P26572 (MGAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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=GNT-I
Short name=GlcNAc-T I

Gene names

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

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	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.
Cofactor	Manganese. The cofactor is mostly bound to the substrate By similarity.
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 Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine catabolic process Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara 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 integral to membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	acetylglucosaminyltransferase activity Traceable author statement Ref.1. Source: ProtInc alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	30 – 445	416	Lumenal Potential
Sites
	Active site	289	1	Proton acceptor Potential
	Metal binding	211	1	Manganese By similarity
	Binding site	115	1	Substrate By similarity
	Binding site	142	1	Substrate By similarity
	Binding site	188	1	Substrate By similarity
	Binding site	210	1	Substrate By similarity
	Binding site	320	1	Substrate By similarity
Amino acid modifications
	Disulfide bond	113 ↔ 143		By similarity
	Disulfide bond	237 ↔ 303		By similarity
Natural variations
	Natural variant	223	1	R → Q. Corresponds to variant rs7726005 [ dbSNP | Ensembl ].		VAR_028272
	Natural variant	435	1	L → P. Ref.2 Ref.4 Ref.7 Corresponds to variant rs634501 [ dbSNP | Ensembl ].		VAR_028273

Sequences

	Sequence		Length	Mass (Da)
	P26572 [UniParc]. Last modified November 2, 2010. Version 2. Checksum: 13402302ED69C302	FASTA	445	50,878
	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 LAPPLTWEGY DPSWN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-435. Tissue: Myeloid leukemia cell.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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], VARIANT PRO-435.
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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], VARIANT PRO-435. 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	M55621 mRNA. Translation: AAA52563.1. M61829 Genomic DNA. Translation: AAA75523.1. AK094130 mRNA. Translation: BAG52821.1. AK290769 mRNA. Translation: BAF83458.1. CR456861 mRNA. Translation: CAG33142.1. AC022413 Genomic DNA. No translation available. CH471165 Genomic DNA. Translation: EAW53739.1. CH471165 Genomic DNA. Translation: EAW53740.1. CH471165 Genomic DNA. Translation: EAW53741.1. CH471165 Genomic DNA. Translation: EAW53742.1. CH471165 Genomic DNA. Translation: EAW53743.1. CH471165 Genomic DNA. Translation: EAW53744.1. BC003575 mRNA. Translation: AAH03575.1.
IPI	IPI00000138.
PIR	XUHUMB. JH0397.
RefSeq	NP_001108089.1. NM_001114617.1. NP_001108090.1. NM_001114618.1. NP_001108091.1. NM_001114619.1. NP_001108092.1. NM_001114620.1. NP_002397.2. NM_002406.3.
UniGene	Hs.519818.
3D structure databases
ProteinModelPortal	P26572.
SMR	P26572. Positions 104-444.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1196185.
STRING	9606.ENSP00000311888.
Protein family/group databases
CAZy	GT13. Glycosyltransferase Family 13.
PTM databases
PhosphoSite	P26572.
Polymorphism databases
DMDM	311033399.
Proteomic databases
PaxDb	P26572.
PRIDE	P26572.
Protocols and materials databases
DNASU	4245.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000307826; ENSP00000311888; ENSG00000131446. ENST00000333055; ENSP00000332073; ENSG00000131446. ENST00000393340; ENSP00000377010; ENSG00000131446. ENST00000427865; ENSP00000402838; ENSG00000131446. ENST00000446023; ENSP00000404718; ENSG00000131446.
GeneID	4245.
KEGG	hsa:4245.
UCSC	uc003mmg.4. human.
Organism-specific databases
CTD	4245.
GeneCards	GC05M180218.
H-InvDB	HIX0005500. HIX0164288.
HGNC	HGNC:7044. MGAT1.
HPA	HPA017432.
MIM	160995. gene.
neXtProt	NX_P26572.
PharmGKB	PA30779.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG148227.
HOVERGEN	HBG052466.
InParanoid	P26572.
KO	K00726.
OMA	PPDHRKF.
OrthoDB	EOG4PNXGX.
PhylomeDB	P26572.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
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. PTHR10468. 1 hit.
Pfam	PF03071. GNT-I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MGAT1. human.
GenomeRNAi	4245.
NextBio	16733.
SOURCE	Search...

Entry information

Entry name

MGAT1_HUMAN

Accession

Primary (citable) accession number: P26572
Secondary accession number(s): A8K404, D3DWR1, Q6IBE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	November 2, 2010
Last modified:	April 3, 2013
This is version 123 of the entry and version 2 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.