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Q10469 (MGAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MGAT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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 modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein.

Involvement in disease

Congenital disorder of glycosylation 2A (CDG2A) [MIM:212066]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
PRO_0000080517

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 2920Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 447418Lumenal Potential

Amino acid modifications

Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation861N-linked (GlcNAc...) Potential

Natural variations

Natural variant2621H → R in CDG2A. Ref.5
VAR_003415
Natural variant2901S → F in CDG2A. Ref.5
VAR_003416
Natural variant3181N → D in CDG2A. Ref.6
VAR_012343

Sequences

Sequence LengthMass (Da)Tools
Q10469 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 533B76D08BD8A572

FASTA44751,550
        10         20         30         40         50         60 
MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKNEALAPP LLDAEPARGA GGRGGDHPSV 

        70         80         90        100        110        120 
AVGIRRVSNV SAASLVPAVP QPEADNLTLR YRSLVYQLNF DQTLRNVDKA GTWAPRELVL 

       130        140        150        160        170        180 
VVQVHNRPEY LRLLLDSLRK AQGIDNVLVI FSHDFWSTEI NQLIAGVNFC PVLQVFFPFS 

       190        200        210        220        230        240 
IQLYPNEFPG SDPRDCPRDL PKNAALKLGC INAEYPDSFG HYREAKFSQT KHHWWWKLHF 

       250        260        270        280        290        300 
VWERVKILRD YAGLILFLEE DHYLAPDFYH VFKKMWKLKQ QECPECDVLS LGTYSASRSF 

       310        320        330        340        350        360 
YGMADKVDVK TWKSTEHNMG LALTRNAYQK LIECTDTFCT YDDYNWDWTL QYLTVSCLPK 

       370        380        390        400        410        420 
FWKVLVPQIP RIFHAGDCGM HHKKTCRPST QSAQIESLLN NNKQYMFPET LTISEKFTVV 

       430        440 
AISPPRKNGG WGDIRDHELC KSYRRLQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.

Web resources

GeneReviews
GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15128 Genomic DNA. Translation: AAA86956.1.
AK056167 mRNA. Translation: BAG51637.1.
CH471078 Genomic DNA. Translation: EAW65758.1.
BC006390 mRNA. Translation: AAH06390.1.
PIRS66256.
RefSeqNP_002399.1. NM_002408.3.
UniGeneHs.93338.

3D structure databases

ProteinModelPortalQ10469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000307423.

Chemistry

ChEMBLCHEMBL2321630.

Protein family/group databases

CAZyGT16. Glycosyltransferase Family 16.

PTM databases

PhosphoSiteQ10469.

Polymorphism databases

DMDM1708004.

Proteomic databases

PaxDbQ10469.
PeptideAtlasQ10469.
PRIDEQ10469.

Protocols and materials databases

DNASU4247.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305386; ENSP00000307423; ENSG00000168282.
GeneID4247.
KEGGhsa:4247.
UCSCuc001wwr.3. human.

Organism-specific databases

CTD4247.
GeneCardsGC14P050087.
H-InvDBHIX0211283.
HGNCHGNC:7045. MGAT2.
HPAHPA043721.
MIM212066. phenotype.
602616. gene.
neXtProtNX_Q10469.
Orphanet79329. MGAT2-CDG.
PharmGKBPA30780.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239633.
HOVERGENHBG052467.
InParanoidQ10469.
KOK00736.
OMAHAGDCGM.
OrthoDBEOG7TF79W.
PhylomeDBQ10469.
TreeFamTF314772.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ10469.
BgeeQ10469.
CleanExHS_MGAT2.
GenevestigatorQ10469.

Family and domain databases

InterProIPR007754. GlcNAc_II.
[Graphical view]
PANTHERPTHR12871. PTHR12871. 1 hit.
PfamPF05060. MGAT2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMGAT2.
GenomeRNAi4247.
NextBio16741.
PROQ10469.
SOURCESearch...

Entry information

Entry nameMGAT2_HUMAN
AccessionPrimary (citable) accession number: Q10469
Secondary accession number(s): B3KPC5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM