Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q07075 (AMPE_HUMAN)

Protein

Glutamyl aminopeptidase

Gene

ENPEP

Organism
Homo sapiens (Human)
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

Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II.1 Publication

<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

  • Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.2 Publications EC:3.4.11.7

<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

Substrate specificity is modulated by calcium which enhances the enzymatic activity for cleavage of acidic residues while reducing its activity with basic residues. Inhibited by aminopeptidase inhibitors amastatin and bestatin.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei221Binds calcium which modulates its enzyme activity1 Publication1
<p>This subsection of the ‘Function’ 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 sitei223SubstrateCombined sources1 Publication1
<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 bindingi393Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1
<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 sitei394Proton acceptorPROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi397Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi416Zinc; catalyticPROSITE-ProRule annotationCombined sources1 Publication1
Sitei479Transition state stabilizerCombined sources1 Publication1
Binding sitei887SubstrateCombined sources1 Publication1

<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

  • aminopeptidase activity Source: UniProtKB
  • metalloaminopeptidase activity Source: UniProtKB
  • metallopeptidase activity Source: Reactome
  • peptide binding Source: GO_Central
  • zinc ion binding Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 functionAminopeptidase, Hydrolase, Metalloprotease, Protease
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins

Protein family/group databases

MEROPS protease database

More...MEROPSi		M01.003

<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:
Glutamyl aminopeptidase (EC:3.4.11.72 Publications)
Short name:
EAP
Alternative name(s):
Aminopeptidase A
Short name:
AP-A
Differentiation antigen gp160
CD_antigen: CD249
<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:ENPEP
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000138792.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:3355 ENPEP

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		138297 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q07075

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 – 18CytoplasmicSequence analysisAdd BLAST18
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei19 – 39Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini40 – 957ExtracellularSequence analysisAdd BLAST918

Keywords - Cellular componenti

Cell membrane, Membrane

<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>Mutagenesisi356T → V: Reduced enzyme activity. 1 Publication1
Mutagenesisi887R → A: Reduced enzyme activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		2028

Open Targets

More...OpenTargetsi		ENSG00000138792

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27790

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3439

Drug and drug target database

More...DrugBanki		DB00142 L-Glutamic Acid

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ENPEP

Domain mapping of disease mutations (DMDM)

More...DMDMi		296439445

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000950951 – 957Glutamyl aminopeptidaseAdd BLAST957

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi98N-linked (GlcNAc...) asparagine; atypicalCombined sources1 Publication1
Glycosylationi124N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi197N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi324N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Glycosylationi340N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi554N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi589N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi597N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi607N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi678N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi763N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Glycosylationi773N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi801N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi828N-linked (GlcNAc...) asparagineCombined sources1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q07075

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q07075

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

More...PaxDbi		Q07075

PeptideAtlas

More...PeptideAtlasi		Q07075

PRoteomics IDEntifications database

More...PRIDEi		Q07075

ProteomicsDB human proteome resource

More...ProteomicsDBi		58502

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q07075

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

More...PhosphoSitePlusi		Q07075

<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

Expressed in choriocarcinoma cancer cell lines (at protein level) (PubMed:10692253). Expressed by epithelial cells of the proximal tubule cells and the glomerulus of the nephron. Also found in a variety of other tissues.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000138792 Expressed in 154 organ(s), highest expression level in jejunal mucosa

CleanEx database of gene expression profiles

More...CleanExi		HS_ENPEP

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q07075 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q07075 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA002821
HPA005128

<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

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108342, 5 interactors

Protein interaction database and analysis system

More...IntActi		Q07075, 3 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000265162

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q07075

<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

1957
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q07075

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

More...SMRi		Q07075

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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>Regioni357 – 361Substrate bindingCombined sources1 Publication5

<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 peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1046 Eukaryota
COG0308 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156946

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000106482

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG006616

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q07075

KEGG Orthology (KO)

More...KOi		K11141

Identification of Orthologs from Complete Genome Data

More...OMAi		PTRHLWL

Database of Orthologous Groups

More...OrthoDBi		EOG091G01GH

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q07075

TreeFam database of animal gene trees

More...TreeFami		TF300395

Family and domain databases

Conserved Domains Database

More...CDDi		cd09601 M1_APN_2, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR033508 Aminopeptidase_A
IPR024571 ERAP1-like_C_dom
IPR034016 M1_APN-typ
IPR001930 Peptidase_M1
IPR014782 Peptidase_M1_N

The PANTHER Classification System

More...PANTHERi		PTHR11533 PTHR11533, 1 hit
PTHR11533:SF242 PTHR11533:SF242, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF11838 ERAP1_C, 1 hit
PF01433 Peptidase_M1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00756 ALADIPTASE

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00142 ZINC_PROTEASE, 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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q07075-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNFAEREGSK RYCIQTKHVA ILCAVVVGVG LIVGLAVGLT RSCDSSGDGG 
        60         70         80         90        100
PGTAPAPSHL PSSTASPSGP PAQDQDICPA SEDESGQWKN FRLPDFVNPV 
       110        120        130        140        150
HYDLHVKPLL EEDTYTGTVS ISINLSAPTR YLWLHLRETR ITRLPELKRP 
       160        170        180        190        200
SGDQVQVRRC FEYKKQEYVV VEAEEELTPS SGDGLYLLTM EFAGWLNGSL 
       210        220        230        240        250
VGFYRTTYTE NGQVKSIVAT DHEPTDARKS FPCFDEPNKK ATYTISITHP 
       260        270        280        290        300
KEYGALSNMP VAKEESVDDK WTRTTFEKSV PMSTYLVCFA VHQFDSVKRI 
       310        320        330        340        350
SNSGKPLTIY VQPEQKHTAE YAANITKSVF DYFEEYFAMN YSLPKLDKIA 
       360        370        380        390        400
IPDFGTGAME NWGLITYRET NLLYDPKESA SSNQQRVATV VAHELVHQWF 
       410        420        430        440        450
GNIVTMDWWE DLWLNEGFAS FFEFLGVNHA ETDWQMRDQM LLEDVLPVQE 
       460        470        480        490        500
DDSLMSSHPI IVTVTTPDEI TSVFDGISYS KGSSILRMLE DWIKPENFQK 
       510        520        530        540        550
GCQMYLEKYQ FKNAKTSDFW AALEEASRLP VKEVMDTWTR QMGYPVLNVN 
       560        570        580        590        600
GVKNITQKRF LLDPRANPSQ PPSDLGYTWN IPVKWTEDNI TSSVLFNRSE 
       610        620        630        640        650
KEGITLNSSN PSGNAFLKIN PDHIGFYRVN YEVATWDSIA TALSLNHKTF 
       660        670        680        690        700
SSADRASLID DAFALARAQL LDYKVALNLT KYLKREENFL PWQRVISAVT 
       710        720        730        740        750
YIISMFEDDK ELYPMIEEYF QGQVKPIADS LGWNDAGDHV TKLLRSSVLG 
       760        770        780        790        800
FACKMGDREA LNNASSLFEQ WLNGTVSLPV NLRLLVYRYG MQNSGNEISW 
       810        820        830        840        850
NYTLEQYQKT SLAQEKEKLL YGLASVKNVT LLSRYLDLLK DTNLIKTQDV 
       860        870        880        890        900
FTVIRYISYN SYGKNMAWNW IQLNWDYLVN RYTLNNRNLG RIVTIAEPFN 
       910        920        930        940        950
TELQLWQMES FFAKYPQAGA GEKPREQVLE TVKNNIEWLK QHRNTIREWF 

FNLLESG
Length:957
Mass (Da):109,244
Last modified:May 18, 2010 - v3
<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:iAB6407432A45A7C6
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YA67H0YA67_HUMAN
Glutamyl aminopeptidase
ENPEP
144Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_030359213Q → R4 PublicationsCorresponds to variant dbSNP:rs10004516Ensembl.1
Natural variantiVAR_030360218V → A1 PublicationCorresponds to variant dbSNP:rs1126483Ensembl.1
Natural variantiVAR_057056437R → H. Corresponds to variant dbSNP:rs34949711Ensembl.1
Natural variantiVAR_057057861S → R. Corresponds to variant dbSNP:rs35812243Ensembl.1
Natural variantiVAR_036047887R → T in a breast cancer sample; somatic mutation. 1 Publication1

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
L14721 mRNA Translation: AAA35522.1
L12468 mRNA Translation: AAA16876.1
AC017068 Genomic DNA No translation available.
AC098798 Genomic DNA No translation available.
BC094770 mRNA Translation: AAH94770.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3691.1

Protein sequence database of the Protein Information Resource

More...PIRi		A47531

NCBI Reference Sequences

More...RefSeqi		NP_001968.3, NM_001977.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.435765

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000265162; ENSP00000265162; ENSG00000138792

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2028

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2028

UCSC genome browser

More...UCSCi		uc003iab.5 human

Keywords - Coding sequence diversityi

Polymorphism

<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
L14721 mRNA Translation: AAA35522.1
L12468 mRNA Translation: AAA16876.1
AC017068 Genomic DNA No translation available.
AC098798 Genomic DNA No translation available.
BC094770 mRNA Translation: AAH94770.1
CCDSiCCDS3691.1
PIRiA47531
RefSeqiNP_001968.3, NM_001977.3
UniGeneiHs.435765

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KX7X-ray2.15A76-957[»]
4KX8X-ray2.40A76-957[»]
4KX9X-ray2.25A76-957[»]
4KXAX-ray2.40A76-957[»]
4KXBX-ray2.40A76-957[»]
4KXCX-ray2.40A76-957[»]
4KXDX-ray2.15A76-957[»]
ProteinModelPortaliQ07075
SMRiQ07075
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108342, 5 interactors
IntActiQ07075, 3 interactors
STRINGi9606.ENSP00000265162

Chemistry databases

BindingDBiQ07075
ChEMBLiCHEMBL3439
DrugBankiDB00142 L-Glutamic Acid

Protein family/group databases

MEROPSiM01.003

PTM databases

iPTMnetiQ07075
PhosphoSitePlusiQ07075

Polymorphism and mutation databases

BioMutaiENPEP
DMDMi296439445

Proteomic databases

EPDiQ07075
MaxQBiQ07075
PaxDbiQ07075
PeptideAtlasiQ07075
PRIDEiQ07075
ProteomicsDBi58502

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265162; ENSP00000265162; ENSG00000138792
GeneIDi2028
KEGGihsa:2028
UCSCiuc003iab.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2028
DisGeNETi2028
EuPathDBiHostDB:ENSG00000138792.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		ENPEP

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0024609
HGNCiHGNC:3355 ENPEP
HPAiHPA002821
HPA005128
MIMi138297 gene
neXtProtiNX_Q07075
OpenTargetsiENSG00000138792
PharmGKBiPA27790

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1046 Eukaryota
COG0308 LUCA
GeneTreeiENSGT00940000156946
HOGENOMiHOG000106482
HOVERGENiHBG006616
InParanoidiQ07075
KOiK11141
OMAiPTRHLWL
OrthoDBiEOG091G01GH
PhylomeDBiQ07075
TreeFamiTF300395

Enzyme and pathway databases

ReactomeiR-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		ENPEP human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2028

Protein Ontology

More...PROi		PR:Q07075

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000138792 Expressed in 154 organ(s), highest expression level in jejunal mucosa
CleanExiHS_ENPEP
ExpressionAtlasiQ07075 baseline and differential
GenevisibleiQ07075 HS

Family and domain databases

CDDicd09601 M1_APN_2, 1 hit
InterProiView protein in InterPro
IPR033508 Aminopeptidase_A
IPR024571 ERAP1-like_C_dom
IPR034016 M1_APN-typ
IPR001930 Peptidase_M1
IPR014782 Peptidase_M1_N
PANTHERiPTHR11533 PTHR11533, 1 hit
PTHR11533:SF242 PTHR11533:SF242, 1 hit
PfamiView protein in Pfam
PF11838 ERAP1_C, 1 hit
PF01433 Peptidase_M1, 1 hit
PRINTSiPR00756 ALADIPTASE
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...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 nameiAMPE_HUMAN
<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: Q07075
Secondary accession number(s): Q504U2
<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: October 1, 1994
Last sequence update: May 18, 2010
Last modified: December 5, 2018
This is version 179 of the entry and version 3 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
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.

<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, Direct protein sequencing, 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. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  4. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  8. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again