVSTNHTVNHTYVLNG
EECCCEECEEEEECC		23.9619159218
306N-linked_GlycosylationVNHTYVLNGTFSLNL
ECEEEEECCEEEEEE		37.1019159218
312N-linked_GlycosylationLNGTFSLNLTVKAAA
ECCEEEEEEEEEECC		32.25UniProtKB CARBOHYD
350O-linked_GlycosylationLKSYDSNTPGPAGDN
HHHCCCCCCCCCCCC		33.31OGP
457PhosphorylationCLLTVRRTFNGSGTY
EEEEEEECCCCCCEE		15.7625332170
459N-linked_GlycosylationLTVRRTFNGSGTYCV
EEEEECCCCCCEEEE		43.01UniProtKB CARBOHYD
467N-linked_GlycosylationGSGTYCVNLTLGDDT
CCCEEEEEEEECCCC		24.60UniProtKB CARBOHYD
474PhosphorylationNLTLGDDTSLALTST
EEEECCCCEEEEEEE		30.3125332170
480PhosphorylationDTSLALTSTLISVPD
CCEEEEEEEEEECCC		23.2825332170
499PhosphorylationSPLRMANSALISVGC
CHHHHHHHHHHHHHH		18.21-
503PhosphorylationMANSALISVGCLAIF
HHHHHHHHHHHHHHH		17.20-
523UbiquitinationLLVYKKHKEYNPIEN
HHHHHHCCCCCCCCC		71.43-
531PhosphorylationEYNPIENSPGNVVRS
CCCCCCCCCCCCEEC		22.7629255136
539UbiquitinationPGNVVRSKGLSVFLN
CCCCEECCCHHHHCC		53.99-
542PhosphorylationVVRSKGLSVFLNRAK
CEECCCHHHHCCCCE		21.3529514088
549UbiquitinationSVFLNRAKAVFFPGN
HHHCCCCEEEEECCC		41.67-
559UbiquitinationFFPGNQEKDPLLKNQ
EECCCCCCCCCCCCC		55.68-
564UbiquitinationQEKDPLLKNQEFKGV
CCCCCCCCCCCCCCC		65.35-
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 GPNMB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPNMB_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 GPNMB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GPNMB_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
D09623 Glembatumumab (USAN/INN)
D09912 Glembatumumab vedotin (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPNMB_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-200; ASN-249; ASN-275;ASN-296; ASN-300 AND ASN-306, AND MASS SPECTROMETRY.

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