GLT11_HUMAN - dbPTM
GLT11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLT11_HUMAN
UniProt AC Q8NCW6
Protein Name Polypeptide N-acetylgalactosaminyltransferase 11
Gene Name GALNT11
Organism Homo sapiens (Human).
Sequence Length 608
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein .
Protein Description Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO)..
Protein Sequence MGSVTVRYFCYGCLFTSATWTVLLFVYFNFSEVTQPLKNVPVKGSGPHGPSPKKFYPRFTRGPSRVLEPQFKANKIDDVIDSRVEDPEEGHLKFSSELGMIFNERDQELRDLGYQKHAFNMLISDRLGYHRDVPDTRNAACKEKFYPPDLPAASVVICFYNEAFSALLRTVHSVIDRTPAHLLHEIILVDDDSDFDDLKGELDEYVQKYLPGKIKVIRNTKREGLIRGRMIGAAHATGEVLVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYSSSPVVRGGFNWGLHFKWDLVPLSELGRAEGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFRIWMCGGKLFIIPCSRVGHIFRKRRPYGSPEGQDTMTHNSLRLAHVWLDEYKEQYFSLRPDLKTKSYGNISERVELRKKLGCKSFKWYLDNVYPEMQISGSHAKPQQPIFVNRGPKRPKVLQRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMSETRSSDPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLRAVDPLGQKGSVAMAICDGSSSQQWHLEG
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
5Phosphorylation---MGSVTVRYFCYG
---CCCEEHHHEEHH
10.8524719451
82PhosphorylationKIDDVIDSRVEDPEE
CCHHHHHCCCCCCCC
27.4025850435
95PhosphorylationEEGHLKFSSELGMIF
CCCCCCCCHHHHCCC
22.70-
388PhosphorylationRKRRPYGSPEGQDTM
HCCCCCCCCCCCCCC
17.5928857561
414PhosphorylationLDEYKEQYFSLRPDL
HHHHHHHHHHCCCCC
9.02-
425PhosphorylationRPDLKTKSYGNISER
CCCCCCCCCCCHHHH
43.4322210691
426PhosphorylationPDLKTKSYGNISERV
CCCCCCCCCCHHHHH
18.7522210691
428N-linked_GlycosylationLKTKSYGNISERVEL
CCCCCCCCHHHHHHH
26.78UniProtKB CARBOHYD
460O-linked_GlycosylationPEMQISGSHAKPQQP
CCCCCCCCCCCCCCC
17.30OGP
533PhosphorylationEHELVLNSLLCLDMS
CHHHHHHHHEEECCC
20.68-
540PhosphorylationSLLCLDMSETRSSDP
HHEEECCCCCCCCCC
35.17-

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 GLT11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLT11_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 GLT11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GLT11_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLT11_HUMAN

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Related Literatures of Post-Translational Modification

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