MGT4B_HUMAN - dbPTM
MGT4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MGT4B_HUMAN
UniProt AC Q9UQ53
Protein Name Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
Gene Name MGAT4B
Organism Homo sapiens (Human).
Sequence Length 548
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein.
Protein Description Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N-glycan biosynthesis..
Protein Sequence MRLRNGTFLTLLLFCLCAFLSLSWYAALSGQKGDVVDVYQREFLALRDRLHAAEQESLKRSKELNLVLDEIKRAVSERQALRDGDGNRTWGRLTEDPRLKPWNGSHRHVLHLPTVFHHLPHLLAKESSLQPAVRVGQGRTGVSVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVIVVLIAETDSQYTSAVTENIKALFPTEIHSGLLEVISPSPHFYPDFSRLRESFGDPKERVRWRTKQNLDYCFLMMYAQSKGIYYVQLEDDIVAKPNYLSTMKNFALQQPSEDWMILEFSQLGFIGKMFKSLDLSLIVEFILMFYRDKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIRFKPSLFQHVGTHSSLAGKIQKLKDKDFGKQALRKEHVNPPAEVSTSLKTYQHFTLEKAYLREDFFWAFTPAAGDFIRFRFFQPLRLERFFFRSGNIEHPEDKLFNTSVEVLPFDNPQSDKEALQEGRTATLRYPRSPDGYLQIGSFYKGVAEGEVDPAFGPLEALRLSIQTDSPVWVILSEIFLKKAD
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
8DimethylationMRLRNGTFLTLLLFC
CCCCCHHHHHHHHHH
5.34-
17DimethylationTLLLFCLCAFLSLSW
HHHHHHHHHHHHHHH
2.37-
59 (in isoform 2)Ubiquitination-65.0021906983
59UbiquitinationAAEQESLKRSKELNL
HHHHHHHHHHHHHHH
65.0021906983
59 (in isoform 1)Ubiquitination-65.0021906983
62UbiquitinationQESLKRSKELNLVLD
HHHHHHHHHHHHHHH
70.9729967540
72UbiquitinationNLVLDEIKRAVSERQ
HHHHHHHHHHHHHHH
32.0529967540
77UbiquitinationEIKRAVSERQALRDG
HHHHHHHHHHHHHCC
42.0629967540
87N-linked_GlycosylationALRDGDGNRTWGRLT
HHHCCCCCCCCCCCC
42.84UniProtKB CARBOHYD
87UbiquitinationALRDGDGNRTWGRLT
HHHCCCCCCCCCCCC
42.8429967540
103N-linked_GlycosylationDPRLKPWNGSHRHVL
CCCCCCCCCCCCCEE
51.09UniProtKB CARBOHYD
140PhosphorylationVRVGQGRTGVSVVMG
EECCCCCCCCEEEEC
49.0824043423
143PhosphorylationGQGRTGVSVVMGIPS
CCCCCCCEEEECCHH
15.4430257219
150PhosphorylationSVVMGIPSVRREVHS
EEEECCHHHHHHHHH
26.7424043423
187PhosphorylationIVVLIAETDSQYTSA
EEEEEEECCCHHHHH
31.74-
191PhosphorylationIAETDSQYTSAVTEN
EEECCCHHHHHHHHH
13.45-
216PhosphorylationSGLLEVISPSPHFYP
CCCEEHHCCCCCCCC
25.22-
262PhosphorylationYAQSKGIYYVQLEDD
HHHHCCEEEEEECCC
13.2729083192
263PhosphorylationAQSKGIYYVQLEDDI
HHHCCEEEEEECCCC
4.6423532336
276PhosphorylationDIVAKPNYLSTMKNF
CCEECCCHHHHHCCH
15.5729083192
278PhosphorylationVAKPNYLSTMKNFAL
EECCCHHHHHCCHHC
18.9829083192
279PhosphorylationAKPNYLSTMKNFALQ
ECCCHHHHHCCHHCC
29.5723532336
364PhosphorylationLRIRFKPSLFQHVGT
HEEEECHHHHHHCCC
42.2630622161
371PhosphorylationSLFQHVGTHSSLAGK
HHHHHCCCCHHHHHH
19.9330622161
373PhosphorylationFQHVGTHSSLAGKIQ
HHHCCCCHHHHHHHH
27.2130622161
374PhosphorylationQHVGTHSSLAGKIQK
HHCCCCHHHHHHHHH
18.0330622161
389UbiquitinationLKDKDFGKQALRKEH
HCCCCHHHHHHHHHC
32.1829967540
394UbiquitinationFGKQALRKEHVNPPA
HHHHHHHHHCCCCCH
53.6929967540
404UbiquitinationVNPPAEVSTSLKTYQ
CCCCHHHCHHHCCCC
12.0929967540
404PhosphorylationVNPPAEVSTSLKTYQ
CCCCHHHCHHHCCCC
12.0921214269
405PhosphorylationNPPAEVSTSLKTYQH
CCCHHHCHHHCCCCC
43.1621214269
409UbiquitinationEVSTSLKTYQHFTLE
HHCHHHCCCCCEEEC
33.4429967540
410PhosphorylationVSTSLKTYQHFTLEK
HCHHHCCCCCEEECH
9.8221214269
419PhosphorylationHFTLEKAYLREDFFW
CEEECHHHCCCCEEE
19.84-
479 (in isoform 2)Ubiquitination-47.7921906983
480UbiquitinationFDNPQSDKEALQEGR
CCCCCCHHHHHHCCC
50.5721906983
480 (in isoform 1)Ubiquitination-50.5721906983
490O-linked_GlycosylationLQEGRTATLRYPRSP
HHCCCCEEECCCCCC
15.9157782045

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 MGT4B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MGT4B_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 MGT4B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYJ2B_HUMANSYNJ2BPphysical
22939629
UCRI_HUMANUQCRFS1physical
22939629
S26A2_HUMANSLC26A2physical
22939629
SFXN2_HUMANSFXN2physical
22939629
VDAC1_HUMANVDAC1physical
22939629
HBB_HUMANHBBphysical
26186194
HBB_HUMANHBBphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MGT4B_HUMAN

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Related Literatures of Post-Translational Modification

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