| Tag | Content |
|---|
| CPLM ID | CPLM-023306 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B |
Protein Synonyms/Alias | N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVb; GlcNAc-T IVb; GnT-IVb; N-acetylglucosaminyltransferase IVb; UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb |
Gene Name | MGAT4B |
Gene Synonyms/Alias | UNQ906/PRO1927 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 59 | AAEQESLKRSKELNL | ubiquitination | [1] | | 480 | FDNPQSDKEALQEGR | ubiquitination | [1] |
|
Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional 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. |
Sequence Annotation | CARBOHYD 87 87 N-linked (GlcNAc...) (Potential).
CARBOHYD 103 103 N-linked (GlcNAc...) (Potential). |
Keyword | Alternative splicing; Coiled coil; Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane; Metal-binding; Polymorphism; Reference proteome; Signal-anchor; Transferase; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 548 AA |
Protein Sequence | MRLRNGTFLT LLLFCLCAFL SLSWYAALSG QKGDVVDVYQ REFLALRDRL HAAEQESLKR 60
SKELNLVLDE IKRAVSERQA LRDGDGNRTW GRLTEDPRLK PWNGSHRHVL HLPTVFHHLP 120
HLLAKESSLQ PAVRVGQGRT GVSVVMGIPS VRREVHSYLT DTLHSLISEL SPQEKEDSVI 180
VVLIAETDSQ YTSAVTENIK ALFPTEIHSG LLEVISPSPH FYPDFSRLRE SFGDPKERVR 240
WRTKQNLDYC FLMMYAQSKG IYYVQLEDDI VAKPNYLSTM KNFALQQPSE DWMILEFSQL 300
GFIGKMFKSL DLSLIVEFIL MFYRDKPIDW LLDHILWVKV CNPEKDAKHC DRQKANLRIR 360
FKPSLFQHVG THSSLAGKIQ KLKDKDFGKQ ALRKEHVNPP AEVSTSLKTY QHFTLEKAYL 420
REDFFWAFTP AAGDFIRFRF FQPLRLERFF FRSGNIEHPE DKLFNTSVEV LPFDNPQSDK 480
EALQEGRTAT LRYPRSPDGY LQIGSFYKGV AEGEVDPAFG PLEALRLSIQ TDSPVWVILS 540
EIFLKKAD 548 |
Gene Ontology | GO:0000139; C:Golgi membrane; TAS:Reactome. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0008454; F:alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; TAS:ProtInc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006491; P:N-glycan processing; TAS:ProtInc. GO:0043687; P:post-translational protein modification; TAS:Reactome. GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |