Reviewed, UniProtKB/Swiss-Prot P26572 (MGAT1_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
    EC=2.4.1.101
Alternative name(s):
    N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
      Short name=GlcNAc-T I
      Short name=GNT-I

Gene names

Name:	MGAT1
Synonyms:	GGNT1, GLCT1, GLYT1, MGAT

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
Catalytic activity	UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(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.
Tissue specificity	Appears to be present in all tissues.
Sequence similarities	Belongs to the glycosyltransferase 13 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid N-linked glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: InterPro integral to membrane Ref.2 Traceable author statement. Source: ProtInc
Molecular function	alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 445	445	Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase		PRO_0000191384
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 29	23	Signal-anchor for type II membrane protein Potential
	Topological domain	30 – 445	416	Lumenal Potential
Natural variations
	Natural variant	223	1	R → Q: dbSNP rs7726005.		VAR_028272
	Natural variant	435	1	P → L: dbSNP rs634501. Ref.2 Ref.3 Ref.5		VAR_028273

Sequences

	Sequence		Length	Mass (Da)
	P26572-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 1340386EED69C302	FASTA	445	50,862
	10 20 30 40 50 60 MLKKQSAGLV LWGAILFVAW NALLLLFFWT RPAPGRPPSV SALDGDPASL TREVIRLAQD 70 80 90 100 110 120 AEVELERQRG LLQQIGDALS SQRGRVPTAA PPAQPRVPVT PAPAVIPILV IACDRSTVRR 130 140 150 160 170 180 CLDKLLHYRP SAELFPIIVS QDCGHEETAQ AIASYGSAVT HIRQPDLSSI AVPPDHRKFQ 190 200 210 220 230 240 GYYKIARHYR WALGQVFRQF RFPAAVVVED DLEVAPDFFE YFRATYPLLK ADPSLWCVSA 250 260 270 280 290 300 WNDNGKEQMV DASRPELLYR TDFFPGLGWL LLAELWAELE PKWPKAFWDD WMRRPEQRQG 310 320 330 340 350 360 RACIRPEISR TMTFGRKGVS HGQFFDQHLK FIKLNQQFVH FTQLDLSYLQ REAYDRDFLA 370 380 390 400 410 420 RVYGAPQLQV EKVRTNDRKE LGEVRVQYTG RDSFKAFAKA LGVMDDLKSG VPRAGYRGIV 430 440 TFQFRGRRVH LAPPPTWEGY DPSWN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and localization to chromosome 5 of the human UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I gene." Hull E., Sarkar M., Spruijt M.P.N., Hoeppener J.W.M., Dunn R., Schachter H. Biochem. Biophys. Res. Commun. 176:608-615(1991) [PubMed: 1827260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Myeloid leukemia cell.
[2]	"Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation." Kumar R., Yang J., Larsen R.D., Stanley P. Proc. Natl. Acad. Sci. U.S.A. 87:9948-9952(1990) [PubMed: 1702225] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-435.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-435.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	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], VARIANT LEU-435.
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

Cross-references

Sequence databases
EMBL GenBank DDBJ	M61829 Genomic DNA. Translation: AAA75523.1. M55621 mRNA. Translation: AAA52563.1. AK094130 mRNA. Translation: BAG52821.1. AK290769 mRNA. Translation: BAF83458.1. CR456861 mRNA. Translation: CAG33142.1. CH471165 Genomic DNA. Translation: EAW53739.1. BC003575 mRNA. Translation: AAH03575.1.
IPI	IPI00000138.
PIR	XUHUMB. JH0397.
RefSeq	NP_001108089.1. NP_001108090.1. NP_001108091.1. NP_001108092.1. NP_002397.2.
UniGene	Hs.519818
3D structure databases
SMR	P26572. Positions 104-444.
ModBase	Search...
Protein-protein interaction databases
STRING	P26572.
Protein family/group databases
CAZy	GT13. Glycosyltransferase Family 13.
PTM databases
PhosphoSite	P26572.
Proteomic databases
PRIDE	P26572.
Genome annotation databases
Ensembl	ENST00000307826; ENSP00000311888; ENSG00000131446; Homo sapiens. [Genome view] ENST00000333055; ENSP00000332073; ENSG00000131446; Homo sapiens. [Genome view] ENST00000393340; ENSP00000377010; ENSG00000131446; Homo sapiens. [Genome view] ENST00000427865; ENSP00000402838; ENSG00000131446; Homo sapiens. [Genome view] ENST00000446023; ENSP00000404718; ENSG00000131446; Homo sapiens. [Genome view] ENST00000452920; ENSP00000412647; ENSG00000131446; Homo sapiens. [Genome view]
GeneID	4245.
KEGG	hsa:4245.
Organism-specific databases
CTD	4245.
GeneCards	GC05M180150.
H-InvDB	HIX0005500.
HGNC	HGNC:7044. MGAT1.
HPA	HPA017432.
MIM	160995. gene.
PharmGKB	PA30779.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18878.
HOVERGEN	P26572.
InParanoid	P26572.
Enzyme and pathway databases
BRENDA	2.4.1.101. 247.
Gene expression databases
ArrayExpress	P26572.
Bgee	P26572.
CleanEx	HS_MGAT1.
Genevestigator	P26572.
GermOnline	ENSG00000131446. Homo sapiens.
Family and domain databases
InterPro	IPR004139. Glyco_trans_13. [Graphical view]
PANTHER	PTHR10468. Glyco_trans_13. 1 hit.
Pfam	PF03071. GNT-I. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	16733.
SOURCE	Search...

Entry information

Entry name

MGAT1_HUMAN

Accession

Primary (citable) accession number: P26572
Secondary accession number(s): A8K404, Q6IBE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	January 19, 2010
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.