GLT10_HUMAN - dbPTM
GLT10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLT10_HUMAN
UniProt AC Q86SR1
Protein Name Polypeptide N-acetylgalactosaminyltransferase 10
Gene Name GALNT10
Organism Homo sapiens (Human).
Sequence Length 603
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein.
Protein Description Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates..
Protein Sequence MRRKEKRLLQAVALVLAALVLLPNVGLWALYRERQPDGTPGGSGAAVAPAAGQGSHSRQKKTFFLGDGQKLKDWHDKEAIRRDAQRVGNGEQGRPYPMTDAERVDQAYRENGFNIYVSDKISLNRSLPDIRHPNCNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEIVLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHCEANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIPPELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRMEDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDVAVQKKLRSSLNCKSFKWFMTKIAWDLPKFYPPVEPPAAAWGEIRNVGTGLCADTKHGALGSPLRLEGCVRGRGEAAWNNMQVFTFTWREDIRPGDPQHTKKFCFDAISHTSPVTLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRIFMNTCNPSSLTQQWLFEHTNSTVLEKFNRN
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
39O-linked_GlycosylationRERQPDGTPGGSGAA
HCCCCCCCCCCCCCC		26.5855831425
43O-linked_GlycosylationPDGTPGGSGAAVAPA
CCCCCCCCCCCCCCC		31.0455831429
43PhosphorylationPDGTPGGSGAAVAPA
CCCCCCCCCCCCCCC		31.0423898821
55PhosphorylationAPAAGQGSHSRQKKT
CCCCCCCCCCCCEEE		15.4823898821
57PhosphorylationAAGQGSHSRQKKTFF
CCCCCCCCCCEEEEE		37.8023898821
62O-linked_GlycosylationSHSRQKKTFFLGDGQ
CCCCCEEEEECCCCC		27.0155824397
124N-linked_GlycosylationVSDKISLNRSLPDIR
ECCCCCCCCCCCCCC		25.3816650853
146N-linked_GlycosylationRYLETLPNTSIIIPF
HHHHCCCCCEEEEEC		49.9616650853
160PhosphorylationFHNEGWSSLLRTVHS
CCCCHHHHHHHHHHH		25.5524719451
220PhosphorylationKREGLIRTRMLGASV
CCCCCCHHHHHCCCC		17.2825332170
226PhosphorylationRTRMLGASVATGDVI
HHHHHCCCCCCCCHH		15.5325332170
238PhosphorylationDVITFLDSHCEANVN
CHHHHCHHHHCHHCC		31.9825332170
260PhosphorylationRIARNRKTIVCPMID
HHHHCCCEEEEEECC		18.5322210691
276PhosphorylationIDHDDFRYETQAGDA
CCCCCCCEECCCHHH		24.2622817900
278PhosphorylationHDDFRYETQAGDAMR
CCCCCEECCCHHHHC		18.1322210691
293PhosphorylationGAFDWEMYYKRIPIP
CCCCHHHHHCCCCCC		8.3622817900
294PhosphorylationAFDWEMYYKRIPIPP
CCCHHHHHCCCCCCH		7.7722817900
350PhosphorylationGGEQYEISFKVWMCG
CCCEEEEEEEEEECC		13.6924719451
372PhosphorylationCSRVGHIYRKYVPYK
CCHHHEEEHHCCCCC		8.7220068231
375PhosphorylationVGHIYRKYVPYKVPA
HHEEEHHCCCCCCCC		9.5420049867
385PhosphorylationYKVPAGVSLARNLKR
CCCCCCHHHHHHHHH		18.52-
4242-HydroxyisobutyrylationAGDVAVQKKLRSSLN
HHHHHHHHHHHHHCC		47.37-
424UbiquitinationAGDVAVQKKLRSSLN
HHHHHHHHHHHHHCC		47.3729967540
425UbiquitinationGDVAVQKKLRSSLNC
HHHHHHHHHHHHCCC		31.85-
474PhosphorylationGTGLCADTKHGALGS
CCCCCCCCCCCCCCC		13.3522817900
475UbiquitinationTGLCADTKHGALGSP
CCCCCCCCCCCCCCC		40.36-
481PhosphorylationTKHGALGSPLRLEGC
CCCCCCCCCEEEECC		22.9323898821
530O-linked_GlycosylationCFDAISHTSPVTLYD
EHHCCCCCCCCEEEE		28.12OGP
593N-linked_GlycosylationQWLFEHTNSTVLEKF
HHHHHHCCHHHHHHH		37.2816650853
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 GLT10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLT10_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 GLT10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GLT10_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 GLT10_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10).";
Kubota T., Shiba T., Sugioka S., Furukawa S., Sawaki H., Kato R.,Wakatsuki S., Narimatsu H.;
J. Mol. Biol. 359:708-727(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-603 IN COMPLEX WITHUDP-GALNAC AND GALNAC-SERINE, DISULFIDE BOND, MANGANESE-BINDING SITES,AND GLYCOSYLATION AT ASN-124; ASN-146 AND ASN-593.

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