MGT5B_HUMAN - dbPTM
MGT5B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MGT5B_HUMAN
UniProt AC Q3V5L5
Protein Name Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B
Gene Name MGAT5B
Organism Homo sapiens (Human).
Sequence Length 792
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein.
Protein Description Glycosyltransferase that acts on alpha-linked mannose of N-glycans and O-mannosyl glycans. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to the beta 1-6 linkage of the mannose residue of GlcNAcbeta1,2-Manalpha on both the alpha1,3- and alpha1,6-linked mannose arms in the core structure of N-glycan. Also acts on the GlcNAcbeta1,2-Manalpha1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan. Plays an active role in modulating integrin and laminin-dependent adhesion and migration of neuronal cells via its activity in the O-mannosyl glycan pathway..
Protein Sequence MITVNPDGKIMVRRCLVTLRPFRLFVLGIGFFTLCFLMTSLGGQFSARRLGDSPFTIRTEVMGGPESRGVLRKMSDLLELMVKRMDALARLENSSELHRAGGDLHFPADRMPPGAGLMERIQAIAQNVSDIAVKVDQILRHSLLLHSKVSEGRRDQCEAPSDPKFPDCSGKVEWMRARWTSDPCYAFFGVDGTECSFLIYLSEVEWFCPPLPWRNQTAAQRAPKPLPKVQAVFRSNLSHLLDLMGSGKESLIFMKKRTKRLTAQWALAAQRLAQKLGATQRDQKQILVHIGFLTEESGDVFSPRVLKGGPLGEMVQWADILTALYVLGHGLRVTVSLKELQSNLGVPPGRGSCPLTMPLPFDLIYTDYHGLQQMKRHMGLSFKKYRCRIRVIDTFGTEPAYNHEEYATLHGYRTNWGYWNLNPKQFMTMFPHTPDNSFMGFVSEELNETEKRLIKGGKASNMAVVYGKEASIWKLQGKEKFLGILNKYMEIHGTVYYESQRPPEVPAFVKNHGLLPQPEFQQLLRKAKLFIGFGFPYEGPAPLEAIANGCIFLQSRFSPPHSSLNHEFFRGKPTSREVFSQHPYAENFIGKPHVWTVDYNNSEEFEAAIKAIMRTQVDPYLPYEYTCEGMLERIHAYIQHQDFCRAPDPALPEAHAPQSPFVLAPNATHLEWARNTSLAPGAWPPAHALRAWLAVPGRACTDTCLDHGLICEPSFFPFLNSQDAFLKLQVPCDSTESEMNHLYPAFAQPGQECYLQKEPLLFSCAGSNTKYRRLCPCRDFRKGQVALCQGCL
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
3Phosphorylation-----MITVNPDGKI
-----CEEECCCCCE
16.9724719451
56PhosphorylationRLGDSPFTIRTEVMG
HHCCCCCEEEEEECC
16.9724719451
75PhosphorylationRGVLRKMSDLLELMV
HHHHHHHHHHHHHHH
28.30-
94PhosphorylationALARLENSSELHRAG
HHHHHHCHHHHHHCC
18.80-
127N-linked_GlycosylationRIQAIAQNVSDIAVK
HHHHHHHCHHHHHHH
26.66UniProtKB CARBOHYD
259UbiquitinationIFMKKRTKRLTAQWA
EEEEHHHHHHHHHHH
49.8229967540
270UbiquitinationAQWALAAQRLAQKLG
HHHHHHHHHHHHHHC
35.0029967540
275UbiquitinationAAQRLAQKLGATQRD
HHHHHHHHHCCCHHH
43.1929967540
286UbiquitinationTQRDQKQILVHIGFL
CHHHHHHHEEEEEEE
5.8229967540
368PhosphorylationFDLIYTDYHGLQQMK
CCEEEECCHHHHHHH
7.03-
381PhosphorylationMKRHMGLSFKKYRCR
HHHHHCCCCCCEEEE
29.3224719451
449 (in isoform 5)Phosphorylation-45.8122468782
460 (in isoform 2)Phosphorylation-30.5322468782
466 (in isoform 5)Phosphorylation-18.8422468782
477 (in isoform 2)Phosphorylation-50.9922468782
480UbiquitinationWKLQGKEKFLGILNK
EEECCHHHHHHHHHH
49.7529967540
771PhosphorylationCAGSNTKYRRLCPCR
CCCCCCCCEEECCCC
10.03-

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 MGT5B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MGT5B_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 MGT5B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR195_HUMANKRTAP19-5physical
25416956
KLH38_HUMANKLHL38physical
25416956
KR122_HUMANKRTAP12-2physical
25416956
KR261_HUMANKRTAP26-1physical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MGT5B_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP