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Q6P179

- ERAP2_HUMAN

UniProt

Q6P179 - ERAP2_HUMAN

Protein

Endoplasmic reticulum aminopeptidase 2

Gene

ERAP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      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. Preferentially hydrolyzes the basic residues Arg and Lys.3 Publications

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei200 – 2001Substrate1 Publication
    Metal bindingi370 – 3701Zinc; catalytic
    Active sitei371 – 3711Proton acceptor1 PublicationPROSITE-ProRule annotation
    Metal bindingi374 – 3741Zinc; catalytic
    Metal bindingi393 – 3931Zinc; catalytic
    Sitei455 – 4551Transition state stabilizer

    GO - Molecular functioni

    1. aminopeptidase activity Source: HGNC
    2. metallopeptidase activity Source: HGNC
    3. zinc ion binding Source: HGNC

    GO - Biological processi

    1. antigen processing and presentation of endogenous peptide antigen via MHC class I Source: HGNC
    2. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    3. regulation of blood pressure Source: HGNC

    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.
    SABIO-RKQ6P179.

    Protein family/group databases

    MEROPSiM01.024.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmic reticulum aminopeptidase 2 (EC:3.4.11.-)
    Alternative name(s):
    Leukocyte-derived arginine aminopeptidase
    Short name:
    L-RAP
    Gene namesi
    Name:ERAP2
    Synonyms:LRAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:29499. ERAP2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: HGNC
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162385208.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 960960Endoplasmic reticulum aminopeptidase 2PRO_0000315719Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi85 – 851N-linked (GlcNAc...)2 Publications
    Glycosylationi119 – 1191N-linked (GlcNAc...)2 Publications
    Glycosylationi405 – 4051N-linked (GlcNAc...)2 Publications
    Disulfide bondi421 ↔ 4601 Publication
    Glycosylationi650 – 6501N-linked (GlcNAc...)2 Publications
    Disulfide bondi759 ↔ 7661 Publication

    Post-translational modificationi

    N-glycosylated.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ6P179.
    PaxDbiQ6P179.
    PeptideAtlasiQ6P179.
    PRIDEiQ6P179.

    PTM databases

    PhosphoSiteiQ6P179.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Highly expressed in spleen and leukocytes.1 Publication

    Inductioni

    By IFNG/IFN-gamma.2 Publications

    Gene expression databases

    ArrayExpressiQ6P179.
    BgeeiQ6P179.
    CleanExiHS_ERAP2.
    GenevestigatoriQ6P179.

    Organism-specific databases

    HPAiCAB025618.
    HPA034498.

    Interactioni

    Subunit structurei

    Heterodimer with ERAP1.2 Publications

    Protein-protein interaction databases

    IntActiQ6P179. 1 interaction.
    STRINGi9606.ENSP00000342447.

    Structurei

    Secondary structure

    1
    960
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi57 – 604
    Beta strandi66 – 683
    Beta strandi71 – 8515
    Turni86 – 894
    Beta strandi90 – 10314
    Beta strandi106 – 1116
    Beta strandi116 – 1249
    Beta strandi138 – 1425
    Helixi143 – 1453
    Beta strandi147 – 1515
    Beta strandi161 – 17111
    Beta strandi173 – 18513
    Beta strandi191 – 1988
    Turni200 – 2034
    Helixi204 – 2063
    Beta strandi218 – 2269
    Beta strandi231 – 2366
    Beta strandi238 – 2436
    Beta strandi249 – 2535
    Helixi261 – 2633
    Beta strandi266 – 2694
    Beta strandi272 – 2776
    Beta strandi283 – 2886
    Helixi290 – 2967
    Helixi297 – 31418
    Beta strandi319 – 33012
    Beta strandi332 – 3365
    Beta strandi341 – 3455
    Helixi346 – 3494
    Turni353 – 3553
    Helixi358 – 37619
    Turni378 – 3803
    Beta strandi381 – 3855
    Helixi386 – 3894
    Helixi390 – 40718
    Helixi409 – 4113
    Helixi413 – 4175
    Helixi418 – 42811
    Helixi443 – 4475
    Turni452 – 4554
    Helixi456 – 46914
    Helixi471 – 48414
    Turni485 – 4873
    Beta strandi488 – 4903
    Helixi492 – 5009
    Helixi534 – 54310
    Beta strandi548 – 5558
    Beta strandi558 – 5658
    Beta strandi590 – 5923
    Beta strandi594 – 5963
    Beta strandi601 – 6033
    Beta strandi607 – 6137
    Beta strandi621 – 6244
    Helixi625 – 6273
    Beta strandi632 – 6365
    Helixi639 – 64810
    Helixi651 – 6533
    Helixi656 – 67015
    Turni671 – 6733
    Helixi677 – 6815
    Turni682 – 6854
    Helixi686 – 6883
    Helixi693 – 71220
    Helixi716 – 72813
    Helixi731 – 7355
    Helixi745 – 76016
    Helixi764 – 78017
    Helixi788 – 79811
    Helixi802 – 81211
    Helixi818 – 82912
    Helixi834 – 84613
    Beta strandi848 – 8503
    Helixi852 – 8543
    Helixi855 – 86410
    Helixi866 – 87813
    Helixi880 – 8867
    Helixi892 – 90211
    Helixi908 – 92013
    Beta strandi923 – 9253
    Helixi930 – 95930

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SE6X-ray3.08A/B1-960[»]
    4E36X-ray3.22A/B1-960[»]
    4JBSX-ray2.79A/B3-960[»]
    ProteinModelPortaliQ6P179.
    SMRiQ6P179. Positions 54-960.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini41 – 960920LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 4020Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni334 – 3385Substrate binding

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOGENOMiHOG000106482.
    HOVERGENiHBG108296.
    InParanoidiQ6P179.
    KOiK13723.
    OMAiYLDINRE.
    OrthoDBiEOG754HNR.
    PhylomeDBiQ6P179.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6P179-1) [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

    MFHSSAMVNS HRKPMFNIHR GFYCLTAILP QICICSQFSV PSSYHFTEDP    50
    GAFPVATNGE RFPWQELRLP SVVIPLHYDL FVHPNLTSLD FVASEKIEVL 100
    VSNATQFIIL HSKDLEITNA TLQSEEDSRY MKPGKELKVL SYPAHEQIAL 150
    LVPEKLTPHL KYYVAMDFQA KLGDGFEGFY KSTYRTLGGE TRILAVTDFE 200
    PTQARMAFPC FDEPLFKANF SIKIRRESRH IALSNMPKVK TIELEGGLLE 250
    DHFETTVKMS TYLVAYIVCD FHSLSGFTSS GVKVSIYASP DKRNQTHYAL 300
    QASLKLLDFY EKYFDIYYPL SKLDLIAIPD FAPGAMENWG LITYRETSLL 350
    FDPKTSSASD KLWVTRVIAH ELAHQWFGNL VTMEWWNDIW LKEGFAKYME 400
    LIAVNATYPE LQFDDYFLNV CFEVITKDSL NSSRPISKPA ETPTQIQEMF 450
    DEVSYNKGAC ILNMLKDFLG EEKFQKGIIQ YLKKFSYRNA KNDDLWSSLS 500
    NSCLESDFTS GGVCHSDPKM TSNMLAFLGE NAEVKEMMTT WTLQKGIPLL 550
    VVKQDGCSLR LQQERFLQGV FQEDPEWRAL QERYLWHIPL TYSTSSSNVI 600
    HRHILKSKTD TLDLPEKTSW VKFNVDSNGY YIVHYEGHGW DQLITQLNQN 650
    HTLLRPKDRV GLIHDVFQLV GAGRLTLDKA LDMTYYLQHE TSSPALLEGL 700
    SYLESFYHMM DRRNISDISE NLKRYLLQYF KPVIDRQSWS DKGSVWDRML 750
    RSALLKLACD LNHAPCIQKA AELFSQWMES SGKLNIPTDV LKIVYSVGAQ 800
    TTAGWNYLLE QYELSMSSAE QNKILYALST SKHQEKLLKL IELGMEGKVI 850
    KTQNLAALLH AIARRPKGQQ LAWDFVRENW THLLKKFDLG SYDIRMIISG 900
    TTAHFSSKDK LQEVKLFFES LEAQGSHLDI FQTVLETITK NIKWLEKNLP 950
    TLRTWLMVNT 960
    Length:960
    Mass (Da):110,462
    Last modified:January 15, 2008 - v2
    Checksum:i261EFC06870D644E
    GO
    Isoform 2 (identifier: Q6P179-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         525-532: LAFLGENA → VRIKRVTE
         533-960: Missing.

