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Q9NQW7

- XPP1_HUMAN

UniProt

Q9NQW7 - XPP1_HUMAN

Protein

Xaa-Pro aminopeptidase 1

Gene

XPNPEP1

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 122 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.

    Catalytic activityi

    Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.2 Publications

    Cofactori

    Binds 2 manganese ions per subunit.2 Publications

    Enzyme regulationi

    Inhibited by apstatin and the metal ion chelators EDTA and 1,10-phenanthroline. Partially inhibited by dithiothreitol. Not inhibited by enalaprilat or amastatin.1 Publication

    Kineticsi

    1. KM=100.6 µM for bradykinin2 Publications
    2. KM=308 µM for the tripeptide Arg-Pro-Pro2 Publications

    pH dependencei

    Optimum pH is 8.2.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi415 – 4151Manganese 1
    Metal bindingi426 – 4261Manganese 1
    Metal bindingi426 – 4261Manganese 2
    Metal bindingi489 – 4891Manganese 2
    Metal bindingi523 – 5231Manganese 2
    Metal bindingi537 – 5371Manganese 1
    Metal bindingi537 – 5371Manganese 2

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. manganese ion binding Source: UniProtKB
    3. metalloaminopeptidase activity Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. bradykinin catabolic process Source: UniProtKB
    2. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.11.9. 2681.

    Protein family/group databases

    MEROPSiM24.009.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xaa-Pro aminopeptidase 1 (EC:3.4.11.9)
    Alternative name(s):
    Aminoacylproline aminopeptidase
    Cytosolic aminopeptidase P
    Soluble aminopeptidase P
    Short name:
    sAmp
    X-Pro aminopeptidase 1
    X-prolyl aminopeptidase 1, soluble
    Gene namesi
    Name:XPNPEP1Imported
    Synonyms:XPNPEPLImported, XPNPEPL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:12822. XPNPEP1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi41 – 411E → A: Reduces activity by 10%. 1 Publication
    Mutagenesisi477 – 4771W → E: Interferes with dimerization and reduces activity by 94%. 1 Publication

    Organism-specific databases

    PharmGKBiPA37415.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 623622Xaa-Pro aminopeptidase 1PRO_0000185083Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei304 – 3041N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NQW7.
    PaxDbiQ9NQW7.
    PRIDEiQ9NQW7.

    PTM databases

    PhosphoSiteiQ9NQW7.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested, including pancreas, heart, muscle, kidney, liver, lung and brain. Highest levels in pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ9NQW7.
    BgeeiQ9NQW7.
    CleanExiHS_XPNPEP1.
    GenevestigatoriQ9NQW7.

    Organism-specific databases

    HPAiCAB025196.
    HPA030419.
    HPA030420.
    HPA030422.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi113346. 39 interactions.
    IntActiQ9NQW7. 7 interactions.
    MINTiMINT-3039782.
    STRINGi9606.ENSP00000358694.

    Structurei

    Secondary structure

    1
    623
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 1610
    Turni20 – 223
    Beta strandi28 – 325
    Helixi45 – 473
    Helixi49 – 546
    Beta strandi62 – 687
    Beta strandi70 – 745
    Helixi76 – 783
    Helixi79 – 857
    Beta strandi90 – 945
    Helixi103 – 1108
    Beta strandi116 – 1194
    Helixi121 – 1233
    Helixi126 – 13813
    Beta strandi142 – 1454
    Helixi150 – 1545
    Helixi171 – 1744
    Helixi178 – 19013
    Turni191 – 1933
    Beta strandi194 – 1996
    Helixi202 – 2098
    Beta strandi215 – 2195
    Beta strandi225 – 2317
    Beta strandi233 – 2364
    Helixi240 – 2434
    Helixi245 – 2506
    Turni251 – 2544
    Helixi259 – 2613
    Beta strandi263 – 2664
    Helixi268 – 2703
    Helixi271 – 28010
    Beta strandi287 – 2915
    Helixi296 – 3016
    Helixi304 – 3063
    Beta strandi307 – 3126
    Helixi314 – 3207
    Helixi324 – 35128
    Helixi352 – 3543
    Helixi359 – 37113
    Beta strandi376 – 3816
    Beta strandi384 – 3874
    Helixi388 – 3925
    Helixi400 – 4023
    Beta strandi412 – 4165
    Beta strandi418 – 4203
    Beta strandi427 – 4315
    Helixi438 – 45518
    Helixi465 – 4728
    Helixi474 – 4785
    Beta strandi487 – 4904
    Beta strandi493 – 4953
    Beta strandi519 – 5224
    Beta strandi525 – 5284
    Turni529 – 5313
    Beta strandi532 – 5354
    Beta strandi537 – 5459
    Beta strandi552 – 5543
    Beta strandi556 – 5616
    Helixi569 – 5713
    Helixi574 – 5763
    Helixi579 – 60224
    Helixi606 – 6149

