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Protein

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

Gene

MGAT2

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

Functioni

Catalyzes an essential step in the conversion of oligo-mannose to complex N-glycans.

Catalytic activityi

UDP-N-acetyl-D-glucosamine + 6-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.

Pathway: 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:HS09725-MONOMER.
ReactomeiREACT_25302. Reactions specific to the complex N-glycan synthesis pathway.
REACT_268600. Defective MGAT2 causes MGAT2-CDG (CDG-2a).
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT16. Glycosyltransferase Family 16.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC:2.4.1.143)
Alternative name(s):
Beta-1,2-N-acetylglucosaminyltransferase II
GlcNAc-T II
Short name:
GNT-II
Mannoside acetylglucosaminyltransferase 2
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
Gene namesi
Name:MGAT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:7045. MGAT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 2920Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 447418LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • Golgi apparatus Source: HPA
  • Golgi membrane Source: Reactome
  • Golgi stack Source: InterPro
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 2A (CDG2A)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.

See also OMIM:212066
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti262 – 2621H → R in CDG2A. 1 Publication
VAR_003415
Natural varianti290 – 2901S → F in CDG2A. 1 Publication
VAR_003416
Natural varianti318 – 3181N → D in CDG2A. 1 Publication
VAR_012343

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

MIMi212066. phenotype.
Orphaneti79329. MGAT2-CDG.
PharmGKBiPA30780.

Polymorphism and mutation databases

BioMutaiMGAT2.
DMDMi1708004.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferasePRO_0000080517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi69 – 691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ10469.
PaxDbiQ10469.
PeptideAtlasiQ10469.
PRIDEiQ10469.

PTM databases

PhosphoSiteiQ10469.

Expressioni

Gene expression databases

BgeeiQ10469.
CleanExiHS_MGAT2.
GenevisibleiQ10469. HS.

Organism-specific databases

HPAiHPA043721.
HPA056824.

Interactioni

Protein-protein interaction databases

BioGridi110403. 2 interactions.
STRINGi9606.ENSP00000307423.

Structurei

3D structure databases

ProteinModelPortaliQ10469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239633.
GeneTreeiENSGT00390000007341.
HOVERGENiHBG052467.
InParanoidiQ10469.
KOiK00736.
OMAiCTFDEYN.
OrthoDBiEOG7TF79W.
PhylomeDBiQ10469.
TreeFamiTF314772.

Family and domain databases

Gene3Di3.90.550.10. 2 hits.
InterProiIPR007754. GlcNAc_II.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR12871. PTHR12871. 1 hit.
PfamiPF05060. MGAT2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.

Sequencei

Sequence statusi: Complete.

Q10469-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKNEALAPP LLDAEPARGA
60 70 80 90 100
GGRGGDHPSV AVGIRRVSNV SAASLVPAVP QPEADNLTLR YRSLVYQLNF
110 120 130 140 150
DQTLRNVDKA GTWAPRELVL VVQVHNRPEY LRLLLDSLRK AQGIDNVLVI
160 170 180 190 200
FSHDFWSTEI NQLIAGVNFC PVLQVFFPFS IQLYPNEFPG SDPRDCPRDL
210 220 230 240 250
PKNAALKLGC INAEYPDSFG HYREAKFSQT KHHWWWKLHF VWERVKILRD
260 270 280 290 300
YAGLILFLEE DHYLAPDFYH VFKKMWKLKQ QECPECDVLS LGTYSASRSF
310 320 330 340 350
YGMADKVDVK TWKSTEHNMG LALTRNAYQK LIECTDTFCT YDDYNWDWTL
360 370 380 390 400
QYLTVSCLPK FWKVLVPQIP RIFHAGDCGM HHKKTCRPST QSAQIESLLN
410 420 430 440
NNKQYMFPET LTISEKFTVV AISPPRKNGG WGDIRDHELC KSYRRLQ
Length:447
Mass (Da):51,550
Last modified:October 1, 1996 - v1
Checksum:i533B76D08BD8A572
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti299 – 2991S → R in BAG52082 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti262 – 2621H → R in CDG2A. 1 Publication
VAR_003415
Natural varianti290 – 2901S → F in CDG2A. 1 Publication
VAR_003416
Natural varianti318 – 3181N → D in CDG2A. 1 Publication
VAR_012343

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15128 Genomic DNA. Translation: AAA86956.1.
AK056167 mRNA. Translation: BAG51637.1.
AK075199 mRNA. Translation: BAG52082.1.
CH471078 Genomic DNA. Translation: EAW65758.1.
BC006390 mRNA. Translation: AAH06390.1.
CCDSiCCDS9690.1.
PIRiS66256.
RefSeqiNP_002399.1. NM_002408.3.
UniGeneiHs.93338.

Genome annotation databases

EnsembliENST00000305386; ENSP00000307423; ENSG00000168282.
GeneIDi4247.
KEGGihsa:4247.
UCSCiuc001wwr.3. human.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15128 Genomic DNA. Translation: AAA86956.1.
AK056167 mRNA. Translation: BAG51637.1.
AK075199 mRNA. Translation: BAG52082.1.
CH471078 Genomic DNA. Translation: EAW65758.1.
BC006390 mRNA. Translation: AAH06390.1.
CCDSiCCDS9690.1.
PIRiS66256.
RefSeqiNP_002399.1. NM_002408.3.
UniGeneiHs.93338.

3D structure databases

ProteinModelPortaliQ10469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110403. 2 interactions.
STRINGi9606.ENSP00000307423.

Chemistry

BindingDBiQ10469.
ChEMBLiCHEMBL2321630.

Protein family/group databases

CAZyiGT16. Glycosyltransferase Family 16.

PTM databases

PhosphoSiteiQ10469.

Polymorphism and mutation databases

BioMutaiMGAT2.
DMDMi1708004.

Proteomic databases

MaxQBiQ10469.
PaxDbiQ10469.
PeptideAtlasiQ10469.
PRIDEiQ10469.

Protocols and materials databases

DNASUi4247.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305386; ENSP00000307423; ENSG00000168282.
GeneIDi4247.
KEGGihsa:4247.
UCSCiuc001wwr.3. human.

Organism-specific databases

CTDi4247.
GeneCardsiGC14P050087.
GeneReviewsiMGAT2.
H-InvDBHIX0211283.
HGNCiHGNC:7045. MGAT2.
HPAiHPA043721.
HPA056824.
MIMi212066. phenotype.
602616. gene.
neXtProtiNX_Q10469.
Orphaneti79329. MGAT2-CDG.
PharmGKBiPA30780.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG239633.
GeneTreeiENSGT00390000007341.
HOVERGENiHBG052467.
InParanoidiQ10469.
KOiK00736.
OMAiCTFDEYN.
OrthoDBiEOG7TF79W.
PhylomeDBiQ10469.
TreeFamiTF314772.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:HS09725-MONOMER.
ReactomeiREACT_25302. Reactions specific to the complex N-glycan synthesis pathway.
REACT_268600. Defective MGAT2 causes MGAT2-CDG (CDG-2a).

Miscellaneous databases

GeneWikiiMGAT2.
GenomeRNAii4247.
NextBioi16741.
PROiQ10469.
SOURCEiSearch...

Gene expression databases

BgeeiQ10469.
CleanExiHS_MGAT2.
GenevisibleiQ10469. HS.

Family and domain databases

Gene3Di3.90.550.10. 2 hits.
InterProiIPR007754. GlcNAc_II.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR12871. PTHR12871. 1 hit.
PfamiPF05060. MGAT2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2-N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein."
    Tan J., D'Agostaro A.F., Bendiak B., Reck F., Sarkar M., Squire J.A., Leong P., Schachter H.
    Eur. J. Biochem. 231:317-328(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16.
    Tissue: Leukocyte.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  3. 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: Brain.
  5. "Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause carbohydrate-deficient glycoprotein syndrome type II, an autosomal recessive disease with defective brain development."
    Tan J., Dunn J., Jaeken J., Schachter H.
    Am. J. Hum. Genet. 59:810-817(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CDG2A ARG-262 AND PHE-290.
  6. "Congenital disorders of glycosylation IIa cause growth retardation, mental retardation, and facial dysmorphism."
    Cormier-Daire V., Amiel J., Vuillaumier-Barrot S., Tan J., Durand G., Munnich A., Le Merrer M., Seta N.
    J. Med. Genet. 37:875-877(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDG2A ASP-318.

Entry informationi

Entry nameiMGAT2_HUMAN
AccessioniPrimary (citable) accession number: Q10469
Secondary accession number(s): B3KPC5, B3KQM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 146 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

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 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.