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Protein

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

Gene

MGAT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.

Catalytic activityi

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.

Cofactori

Mn2+By similarityNote: The cofactor is mostly bound to the substrate.By similarity

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151SubstrateBy similarity
Binding sitei142 – 1421SubstrateBy similarity
Binding sitei188 – 1881SubstrateBy similarity
Binding sitei210 – 2101SubstrateBy similarity
Metal bindingi211 – 2111ManganeseBy similarity
Active sitei289 – 2891Proton acceptorSequence Analysis
Binding sitei320 – 3201SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05528-MONOMER.
ReactomeiREACT_25210. N-glycan trimming and elongation in the cis-Golgi.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT13. Glycosyltransferase Family 13.

Names & Taxonomyi

Protein namesi
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 namesi
Name:MGAT1
Synonyms:GGNT1, GLCT1, GLYT1, MGAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:7044. MGAT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 445416LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular vesicle Source: UniProtKB
  • Golgi membrane Source: Reactome
  • integral component of membrane Source: ProtInc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30779.

Polymorphism and mutation databases

BioMutaiMGAT1.
DMDMi311033399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferasePRO_0000191384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi113 ↔ 143By similarity
Disulfide bondi237 ↔ 303By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP26572.
PaxDbiP26572.
PRIDEiP26572.

PTM databases

PhosphoSiteiP26572.

Expressioni

Tissue specificityi

Appears to be present in all tissues.

Gene expression databases

BgeeiP26572.
CleanExiHS_MGAT1.
ExpressionAtlasiP26572. baseline and differential.
GenevisibleiP26572. HS.

Organism-specific databases

HPAiHPA017432.

Interactioni

Protein-protein interaction databases

BioGridi110401. 5 interactions.
IntActiP26572. 2 interactions.
MINTiMINT-1196185.
STRINGi9606.ENSP00000311888.

Structurei

3D structure databases

ProteinModelPortaliP26572.
SMRiP26572. Positions 104-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 13 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG148227.
GeneTreeiENSGT00530000063632.
HOVERGENiHBG052466.
InParanoidiP26572.
KOiK00726.
OMAiWIELSPK.
OrthoDBiEOG7R56SN.
PhylomeDBiP26572.
TreeFamiTF320555.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004139. Glyco_trans_13.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10468. PTHR10468. 1 hit.
PfamiPF03071. GNT-I. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P26572-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKQSAGLV LWGAILFVAW NALLLLFFWT RPAPGRPPSV SALDGDPASL
60 70 80 90 100
TREVIRLAQD AEVELERQRG LLQQIGDALS SQRGRVPTAA PPAQPRVPVT
110 120 130 140 150
PAPAVIPILV IACDRSTVRR CLDKLLHYRP SAELFPIIVS QDCGHEETAQ
160 170 180 190 200
AIASYGSAVT HIRQPDLSSI AVPPDHRKFQ GYYKIARHYR WALGQVFRQF
210 220 230 240 250
RFPAAVVVED DLEVAPDFFE YFRATYPLLK ADPSLWCVSA WNDNGKEQMV
260 270 280 290 300
DASRPELLYR TDFFPGLGWL LLAELWAELE PKWPKAFWDD WMRRPEQRQG
310 320 330 340 350
RACIRPEISR TMTFGRKGVS HGQFFDQHLK FIKLNQQFVH FTQLDLSYLQ
360 370 380 390 400
REAYDRDFLA RVYGAPQLQV EKVRTNDRKE LGEVRVQYTG RDSFKAFAKA
410 420 430 440
LGVMDDLKSG VPRAGYRGIV TFQFRGRRVH LAPPLTWEGY DPSWN
Length:445
Mass (Da):50,878
Last modified:November 2, 2010 - v2
Checksum:i13402302ED69C302
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti291 – 2911W → R in BAG52510 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti223 – 2231R → Q.
Corresponds to variant rs7726005 [ dbSNP | Ensembl ].
VAR_028272
Natural varianti435 – 4351L → P.4 Publications
Corresponds to variant rs634501 [ dbSNP | Ensembl ].
VAR_028273

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4458.1.
PIRiJH0397. XUHUMB.
RefSeqiNP_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.
UniGeneiHs.519818.

Genome annotation databases

EnsembliENST00000307826; ENSP00000311888; ENSG00000131446.
ENST00000333055; ENSP00000332073; ENSG00000131446.
ENST00000393340; ENSP00000377010; ENSG00000131446.
ENST00000427865; ENSP00000402838; ENSG00000131446.
ENST00000446023; ENSP00000404718; ENSG00000131446.
GeneIDi4245.
KEGGihsa:4245.
UCSCiuc003mmg.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4458.1.
PIRiJH0397. XUHUMB.
RefSeqiNP_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.
UniGeneiHs.519818.

3D structure databases

ProteinModelPortaliP26572.
SMRiP26572. Positions 104-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110401. 5 interactions.
IntActiP26572. 2 interactions.
MINTiMINT-1196185.
STRINGi9606.ENSP00000311888.

Chemistry

BindingDBiP26572.
ChEMBLiCHEMBL2375207.

Protein family/group databases

CAZyiGT13. Glycosyltransferase Family 13.

PTM databases

PhosphoSiteiP26572.

Polymorphism and mutation databases

BioMutaiMGAT1.
DMDMi311033399.

Proteomic databases

MaxQBiP26572.
PaxDbiP26572.
PRIDEiP26572.

Protocols and materials databases

DNASUi4245.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307826; ENSP00000311888; ENSG00000131446.
ENST00000333055; ENSP00000332073; ENSG00000131446.
ENST00000393340; ENSP00000377010; ENSG00000131446.
ENST00000427865; ENSP00000402838; ENSG00000131446.
ENST00000446023; ENSP00000404718; ENSG00000131446.
GeneIDi4245.
KEGGihsa:4245.
UCSCiuc003mmg.4. human.

Organism-specific databases

CTDi4245.
GeneCardsiGC05M180218.
H-InvDBHIX0005500.
HIX0164288.
HGNCiHGNC:7044. MGAT1.
HPAiHPA017432.
MIMi160995. gene.
neXtProtiNX_P26572.
PharmGKBiPA30779.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG148227.
GeneTreeiENSGT00530000063632.
HOVERGENiHBG052466.
InParanoidiP26572.
KOiK00726.
OMAiWIELSPK.
OrthoDBiEOG7R56SN.
PhylomeDBiP26572.
TreeFamiTF320555.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:HS05528-MONOMER.
ReactomeiREACT_25210. N-glycan trimming and elongation in the cis-Golgi.

Miscellaneous databases

ChiTaRSiMGAT1. human.
GeneWikiiMGAT1.
GenomeRNAii4245.
NextBioi16733.
PROiP26572.
SOURCEiSearch...

Gene expression databases

BgeeiP26572.
CleanExiHS_MGAT1.
ExpressionAtlasiP26572. baseline and differential.
GenevisibleiP26572. HS.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004139. Glyco_trans_13.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10468. PTHR10468. 1 hit.
PfamiPF03071. GNT-I. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], 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.
    , 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. 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.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMGAT1_HUMAN
AccessioniPrimary (citable) accession number: P26572
Secondary accession number(s): A8K404
, B3KRU8, D3DWR1, Q6IBE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 2, 2010
Last modified: June 24, 2015
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.