GNPTA_HUMAN - dbPTM
GNPTA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNPTA_HUMAN
UniProt AC Q3T906
Protein Name N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
Gene Name GNPTAB
Organism Homo sapiens (Human).
Sequence Length 1256
Subcellular Localization N-acetylglucosamine-1-phosphotransferase subunit alpha: Golgi apparatus membrane
Single-pass type I membrane protein .
N-acetylglucosamine-1-phosphotransferase subunit beta: Golgi apparatus membrane
Single-pass type II membrane protein .
Protein Description Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment..
Protein Sequence MLFKLLQRQTYTCLSHRYGLYVCFLGVVVTIVSAFQFGEVVLEWSRDQYHVLFDSYRDNIAGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELQQVREQMEEEQKAMREILGKNTTEPTKKSEKQLECLLTHCIKVPMLVLDPALPANITLKDLPSLYPSFHSASDIFNVAKPKNPSTNVSVVVFDSTKDVEDAHSGLLKGNSRQTVWRGYLTTDKEVPGLVLMQDLAFLSGFPPTFKETNQLKTKLPENLSSKVKLLQLYSEASVALLKLNNPKDFQELNKQTKKNMTIDGKELTISPAYLLWDLSAISQSKQDEDISASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNLDNPRVTIVTHQDVFRNLSHLPTFSSPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDFYSHSKGQKVYLTWPVPNCAEGCPGSWIKDGYCDKACNNSACDWDGGDCSGNSGGSRYIAGGGGTGSIGVGQPWQFGGGINSVSYCNQGCANSWLADKFCDQACNVLSCGFDAGDCGQDHFHELYKVILLPNQTHYIIPKGECLPYFSFAEVAKRGVEGAYSDNPIIRHASIANKWKTIHLIMHSGMNATTIHFNLTFQNTNDEEFKMQITVEVDTREGPKLNSTAQKGYENLVSPITLLPEAEILFEDIPKEKRFPKFKRHDVNSTRRAQEEVKIPLVNISLLPKDAQLSLNTLDLQLEHGDITLKGYNLSKSALLRSFLMNSQHAKIKNQAIITDETNDSLVAPQEKQVHKSILPNSLGVSERLQRLTFPAVSVKVNGHDQGQNPPLDLETTARFRVETHTQKTIGGNVTKEKPPSLIVPLESQMTKEKKITGKEKENSRMEENAENHIGVTEVLLGRKLQHYTDSYLGFLPWEKKKYFQDLLDEEESLKTQLAYFTDSKNTGRQLKDTFADSLRYVNKILNSKFGFTSRKVPAHMPHMIDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFDEVDTDQSGVLSDREIRTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYDPNLPPVTKSLVTNCKPVTDKIHKAYKDKNKYRFEIMGEEEIAFKMIRTNVSHVVGQLDDIRKNPRKFVCLNDNIDHNHKDAQTVKAVLRDFYESMFPIPSQFELPREYRNRFLHMHELQEWRAYRDKLKFWTHCVLATLIMFTIFSFFAEQLIALKRKIFPRRRIHKEASPNRIRV
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
4Ubiquitination----MLFKLLQRQTY
----CHHHHHHHHHH		62.0121890473
4 (in isoform 2)Ubiquitination-62.0121890473
4 (in isoform 1)Ubiquitination-62.0121890473
49PhosphorylationLEWSRDQYHVLFDSY
EEECHHCEEEEEHHH		9.74-
83N-linked_GlycosylationDVVYTWVNGTDLELL
CEEEEEECCCCHHHH		38.93UniProtKB CARBOHYD
114N-linked_GlycosylationMREILGKNTTEPTKK
HHHHHCCCCCCCCCC		50.89UniProtKB CARBOHYD
115PhosphorylationREILGKNTTEPTKKS
HHHHCCCCCCCCCCC		35.70-
131PhosphorylationKQLECLLTHCIKVPM