    Show »
    Length:532
    Mass (Da):60,952
    Checksum:iDA0F49B61F79B920
    GO
    Isoform 3 (identifier: Q6P179-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         238-282: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:915
    Mass (Da):105,526
    Checksum:i10075BE1C076377F
    GO
    Isoform 4 (identifier: Q6P179-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         324-350: DLIAIPDFAPGAMENWGLITYRETSLL → GMFKFHIIVFIFAHKTCFDLFPLSLSM
         351-960: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:350
    Mass (Da):40,088
    Checksum:i189B8EF5D9D4BD11
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti129 – 1291R → K in AAH17927. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti214 – 2141P → L.
    Corresponds to variant rs3733905 [ dbSNP | Ensembl ].
    VAR_038285
    Natural varianti392 – 3921K → N.2 Publications
    Corresponds to variant rs2549782 [ dbSNP | Ensembl ].
    VAR_038286
    Natural varianti411 – 4111L → R.
    Corresponds to variant rs34261036 [ dbSNP | Ensembl ].
    VAR_051569
    Natural varianti669 – 6691L → Q.
    Corresponds to variant rs17408150 [ dbSNP | Ensembl ].
    VAR_038287

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei238 – 28245Missing in isoform 3. 1 PublicationVSP_030671Add
    BLAST
    Alternative sequencei324 – 35027DLIAI…ETSLL → GMFKFHIIVFIFAHKTCFDL FPLSLSM in isoform 4. 1 PublicationVSP_030672Add
    BLAST
    Alternative sequencei351 – 960610Missing in isoform 4. 1 PublicationVSP_030673Add
    BLAST
    Alternative sequencei525 – 5328LAFLGENA → VRIKRVTE in isoform 2. 1 PublicationVSP_030674
    Alternative sequencei533 – 960428Missing in isoform 2. 1 PublicationVSP_030675Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB109031 mRNA. Translation: BAC78818.1.
    AB163917 mRNA. Translation: BAD90015.1.
    AY028805 mRNA. Translation: AAK37776.1.
    AF191545 mRNA. Translation: AAG28383.1.
    CH471084 Genomic DNA. Translation: EAW96080.1.
    BC065240 mRNA. Translation: AAH65240.1.
    BC017927 mRNA. Translation: AAH17927.1.
    CCDSiCCDS4086.1. [Q6P179-1]
    RefSeqiNP_001123612.1. NM_001130140.1. [Q6P179-1]
    NP_071745.1. NM_022350.3. [Q6P179-1]
    UniGeneiHs.482910.

    Genome annotation databases

    EnsembliENST00000379904; ENSP00000369235; ENSG00000164308. [Q6P179-3]
    ENST00000437043; ENSP00000400376; ENSG00000164308. [Q6P179-1]
    ENST00000510309; ENSP00000425758; ENSG00000164308. [Q6P179-4]
    ENST00000513084; ENSP00000421849; ENSG00000164308. [Q6P179-2]
    GeneIDi64167.
    KEGGihsa:64167.
    UCSCiuc003kmq.3. human. [Q6P179-1]
    uc003kms.3. human. [Q6P179-3]

    Polymorphism databases

    DMDMi166232401.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB109031 mRNA. Translation: BAC78818.1 .
    AB163917 mRNA. Translation: BAD90015.1 .
    AY028805 mRNA. Translation: AAK37776.1 .
    AF191545 mRNA. Translation: AAG28383.1 .
    CH471084 Genomic DNA. Translation: EAW96080.1 .
    BC065240 mRNA. Translation: AAH65240.1 .
    BC017927 mRNA. Translation: AAH17927.1 .
    CCDSi CCDS4086.1. [Q6P179-1 ]
    RefSeqi NP_001123612.1. NM_001130140.1. [Q6P179-1 ]
    NP_071745.1. NM_022350.3. [Q6P179-1 ]
    UniGenei Hs.482910.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SE6 X-ray 3.08 A/B 1-960 [» ]
    4E36 X-ray 3.22 A/B 1-960 [» ]
    4JBS X-ray 2.79 A/B 3-960 [» ]
    ProteinModelPortali Q6P179.
    SMRi Q6P179. Positions 54-960.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q6P179. 1 interaction.
    STRINGi 9606.ENSP00000342447.

    Chemistry

    ChEMBLi CHEMBL5043.

