Q10469 (MGAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

MGAT2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Disease	Congenital disorder of glycosylation Disease mutation
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	oligosaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro oligosaccharide metabolic process Traceable author statement Ref.1. Source: ProtInc post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome Golgi stack Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Traceable author statement Ref.1. Source: ProtInc carbohydrate binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 447	447	Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase		PRO_0000080517
Regions
	Topological domain	1 – 9	9	Cytoplasmic Potential
	Transmembrane	10 – 29	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	30 – 447	418	Lumenal Potential
Amino acid modifications
	Glycosylation	69	1	N-linked (GlcNAc...) Potential
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	262	1	H → R in CDG2A. Ref.5		VAR_003415
	Natural variant	290	1	S → F in CDG2A. Ref.5		VAR_003416
	Natural variant	318	1	N → D in CDG2A. Ref.6		VAR_012343

Sequences

	Sequence		Length	Mass (Da)
	Q10469 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 533B76D08BD8A572	FASTA	447	51,550
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI01010309.
PIR	S66256.
RefSeq	NP_002399.1. NM_002408.3.
UniGene	Hs.93338.
3D structure databases
ProteinModelPortal	Q10469.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000307423.
Protein family/group databases
CAZy	GT16. Glycosyltransferase Family 16.
PTM databases
PhosphoSite	Q10469.
Polymorphism databases
DMDM	1708004.
Proteomic databases
PaxDb	Q10469.
PeptideAtlas	Q10469.
PRIDE	Q10469.
Protocols and materials databases
DNASU	4247.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000305386; ENSP00000307423; ENSG00000168282.
GeneID	4247.
KEGG	hsa:4247.
UCSC	uc001wwr.3. human.
Organism-specific databases
CTD	4247.
GeneCards	GC14P050087.
H-InvDB	HIX0211283.
HGNC	HGNC:7045. MGAT2.
HPA	HPA043721.
MIM	212066. phenotype. 602616. gene.
neXtProt	NX_Q10469.
Orphanet	79329. CDG syndrome type IIa.
PharmGKB	PA30780.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG239633.
HOVERGEN	HBG052467.
InParanoid	Q10469.
KO	K00736.
OrthoDB	EOG4VX255.
PhylomeDB	Q10469.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q10469.
Bgee	Q10469.
CleanEx	HS_MGAT2.
Genevestigator	Q10469.
GermOnline	ENSG00000168282. Homo sapiens.
Family and domain databases
InterPro	IPR007754. GlcNAc_II. [Graphical view]
PANTHER	PTHR12871. PTHR12871. 1 hit.
Pfam	PF05060. MGAT2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	4247.
NextBio	16741.
SOURCE	Search...

Entry information

Entry name

MGAT2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.