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Protein

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

Gene

Mgat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei117 – 1171SubstrateBy similarity
Binding sitei144 – 1441SubstrateBy similarity
Binding sitei190 – 1901SubstrateBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Metal bindingi213 – 2131ManganeseBy similarity
Active sitei291 – 2911Proton acceptorSequence Analysis
Binding sitei322 – 3221SubstrateBy similarity

GO - Molecular functioni

  1. acetylglucosaminyltransferase activity Source: MGI
  2. alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. in utero embryonic development Source: MGI
  2. protein glycosylation Source: UniProtKB-UniPathway
  3. UDP-N-acetylglucosamine catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_324693. 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:Gnt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:96973. 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 – 447418LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. Golgi membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: MGI
  5. vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferasePRO_0000191385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi115 ↔ 145By similarity
Disulfide bondi239 ↔ 305By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP27808.
PaxDbiP27808.
PRIDEiP27808.

PTM databases

PhosphoSiteiP27808.

Expressioni

Tissue specificityi

Appears to be present in all tissues.

Gene expression databases

BgeeiP27808.
CleanExiMM_MGAT1.
ExpressionAtlasiP27808. baseline and differential.
GenevestigatoriP27808.

Interactioni

Protein-protein interaction databases

MINTiMINT-1836159.

Structurei

3D structure databases

ProteinModelPortaliP27808.
SMRiP27808. Positions 108-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 13 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG148227.
HOGENOMiHOG000247055.
HOVERGENiHBG052466.
InParanoidiP27808.
KOiK00726.
OMAiHELEPIW.
OrthoDBiEOG7R56SN.
PhylomeDBiP27808.
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.

P27808-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKQTAGLV LWGAIIFVGW NALLLLFFWT RPAPGRLPSD SALGDDPASL
60 70 80 90 100
TREVIHLAED AEAELERQRG LLQQIKEHYA LWRQRWRVPT VAPPAWPRVP
110 120 130 140 150
VTPSPVQIPI LVIACDRSTV RRCLDKLLHY RPSAERFPII VSQDCGHEET
160 170 180 190 200
AQVIASYGTA VTHIRQPDLS NIAVQPDHRK FQGYYKIARH YRWALGQIFN
210 220 230 240 250
KFKFPAAVVV EDDLEVAPDF FEYFQATYPL LRTDPSLWCV SAWNDNGKEQ
260 270 280 290 300
MVDSSKPELL YRTDFFPGLG WLLLADLWAE LEPKWPKAFW DDWMRRPEQR
310 320 330 340 350
KGRACIRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY
360 370 380 390 400
LQQEAYDRDF LAQVYGAPQL QVEKVRTNDQ KELGEVRVQY TSRDSFKAFA
410 420 430 440
KALGVMDDLK SGVPRAGYRG IVTFQFRGRR VHLAPPQTWT GYDPSWN
Length:447
Mass (Da):51,690
Last modified:August 1, 1992 - v1
Checksum:iE7C65EA8C8B34E6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73491 Genomic DNA. Translation: AAA37698.1.
L07037 mRNA. Translation: AAA40478.1.
AK087959 mRNA. Translation: BAC40058.1.
BC006629 mRNA. Translation: AAH06629.1.
CCDSiCCDS24602.1.
PIRiA42500.
RefSeqiNP_001103618.1. NM_001110148.1.
NP_001103619.1. NM_001110149.1.
NP_001103620.1. NM_001110150.1.
NP_034924.3. NM_010794.3.
XP_006532460.1. XM_006532397.2.
XP_006532461.1. XM_006532398.2.
XP_006532462.1. XM_006532399.1.
XP_006532463.1. XM_006532400.2.
XP_006532464.1. XM_006532401.2.
UniGeneiMm.196933.

Genome annotation databases

EnsembliENSMUST00000081794; ENSMUSP00000080484; ENSMUSG00000020346.
ENSMUST00000101293; ENSMUSP00000098851; ENSMUSG00000020346.
ENSMUST00000109194; ENSMUSP00000104817; ENSMUSG00000020346.
ENSMUST00000167400; ENSMUSP00000126303; ENSMUSG00000020346.
GeneIDi17308.
KEGGimmu:17308.
UCSCiuc007iqb.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

alpha-1,3-mannosyl-glycoprotein beta 1,2-GlcNAc T I (Mgat1)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73491 Genomic DNA. Translation: AAA37698.1.
L07037 mRNA. Translation: AAA40478.1.
AK087959 mRNA. Translation: BAC40058.1.
BC006629 mRNA. Translation: AAH06629.1.
CCDSiCCDS24602.1.
PIRiA42500.
RefSeqiNP_001103618.1. NM_001110148.1.
NP_001103619.1. NM_001110149.1.
NP_001103620.1. NM_001110150.1.
NP_034924.3. NM_010794.3.
XP_006532460.1. XM_006532397.2.
XP_006532461.1. XM_006532398.2.
XP_006532462.1. XM_006532399.1.
XP_006532463.1. XM_006532400.2.
XP_006532464.1. XM_006532401.2.
UniGeneiMm.196933.

3D structure databases

ProteinModelPortaliP27808.
SMRiP27808. Positions 108-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1836159.

Protein family/group databases

CAZyiGT13. Glycosyltransferase Family 13.

PTM databases

PhosphoSiteiP27808.

Proteomic databases

MaxQBiP27808.
PaxDbiP27808.
PRIDEiP27808.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081794; ENSMUSP00000080484; ENSMUSG00000020346.
ENSMUST00000101293; ENSMUSP00000098851; ENSMUSG00000020346.
ENSMUST00000109194; ENSMUSP00000104817; ENSMUSG00000020346.
ENSMUST00000167400; ENSMUSP00000126303; ENSMUSG00000020346.
GeneIDi17308.
KEGGimmu:17308.
UCSCiuc007iqb.2. mouse.

Organism-specific databases

CTDi4245.
MGIiMGI:96973. Mgat1.

Phylogenomic databases

eggNOGiNOG148227.
HOGENOMiHOG000247055.
HOVERGENiHBG052466.
InParanoidiP27808.
KOiK00726.
OMAiHELEPIW.
OrthoDBiEOG7R56SN.
PhylomeDBiP27808.
TreeFamiTF320555.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_324693. N-glycan trimming and elongation in the cis-Golgi.

Miscellaneous databases

ChiTaRSiMgat1. mouse.
NextBioi291856.
PROiP27808.
SOURCEiSearch...

Gene expression databases

BgeeiP27808.
CleanExiMM_MGAT1.
ExpressionAtlasiP27808. baseline and differential.
GenevestigatoriP27808.

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. "Molecular cloning and characterization of the mouse UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I gene."
    Pownall S., Kozak C.A., Schappert K.T., Sarkar M., Hull E., Schachter H., Math J.D.
    Genomics 12:699-704(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and expression of the murine gene and chromosomal location of the human gene encoding N-acetylglucosaminyltransferase I."
    Kumar R., Yang J., Eddy R.L., Byers M.G., Shows T.B., Stanley P.
    Glycobiology 2:383-393(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Thymus.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.

Entry informationi

Entry nameiMGAT1_MOUSE
AccessioniPrimary (citable) accession number: P27808
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 1, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.