    Protein family/group databases

    MEROPSi M01.024.

    PTM databases

    PhosphoSitei Q6P179.

    Polymorphism databases

    DMDMi 166232401.

    Proteomic databases

    MaxQBi Q6P179.
    PaxDbi Q6P179.
    PeptideAtlasi Q6P179.
    PRIDEi Q6P179.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379904 ; ENSP00000369235 ; ENSG00000164308 . [Q6P179-3 ]
    ENST00000437043 ; ENSP00000400376 ; ENSG00000164308 . [Q6P179-1 ]
    ENST00000510309 ; ENSP00000425758 ; ENSG00000164308 . [Q6P179-4 ]
    ENST00000513084 ; ENSP00000421849 ; ENSG00000164308 . [Q6P179-2 ]
    GeneIDi 64167.
    KEGGi hsa:64167.
    UCSCi uc003kmq.3. human. [Q6P179-1 ]
    uc003kms.3. human. [Q6P179-3 ]

    Organism-specific databases

    CTDi 64167.
    GeneCardsi GC05P096238.
    H-InvDB HIX0005053.
    HGNCi HGNC:29499. ERAP2.
    HPAi CAB025618.
    HPA034498.
    MIMi 609497. gene.
    neXtProti NX_Q6P179.
    PharmGKBi PA162385208.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000106482.
    HOVERGENi HBG108296.
    InParanoidi Q6P179.
    KOi K13723.
    OMAi YLDINRE.
    OrthoDBi EOG754HNR.
    PhylomeDBi Q6P179.
    TreeFami TF300395.

    Enzyme and pathway databases

    Reactomei REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
    SABIO-RK Q6P179.

    Miscellaneous databases

    GenomeRNAii 64167.
    NextBioi 66072.
    PROi Q6P179.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6P179.
    Bgeei Q6P179.
    CleanExi HS_ERAP2.
    Genevestigatori Q6P179.

    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. "Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases."
      Tanioka T., Hattori A., Masuda S., Nomura Y., Nakayama H., Mizutani S., Tsujimoto M.
      J. Biol. Chem. 278:32275-32283(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION, TOPOLOGY, TISSUE SPECIFICITY, VARIANT ASN-392.
    2. "Regulation of the human leukocyte-derived arginine aminopeptidase/endoplasmic reticulum-aminopeptidase 2 gene by interferon-gamma."
      Tanioka T., Hattori A., Mizutani S., Tsujimoto M.
      FEBS J. 272:916-928(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION BY IFNG, VARIANT ASN-392.
    3. "Molecular characterization of aminopeptidase MAMS."
      Schomburg L.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 3 AND 4).
      Tissue: Skeletal muscle and Skin.
    6. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119.
      Tissue: Plasma.
    7. "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, SUBUNIT, INDUCTION BY IFNG.
    8. "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.
    9. "Expression of endoplasmic reticulum aminopeptidases in EBV-B cell lines from healthy donors and in leukemia/lymphoma, carcinoma, and melanoma cell lines."
      Fruci D., Ferracuti S., Limongi M.Z., Cunsolo V., Giorda E., Fraioli R., Sibilio L., Carroll O., Hattori A., van Endert P.M., Giacomini P.
      J. Immunol. 176:4869-4879(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE REGULATION.
    10. "Inactivation of RB1 in mantle-cell lymphoma detected by nonsense-mediated mRNA decay pathway inhibition and microarray analysis."
      Pinyol M., Bea S., Pla L., Ribrag V., Bosq J., Rosenwald A., Campo E., Jares P.
      Blood 109:5422-5429(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing."
      Birtley J.R., Saridakis E., Stratikos E., Mavridis I.M.
      Biochemistry 51:286-295(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 3-960 IN COMPLEX WITH SUBSTRATE, GLYCOSYLATION AT ASN-85; ASN-219; ASN-405 AND ASN-650, ACTIVE SITE, ZINC-BINDING SITES, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiERAP2_HUMAN
    AccessioniPrimary (citable) accession number: Q6P179
    Secondary accession number(s): Q7Z5K1
    , Q8TD32, Q8WVJ4, Q9HBX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 96 of the entry and version 2 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

    Miscellaneous

    Defects in the expression of this gene may cause improper antigen processing, possibly leading to favor tumor escape from the immune surveillance.

    Keywords - Technical termi

    3D-structure, Complete proteome, 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