PMGT2_HUMAN - dbPTM
PMGT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMGT2_HUMAN
UniProt AC Q8NAT1
Protein Name Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 {ECO:0000303|PubMed:23929950}
Gene Name POMGNT2
Organism Homo sapiens (Human).
Sequence Length 580
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description O-linked mannose beta-1,4-N-acetylglucosaminyltransferase that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D-mannosylprotein. Involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity..
Protein Sequence MHLSAVFNALLVSVLAAVLWKHVRLREHAATLEEELALSRQATEPAPALRIDYPKALQILMEGGTHMVCTGRTHTDRICRFKWLCYSNEAEEFIFFHGNTSVMLPNLGSRRFQPALLDLSTVEDHNTQYFNFVELPAAALRFMPKPVFVPDVALIANRFNPDNLMHVFHDDLLPLFYTLRQFPGLAHEARLFFMEGWGEGAHFDLYKLLSPKQPLLRAQLKTLGRLLCFSHAFVGLSKITTWYQYGFVQPQGPKANILVSGNEIRQFARFMTEKLNVSHTGVPLGEEYILVFSRTQNRLILNEAELLLALAQEFQMKTVTVSLEDHTFADVVRLVSNASMLVSMHGAQLVTTLFLPRGATVVELFPYAVNPDHYTPYKTLAMLPGMDLQYVAWRNMMPENTVTHPERPWDQGGITHLDRAEQARILQSREVPRHLCCRNPEWLFRIYQDTKVDIPSLIQTIRRVVKGRPGPRKQKWTVGLYPGKVREARCQASVHGASEARLTVSWQIPWNLKYLKVREVKYEVWLQEQGENTYVPYILALQNHTFTENIKPFTTYLVWVRCIFNKILLGPFADVLVCNT
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
13PhosphorylationVFNALLVSVLAAVLW
HHHHHHHHHHHHHHH
50563987
39PhosphorylationLEEELALSRQATEPA
HHHHHHHHCCCCCCC
24719451
43O-linked_GlycosylationLALSRQATEPAPALR
HHHHCCCCCCCCCCC
55831349
65PhosphorylationQILMEGGTHMVCTGR
HHHHCCCCEEEECCC
46160439
70PhosphorylationGGTHMVCTGRTHTDR
CCCEEEECCCCCHHC
46160445
86PhosphorylationCRFKWLCYSNEAEEF
EEEEEEEECCCCCEE
24043423
87PhosphorylationRFKWLCYSNEAEEFI
EEEEEEECCCCCEEE
24043423
99N-linked_GlycosylationEFIFFHGNTSVMLPN
EEEEEECCCEEECCC
UniProtKB CARBOHYD
100PhosphorylationFIFFHGNTSVMLPNL
EEEEECCCEEECCCC
24043423
101PhosphorylationIFFHGNTSVMLPNLG
EEEECCCEEECCCCC
24043423
109PhosphorylationVMLPNLGSRRFQPAL
EECCCCCCCCCCEEE
24043423
145UbiquitinationAALRFMPKPVFVPDV
HHHHHCCCCCCCCCH
-
178PhosphorylationDLLPLFYTLRQFPGL
CHHHHHHHHHHCCCC
24719451
210PhosphorylationFDLYKLLSPKQPLLR
CCHHHHCCCCCHHHH
24719451
276N-linked_GlycosylationRFMTEKLNVSHTGVP
HHHHHCCCCCCCCCC
UniProtKB CARBOHYD
379PhosphorylationDHYTPYKTLAMLPGM
CCCCCCHHHHCCCCC
68744237
390PhosphorylationLPGMDLQYVAWRNMM
CCCCCHHHHHHHHCC
68744243
493PhosphorylationREARCQASVHGASEA
CEEEEEEEECCCCCE
68699121

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 PMGT2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMGT2_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 PMGT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NT2NL_HUMANNOTCH2NLphysical
25416956
PECR_HUMANPECRphysical
28514442
FKB14_HUMANFKBP14physical
28514442
NOB1_HUMANNOB1physical
28514442
IF4E2_HUMANEIF4E2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMGT2_HUMAN

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Related Literatures of Post-Translational Modification

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