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P26572 (MGAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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-1,3-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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentGolgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandManganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processUDP-N-acetylglucosamine catabolic process

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement Ref.1. Source: ProtInc

cellular protein metabolic process

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein glycosylation

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 23376485. Source: UniProt

integral component of membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionacetylglucosaminyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
PRO_0000191384

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 445416Lumenal Potential

Sites

Active site2891Proton acceptor Potential
Metal binding2111Manganese By similarity
Binding site1151Substrate By similarity
Binding site1421Substrate By similarity
Binding site1881Substrate By similarity
Binding site2101Substrate By similarity
Binding site3201Substrate By similarity

Amino acid modifications

Disulfide bond113 ↔ 143 By similarity
Disulfide bond237 ↔ 303 By similarity

Natural variations

Natural variant2231R → Q.
Corresponds to variant rs7726005 [ dbSNP | Ensembl ].
VAR_028272
Natural variant4351L → P. Ref.2 Ref.3 Ref.4 Ref.7
Corresponds to variant rs634501 [ dbSNP | Ensembl ].
VAR_028273

Experimental info

Sequence conflict2911W → R in BAG52510. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P26572 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: 13402302ED69C302

FASTA44550,878
        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 

« Hide

References

« Hide '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. 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], VARIANT PRO-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], 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. expand/collapse author list , 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. 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].
[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.
AK092256 mRNA. Translation: BAG52510.1.
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.
CCDSCCDS4458.1.
PIRXUHUMB. JH0397.
RefSeqNP_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.
XP_005265972.1. XM_005265915.1.
XP_005265973.1. XM_005265916.1.
XP_006714929.1. XM_006714866.1.
XP_006714930.1. XM_006714867.1.
UniGeneHs.519818.

3D structure databases

ProteinModelPortalP26572.
SMRP26572. Positions 104-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110401. 4 interactions.
IntActP26572. 2 interactions.
MINTMINT-1196185.
STRING9606.ENSP00000311888.

Chemistry

ChEMBLCHEMBL2375207.

Protein family/group databases

CAZyGT13. Glycosyltransferase Family 13.

PTM databases

PhosphoSiteP26572.

Polymorphism databases

DMDM311033399.

Proteomic databases

MaxQBP26572.
PaxDbP26572.
PRIDEP26572.

Protocols and materials databases

DNASU4245.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307826; ENSP00000311888; ENSG00000131446.
ENST00000333055; ENSP00000332073; ENSG00000131446.
ENST00000393340; ENSP00000377010; ENSG00000131446.
ENST00000427865; ENSP00000402838; ENSG00000131446.
ENST00000446023; ENSP00000404718; ENSG00000131446.
GeneID4245.
KEGGhsa:4245.
UCSCuc003mmg.4. human.

Organism-specific databases

CTD4245.
GeneCardsGC05M180218.
H-InvDBHIX0005500.
HIX0164288.
HGNCHGNC:7044. MGAT1.
HPAHPA017432.
MIM160995. gene.
neXtProtNX_P26572.
PharmGKBPA30779.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148227.
HOVERGENHBG052466.
InParanoidP26572.
KOK00726.
OMAHEETAQV.
OrthoDBEOG7R56SN.
PhylomeDBP26572.
TreeFamTF320555.

Enzyme and pathway databases

BioCycMetaCyc:HS05528-MONOMER.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressP26572.
BgeeP26572.
CleanExHS_MGAT1.
GenevestigatorP26572.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR004139. Glyco_trans_13.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERPTHR10468. PTHR10468. 1 hit.
PfamPF03071. GNT-I. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMGAT1. human.
GeneWikiMGAT1.
GenomeRNAi4245.
NextBio16733.
PROP26572.
SOURCESearch...

Entry information

Entry nameMGAT1_HUMAN
AccessionPrimary (citable) accession number: P26572
Secondary accession number(s): A8K404 expand/collapse secondary AC list , B3KRU8, D3DWR1, Q6IBE3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 134 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

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 5

Human chromosome 5: entries, gene names and cross-references to MIM