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P15144

- AMPN_HUMAN

UniProt

P15144 - AMPN_HUMAN

Protein

Aminopeptidase N

Gene

ANPEP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 4 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.5 Publications

    Catalytic activityi

    Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi388 – 3881Zinc; catalytic
    Active sitei389 – 3891Proton acceptor1 PublicationPROSITE-ProRule annotation
    Metal bindingi392 – 3921Zinc; catalytic
    Metal bindingi411 – 4111Zinc; catalytic
    Sitei477 – 4771Transition state stabilizer

    GO - Molecular functioni

    1. aminopeptidase activity Source: ProtInc
    2. metallopeptidase activity Source: ProtInc
    3. receptor activity Source: ProtInc
    4. virus receptor activity Source: UniProtKB-KW
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. angiotensin maturation Source: Reactome
    3. cell differentiation Source: UniProtKB-KW
    4. cellular protein metabolic process Source: Reactome
    5. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminopeptidase, Developmental protein, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor

    Keywords - Biological processi

    Angiogenesis, Differentiation, Host-virus interaction

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.11.2. 2681.
    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RKP15144.

    Protein family/group databases

    MEROPSiM01.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase N (EC:3.4.11.2)
    Short name:
    AP-N
    Short name:
    hAPN
    Alternative name(s):
    Alanyl aminopeptidase
    Aminopeptidase M
    Short name:
    AP-M
    Microsomal aminopeptidase
    Myeloid plasma membrane glycoprotein CD13
    gp150
    CD_antigen: CD13
    Gene namesi
    Name:ANPEP
    Synonyms:APN, CD13, PEPN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:500. ANPEP.

    Subcellular locationi

    Cell membrane; Single-pass type II membrane protein. Cytoplasmcytosol Curated
    Note: A soluble form has also been detected.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    3. external side of plasma membrane Source: Ensembl
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProtKB
    6. integral component of plasma membrane Source: ProtInc
    7. lysosomal membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi288 – 2958DYVEKQAS → QSVEETAQ: No change in receptor activity and HCoV-229E infection.
    Mutagenesisi288 – 2958DYVEKQAS → QSVNEQAQ: No change in receptor activity and HCoV-229E infection.
    Mutagenesisi288 – 2958DYVEKQAS → QSVNETAQ: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity.
    Mutagenesisi291 – 2933EKQ → NKT: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity.
    Mutagenesisi291 – 2911E → N: No change of receptor activity and HCoV-229E infection.
    Mutagenesisi293 – 2931Q → T: No change of receptor activity and HCoV-229E infection.
    Mutagenesisi818 – 8181N → E: Very low receptor activity and HCoV-229E infection. 1 Publication

    Organism-specific databases

    PharmGKBiPA24815.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 967966Aminopeptidase NPRO_0000095081Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi128 – 1281N-linked (GlcNAc...)3 Publications
    Modified residuei176 – 1761SulfotyrosineSequence Analysis
    Glycosylationi234 – 2341N-linked (GlcNAc...)3 Publications
    Glycosylationi265 – 2651N-linked (GlcNAc...)4 Publications
    Glycosylationi319 – 3191N-linked (GlcNAc...)1 Publication
    Modified residuei419 – 4191SulfotyrosineSequence Analysis
    Modified residuei424 – 4241SulfotyrosineSequence Analysis
    Glycosylationi527 – 5271N-linked (GlcNAc...)1 Publication
    Glycosylationi573 – 5731N-linked (GlcNAc...)1 Publication
    Glycosylationi625 – 6251N-linked (GlcNAc...)1 Publication
    Glycosylationi681 – 6811N-linked (GlcNAc...)3 Publications
    Glycosylationi735 – 7351N-linked (GlcNAc...)
    Disulfide bondi761 ↔ 7681 Publication
    Disulfide bondi798 ↔ 8341 Publication
    Glycosylationi818 – 8181N-linked (GlcNAc...)3 Publications
    Modified residuei913 – 9131SulfotyrosineSequence Analysis

    Post-translational modificationi

    Sulfated.By similarity
    N- and O-glycosylated.6 Publications
    May undergo proteolysis and give rise to a soluble form.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Sulfation

    Proteomic databases

    MaxQBiP15144.
    PaxDbiP15144.
    PRIDEiP15144.

