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Entry version 134 (02 Dec 2020)
Sequence version 1 (01 Feb 1995)
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Protein

Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A

Gene

Mgat5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides (PubMed:8340368, PubMed:7615638). Catalyzes an important step in the biosynthesis of branched, complex-type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2 (By similarity). Via its role in the biosynthesis of complex N-glycans, plays an important role in the activation of cellular signaling pathways, reorganization of the actin cytoskeleton, cell-cell adhesion and cell migration (PubMed:7615638). MGAT5-dependent EGFR N-glycosylation enhances the interaction between EGFR and LGALS3 and thereby prevents rapid EGFR endocytosis and prolongs EGFR signaling. Required for efficient interaction between TGFB1 and its receptor. Enhances activation of intracellular signaling pathways by several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF. MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to the regulation of downstream signaling pathways. Promotes cell migration. Contributes to the regulation of the inflammatory response. MGAT5-dependent TCR N-glycosylation enhances the interaction between TCR and LGALS3, limits agonist-induced TCR clustering, and thereby dampens TCR-mediated responses to antigens. Required for normal leukocyte evasation and accumulation at sites of inflammation (By similarity). Inhibits attachment of monocytes to the vascular endothelium and subsequent monocyte diapedesis (By similarity).By similarity2 Publications
Promotes proliferation of umbilical vein endothelial cells and angiogenesis, at least in part by promoting the release of the growth factor FGF2 from the extracellular matrix.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.2 Publications
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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei525UDP-GlcNAcBy similarity1
Binding sitei553SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosyltransferase, Transferase

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-975577, N-Glycan antennae elongation

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT18, Glycosyltransferase Family 18

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A (EC:2.4.1.1552 Publications)
Alternative name(s):
Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase
GlcNAc-T V2 Publications
Short name:
GNT-V
Mannoside acetylglucosaminyltransferase 5
N-acetylglucosaminyl-transferase V1 Publication
Cleaved into the following chain:
Alternative name(s):
Secreted beta-1,6-N-acetylglucosaminyltransferase VCurated
Short name:
Secreted GNT-VCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Mgat5
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Rat genome database

More...
RGDi
620100, Mgat5

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 13CytoplasmicSequence analysisAdd BLAST13
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei14 – 30Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST17
Topological domaini31 – 740LumenalSequence analysisAdd BLAST710

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1795132

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000805241 – 740Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase AAdd BLAST740
ChainiPRO_000044569431 – 740Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase ABy similarityAdd BLAST710

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi109N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi114N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi117N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi144 ↔ 182By similarity
Disulfide bondi155 ↔ 195By similarity
Disulfide bondi171 ↔ 337By similarity
Glycosylationi333N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi371 ↔ 625By similarity
Glycosylationi432N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi446N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi648 ↔ 723By similarity
Disulfide bondi652 ↔ 725By similarity
Disulfide bondi659 ↔ 712By similarity
Disulfide bondi680 ↔ 701By similarity
Disulfide bondi736 ↔ 739By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.By similarity
A secreted form is released from the membrane after cleavage by gamma-secretase.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q08834

PRoteomics IDEntifications database

More...
PRIDEi
Q08834

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q08834, 6 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q08834

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q08834

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in kidney (at protein level). Detected in kidney.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000003614, Expressed in frontal cortex and 20 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q08834, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q08834, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000004995

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q08834

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni212 – 740Sufficient for catalytic activityBy similarityAdd BLAST529
Regioni377 – 378Substrate bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyltransferase 18 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QTNG, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153470

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_016749_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q08834

Identification of Orthologs from Complete Genome Data

More...
OMAi
IIHSYME

Database of Orthologous Groups

More...
OrthoDBi
179031at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q08834

TreeFam database of animal gene trees

More...
TreeFami
TF313714

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027833, DUF4525
IPR026116, GlyclTrfase_18

