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Protein

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

Gene

Mgat2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes an essential step in the conversion of oligo-mannose to complex N-glycans.By similarity

Catalytic activityi

UDP-N-acetyl-D-glucosamine + 6-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.

Pathway:iprotein 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.

GO - Molecular functioni

  • alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Source: MGI
  • carbohydrate binding Source: Ensembl

GO - Biological processi

  • oligosaccharide biosynthetic process Source: InterPro
  • protein N-linked glycosylation via asparagine Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_278515. Reactions specific to the complex N-glycan synthesis pathway.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT16. Glycosyltransferase Family 16.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC:2.4.1.143)
Alternative name(s):
Beta-1,2-N-acetylglucosaminyltransferase II
GlcNAc-T II
Short name:
GNT-II
Mannoside acetylglucosaminyltransferase 2
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
Gene namesi
Name:Mgat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2384966. Mgat2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 2920Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 442413LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 442442Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferasePRO_0000080518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ921V5.
PaxDbiQ921V5.
PRIDEiQ921V5.

PTM databases

PhosphoSiteiQ921V5.

Expressioni

Gene expression databases

BgeeiQ921V5.
CleanExiMM_MGAT2.
GenevisibleiQ921V5. MM.

Interactioni

Protein-protein interaction databases

IntActiQ921V5. 1 interaction.
MINTiMINT-1864592.
STRINGi10090.ENSMUSP00000057905.

Structurei

3D structure databases

ProteinModelPortaliQ921V5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239633.
GeneTreeiENSGT00390000007341.
HOGENOMiHOG000261661.
HOVERGENiHBG052467.
InParanoidiQ921V5.
KOiK00736.
OMAiLSMVVPM.
OrthoDBiEOG7TF79W.
PhylomeDBiQ921V5.
TreeFamiTF314772.

Family and domain databases

Gene3Di3.90.550.10. 2 hits.
InterProiIPR007754. GlcNAc_II.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR12871. PTHR12871. 1 hit.
PfamiPF05060. MGAT2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.

Sequencei

Sequence statusi: Complete.

Q921V5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKSDALGPP LLDAEPVRGA
60 70 80 90 100
GHLAVSVGIR RVSNESAAPL VPAVPRPEVD NLTLRYRSLV YQLNFDQMLR
110 120 130 140 150
NVGNDGTWSP GELVLVVQVH NRPEYLRLLI DSLRKAQGIQ EVLVIFSHDF
160 170 180 190 200
WSAEINSLIS RVDFCPVLQV FFPFSIQLYP NEFPGSDPRD CPRDLKKNAA
210 220 230 240 250
LKLGCINAEY PDSFGHYREA KFSQTKHHWW WKLHFVWERV KVLQDYTGLI
260 270 280 290 300
LFLEEDHYLA PDFYHVFKKM WKLKQQECPG CDVLSLGTYT TIRSFYGIAD
310 320 330 340 350
KVDVKTWKST EHNMGLALTR DAYQKLIECT DTFCTYDDYN WDWTLQYLTL
360 370 380 390 400
ACLPKIWKVL VPQAPRIFHA GDCGMHHKKT CRPSTQSAQI ESLLNSNKQY
410 420 430 440
LFPETLVIGE KFPMAAISPP RKNGGWGDIR DHELCKSYRR LQ
Length:442
Mass (Da):51,030
Last modified:December 1, 2001 - v1
Checksum:iE32D078C4F209843
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91K → E in BAC38888 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK083370 mRNA. Translation: BAC38888.1.
AK152925 mRNA. Translation: BAE31600.1.
BC010583 mRNA. Translation: AAH10583.1.
BC027169 mRNA. Translation: AAH27169.1.
CCDSiCCDS25947.1.
RefSeqiNP_666147.1. NM_146035.2.
UniGeneiMm.206642.
Mm.398746.
Mm.483133.

Genome annotation databases

EnsembliENSMUST00000060579; ENSMUSP00000057905; ENSMUSG00000043998.
GeneIDi217664.
KEGGimmu:217664.
UCSCiuc011ymy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK083370 mRNA. Translation: BAC38888.1.
AK152925 mRNA. Translation: BAE31600.1.
BC010583 mRNA. Translation: AAH10583.1.
BC027169 mRNA. Translation: AAH27169.1.
CCDSiCCDS25947.1.
RefSeqiNP_666147.1. NM_146035.2.
UniGeneiMm.206642.
Mm.398746.
Mm.483133.

3D structure databases

ProteinModelPortaliQ921V5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ921V5. 1 interaction.
MINTiMINT-1864592.
STRINGi10090.ENSMUSP00000057905.

Chemistry

BindingDBiQ921V5.
ChEMBLiCHEMBL2375203.

Protein family/group databases

CAZyiGT16. Glycosyltransferase Family 16.

PTM databases

PhosphoSiteiQ921V5.

Proteomic databases

MaxQBiQ921V5.
PaxDbiQ921V5.
PRIDEiQ921V5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060579; ENSMUSP00000057905; ENSMUSG00000043998.
GeneIDi217664.
KEGGimmu:217664.
UCSCiuc011ymy.1. mouse.

Organism-specific databases

CTDi4247.
MGIiMGI:2384966. Mgat2.

Phylogenomic databases

eggNOGiNOG239633.
GeneTreeiENSGT00390000007341.
HOGENOMiHOG000261661.
HOVERGENiHBG052467.
InParanoidiQ921V5.
KOiK00736.
OMAiLSMVVPM.
OrthoDBiEOG7TF79W.
PhylomeDBiQ921V5.
TreeFamiTF314772.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_278515. Reactions specific to the complex N-glycan synthesis pathway.

Miscellaneous databases

NextBioi375938.
PROiQ921V5.
SOURCEiSearch...

Gene expression databases

BgeeiQ921V5.
CleanExiMM_MGAT2.
GenevisibleiQ921V5. MM.

Family and domain databases

Gene3Di3.90.550.10. 2 hits.
InterProiIPR007754. GlcNAc_II.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR12871. PTHR12871. 1 hit.
PfamiPF05060. MGAT2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiMGAT2_MOUSE
AccessioniPrimary (citable) accession number: Q921V5
Secondary accession number(s): Q3U6X4, Q8C3Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 106 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

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.