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Q9NZ08

- ERAP1_HUMAN

UniProt

Q9NZ08 - ERAP1_HUMAN

Protein

Endoplasmic reticulum aminopeptidase 1

Gene

ERAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (24 Jul 2007)
      Previous versions | rss
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    Functioni

    Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.3 Publications

    Catalytic activityi

    Release of an N-terminal amino acid, Xaa-|-Xbb-, in which Xaa is preferably Leu, but may be other amino acids including Met, Cys and Phe.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei183 – 1831SubstrateBy similarity
    Metal bindingi353 – 3531Zinc; catalytic
    Active sitei354 – 3541Proton acceptorPROSITE-ProRule annotation
    Metal bindingi357 – 3571Zinc; catalytic
    Metal bindingi376 – 3761Zinc; catalytic
    Sitei438 – 4381Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. interleukin-1, Type II receptor binding Source: HGNC
    3. interleukin-6 receptor binding Source: UniProtKB
    4. metalloexopeptidase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: HGNC
    2. antigen processing and presentation of endogenous peptide antigen via MHC class I Source: UniProtKB
    3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    4. fat cell differentiation Source: UniProtKB
    5. membrane protein ectodomain proteolysis Source: UniProtKB
    6. positive regulation of angiogenesis Source: Ensembl
    7. regulation of blood pressure Source: UniProtKB
    8. regulation of innate immune response Source: UniProtKB
    9. response to bacterium Source: BHF-UCL

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Protein family/group databases

    MEROPSiM01.018.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmic reticulum aminopeptidase 1 (EC:3.4.11.-)
    Alternative name(s):
    ARTS-1
    Adipocyte-derived leucine aminopeptidase
    Short name:
    A-LAP
    Aminopeptidase PILS
    Puromycin-insensitive leucyl-specific aminopeptidase
    Short name:
    PILS-AP
    Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
    Gene namesi
    Name:ERAP1
    Synonyms:APPILS, ARTS1, KIAA0525
    ORF Names:UNQ584/PRO1154
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:18173. ERAP1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. endoplasmic reticulum lumen Source: HGNC
    4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    5. extracellular region Source: UniProtKB
    6. extracellular space Source: UniProt
    7. extracellular vesicular exosome Source: UniProt
    8. integral component of membrane Source: UniProtKB
    9. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi438 – 4381Y → F: Loss of enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA162385163.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 941941Endoplasmic reticulum aminopeptidase 1PRO_0000026751Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi70 – 701N-linked (GlcNAc...)2 Publications
    Glycosylationi154 – 1541N-linked (GlcNAc...)2 Publications
    Disulfide bondi404 ↔ 443
    Glycosylationi414 – 4141N-linked (GlcNAc...)2 Publications
    Disulfide bondi736 ↔ 743
    Glycosylationi760 – 7601N-linked (GlcNAc...)1 Publication
    Glycosylationi901 – 9011N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9NZ08.
    PaxDbiQ9NZ08.
    PRIDEiQ9NZ08.

    PTM databases

    PhosphoSiteiQ9NZ08.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Inductioni

    By IFNG/IFN-gamma.1 Publication

    Gene expression databases

    ArrayExpressiQ9NZ08.
    BgeeiQ9NZ08.
    CleanExiHS_ERAP1.
    GenevestigatoriQ9NZ08.

    Organism-specific databases

    HPAiCAB025095.
    HPA042317.

    Interactioni

    Subunit structurei

    Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX.4 Publications

    Protein-protein interaction databases

    BioGridi119713. 3 interactions.
    IntActiQ9NZ08. 3 interactions.
    STRINGi9606.ENSP00000296754.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 7015
    Turni71 – 744
    Beta strandi75 – 8814
    Beta strandi90 – 967
    Beta strandi101 – 1099
    Beta strandi116 – 1194
    Beta strandi121 – 1255
    Turni126 – 1294
    Beta strandi130 – 13910
    Beta strandi145 – 15410
    Beta strandi156 – 16813
    Beta strandi174 – 1818
    Turni183 – 1864
    Helixi187 – 1904
    Beta strandi201 – 2099
    Beta strandi214 – 2196
    Beta strandi221 – 2288
    Beta strandi231 – 2366
    Helixi244 – 2463
    Beta strandi249 – 2524
    Beta strandi255 – 2606
    Beta strandi266 – 2716
    Turni273 – 2753
    Helixi276 – 2783
    Helixi280 – 29617
    Beta strandi303 – 31311
    Beta strandi315 – 3195
    Beta strandi324 – 3285
    Helixi329 – 3313
    Turni336 – 3383
    Helixi341 – 35616
    Turni357 – 3593
    Turni361 – 3633
    Beta strandi364 – 3685
    Helixi369 – 3724
    Helixi373 – 39018
    Helixi392 – 3943
    Helixi396 – 3994
    Helixi400 – 41112
    Helixi426 – 4316
    Helixi435 – 45117
    Helixi454 – 46815
    Beta strandi471 – 4733
    Helixi475 – 4839
    Helixi517 – 5259
    Beta strandi530 – 5389
    Beta strandi541 – 5499
    Beta strandi565 – 5739
    Beta strandi578 – 5825
    Beta strandi584 – 5907
    Beta strandi598 – 6069
    Beta strandi609 – 6113
    Helixi613 – 62715
    Helixi628 – 6303
    Helixi633 – 64816
    Helixi654 – 6618
    Helixi662 – 6665
    Helixi670 – 68718
    Helixi693 – 71321
    Beta strandi716 – 7183
    Helixi722 – 73716
    Helixi741 – 75616
    Turni757 – 7593
    Helixi765 – 7673
    Helixi768 – 7758
    Helixi779 – 79113
    Helixi795 – 80511
    Helixi811 – 82313
    Beta strandi824 – 8274
    Helixi829 – 8313
    Helixi832 – 8409
    Turni843 – 8453
    Helixi846 – 86419
    Helixi869 – 8779
    Turni878 – 8814
    Helixi885 – 89612
    Turni897 – 9004
    Turni902 – 9043
    Helixi906 – 94136

