GALT7_HUMAN - dbPTM
GALT7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GALT7_HUMAN
UniProt AC Q86SF2
Protein Name N-acetylgalactosaminyltransferase 7
Gene Name GALNT7
Organism Homo sapiens (Human).
Sequence Length 657
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein.
Protein Description Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified..
Protein Sequence MRLKIGFILRSLLVVGSFLGLVVLWSSLTPRPDDPSPLSRMREDRDVNDPMPNRGGNGLAPGEDRFKPVVPWPHVEGVEVDLESIRRINKAKNEQEHHAGGDSQKDIMQRQYLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGEKAKPLVLGPEFKQAIQASIKEFGFNMVASDMISLDRSVNDLRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWYAPLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGYARGAWDWSMLWKRVPLTPQEKRLRKTKTEPYRSPAMAGGLFAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEVWWDEYKDYFYASRPESQALPYGDISELKKFREDHNCKSFKWFMEEIAYDITSHYPLPPKNVDWGEIRGFETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHCNLNEFKEWQYFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNNIHSV
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
29O-linked_GlycosylationVVLWSSLTPRPDDPS
HHHHHCCCCCCCCCC
21.14OGP
36PhosphorylationTPRPDDPSPLSRMRE
CCCCCCCCHHHHCCC
45.5321406692
39PhosphorylationPDDPSPLSRMREDRD
CCCCCHHHHCCCCCC
27.6721406692
103PhosphorylationEHHAGGDSQKDIMQR
CCCCCCCCHHHHHHH
42.2629255136
114O-linked_GlycosylationIMQRQYLTFKPQTFT
HHHHHHEEECCCEEE
25.36OGP
119O-linked_GlycosylationYLTFKPQTFTYHDPV
HEEECCCEEEECCCC
26.86OGP
121O-linked_GlycosylationTFKPQTFTYHDPVLR
EECCCEEEECCCCCC
24.27OGP
154UbiquitinationGGPGEKAKPLVLGPE
CCCCCCCCCCEECHH
50.37-
180PhosphorylationFGFNMVASDMISLDR
HCCCCHHHHHHCCCC
19.1222210691
2322-HydroxyisobutyrylationRTVHSVIKRTPRKYL
HHHHHHHHHCCHHHH
48.33-
257UbiquitinationNKEHLKEKLDEYIKL
CHHHHHHHHHHHHHH
60.7029967540
270AcetylationKLWNGLVKVFRNERR
HHHHHHHHHHHHHCC
40.4788327
368PhosphorylationLWKRVPLTPQEKRLR
HHHHCCCCHHHHHHH
19.49-
372AcetylationVPLTPQEKRLRKTKT
CCCCHHHHHHHCCCC
52.0330588873
3722-HydroxyisobutyrylationVPLTPQEKRLRKTKT
CCCCHHHHHHHCCCC
52.03-
372UbiquitinationVPLTPQEKRLRKTKT
CCCCHHHHHHHCCCC
52.0329967540
422UbiquitinationENFEISYKIWQCGGK
CCCEEEEEEEEECCE
30.5821963094
442PhosphorylationCSRVGHIYRLEGWQG
CCCCCEEEEECCCCC
11.9420068231
447UbiquitinationHIYRLEGWQGNPPPI
EEEEECCCCCCCCCE
8.1121963094
459PhosphorylationPPIYVGSSPTLKNYV
CCEEECCCHHHHHCE
18.90-
461PhosphorylationIYVGSSPTLKNYVRV
EEECCCHHHHHCEEE
52.92-
463UbiquitinationVGSSPTLKNYVRVVE
ECCCHHHHHCEEEEE
49.0321963094
476PhosphorylationVEVWWDEYKDYFYAS
EEEEHHHHHHHEEEC
13.49-
479PhosphorylationWWDEYKDYFYASRPE
EHHHHHHHEEECCCH
8.37-
483O-linked_GlycosylationYKDYFYASRPESQAL
HHHHEEECCCHHHCC
36.67OGP
499UbiquitinationYGDISELKKFREDHN
CCCHHHHHHHHHHCC
45.9029967540
508UbiquitinationFREDHNCKSFKWFME
HHHHCCCCCHHHHHH
65.33-
519PhosphorylationWFMEEIAYDITSHYP
HHHHHHHHHHHCCCC
17.3420068231
522PhosphorylationEEIAYDITSHYPLPP
HHHHHHHHCCCCCCC
13.4220068231
523PhosphorylationEIAYDITSHYPLPPK
HHHHHHHCCCCCCCC
22.7427251275
525PhosphorylationAYDITSHYPLPPKNV
HHHHHCCCCCCCCCC
13.2620068231
544PhosphorylationIRGFETAYCIDSMGK
CCCEEEEEEECCCCC
9.43-
547UbiquitinationFETAYCIDSMGKTNG
EEEEEEECCCCCCCC
29.0721963094
572UbiquitinationMGGNQLFRINEANQL
CCCCEEEEECHHHHH
39.1421963094
588UbiquitinationQYDQCLTKGADGSKV
CHHHHHCCCCCCCEE
38.8721963094
622PhosphorylationHRFTHIPSGKCLDRS
HHCCCCCCCCCCCHH
50.7324719451
624UbiquitinationFTHIPSGKCLDRSEV
CCCCCCCCCCCHHHH
35.64-
638PhosphorylationVLHQVFISNCDSSKT
HHHHHHHHCCCCCCC
21.6823312004
642PhosphorylationVFISNCDSSKTTQKW
HHHHCCCCCCCCCEE
35.6123312004
643PhosphorylationFISNCDSSKTTQKWE
HHHCCCCCCCCCEEE
22.2923312004
648UbiquitinationDSSKTTQKWEMNNIH
CCCCCCCEEECCCCC
42.92-

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 GALT7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GALT7_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 GALT7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK06_HUMANMAPK6physical
21988832
SL9A1_HUMANSLC9A1physical
28514442
GLT12_HUMANGALNT12physical
28514442
MA2A2_HUMANMAN2A2physical
28514442
GALT4_HUMANGALNT4physical
28514442
LYAG_HUMANGAAphysical
28514442
CLH2_HUMANCLTCL1physical
28514442
RMND1_HUMANRMND1physical
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 GALT7_HUMAN

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Related Literatures of Post-Translational Modification

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