    PTM databases

    PhosphoSiteiP15144.

    Expressioni

    Tissue specificityi

    Expressed in epithelial cells of the kidney, intestine, and respiratory tract; granulocytes, monocytes, fibroblasts, endothelial cells, cerebral pericytes at the blood-brain barrier, synaptic membranes of cells in the CNS. Also expressed in endometrial stromal cells, but not in the endometrial glandular cells. Found in the vasculature of tissues that undergo angiogenesis and in malignant gliomas and lymph node metastases from multiple tumor types but not in blood vessels of normal tissues. A soluble form has been found in plasma. It is found to be elevated in plasma and effusions of cancer patients.

    Inductioni

    Estradiol and IL8/interleukin-8 decrease enzymatic activity in vitro in endometrial stromal cells by 40% and 30%, respectively.1 Publication

    Gene expression databases

    ArrayExpressiP15144.
    BgeeiP15144.
    CleanExiHS_ANPEP.
    GenevestigatoriP15144.

    Organism-specific databases

    HPAiCAB002417.
    HPA004625.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the S1 domain of HCoV-229E spike protein.4 Publications

    Protein-protein interaction databases

    BioGridi106787. 2 interactions.
    IntActiP15144. 5 interactions.
    STRINGi9606.ENSP00000300060.

    Structurei

    Secondary structure

    1
    967
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi70 – 723
    Beta strandi73 – 753
    Beta strandi78 – 9114
    Beta strandi102 – 11514
    Beta strandi118 – 1236
    Beta strandi135 – 1428
    Beta strandi150 – 1567
    Turni157 – 1604
    Beta strandi161 – 1688
    Beta strandi175 – 18511
    Beta strandi188 – 20013
    Beta strandi203 – 2119
    Turni213 – 2164
    Helixi217 – 2193
    Beta strandi231 – 24010
    Beta strandi243 – 2497
    Beta strandi251 – 2533
    Beta strandi256 – 2583
    Beta strandi261 – 2699
    Helixi277 – 2793
    Beta strandi282 – 2854
    Beta strandi288 – 2936
    Beta strandi299 – 3046
    Helixi306 – 3105
    Turni311 – 3144
    Helixi315 – 33117
    Beta strandi338 – 34811
    Beta strandi350 – 3545
    Beta strandi359 – 3635
    Helixi364 – 3674
    Turni371 – 3733
    Helixi376 – 39419
    Turni396 – 3983
    Beta strandi399 – 4035
    Helixi404 – 4074
    Helixi408 – 42518
    Helixi427 – 4293
    Helixi431 – 4344
    Helixi435 – 4384
    Helixi440 – 4478
    Helixi459 – 4613
    Helixi465 – 4706
    Helixi474 – 49118
    Helixi493 – 50715
    Beta strandi510 – 5123
    Helixi514 – 52714
    Helixi536 – 5449
    Beta strandi550 – 5556
    Turni556 – 5594
    Beta strandi560 – 5656
    Turni579 – 5824
    Beta strandi586 – 5883
    Beta strandi590 – 5923
    Beta strandi600 – 6023
    Beta strandi604 – 6085
    Helixi610 – 6123
    Beta strandi620 – 6234
    Helixi624 – 6263
    Beta strandi631 – 6344
    Helixi636 – 64914
    Helixi650 – 6523
    Helixi655 – 67016
    Helixi676 – 6816
    Helixi682 – 6887
    Helixi692 – 70918
    Helixi715 – 73622
    Turni737 – 7415
    Helixi747 – 76216
    Helixi766 – 78116
    Helixi790 – 7923
    Helixi793 – 80311
    Helixi806 – 81712
    Helixi822 – 83211
    Helixi838 – 84811
    Turni851 – 8533
    Helixi856 – 8583
    Helixi859 – 86810
    Helixi872 – 88211
    Helixi884 – 8907
    Turni891 – 8944
    Helixi898 – 9069
    Helixi912 – 92413
    Turni925 – 9284
    Helixi931 – 9333
    Helixi934 – 96532

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FYQX-ray1.90A66-967[»]
    4FYRX-ray1.91A66-967[»]
    4FYSX-ray2.01A66-967[»]
    4FYTX-ray1.85A66-967[»]
    ProteinModelPortaliP15144.
    SMRiP15144. Positions 66-967.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 87Cytoplasmic
    Topological domaini33 – 967935ExtracellularAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 3224Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 6836Cytosolic Ser/Thr-rich junctionAdd
    BLAST
    Regioni69 – 967899MetalloproteaseAdd
    BLAST
    Regioni260 – 35394Interaction with HCoV-229EAdd
    BLAST
    Regioni352 – 3565Substrate binding

    Domaini

    Amino acids 260-353 are essential to mediate susceptibility to infection with HCoV-229E (in porcine/human chimeric studies) and more specifically amino acids 288-295 (mutagenesis studies).

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOVERGENiHBG006616.
    InParanoidiP15144.
    KOiK11140.
    OMAiWVLLNLN.
    OrthoDBiEOG754HNR.
    PhylomeDBiP15144.
    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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15144-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKGFYISKS LGILGILLGV AAVCTIIALS VVYSQEKNKN ANSSPVASTT    50
    PSASATTNPA SATTLDQSKA WNRYRLPNTL KPDSYRVTLR PYLTPNDRGL 100
    YVFKGSSTVR FTCKEATDVI IIHSKKLNYT LSQGHRVVLR GVGGSQPPDI 150
    DKTELVEPTE YLVVHLKGSL VKDSQYEMDS EFEGELADDL AGFYRSEYME 200
    GNVRKVVATT QMQAADARKS FPCFDEPAMK AEFNITLIHP KDLTALSNML 250
    PKGPSTPLPE DPNWNVTEFH TTPKMSTYLL AFIVSEFDYV EKQASNGVLI 300
    RIWARPSAIA AGHGDYALNV TGPILNFFAG HYDTPYPLPK SDQIGLPDFN 350
    AGAMENWGLV TYRENSLLFD PLSSSSSNKE RVVTVIAHEL AHQWFGNLVT 400
    IEWWNDLWLN EGFASYVEYL GADYAEPTWN LKDLMVLNDV YRVMAVDALA 450
    SSHPLSTPAS EINTPAQISE LFDAISYSKG ASVLRMLSSF LSEDVFKQGL 500
    ASYLHTFAYQ NTIYLNLWDH LQEAVNNRSI QLPTTVRDIM NRWTLQMGFP 550
    VITVDTSTGT LSQEHFLLDP DSNVTRPSEF NYVWIVPITS IRDGRQQQDY 600
    WLIDVRAQND LFSTSGNEWV LLNLNVTGYY RVNYDEENWR KIQTQLQRDH 650
    SAIPVINRAQ IINDAFNLAS AHKVPVTLAL NNTLFLIEER QYMPWEAALS 700
    SLSYFKLMFD RSEVYGPMKN YLKKQVTPLF IHFRNNTNNW REIPENLMDQ 750
    YSEVNAISTA CSNGVPECEE MVSGLFKQWM ENPNNNPIHP NLRSTVYCNA 800
    IAQGGEEEWD FAWEQFRNAT LVNEADKLRA ALACSKELWI LNRYLSYTLN 850
    PDLIRKQDAT STIISITNNV IGQGLVWDFV QSNWKKLFND YGGGSFSFSN 900
    LIQAVTRRFS TEYELQQLEQ FKKDNEETGF GSGTRALEQA LEKTKANIKW 950
    VKENKEVVLQ WFTENSK 967
    Length:967
    Mass (Da):109,540
    Last modified:April 3, 2007 - v4
    Checksum:i37B6BC1BF0D6B1F2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti536 – 5361V → E in CAA31640. (PubMed:2901990)Curated
    Sequence conflicti887 – 8871L → P in CAA31640. (PubMed:2901990)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201V → M.
    Corresponds to variant rs10152474 [ dbSNP | Ensembl ].
    VAR_031262
    Natural varianti86 – 861R → Q.3 Publications
    Corresponds to variant rs25653 [ dbSNP | Ensembl ].
    VAR_014736
    Natural varianti242 – 2421D → Y.1 Publication
    VAR_006727
    Natural varianti243 – 2431L → P.1 Publication
    VAR_006728
    Natural varianti311 – 3111A → V.
    Corresponds to variant rs17240268 [ dbSNP | Ensembl ].
    VAR_031263
    Natural varianti321 – 3211T → M.
    Corresponds to variant rs8179199 [ dbSNP | Ensembl ].
    VAR_031264
    Natural varianti603 – 6031I → K.
    Corresponds to variant rs17240212 [ dbSNP | Ensembl ].
    VAR_031265
    Natural varianti603 – 6031I → M.1 Publication
    Corresponds to variant rs8192297 [ dbSNP | Ensembl ].
    VAR_031266
    Natural varianti752 – 7521S → N.
    Corresponds to variant rs25651 [ dbSNP | Ensembl ].
    VAR_014737

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13276 mRNA. Translation: CAA31640.1.
    M22324 mRNA. Translation: AAA51719.1.
    AC018988 Genomic DNA. No translation available.
    AC079075 Genomic DNA. No translation available.
    BC058928 mRNA. Translation: AAH58928.1.
    M55522 Genomic DNA. Translation: AAA83399.1.
    AJ421875, AJ421876 Genomic DNA. Translation: CAD19098.2.
    AJ426050 Genomic DNA. Translation: CAD19802.1.
    AJ427985
    , AJ427986, AJ427987, AJ427988 Genomic DNA. Translation: CAD20931.1.
    CCDSiCCDS10356.1.
    PIRiA30325.
    RefSeqiNP_001141.2. NM_001150.2.
    XP_005254949.1. XM_005254892.2.
    UniGeneiHs.1239.

    Genome annotation databases

    EnsembliENST00000300060; ENSP00000300060; ENSG00000166825.
    GeneIDi290.
    KEGGihsa:290.
    UCSCiuc002bop.4. human.

    Polymorphism databases

    DMDMi143811362.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13276 mRNA. Translation: CAA31640.1 .
    M22324 mRNA. Translation: AAA51719.1 .
    AC018988 Genomic DNA. No translation available.
    AC079075 Genomic DNA. No translation available.
    BC058928 mRNA. Translation: AAH58928.1 .
    M55522 Genomic DNA. Translation: AAA83399.1 .
    AJ421875 , AJ421876 Genomic DNA. Translation: CAD19098.2 .
    AJ426050 Genomic DNA. Translation: CAD19802.1 .
    AJ427985
    , AJ427986 , AJ427987 , AJ427988 Genomic DNA. Translation: CAD20931.1 .
    CCDSi CCDS10356.1.
    PIRi A30325.
    RefSeqi NP_001141.2. NM_001150.2.
    XP_005254949.1. XM_005254892.2.
    UniGenei Hs.1239.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FYQ X-ray 1.90 A 66-967 [» ]
    4FYR X-ray 1.91 A 66-967 [» ]
    4FYS X-ray 2.01 A 66-967 [» ]
    4FYT X-ray 1.85 A 66-967 [» ]
    ProteinModelPortali P15144.
    SMRi P15144. Positions 66-967.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106787. 2 interactions.
    IntActi P15144. 5 interactions.
    STRINGi 9606.ENSP00000300060.

    Chemistry

    BindingDBi P15144.
    ChEMBLi CHEMBL1907.
    DrugBanki DB00973. Ezetimibe.

    Protein family/group databases

    MEROPSi M01.001.

    PTM databases

    PhosphoSitei P15144.

    Polymorphism databases

    DMDMi 143811362.

    Proteomic databases

    MaxQBi P15144.
    PaxDbi P15144.
    PRIDEi P15144.

    Protocols and materials databases

    DNASUi 290.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300060 ; ENSP00000300060 ; ENSG00000166825 .
    GeneIDi 290.
    KEGGi hsa:290.
    UCSCi uc002bop.4. human.

    Organism-specific databases

    CTDi 290.
    GeneCardsi GC15M090328.
    H-InvDB HIX0038141.
    HGNCi HGNC:500. ANPEP.
    HPAi CAB002417.
    HPA004625.
    MIMi 151530. gene.
    neXtProti NX_P15144.
    PharmGKBi PA24815.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0308.
    HOVERGENi HBG006616.
    InParanoidi P15144.
    KOi K11140.
    OMAi WVLLNLN.
    OrthoDBi EOG754HNR.
    PhylomeDBi P15144.
    TreeFami TF300395.

    Enzyme and pathway databases

    BRENDAi 3.4.11.2. 2681.
    Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RK P15144.

    Miscellaneous databases

    GeneWikii Alanine_aminopeptidase.
    GenomeRNAii 290.
    NextBioi 1183.
    PROi P15144.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15144.
    Bgeei P15144.
    CleanExi HS_ANPEP.
    Genevestigatori P15144.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLN-86 AND MET-603.
      Tissue: Intestine.
    2. "Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N."
      Look A.T., Ashmun R.A., Shapiro L.H., Peiper S.C.
      J. Clin. Invest. 83:1299-1307(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21, VARIANT GLN-86.
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Pancreas.
    5. "Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells."
      Shapiro L.H., Ashmun R.A., Roberts W.M., Look A.T.
      J. Biol. Chem. 266:11999-12007(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
      Tissue: Intestinal epithelium.
    6. "Genomic organisation of aminopeptidase N."
      Eiz-Vesper B., Fuchs N., Gottschalk D., Mueller K., Reuter S., Blasczyk R.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-479 AND 524-967, VARIANT GLN-86.
      Tissue: Peripheral blood.
    7. "Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N."
      Watanabe Y., Iwaki-Egawa S., Mizukoshi H., Fujimoto Y.
      Biol. Chem. Hoppe-Seyler 376:397-400(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20 AND 70-81.
    8. "Cholesterol crystallization-promoting activity of aminopeptidase-N isolated from the vesicular carrier of biliary lipids."
      Nunez L., Amigo L., Rigotti A., Puglielli L., Mingrone G., Greco A.V., Nervi F.
      FEBS Lett. 329:84-88(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-18.
    9. "Purification and characterization of aminopeptidase N from human plasma."
      Tokioka-Terao M., Hiwada K., Kokubu T.
      Enzyme 32:65-75(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, SUBUNIT.
    10. "Variable O-glycosylation of CD13 (aminopeptidase N)."
      O'Connell P.J., Gerkis V., d'Apice A.J.F.
      J. Biol. Chem. 266:4593-4597(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    11. Cited for: INTERACTION WITH HCOV-229E SPIKE GLYCOPROTEIN, CHARACTERIZATION OF HCOV-229E RECEPTOR FUNCTION.
    12. "CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated."
      Favaloro E.J., Browning T., Facey D.
      Exp. Hematol. 21:1695-1701(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF SOLUBLE FORM.
    13. "CD13 (human aminopeptidase N) mediates human cytomegalovirus infection."
      Soderberg C., Giugni T.D., Zaia J.A., Larsson S., Wahlberg J.M., Moller E.
      J. Virol. 67:6576-6585(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF CMV RECEPTOR FUNCTION.
    14. "Characterization of functional domains in the human coronavirus HCV 229E receptor."
      Kolb A.F., Maile J., Heister A., Siddell S.G.
      J. Gen. Virol. 77:2515-2521(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR HCOV-229E INFECTION.
    15. "Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13) is normally expressed at the cell surface and has full enzymatic activity."
      Noren K., Hansen G.H., Clausen H., Noren O., Sjostrom H., Vogel L.K.
      Exp. Cell Res. 231:112-118(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GLYCOSYLATION.