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YD0X-ray2.70A46-940[»]
    3MDJX-ray2.95A/B/C37-939[»]
    3QNFX-ray3.00A/B/C1-941[»]
    3RJOX-ray2.30A529-941[»]
    ProteinModelPortaliQ9NZ08.
    SMRiQ9NZ08. Positions 46-941.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NZ08.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 11CytoplasmicSequence Analysis
    Topological domaini22 – 941920LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2 – 2120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni317 – 3215Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOVERGENiHBG108296.
    InParanoidiQ9NZ08.
    KOiK09604.
    OMAiLIHANLT.
    OrthoDBiEOG754HNR.
    PhylomeDBiQ9NZ08.
    TreeFamiTF300395.

    Family and domain databases

    InterProiIPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiPF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NZ08-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVFLPLKWSL ATMSFLLSSL LALLTVSTPS WCQSTEASPK RSDGTPFPWN    50
    KIRLPEYVIP VHYDLLIHAN LTTLTFWGTT KVEITASQPT STIILHSHHL 100
    QISRATLRKG AGERLSEEPL QVLEHPRQEQ IALLAPEPLL VGLPYTVVIH 150
    YAGNLSETFH GFYKSTYRTK EGELRILAST QFEPTAARMA FPCFDEPAFK 200
    ASFSIKIRRE PRHLAISNMP LVKSVTVAEG LIEDHFDVTV KMSTYLVAFI 250
    ISDFESVSKI TKSGVKVSVY AVPDKINQAD YALDAAVTLL EFYEDYFSIP 300
    YPLPKQDLAA IPDFQSGAME NWGLTTYRES ALLFDAEKSS ASSKLGITMT 350
    VAHELAHQWF GNLVTMEWWN DLWLNEGFAK FMEFVSVSVT HPELKVGDYF 400
    FGKCFDAMEV DALNSSHPVS TPVENPAQIR EMFDDVSYDK GACILNMLRE 450
    YLSADAFKSG IVQYLQKHSY KNTKNEDLWD SMASICPTDG VKGMDGFCSR 500
    SQHSSSSSHW HQEGVDVKTM MNTWTLQKGF PLITITVRGR NVHMKQEHYM 550
    KGSDGAPDTG YLWHVPLTFI TSKSDMVHRF LLKTKTDVLI LPEEVEWIKF 600
    NVGMNGYYIV HYEDDGWDSL TGLLKGTHTA VSSNDRASLI NNAFQLVSIG 650
    KLSIEKALDL SLYLKHETEI MPVFQGLNEL IPMYKLMEKR DMNEVETQFK 700
    AFLIRLLRDL IDKQTWTDEG SVSERMLRSQ LLLLACVHNY QPCVQRAEGY 750
    FRKWKESNGN LSLPVDVTLA VFAVGAQSTE GWDFLYSKYQ FSLSSTEKSQ 800
    IEFALCRTQN KEKLQWLLDE SFKGDKIKTQ EFPQILTLIG RNPVGYPLAW 850
    QFLRKNWNKL VQKFELGSSS IAHMVMGTTN QFSTRTRLEE VKGFFSSLKE 900
    NGSQLRCVQQ TIETIEENIG WMDKNFDKIR VWLQSEKLER M 941
    Length:941
    Mass (Da):107,235
    Last modified:July 24, 2007 - v3
    Checksum:i22A0795C90155F04
    GO
    Isoform 2 (identifier: Q9NZ08-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         940-941: RM → HDPEADATG

    Show »
    Length:948
    Mass (Da):107,841
    Checksum:iB7DEE159B1D591EE
    GO

    Sequence cautioni

    The sequence BAA25451.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121T → I in AAF07395. (PubMed:10220586)Curated
    Sequence conflicti12 – 121T → I in AAK37777. (PubMed:11481040)Curated
    Sequence conflicti12 – 121T → I in AAK37778. (PubMed:11481040)Curated
    Sequence conflicti514 – 5141G → R in AAF20384. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561E → K.
    Corresponds to variant rs3734016 [ dbSNP | Ensembl ].
    VAR_046681
    Natural varianti127 – 1271R → P.4 Publications
    Corresponds to variant rs26653 [ dbSNP | Ensembl ].
    VAR_012779
    Natural varianti276 – 2761I → M.
    Corresponds to variant rs26618 [ dbSNP | Ensembl ].
    VAR_012780
    Natural varianti346 – 3461G → D.1 Publication
    Corresponds to variant rs27895 [ dbSNP | Ensembl ].
    VAR_012781
    Natural varianti349 – 3491M → V.3 Publications
    Corresponds to variant rs2287987 [ dbSNP | Ensembl ].
    VAR_012782
    Natural varianti528 – 5281K → R.4 Publications
    Corresponds to variant rs30187 [ dbSNP | Ensembl ].
    VAR_012783
    Natural varianti575 – 5751D → G.
    Corresponds to variant rs6863093 [ dbSNP | Ensembl ].
    VAR_046682
    Natural varianti575 – 5751D → N.3 Publications
    Corresponds to variant rs10050860 [ dbSNP | Ensembl ].
    VAR_021555
    Natural varianti725 – 7251R → Q.3 Publications
    Corresponds to variant rs17482078 [ dbSNP | Ensembl ].
    VAR_021556
    Natural varianti730 – 7301Q → E.4 Publications
    Corresponds to variant rs27044 [ dbSNP | Ensembl ].
    VAR_012784

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei940 – 9412RM → HDPEADATG in isoform 2. 2 PublicationsVSP_005450

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106037 mRNA. Translation: AAF07395.1.
    AY028806 mRNA. Translation: AAK37777.1.
    AY028807 mRNA. Translation: AAK37778.1.
    AF183569 mRNA. Translation: AAF20384.1.
    AF222340 mRNA. Translation: AAF34664.1.
    AB011097 mRNA. Translation: BAA25451.2. Different initiation.
    AY358590 mRNA. Translation: AAQ88953.1.
    BC030775 mRNA. Translation: AAH30775.1.
    CCDSiCCDS4085.1. [Q9NZ08-2]
    CCDS47250.1. [Q9NZ08-1]
    RefSeqiNP_001035548.1. NM_001040458.1. [Q9NZ08-1]
    NP_001185470.1. NM_001198541.1. [Q9NZ08-1]
    NP_057526.3. NM_016442.3. [Q9NZ08-2]
    UniGeneiHs.666524.

    Genome annotation databases

    EnsembliENST00000296754; ENSP00000296754; ENSG00000164307. [Q9NZ08-2]
    ENST00000443439; ENSP00000406304; ENSG00000164307. [Q9NZ08-1]
    GeneIDi51752.
    KEGGihsa:51752.
    UCSCiuc003kml.3. human. [Q9NZ08-2]
    uc003kmm.3. human. [Q9NZ08-1]

    Polymorphism databases

    DMDMi158937334.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106037 mRNA. Translation: AAF07395.1 .
    AY028806 mRNA. Translation: AAK37777.1 .
    AY028807 mRNA. Translation: AAK37778.1 .
    AF183569 mRNA. Translation: AAF20384.1 .
    AF222340 mRNA. Translation: AAF34664.1 .
    AB011097 mRNA. Translation: BAA25451.2 . Different initiation.
    AY358590 mRNA. Translation: AAQ88953.1 .
    BC030775 mRNA. Translation: AAH30775.1 .
    CCDSi CCDS4085.1. [Q9NZ08-2 ]
    CCDS47250.1. [Q9NZ08-1 ]
    RefSeqi NP_001035548.1. NM_001040458.1. [Q9NZ08-1 ]
    NP_001185470.1. NM_001198541.1. [Q9NZ08-1 ]
    NP_057526.3. NM_016442.3. [Q9NZ08-2 ]
    UniGenei Hs.666524.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YD0 X-ray 2.70 A 46-940 [» ]
    3MDJ X-ray 2.95 A/B/C 37-939 [» ]
    3QNF X-ray 3.00 A/B/C 1-941 [» ]
    3RJO X-ray 2.30 A 529-941 [» ]
    ProteinModelPortali Q9NZ08.
    SMRi Q9NZ08. Positions 46-941.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119713. 3 interactions.
    IntActi Q9NZ08. 3 interactions.
    STRINGi 9606.ENSP00000296754.

