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P26572

- MGAT1_HUMAN

UniProt

P26572 - MGAT1_HUMAN

Protein

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

Gene

MGAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
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    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

    Manganese. The cofactor is mostly bound to the substrate By similarity.By similarity

    Pathwayi

    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

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. cellular protein metabolic process Source: Reactome
    3. in utero embryonic development Source: Ensembl
    4. post-translational protein modification Source: Reactome
    5. protein glycosylation Source: ProtInc
    6. protein N-linked glycosylation via asparagine Source: Reactome
    7. UDP-N-acetylglucosamine catabolic process Source: Ensembl

    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: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:7044. MGAT1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. Golgi membrane Source: Reactome
    3. integral component of membrane Source: ProtInc
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30779.

    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

    ArrayExpressiP26572.
    BgeeiP26572.
    CleanExiHS_MGAT1.
    GenevestigatoriP26572.

    Organism-specific databases

    HPAiHPA017432.

    Interactioni

    Protein-protein interaction databases

    BioGridi110401. 4 interactions.
    IntActiP26572. 2 interactions.
    MINTiMINT-1196185.
    STRINGi9606.ENSP00000311888.

    Structurei

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini30 – 445416LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 13 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG148227.
    HOVERGENiHBG052466.
    InParanoidiP26572.
    KOiK00726.
    OMAiHEETAQV.
    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

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    MLKKQSAGLV LWGAILFVAW NALLLLFFWT RPAPGRPPSV SALDGDPASL    50
    TREVIRLAQD AEVELERQRG LLQQIGDALS SQRGRVPTAA PPAQPRVPVT 100
    PAPAVIPILV IACDRSTVRR CLDKLLHYRP SAELFPIIVS QDCGHEETAQ 150
    AIASYGSAVT HIRQPDLSSI AVPPDHRKFQ GYYKIARHYR WALGQVFRQF 200
    RFPAAVVVED DLEVAPDFFE YFRATYPLLK ADPSLWCVSA WNDNGKEQMV 250
    DASRPELLYR TDFFPGLGWL LLAELWAELE PKWPKAFWDD WMRRPEQRQG 300
    RACIRPEISR TMTFGRKGVS HGQFFDQHLK FIKLNQQFVH FTQLDLSYLQ 350
    REAYDRDFLA RVYGAPQLQV EKVRTNDRKE LGEVRVQYTG RDSFKAFAKA 400
    LGVMDDLKSG VPRAGYRGIV TFQFRGRRVH LAPPLTWEGY DPSWN 445
    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:
    EMBL
    GenBank
    DDBJ
    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.
    XP_006714930.1. XM_006714867.1.
    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.

    Polymorphism databases

    DMDMi311033399.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4458.1.
    PIRi JH0397. XUHUMB.
    RefSeqi 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.
    XP_005265972.1. XM_005265915.1.
    XP_005265973.1. XM_005265916.1.
    XP_006714929.1. XM_006714866.1.
    XP_006714930.1. XM_006714867.1.
    UniGenei Hs.519818.

    3D structure databases

    ProteinModelPortali P26572.
    SMRi P26572. Positions 104-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110401. 4 interactions.
    IntActi P26572. 2 interactions.
    MINTi MINT-1196185.
    STRINGi 9606.ENSP00000311888.

    Chemistry

    ChEMBLi CHEMBL2375207.

    Protein family/group databases

    CAZyi GT13. Glycosyltransferase Family 13.

    PTM databases

    PhosphoSitei P26572.

    Polymorphism databases

    DMDMi 311033399.

    Proteomic databases

    MaxQBi P26572.
    PaxDbi P26572.
    PRIDEi P26572.

    Protocols and materials databases

    DNASUi 4245.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307826 ; ENSP00000311888 ; ENSG00000131446 .
    ENST00000333055 ; ENSP00000332073 ; ENSG00000131446 .
    ENST00000393340 ; ENSP00000377010 ; ENSG00000131446 .
    ENST00000427865 ; ENSP00000402838 ; ENSG00000131446 .
    ENST00000446023 ; ENSP00000404718 ; ENSG00000131446 .
    GeneIDi 4245.
    KEGGi hsa:4245.
    UCSCi uc003mmg.4. human.

    Organism-specific databases

    CTDi 4245.
    GeneCardsi GC05M180218.
    H-InvDB HIX0005500.
    HIX0164288.
    HGNCi HGNC:7044. MGAT1.
    HPAi HPA017432.
    MIMi 160995. gene.
    neXtProti NX_P26572.
    PharmGKBi PA30779.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG148227.
    HOVERGENi HBG052466.
    InParanoidi P26572.
    KOi K00726.
    OMAi HEETAQV.
    OrthoDBi EOG7R56SN.
    PhylomeDBi P26572.
    TreeFami TF320555.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci MetaCyc:HS05528-MONOMER.
    Reactomei REACT_25210. N-glycan trimming and elongation in the cis-Golgi.

    Miscellaneous databases

    ChiTaRSi MGAT1. human.
    GeneWikii MGAT1.
    GenomeRNAii 4245.
    NextBioi 16733.
    PROi P26572.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26572.
    Bgeei P26572.
    CleanExi HS_MGAT1.
    Genevestigatori P26572.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR004139. Glyco_trans_13.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    PANTHERi PTHR10468. PTHR10468. 1 hit.
    Pfami PF03071. GNT-I. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 136 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