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Protein

Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase

Gene

Ngly1

Organism
Mus musculus (Mouse)
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

Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. EC:3.5.1.52

<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

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by Z-VAD-fmk, a well-known caspase inhibitor, which inhibits enzyme activity through covalent binding of the carbohydrate to the single Cys-306 residue.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=114 µM for fetuin glycopeptide I1 Publication
  1. Vmax=0.0964 nmol/min/mg enzyme with fetuin glycopeptide I as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi247Zinc1
Metal bindingi250Zinc1
Metal bindingi280Zinc1
Metal bindingi283Zinc1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei306Nucleophile1
Active sitei3331
Active sitei3501

<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

  • metal ion binding Source: UniProtKB-KW
  • peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity Source: MGI

GO - Biological processi

  • glycoprotein catabolic process Source: UniProtKB
  • protein deglycosylation Source: MGI
  • protein quality control for misfolded or incompletely synthesized proteins Source: GO_Central

<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 functionHydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.52 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle

<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_and_taxonomy_section">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:
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC:3.5.1.52)
Short name:
PNGase
Short name:
mPNGase
Alternative name(s):
N-glycanase 1
Peptide:N-glycanase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Ngly1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 14

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1913276 Ngly1

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<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_and_biotech_section">'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>Mutagenesisi41N → P: Abolishes interaction with VCP. 1 Publication1
Mutagenesisi58N → A: Does not affect the interaction with VCP. 1 Publication1
Mutagenesisi79 – 80GF → AA: Abolishes interaction with VCP. 1 Publication2
Mutagenesisi306C → A: Abolishes 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002489732 – 651Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidaseAdd BLAST650

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9JI78

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9JI78

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

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PaxDbi
Q9JI78

PeptideAtlas

More...
PeptideAtlasi
Q9JI78

PRoteomics IDEntifications database

More...
PRIDEi
Q9JI78

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9JI78

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

More...
PhosphoSitePlusi
Q9JI78

<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

Ubiquitously expressed with highest level in testis.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000021785 Expressed in 279 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
MM_NGLY1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9JI78 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9JI78 MM

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with the proteasome components RAD23B and PSMC1. Interacts with directly with VCP. Interacts with DERL1, bringing it close to the endoplasmic reticulum membrane. Interacts with SAKS1.6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
208478, 7 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9JI78

Database of interacting proteins

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DIPi
DIP-41155N

Protein interaction database and analysis system

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IntActi
Q9JI78, 5 interactors

Molecular INTeraction database

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MINTi
Q9JI78

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000022310

<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

Secondary structure

1651
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9JI78

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

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SMRi
Q9JI78

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9JI78

<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_and_domains_section">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>Domaini30 – 91PUBAdd BLAST62
Domaini451 – 651PAWPROSITE-ProRule annotationAdd BLAST201

<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

The PUB domain mediates the interaction with VCP.1 Publication

<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 transglutaminase-like superfamily. PNGase family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0909 Eukaryota
ENOG410XP69 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000006540

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000247069

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG082026

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9JI78

KEGG Orthology (KO)

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KOi
K01456

Identification of Orthologs from Complete Genome Data

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OMAi
KVETDWN

Database of Orthologous Groups

More...
OrthoDBi
EOG091G09YB

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9JI78

TreeFam database of animal gene trees

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TreeFami
TF315254

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.120.1020, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008979 Galactose-bd-like_sf
IPR038765 Papain_like_cys_pep_sf
IPR038680 PAW_sf
IPR006588 Peptide_N_glycanase_PAW_dom
IPR036339 PUB-like_dom_sf
IPR018997 PUB_domain
IPR002931 Transglutaminase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04721 PAW, 1 hit
PF09409 PUB, 1 hit
PF01841 Transglut_core, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00613 PAW, 1 hit
SM00580 PUG, 1 hit
SM00460 TGc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF143503 SSF143503, 1 hit
SSF49785 SSF49785, 1 hit
SSF54001 SSF54001, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51398 PAW, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q9JI78-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASATLGSSS SSASPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPSDEK
60 70 80 90 100
YRSIRIGNTA FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK
110 120 130 140 150
IRDLIAIERS SRLDGSSKKV QFSQHPAAAK LPLEQSEDPA GLIRHSGNQT
160 170 180 190 200
GQLPSLPSAP MVVGDSTILK VLQSNIQHVQ LYENPVLQEK ALTCIPVSEL
210 220 230 240 250
KRKAQEKLFR ARKLDKGTNV SDEDFLLLEL LHWFKEEFFR WVNNIVCSKC
260 270 280 290 300
GGETRSRDEA LLPNDDELKW GAKNVENHYC DACQLSNRFP RYNNPEKLLE
310 320 330 340 350
TRCGRCGEWA NCFTLCCRAL GFEARYVWDY TDHVWTEVYS PSQQRWLHCD
360 370 380 390 400
ACEDVCDKPL LYEIGWGKKL SYIIAFSKDE VVDVTWRYSC KHDEVMSRRT
410 420 430 440 450
KVKEELLRET INGLNKQRQL SLSESRRKEL LQRIIVELVE FISPKTPRPG
460 470 480 490 500
ELGGRVSGSL AWRVARGETG LERKEILFIP SENEKISKQF HLRYDIVRDR
510 520 530 540 550
YIRVSDNNIN ISGWENGVWK MESIFRKVEK DWNMVYLARK EGSSFAYISW
560 570 580 590 600
KFECGSAGLK VDTVSIRTSS QSFESGSVRW KLRSETAQVN LLGDKNLRSY
610 620 630 640 650
NDFSGATEVT LEAELSRGDG DVAWQHTQLF RQSLNDSGEN GLEIIITFND

L
Length:651
Mass (Da):74,275
Last modified:September 5, 2006 - v2
<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:iF9D7A35726482F81
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A286YCI0A0A286YCI0_MOUSE
Peptide-N(4)-(N-acetyl-beta-glucosa...
Ngly1
596Annotation score:

Annotation score:1 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>
A0A286YDI5A0A286YDI5_MOUSE
Peptide-N(4)-(N-acetyl-beta-glucosa...
Ngly1
111Annotation score:

Annotation score:1 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>
A0A286YCZ7A0A286YCZ7_MOUSE
Peptide-N(4)-(N-acetyl-beta-glucosa...
Ngly1
251Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti509I → T in AAF74723 (PubMed:10831608).Curated1
Sequence conflicti509I → T in AAP03060 (PubMed:12711318).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF250927 mRNA Translation: AAF74723.1
AY225417 Genomic DNA Translation: AAP03060.1
AK003279 mRNA Translation: BAB22686.1
AK028248 mRNA Translation: BAC25839.1
BC028961 mRNA Translation: AAH28961.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS26832.1

NCBI Reference Sequences

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RefSeqi
NP_067479.2, NM_021504.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.258381

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000022310; ENSMUSP00000022310; ENSMUSG00000021785

Database of genes from NCBI RefSeq genomes

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GeneIDi
59007

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:59007

UCSC genome browser

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UCSCi
uc007sgz.1 mouse

<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
AF250927 mRNA Translation: AAF74723.1
AY225417 Genomic DNA Translation: AAP03060.1
AK003279 mRNA Translation: BAB22686.1
AK028248 mRNA Translation: BAC25839.1
BC028961 mRNA Translation: AAH28961.1
CCDSiCCDS26832.1
RefSeqiNP_067479.2, NM_021504.3
UniGeneiMm.258381

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D5UNMR-A1-119[»]
2F4MX-ray1.85A164-450[»]
2F4OX-ray2.26A164-450[»]
2G9FX-ray1.90A451-651[»]
2G9GX-ray2.00A451-651[»]
2HPJX-ray1.70A12-110[»]
2HPLX-ray1.80A12-111[»]
2I74X-ray1.75A/B471-651[»]
ProteinModelPortaliQ9JI78
SMRiQ9JI78
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208478, 7 interactors
CORUMiQ9JI78
DIPiDIP-41155N
IntActiQ9JI78, 5 interactors
MINTiQ9JI78
STRINGi10090.ENSMUSP00000022310

PTM databases

iPTMnetiQ9JI78
PhosphoSitePlusiQ9JI78

Proteomic databases

EPDiQ9JI78
MaxQBiQ9JI78
PaxDbiQ9JI78
PeptideAtlasiQ9JI78
PRIDEiQ9JI78

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022310; ENSMUSP00000022310; ENSMUSG00000021785
GeneIDi59007
KEGGimmu:59007
UCSCiuc007sgz.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
55768
MGIiMGI:1913276 Ngly1

Phylogenomic databases

eggNOGiKOG0909 Eukaryota
ENOG410XP69 LUCA
GeneTreeiENSGT00390000006540
HOGENOMiHOG000247069
HOVERGENiHBG082026
InParanoidiQ9JI78
KOiK01456
OMAiKVETDWN
OrthoDBiEOG091G09YB
PhylomeDBiQ9JI78
TreeFamiTF315254

Enzyme and pathway databases

BRENDAi3.5.1.52 3474
ReactomeiR-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle

Miscellaneous databases

EvolutionaryTraceiQ9JI78

Protein Ontology

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PROi
PR:Q9JI78

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000021785 Expressed in 279 organ(s), highest expression level in testis
CleanExiMM_NGLY1
ExpressionAtlasiQ9JI78 baseline and differential
GenevisibleiQ9JI78 MM

Family and domain databases

Gene3Di2.60.120.1020, 1 hit
InterProiView protein in InterPro
IPR008979 Galactose-bd-like_sf
IPR038765 Papain_like_cys_pep_sf
IPR038680 PAW_sf
IPR006588 Peptide_N_glycanase_PAW_dom
IPR036339 PUB-like_dom_sf
IPR018997 PUB_domain
IPR002931 Transglutaminase-like
PfamiView protein in Pfam
PF04721 PAW, 1 hit
PF09409 PUB, 1 hit
PF01841 Transglut_core, 1 hit
SMARTiView protein in SMART
SM00613 PAW, 1 hit
SM00580 PUG, 1 hit
SM00460 TGc, 1 hit
SUPFAMiSSF143503 SSF143503, 1 hit
SSF49785 SSF49785, 1 hit
SSF54001 SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS51398 PAW, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiNGLY1_MOUSE
<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: Q9JI78
Secondary accession number(s): Q8K113, Q9CTK3
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: December 5, 2018
This is version 121 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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