    Chemistry

    ChEMBLi CHEMBL5939.

    Protein family/group databases

    MEROPSi M01.018.

    PTM databases

    PhosphoSitei Q9NZ08.

    Polymorphism databases

    DMDMi 158937334.

    Proteomic databases

    MaxQBi Q9NZ08.
    PaxDbi Q9NZ08.
    PRIDEi Q9NZ08.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296754 ; ENSP00000296754 ; ENSG00000164307 . [Q9NZ08-2 ]
    ENST00000443439 ; ENSP00000406304 ; ENSG00000164307 . [Q9NZ08-1 ]
    GeneIDi 51752.
    KEGGi hsa:51752.
    UCSCi uc003kml.3. human. [Q9NZ08-2 ]
    uc003kmm.3. human. [Q9NZ08-1 ]

    Organism-specific databases

    CTDi 51752.
    GeneCardsi GC05M096124.
    H-InvDB HIX0164377.
    HGNCi HGNC:18173. ERAP1.
    HPAi CAB025095.
    HPA042317.
    MIMi 606832. gene.
    neXtProti NX_Q9NZ08.
    PharmGKBi PA162385163.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0308.
    HOVERGENi HBG108296.
    InParanoidi Q9NZ08.
    KOi K09604.
    OMAi LIHANLT.
    OrthoDBi EOG754HNR.
    PhylomeDBi Q9NZ08.
    TreeFami TF300395.

    Enzyme and pathway databases

    Reactomei REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Miscellaneous databases

    EvolutionaryTracei Q9NZ08.
    GeneWikii ARTS-1.
    GenomeRNAii 51752.
    NextBioi 55845.
    PROi Q9NZ08.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZ08.
    Bgeei Q9NZ08.
    CleanExi HS_ERAP1.
    Genevestigatori Q9NZ08.

    Family and domain databases

    InterProi IPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    Pfami PF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase."
      Hattori A., Matsumoto H., Mizutani S., Tsujimoto M.
      J. Biochem. 125:931-938(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-127.
      Tissue: White adipose tissue.
    2. "Genomic organization of the human adipocyte-derived leucine aminopeptidase gene and its relationship to the placental leucine aminopeptidase/oxytocinase gene."
      Hattori A., Matsumoto K., Mizutani S., Tsujimoto M.
      J. Biochem. 130:235-241(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730.
      Tissue: Leukocyte.
    3. "Molecular characterization of human aminopeptidase PILS."
      Schomburg L.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-346; ARG-528 AND GLU-730.
    4. "Identification of an aminopeptidase regulator of type I tumor necrosis factor receptor shedding."
      Cui X., Alsaaty S., Lawrence M., Combs C.A., Rouhani F.N., Levine S.J.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730.
      Tissue: Brain.
    6. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730.
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    9. "Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in Chinese hamster ovary cells."
      Hattori A., Kitatani K., Matsumoto H., Miyazawa S., Rogi T., Tsuruoka N., Mizutani S., Natori Y., Tsujimoto M.
      J. Biochem. 128:755-762(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 37-49, CHARACTERIZATION.
    10. "Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum."
      Saveanu L., Carroll O., Lindo V., Del Val M., Lopez D., Lepelletier Y., Greer F., Schomburg L., Fruci D., Niedermann G., van Endert P.M.
      Nat. Immunol. 6:689-697(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INDUCTION BY IFNG.
    11. "The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a 'molecular ruler' mechanism."
      Chang S.-C., Momburg F., Bhutani N., Goldberg A.L.
      Proc. Natl. Acad. Sci. U.S.A. 102:17107-17112(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "An association between RBMX, a heterogeneous nuclear ribonucleoprotein, and ARTS-1 regulates extracellular TNFR1 release."
      Adamik B., Islam A., Rouhani F.N., Hawari F.I., Zhang J., Levine S.J.
      Biochem. Biophys. Res. Commun. 371:505-509(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBMX.
    13. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-414.
      Tissue: Liver.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1."
      Structural genomics consortium (SGC)
      Submitted (MAY-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 46-940 IN COMPLEX WITH ZINC IONS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-414.
    16. "Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1."
      Nguyen T.T., Chang S.C., Evnouchidou I., York I.A., Zikos C., Rock K.L., Goldberg A.L., Stratikos E., Stern L.J.
      Nat. Struct. Mol. Biol. 18:604-613(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 37-939 IN COMPLEX WITH ZINC IONS AND BESTATIN, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-760, ACTIVE SITE, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF TYR-438.

    Entry informationi

    Entry nameiERAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZ08
    Secondary accession number(s): O60278
    , Q6UWY6, Q8NEL4, Q8TAD0, Q9UHF8, Q9UKY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 140 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    It is uncertain whether Met-1 or Met-13 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3