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UniProtKB - Q10473 (GALT1_RAT)

Entry version 155 (02 Dec 2020)
Sequence version 1 (01 Oct 1996)
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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

Galnt1

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 initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7.

<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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+

<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.
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 sitei156SubstrateBy similarity1
Binding sitei186SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi209ManganeseBy similarity1
Metal bindingi211ManganeseBy similarity1
Binding sitei316SubstrateBy similarity1
Metal bindingi344ManganeseBy similarity1
Binding sitei347SubstrateBy similarity1
Binding sitei352SubstrateBy 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

  • carbohydrate binding Source: UniProtKB-KW
  • manganese ion binding Source: UniProtKB
  • polypeptide N-acetylgalactosaminyltransferase activity Source: RGD
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
LigandLectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.1.41, 5301

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic
R-RNO-913709, O-linked glycosylation of mucins

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

More...UniPathwayi		UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		CBM13, Carbohydrate-Binding Module Family 13
GT27, Glycosyltransferase Family 27

<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:
Polypeptide N-acetylgalactosaminyltransferase 1 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 1
Short name:
GalNAc-T1
Short name:
pp-GaNTase 1
Protein-UDP acetylgalactosaminyltransferase 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
Cleaved into the following chain:
Polypeptide N-acetylgalactosaminyltransferase 1 soluble form
<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:Galnt1
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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 18

Organism-specific databases

Rat genome database

More...RGDi		620358, Galnt1

<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 – 8CytoplasmicSequence analysis8
<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>Transmembranei9 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini29 – 559LumenalSequence analysisAdd BLAST531

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi106C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi212C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. 1 Publication1
Mutagenesisi214C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. 1 Publication1
Mutagenesisi235C → A: No effect. 1 Publication1
Mutagenesisi330C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi339C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi408C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi442C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi444D → A: Induces a strong decrease in activity; loss of function; when associated with A-484 and A-525. 2 Publications1
Mutagenesisi455G → Q: Induces a decrease in activity. 1 Publication1
Mutagenesisi457F → A: Little or no effect. 1 Publication1
Mutagenesisi459C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi465N → A: Little or no effect. 1 Publication1
Mutagenesisi466Q → A: Induces a decrease in activity. 1 Publication1
Mutagenesisi468F → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi468F → W or Y: Little or no effect. 1 Publication1
Mutagenesisi482C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi484D → A: Loss of enzyme activity; when associated with A-444 and A-525. 2 Publications1
Mutagenesisi497C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi523C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi525D → A: Loss of enzyme activity; when associated with A-444 and A-484. 2 Publications1
Mutagenesisi540C → A: Loss of enzyme activity. 1 Publication1

<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_00002233901 – 559Polypeptide N-acetylgalactosaminyltransferase 1Add BLAST559
ChainiPRO_000001226341 – 559Polypeptide N-acetylgalactosaminyltransferase 1 soluble formAdd BLAST519

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>Glycosylationi95N-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 bondi106 ↔ 339PROSITE-ProRule annotation
Disulfide bondi330 ↔ 408PROSITE-ProRule annotation
Disulfide bondi442 ↔ 459PROSITE-ProRule annotation
Disulfide bondi482 ↔ 497PROSITE-ProRule annotation
Disulfide bondi523 ↔ 540PROSITE-ProRule annotation
Glycosylationi552N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

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

More...PaxDbi		Q10473

PRoteomics IDEntifications database

More...PRIDEi		Q10473

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q10473, 2 sites

<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

Heart, brain, spleen, liver, skeletal muscle and kidney.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000016207, Expressed in jejunum and 20 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q10473, 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.ENSRNOP00000022117

<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		Q10473

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini429 – 551Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST123

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>Regioni115 – 225Catalytic subdomain AAdd BLAST111
Regioni285 – 347Catalytic subdomain BAdd BLAST63

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
The ricin B-type lectin domain directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.

