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Protein

Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase

Gene

MGAT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides.

Catalytic activityi

UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R = UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS05168-MONOMER.
ReactomeiR-HSA-975574. Reactions specific to the hybrid N-glycan synthesis pathway.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT17. Glycosyltransferase Family 17.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase (EC:2.4.1.144)
Alternative name(s):
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
Short name:
GNT-III
Short name:
GlcNAc-T III
Short name:
N-acetylglucosaminyltransferase III
Gene namesi
Name:MGAT3
Synonyms:GGNT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:7046. MGAT3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence analysis
Transmembranei8 – 2316Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini24 – 533510LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi membrane Source: Reactome
  • integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30781.

Chemistry

ChEMBLiCHEMBL2375206.

Polymorphism and mutation databases

BioMutaiMGAT3.
DMDMi61252497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 533533Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferasePRO_0000188842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis
Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence analysis
Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ09327.
PeptideAtlasiQ09327.
PRIDEiQ09327.

PTM databases

iPTMnetiQ09327.
PhosphoSiteiQ09327.

Expressioni

Gene expression databases

BgeeiQ09327.
CleanExiHS_MGAT3.
ExpressionAtlasiQ09327. baseline and differential.
GenevisibleiQ09327. HS.

Organism-specific databases

HPAiHPA017598.

Interactioni

Protein-protein interaction databases

BioGridi110404. 1 interaction.
STRINGi9606.ENSP00000345270.

Chemistry

BindingDBiQ09327.

Structurei

3D structure databases

ProteinModelPortaliQ09327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi35 – 8652Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 17 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEQJ. Eukaryota.
ENOG410YQKP. LUCA.
GeneTreeiENSGT00390000008221.
HOGENOMiHOG000113579.
HOVERGENiHBG052468.
InParanoidiQ09327.
KOiK00737.
OMAiYTMPGFR.
OrthoDBiEOG7MPRDD.
PhylomeDBiQ09327.
TreeFamiTF323781.

Family and domain databases

InterProiIPR006813. Glyco_trans_17.
[Graphical view]
PANTHERiPTHR12224. PTHR12224. 2 hits.
PfamiPF04724. Glyco_transf_17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMRRYKLFL MFCMAGLCLI SFLHFFKTLS YVTFPRELAS LSPNLVSSFF
60 70 80 90 100
WNNAPVTPQA SPEPGGPDLL RTPLYSHSPL LQPLPPSKAA EELHRVDLVL
110 120 130 140 150
PEDTTEYFVR TKAGGVCFKP GTKMLERPPP GRPEEKPEGA NGSSARRPPR
160 170 180 190 200
YLLSARERTG GRGARRKWVE CVCLPGWHGP SCGVPTVVQY SNLPTKERLV
210 220 230 240 250
PREVPRRVIN AINVNHEFDL LDVRFHELGD VVDAFVVCES NFTAYGEPRP
260 270 280 290 300
LKFREMLTNG TFEYIRHKVL YVFLDHFPPG GRQDGWIADD YLRTFLTQDG
310 320 330 340 350
VSRLRNLRPD DVFIIDDADE IPARDGVLFL KLYDGWTEPF AFHMRKSLYG
360 370 380 390 400
FFWKQPGTLE VVSGCTVDML QAVYGLDGIR LRRRQYYTMP NFRQYENRTG
410 420 430 440 450
HILVQWSLGS PLHFAGWHCS WCFTPEGIYF KLVSAQNGDF PRWGDYEDKR
460 470 480 490 500
DLNYIRGLIR TGGWFDGTQQ EYPPADPSEH MYAPKYLLKN YDRFHYLLDN
510 520 530
PYQEPRSTAA GGWRHRGPEG RPPARGKLDE AEV
Length:533
Mass (Da):61,313
Last modified:March 15, 2005 - v3
Checksum:i11F56C44A6B173AB
GO

Sequence cautioni

The sequence BAA02937.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti346 – 3461K → T in BAA02937 (PubMed:8370666).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13789 mRNA. Translation: BAA02937.1. Different initiation.
CR456519 mRNA. Translation: CAG30405.1.
AL022312 Genomic DNA. Translation: CAI19177.1.
BC075025 mRNA. Translation: AAH75025.1.
BC075026 mRNA. Translation: AAH75026.1.
BC113383 mRNA. Translation: AAI13384.1.
BC113718 mRNA. Translation: AAI13719.1.
CCDSiCCDS13994.2.
PIRiJN0586.
RefSeqiNP_001091740.1. NM_001098270.1.
NP_002400.3. NM_002409.4.
XP_005261666.1. XM_005261609.2.
XP_011528486.1. XM_011530184.1.
XP_011528487.1. XM_011530185.1.
XP_011528488.1. XM_011530186.1.
XP_011528489.1. XM_011530187.1.
XP_011528490.1. XM_011530188.1.
XP_011528491.1. XM_011530189.1.
XP_011528492.1. XM_011530190.1.
XP_011528493.1. XM_011530191.1.
XP_011528494.1. XM_011530192.1.
XP_011528495.1. XM_011530193.1.
XP_011528496.1. XM_011530194.1.
UniGeneiHs.276808.