    16. "Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N."
      Kolb A.F., Hegyi A., Siddell S.G.
      J. Gen. Virol. 78:2795-2802(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF RESIDUES CRITICAL FOR HCOV-229E INFECTION.
    17. "Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N."
      Hegyi A., Kolb A.F.
      J. Gen. Virol. 79:1387-1391(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION.
    18. "Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells."
      Dong X., An B., Salvucci Kierstead L., Storkus W.J., Amoscato A.A., Salter R.D.
      J. Immunol. 164:129-135(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
    19. "Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis."
      Pasqualini R., Koivunen E., Kain R., Lahdenranta J., Sakamoto M., Stryhn A., Ashmun R.A., Shapiro L.H., Arap W., Ruoslahti E.
      Cancer Res. 60:722-727(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN ANGIOGENESIS, CHARACTERIZATION OF RECEPTOR FOR TUMOR-HOMING PEPTIDES FUNCTION.
    20. "Expression of aminopeptidase N in human endometrium and regulation of its activity by estrogen."
      Seli E., Senturk L.M., Bahtiyar O.M., Kayisli U.A., Arici A.
      Fertil. Steril. 75:1172-1176(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION BY ESTRADIOL AND IL8.
    21. "Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): influence of N-linked glycosylation."
      Wentworth D.E., Holmes K.V.
      J. Virol. 75:9741-9752(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 288-ASP--SER-295 AND ASN-818.
    22. "Soluble aminopeptidase N/CD13 in malignant and nonmalignant effusions and intratumoral fluid."
      van Hensbergen Y., Broxterman H.J., Hanemaaijer R., Jorna A.S., van Lent N.A., Verheul H.M., Pinedo H.M., Hoekman K.
      Clin. Cancer Res. 8:3747-3754(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF SOLUBLE FORM.
    23. "Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E."
      Bonavia A., Zelus B.D., Wentworth D.E., Talbot P.J., Holmes K.V.
      J. Virol. 77:2530-2538(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCOV-229E SPIKE GLYCOPROTEIN.
    24. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
      Tissue: Bile.
    25. "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-128; ASN-234; ASN-265; ASN-681 AND ASN-818.
      Tissue: Plasma.
    26. "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-128; ASN-234; ASN-265; ASN-573; ASN-681 AND ASN-818.
      Tissue: Liver.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "The X-ray crystal structure of human aminopeptidase N reveals a novel dimer and the basis for peptide processing."
      Wong A.H., Zhou D., Rini J.M.
      J. Biol. Chem. 287:36804-36813(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 66-967 IN COMPLEX WITH ANGIOTENSIN-4 AND INHIBITORS, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE-BINDING REGION, ZINC-BINDING SITES, ACTIVE SITE, GLYCOSYLATION AT ASN-128; ASN-234; ASN-265; ASN-319; ASN-527; ASN-625; ASN-681 AND ASN-818, SUBUNIT, DISULFIDE BONDS.
    29. "Identification of point mutations in the aminopeptidase N gene by SSCP analysis and sequencing."
      Lendeckel U., Wex T., Arndt M., Frank K., Franke A., Ansorge S.
      Hum. Mutat. Suppl. 1:S158-S160(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TYR-242 AND PRO-243.

    Entry informationi

    Entry nameiAMPN_HUMAN
    AccessioniPrimary (citable) accession number: P15144
    Secondary accession number(s): Q16728
    , Q6GT90, Q8IUK3, Q8IVH3, Q9UCE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 175 of the entry and version 4 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

    Found to serve as a receptor for tumor-homing peptides, more specifically NGR peptides. It could serve thus as a target for delivering drugs into tumors. Concentration in human hepatic bile, varies from 17.3 to 57.6 micrograms/ml.

    Keywords - Technical termi

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

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Peptidase families
      Classification of peptidase families and list of entries
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3