HHHHHHHHHHCCCCE		11.1822210691
148N-linked_GlycosylationLDPALPANITLKDLP
CCCCCCCCCCHHCCH		26.32UniProtKB CARBOHYD
150PhosphorylationPALPANITLKDLPSL
CCCCCCCCHHCCHHH		27.8022210691
179N-linked_GlycosylationKPKNPSTNVSVVVFD
CCCCCCCCEEEEEEE		28.53UniProtKB CARBOHYD
245PhosphorylationKETNQLKTKLPENLS
HHHHHHHHCCCCCHH		46.5425003641
250N-linked_GlycosylationLKTKLPENLSSKVKL
HHHCCCCCHHHHHHH		43.19UniProtKB CARBOHYD
289PhosphorylationKQTKKNMTIDGKELT
HHCCCCCEECCEECE		25.88-
312PhosphorylationDLSAISQSKQDEDIS
HHHHHHCCCCCCCCC		26.03-
319PhosphorylationSKQDEDISASRFEDN
CCCCCCCCCCCCCCC		32.30-
321PhosphorylationQDEDISASRFEDNEE
CCCCCCCCCCCCCHH		30.61-
332PhosphorylationDNEELRYSLRSIERH
CCHHHHHHHHHHHHH		15.7524719451
459PhosphorylationCDKACNNSACDWDGG
CCCCCCCCCCCCCCC		19.1124114839
472PhosphorylationGGDCSGNSGGSRYIA
CCCCCCCCCCCCEEC		48.3224114839
475PhosphorylationCSGNSGGSRYIAGGG
CCCCCCCCCEECCCC		25.9924114839
573UbiquitinationFSFAEVAKRGVEGAY
CCHHHHHHHCCCCCC		55.66-
614N-linked_GlycosylationNATTIHFNLTFQNTN
CCEEEEEEEEEECCC		24.82UniProtKB CARBOHYD
654O-linked_GlycosylationKGYENLVSPITLLPE
HCHHCCCCCCHHCCH		17.47OGP
657O-linked_GlycosylationENLVSPITLLPEAEI
HCCCCCCHHCCHHHH		26.15OGP
699N-linked_GlycosylationEVKIPLVNISLLPKD
HCCCCEEECCCCCCC		26.3019159218
713O-linked_GlycosylationDAQLSLNTLDLQLEH
CCCCCCCCEEEEECC		27.26OGP
728PhosphorylationGDITLKGYNLSKSAL
CCEEEEECCCCHHHH		16.02-
729N-linked_GlycosylationDITLKGYNLSKSALL
CEEEEECCCCHHHHH		46.65UniProtKB CARBOHYD
731PhosphorylationTLKGYNLSKSALLRS
EEEECCCCHHHHHHH		22.41-
733PhosphorylationKGYNLSKSALLRSFL
EECCCCHHHHHHHHH		22.29-
755PhosphorylationIKNQAIITDETNDSL
CCCCEEEECCCCCCC		22.9720230923
755O-linked_GlycosylationIKNQAIITDETNDSL
CCCCEEEECCCCCCC		22.97OGP
758PhosphorylationQAIITDETNDSLVAP
CEEEECCCCCCCCCC		47.3224850871
761PhosphorylationITDETNDSLVAPQEK
EECCCCCCCCCCCCH		27.1520230923
773O-linked_GlycosylationQEKQVHKSILPNSLG
CCHHHCHHHCCCCCC		17.93OGP
778O-linked_GlycosylationHKSILPNSLGVSERL
CHHHCCCCCCHHHHH		25.26OGP
782O-linked_GlycosylationLPNSLGVSERLQRLT
CCCCCCHHHHHHHCC		18.3955835617
789O-linked_GlycosylationSERLQRLTFPAVSVK
HHHHHHCCCCEEEEE		29.7555828949
794O-linked_GlycosylationRLTFPAVSVKVNGHD
HCCCCEEEEEECCCC		20.5155828955
812O-linked_GlycosylationNPPLDLETTARFRVE
CCCCCHHHCEEEEEE		32.8155825241
813O-linked_GlycosylationPPLDLETTARFRVET
CCCCHHHCEEEEEEE		13.3755825247
820O-linked_GlycosylationTARFRVETHTQKTIG
CEEEEEEECCCCCCC		27.63OGP
822O-linked_GlycosylationRFRVETHTQKTIGGN