Genome annotation databases

EnsembliENST00000341184; ENSP00000345270; ENSG00000128268.
GeneIDi4248.
KEGGihsa:4248.
UCSCiuc003axv.6. human.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13789 mRNA. Translation: BAA02937.1. Different initiation.
CR456519 mRNA. Translation: CAG30405.1.
AL022312 Genomic DNA. Translation: CAI19177.1.
BC075025 mRNA. Translation: AAH75025.1.
BC075026 mRNA. Translation: AAH75026.1.
BC113383 mRNA. Translation: AAI13384.1.
BC113718 mRNA. Translation: AAI13719.1.
CCDSiCCDS13994.2.
PIRiJN0586.
RefSeqiNP_001091740.1. NM_001098270.1.
NP_002400.3. NM_002409.4.
XP_005261666.1. XM_005261609.2.
XP_011528486.1. XM_011530184.1.
XP_011528487.1. XM_011530185.1.
XP_011528488.1. XM_011530186.1.
XP_011528489.1. XM_011530187.1.
XP_011528490.1. XM_011530188.1.
XP_011528491.1. XM_011530189.1.
XP_011528492.1. XM_011530190.1.
XP_011528493.1. XM_011530191.1.
XP_011528494.1. XM_011530192.1.
XP_011528495.1. XM_011530193.1.
XP_011528496.1. XM_011530194.1.
UniGeneiHs.276808.

3D structure databases

ProteinModelPortaliQ09327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110404. 1 interaction.
STRINGi9606.ENSP00000345270.

Chemistry

BindingDBiQ09327.
ChEMBLiCHEMBL2375206.

Protein family/group databases

CAZyiGT17. Glycosyltransferase Family 17.

PTM databases

iPTMnetiQ09327.
PhosphoSiteiQ09327.

Polymorphism and mutation databases

BioMutaiMGAT3.
DMDMi61252497.

Proteomic databases

PaxDbiQ09327.
PeptideAtlasiQ09327.
PRIDEiQ09327.

Protocols and materials databases

DNASUi4248.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341184; ENSP00000345270; ENSG00000128268.
GeneIDi4248.
KEGGihsa:4248.
UCSCiuc003axv.6. human.

Organism-specific databases

CTDi4248.
GeneCardsiMGAT3.
HGNCiHGNC:7046. MGAT3.
HPAiHPA017598.
MIMi604621. gene.
neXtProtiNX_Q09327.
PharmGKBiPA30781.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEQJ. Eukaryota.
ENOG410YQKP. LUCA.
GeneTreeiENSGT00390000008221.
HOGENOMiHOG000113579.
HOVERGENiHBG052468.
InParanoidiQ09327.
KOiK00737.
OMAiYTMPGFR.
OrthoDBiEOG7MPRDD.
PhylomeDBiQ09327.
TreeFamiTF323781.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:HS05168-MONOMER.
ReactomeiR-HSA-975574. Reactions specific to the hybrid N-glycan synthesis pathway.

Miscellaneous databases

ChiTaRSiMGAT3. human.
GeneWikiiMGAT3.
GenomeRNAii4248.
PROiQ09327.
SOURCEiSearch...

Gene expression databases

BgeeiQ09327.
CleanExiHS_MGAT3.
ExpressionAtlasiQ09327. baseline and differential.
GenevisibleiQ09327. HS.

Family and domain databases

InterProiIPR006813. Glyco_trans_17.
[Graphical view]
PANTHERiPTHR12224. PTHR12224. 2 hits.
PfamiPF04724. Glyco_transf_17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III)."
    Ihara Y., Nishikawa A., Toma T., Soejima H., Niikawa N., Taniguchi N.
    J. Biochem. 113:692-698(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum and Fetal brain.

Entry informationi

Entry nameiMGAT3_HUMAN
AccessioniPrimary (citable) accession number: Q09327
Secondary accession number(s): A6NGD0
, Q14CK5, Q6IC49, Q9UH32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 15, 2005
Last modified: July 6, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.