NAGPA_HUMAN - dbPTM
NAGPA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAGPA_HUMAN
UniProt AC Q9UK23
Protein Name N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
Gene Name NAGPA
Organism Homo sapiens (Human).
Sequence Length 515
Subcellular Localization Golgi apparatus, Golgi stack membrane
Single-pass type I membrane protein . Golgi apparatus, trans-Golgi network . Cis/medial Golgi.
Protein Description Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases..
Protein Sequence MATSTGRWLLLRLALFGFLWEASGGLDSGASRDDDLLLPYPRARARLPRDCTRVRAGNREHESWPPPPATPGAGGLAVRTFVSHFRDRAVAGHLTRAVEPLRTFSVLEPGGPGGCAARRRATVEETARAADCRVAQNGGFFRMNSGECLGNVVSDERRVSSSGGLQNAQFGIRRDGTLVTGYLSEEEVLDTENPFVQLLSGVVWLIRNGSIYINESQATECDETQETGSFSKFVNVISARTAIGHDRKGQLVLFHADGQTEQRGINLWEMAEFLLKQDVVNAINLDGGGSATFVLNGTLASYPSDHCQDNMWRCPRQVSTVVCVHEPRCQPPDCHGHGTCVDGHCQCTGHFWRGPGCDELDCGPSNCSQHGLCTETGCRCDAGWTGSNCSEECPLGWHGPGCQRPCKCEHHCPCDPKTGNCSVSRVKQCLQPPEATLRAGELSFFTRTAWLALTLALAFLLLISTAANLSLLLSRAERNRRLHGDYAYHPLQEMNGEPLAAEKEQPGGAHNPFKD
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
103PhosphorylationRAVEPLRTFSVLEPG
HCCCCCCEEEECCCC
28.13-
105PhosphorylationVEPLRTFSVLEPGGP
CCCCCEEEECCCCCC
25.77-
126PhosphorylationRRATVEETARAADCR
HCCCHHHHHHHHCCE
14.13-
160PhosphorylationVSDERRVSSSGGLQN
ECCCCEECCCCCCCC
19.5823403867
161PhosphorylationSDERRVSSSGGLQNA
CCCCEECCCCCCCCC
30.0923403867
162PhosphorylationDERRVSSSGGLQNAQ
CCCEECCCCCCCCCE
29.4023403867
208N-linked_GlycosylationGVVWLIRNGSIYINE
CEEEEEECCEEEECH
41.38UniProtKB CARBOHYD
214N-linked_GlycosylationRNGSIYINESQATEC
ECCEEEECHHHCCCC
26.37UniProtKB CARBOHYD
229PhosphorylationDETQETGSFSKFVNV
CCCCCCCCHHHHHHH
33.4924719451
296N-linked_GlycosylationGSATFVLNGTLASYP
CEEEEEEECEECCCC
35.78UniProtKB CARBOHYD
365PhosphorylationDELDCGPSNCSQHGL
CCCCCCCCCCCCCCE
35.43-
366N-linked_GlycosylationELDCGPSNCSQHGLC
CCCCCCCCCCCCCEE
32.37UniProtKB CARBOHYD
368PhosphorylationDCGPSNCSQHGLCTE
CCCCCCCCCCCEECC
29.48-
374PhosphorylationCSQHGLCTETGCRCD
CCCCCEECCCCCCCC
41.44-
376PhosphorylationQHGLCTETGCRCDAG
CCCEECCCCCCCCCC
24.35-
388N-linked_GlycosylationDAGWTGSNCSEECPL
CCCCCCCCCCCCCCC
34.38UniProtKB CARBOHYD
420N-linked_GlycosylationPCDPKTGNCSVSRVK
CCCCCCCCCCHHHHH
21.81UniProtKB CARBOHYD
436PhosphorylationCLQPPEATLRAGELS
HCCCCHHEECCCCCC
18.34-
443O-linked_GlycosylationTLRAGELSFFTRTAW
EECCCCCCHHHHHHH
17.63OGP
446O-linked_GlycosylationAGELSFFTRTAWLAL
CCCCCHHHHHHHHHH
25.71OGP
486PhosphorylationNRRLHGDYAYHPLQE
HHHCCCCCCCCCHHH
17.4128796482
488PhosphorylationRLHGDYAYHPLQEMN
HCCCCCCCCCHHHHC
9.5728796482
514UbiquitinationGGAHNPFKD------
CCCCCCCCC------
64.8829967540

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 NAGPA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAGPA_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 NAGPA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPS15_HUMANEPS15physical
11723124
AP2A1_HUMANAP2A1physical
11723124
ZHX2_HUMANZHX2physical
21988832
NGLY1_HUMANNGLY1physical
28514442
TYW3_HUMANTYW3physical
28514442
UBR3_HUMANUBR3physical
28514442
WDR54_HUMANWDR54physical
28514442

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 NAGPA_HUMAN

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Related Literatures of Post-Translational Modification

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