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P26572

- MGAT1_HUMAN

UniProt

P26572 - MGAT1_HUMAN

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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

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
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: Chromosome 5

Organism-specific databases

HGNCiHGNC:7044. MGAT1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. Golgi membrane Source: Reactome
  3. integral component of membrane Source: ProtInc
  4. membrane Source: UniProtKB
  5. vesicle Source: UniProtKB
Complete GO annotation...

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

BgeeiP26572.
CleanExiHS_MGAT1.
ExpressionAtlasiP26572. baseline and differential.
GenevestigatoriP26572.

Organism-specific databases

HPAiHPA017432.

Interactioni

Protein-protein interaction databases

BioGridi110401. 9 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.
GeneTreeiENSGT00530000063632.
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 [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:
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. 9 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.
GeneTreei ENSGT00530000063632.
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

Bgeei P26572.
CleanExi HS_MGAT1.
ExpressionAtlasi P26572. baseline and differential.
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

« 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.

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 29, 2014
This is version 137 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