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF15027, DUF4525, 1 hit
PF15024, Glyco_transf_18, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q08834-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAFFSPWKLS SQKLGFFLVT FGFIWGMMLL HFTIQQRTQP ESSSMLREQI
60 70 80 90 100
LDLSKRYIKA LAEENRNVVD GPYAGVMTAY DLKKTLAVLL DNILQRIGKL
110 120 130 140 150
ESKVDNLVNG TGANSTNSTT AVPSLVSLEK INVADIINGV QEKCVLPPMD
160 170 180 190 200
GYPHCEGKIK WMKDMWRSDP CYADYGVDGT SCSFFIYLSE VENWCPRLPW
210 220 230 240 250
RAKNPYEEAD HNSLAEIRTD FNILYGMMKK HEEFRWMRLR IRRMADAWIQ
260 270 280 290 300
AIKSLAEKQN LEKRKRKKIL VHLGLLTKES GFKIAETAFS GGPLGELVQW
310 320 330 340 350
SDLITSLYLL GHDIRISASL AELKEIMKKV VGNRSGCPTV GDRIVELIYI
360 370 380 390 400
DIVGLAQFKK TLGPSWVHYQ CMLRVLDSFG TEPEFNHASY AQSKGHKTPW
410 420 430 440 450
GKWNLNPQQF YTMFPHTPDN SFLGFVVEQH LNSSDIHHIN EIKRQNQSLV
460 470 480 490 500
YGKVDSFWKN KKIYLDIIHT YMEVHATVYG SSTKNIPSYV KNHGILSGRD
510 520 530 540 550
LQFLLRETKL FVGLGFPYEG PAPLEAIANG CAFLNPKFNP PKSSKNTDFF
560 570 580 590 600
IGKPTLRELT SQHPYAEVFI GRPHVWTVDL NNREEVEDAV KAILNQKIEP
610 620 630 640 650
YMPYEFTCEG MLQRINAFIE KQDFCHGQVM WPPLSALQVK LAEPGQSCKQ
660 670 680 690 700
VCQESQLICE PSFFQHLNKE KDLLKYKVIC QSSELYKDIL VPSFYPKSKH
710 720 730 740
CVFQGDLLLF SCAGAHPTHQ RICPCRDFIK GQVALCKDCL
Length:740
Mass (Da):84,562
Last modified:February 1, 1995 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC0BD7F820FEA959C
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L14284 mRNA Translation: AAA41665.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A47134

NCBI Reference Sequences

More...
RefSeqi
NP_075583.1, NM_023095.1
XP_008767721.2, XM_008769499.2
XP_017454423.1, XM_017598934.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000004995; ENSRNOP00000004995; ENSRNOG00000003614

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
65271

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:65271

UCSC genome browser

More...
UCSCi
RGD:620100, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14284 mRNA Translation: AAA41665.1
PIRiA47134
RefSeqiNP_075583.1, NM_023095.1
XP_008767721.2, XM_008769499.2
XP_017454423.1, XM_017598934.1

3D structure databases

SMRiQ08834
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004995

Chemistry databases

ChEMBLiCHEMBL1795132

Protein family/group databases

CAZyiGT18, Glycosyltransferase Family 18

PTM databases

GlyGeniQ08834, 6 sites
iPTMnetiQ08834
PhosphoSitePlusiQ08834

Proteomic databases

PaxDbiQ08834
PRIDEiQ08834

Genome annotation databases

EnsembliENSRNOT00000004995; ENSRNOP00000004995; ENSRNOG00000003614
GeneIDi65271
KEGGirno:65271
UCSCiRGD:620100, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4249
RGDi620100, Mgat5

Phylogenomic databases

eggNOGiENOG502QTNG, Eukaryota
GeneTreeiENSGT00940000153470
HOGENOMiCLU_016749_1_0_1
InParanoidiQ08834
OMAiIIHSYME
OrthoDBi179031at2759
PhylomeDBiQ08834
TreeFamiTF313714

Enzyme and pathway databases

UniPathwayiUPA00378
ReactomeiR-RNO-975577, N-Glycan antennae elongation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q08834

Gene expression databases

BgeeiENSRNOG00000003614, Expressed in frontal cortex and 20 other tissues
ExpressionAtlasiQ08834, baseline and differential
GenevisibleiQ08834, RN

Family and domain databases

InterProiView protein in InterPro
IPR027833, DUF4525
IPR026116, GlyclTrfase_18
PfamiView protein in Pfam
PF15027, DUF4525, 1 hit
PF15024, Glyco_transf_18, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMGT5A_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q08834
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 2, 2020
This is version 134 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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