<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 2 family. GalNAc-T subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3736, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154732

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_013477_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q10473

Identification of Orthologs from Complete Genome Data

More...OMAi		VAEVWMC

Database of Orthologous Groups

More...OrthoDBi		606683at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q10473

TreeFam database of animal gene trees

More...TreeFami		TF313267

Family and domain databases

Conserved Domains Database

More...CDDi		cd00161, RICIN, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.550.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001173, Glyco_trans_2-like
IPR029044, Nucleotide-diphossugar_trans
IPR035992, Ricin_B-like_lectins
IPR000772, Ricin_B_lectin

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00535, Glycos_transf_2, 1 hit
PF00652, Ricin_B_lectin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00458, RICIN, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50370, SSF50370, 1 hit
SSF53448, SSF53448, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50231, RICIN_B_LECTIN, 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.

Q10473-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKKER GLPAGDVLEL 
        60         70         80         90        100
VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIAFNRSLPD 
       110        120        130        140        150
VRLEGCKTKV YPDSLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE 
       160        170        180        190        200
IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS 
       210        220        230        240        250
KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV ISDDTFEYMA 
       260        270        280        290        300
GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR 
       310        320        330        340        350
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT 
       360        370        380        390        400
PYTFPGGTGQ IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV 
       410        420        430        440        450
GLRHKLQCKP FSWYLENIYP DSQIPRHYFS LGEIRNVETN QCLDNMARKE 
       460        470        480        490        500
NEKVGIFNCH GMGGNQVFSY TANKEIRTDD LCLDVSKLNG PVTMLKCHHL 
       510        520        530        540        550
KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC TGSRSQQWLL 

RNVTLPEIF
Length:559
Mass (Da):64,229
Last modified:October 1, 1996 - 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:i5E36A95D9422C853
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
U35890 mRNA Translation: AAC52511.1

NCBI Reference Sequences

More...RefSeqi		NP_077349.1, NM_024373.1
XP_006254533.1, XM_006254471.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000022117; ENSRNOP00000022117; ENSRNOG00000016207

Database of genes from NCBI RefSeq genomes

More...GeneIDi		79214

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:79214

UCSC genome browser

More...UCSCi		RGD:620358, 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
U35890 mRNA Translation: AAC52511.1
RefSeqiNP_077349.1, NM_024373.1
XP_006254533.1, XM_006254471.3

3D structure databases

SMRiQ10473
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022117

Protein family/group databases

CAZyiCBM13, Carbohydrate-Binding Module Family 13
GT27, Glycosyltransferase Family 27

PTM databases

GlyGeniQ10473, 2 sites

Proteomic databases

PaxDbiQ10473
PRIDEiQ10473

Genome annotation databases

EnsembliENSRNOT00000022117; ENSRNOP00000022117; ENSRNOG00000016207
GeneIDi79214
KEGGirno:79214
UCSCiRGD:620358, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2589
RGDi620358, Galnt1

Phylogenomic databases

eggNOGiKOG3736, Eukaryota
GeneTreeiENSGT00940000154732
HOGENOMiCLU_013477_0_1_1
InParanoidiQ10473
OMAiVAEVWMC
OrthoDBi606683at2759
PhylomeDBiQ10473
TreeFamiTF313267

Enzyme and pathway databases

UniPathwayiUPA00378
BRENDAi2.4.1.41, 5301
ReactomeiR-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic
R-RNO-913709, O-linked glycosylation of mucins

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q10473

Gene expression databases

BgeeiENSRNOG00000016207, Expressed in jejunum and 20 other tissues
GenevisibleiQ10473, RN

Family and domain databases

CDDicd00161, RICIN, 1 hit
Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR001173, Glyco_trans_2-like
IPR029044, Nucleotide-diphossugar_trans
IPR035992, Ricin_B-like_lectins
IPR000772, Ricin_B_lectin
PfamiView protein in Pfam
PF00535, Glycos_transf_2, 1 hit
PF00652, Ricin_B_lectin, 1 hit
SMARTiView protein in SMART
SM00458, RICIN, 1 hit
SUPFAMiSSF50370, SSF50370, 1 hit
SSF53448, SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS50231, RICIN_B_LECTIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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MobiDB: a database of protein disorder and mobility annotations

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<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 nameiGALT1_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: Q10473
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 2, 2020
This is version 155 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

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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