EEEEEECCCCCCCCC		38.90OGP
825PhosphorylationVETHTQKTIGGNVTK
EEECCCCCCCCCCCC		18.29-
829N-linked_GlycosylationTQKTIGGNVTKEKPP
CCCCCCCCCCCCCCC		32.83UniProtKB CARBOHYD
831PhosphorylationKTIGGNVTKEKPPSL
CCCCCCCCCCCCCCE		37.17-
837O-linked_GlycosylationVTKEKPPSLIVPLES
CCCCCCCCEEEECCH		38.9855833983
837PhosphorylationVTKEKPPSLIVPLES
CCCCCCCCEEEECCH		38.98-
844PhosphorylationSLIVPLESQMTKEKK
CEEEECCHHCCCCCC		32.70-
844O-linked_GlycosylationSLIVPLESQMTKEKK
CEEEECCHHCCCCCC		32.7046220749
847O-linked_GlycosylationVPLESQMTKEKKITG
EECCHHCCCCCCCCC		28.5411036755
847PhosphorylationVPLESQMTKEKKITG
EECCHHCCCCCCCCC		28.54-
873O-linked_GlycosylationAENHIGVTEVLLGRK
HHHHCCHHHHHHCCH		18.3755830809
899PhosphorylationLPWEKKKYFQDLLDE
CCHHHHHHHHHHCCH		18.4924719451
909PhosphorylationDLLDEEESLKTQLAY
HHCCHHHHHHHHHHH		38.1424719451
1009N-linked_GlycosylationMSAVQPLNISQVFDE
HHHHCCCCHHHHCCC		38.25UniProtKB CARBOHYD
1011PhosphorylationAVQPLNISQVFDEVD
HHCCCCHHHHCCCCC		21.1526330541
1019PhosphorylationQVFDEVDTDQSGVLS
HHCCCCCCCCCCCCC		40.9122210691
1022PhosphorylationDEVDTDQSGVLSDRE
CCCCCCCCCCCCHHH		33.4122210691
1026PhosphorylationTDQSGVLSDREIRTL
CCCCCCCCHHHHHHH		32.0126330541
1074O-linked_GlycosylationQLNNIPPTQESYYDP
HHCCCCCCCHHHCCC		39.35OGP
1077PhosphorylationNIPPTQESYYDPNLP
CCCCCCHHHCCCCCC		21.1228387310
1079PhosphorylationPPTQESYYDPNLPPV
CCCCHHHCCCCCCCC		33.9228387310
1098O-linked_GlycosylationVTNCKPVTDKIHKAY
HHCCEECCHHHHHHH		39.8555833859
1128PhosphorylationIAFKMIRTNVSHVVG
HHHHHHHHHHHHHHC		29.10-
1129N-linked_GlycosylationAFKMIRTNVSHVVGQ
HHHHHHHHHHHHHCC		24.36UniProtKB CARBOHYD
1131PhosphorylationKMIRTNVSHVVGQLD
HHHHHHHHHHHCCHH		16.78-
1250PhosphorylationRRIHKEASPNRIRV-
CHHCCCCCCCCCCC-		24.6525159151
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 GNPTA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GNPTA_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 GNPTA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
MK01_HUMANMAPK1physical
21988832
Drug and Disease Associations
Kegg Disease
H00143 Mucolipidosis II and III, including: Mucolipidosis II / I-cell disease; Mucolipidosis III A / Pseudo
OMIM Disease
252500Mucolipidosis type II (MLII)
252600Mucolipidosis type III complementation group A (MLIIIA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GNPTA_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-699, AND MASSSPECTROMETRY.

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