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CTZX-ray1.60A1-623[»]
    ProteinModelPortaliQ9NQW7.
    SMRiQ9NQW7. Positions 3-619.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQW7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24B family.Sequence Analysis

    Phylogenomic databases

    eggNOGiCOG0006.
    HOGENOMiHOG000255713.
    HOVERGENiHBG002934.
    InParanoidiQ9NQW7.
    KOiK01262.
    OMAiKWLEREC.
    PhylomeDBiQ9NQW7.
    TreeFamiTF314183.

    Family and domain databases

    Gene3Di3.40.350.10. 2 hits.
    3.90.230.10. 1 hit.
    InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
    IPR028980. Creatinase/Aminopeptidase_P_N.
    IPR000587. Creatinase_N.
    IPR000994. Pept_M24_structural-domain.
    IPR001131. Peptidase_M24B_aminopep-P_CS.
    [Graphical view]
    PfamiPF01321. Creatinase_N. 1 hit.
    PF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    SUPFAMiSSF53092. SSF53092. 1 hit.
    SSF55920. SSF55920. 1 hit.
    PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9NQW7-1) [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

    MPPKVTSELL RQLRQAMRNS EYVTEPIQAY IIPSGDAHQS EYIAPCDCRR    50
    AFVSGFDGSA GTAIITEEHA AMWTDGRYFL QAAKQMDSNW TLMKMGLKDT 100
    PTQEDWLVSV LPEGSRVGVD PLIIPTDYWK KMAKVLRSAG HHLIPVKENL 150
    VDKIWTDRPE RPCKPLLTLG LDYTGISWKD KVADLRLKMA ERNVMWFVVT 200
    ALDEIAWLFN LRGSDVEHNP VFFSYAIIGL ETIMLFIDGD RIDAPSVKEH 250
    LLLDLGLEAE YRIQVHPYKS ILSELKALCA DLSPREKVWV SDKASYAVSE 300
    TIPKDHRCCM PYTPICIAKA VKNSAESEGM RRAHIKDAVA LCELFNWLEK 350
    EVPKGGVTEI SAADKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYAPVP 400
    ETNRTLSLDE VYLIDSGAQY KDGTTDVTRT MHFGTPTAYE KECFTYVLKG 450
    HIAVSAAVFP TGTKGHLLDS FARSALWDSG LDYLHGTGHG VGSFLNVHEG 500
    PCGISYKTFS DEPLEAGMIV TDEPGYYEDG AFGIRIENVV LVVPVKTKYN 550
    FNNRGSLTFE PLTLVPIQTK MIDVDSLTDK ECDWLNNYHL TCRDVIGKEL 600
    QKQGRQEALE WLIRETQPIS KQH 623
    Length:623
    Mass (Da):69,918
    Last modified:January 23, 2007 - v3
    Checksum:iDF4F5AF41E2F3876
    GO
    Isoform 2 (identifier: Q9NQW7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         398-421: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:599
    Mass (Da):67,227
    Checksum:i6F6A7D909E1CC84D
    GO
    Isoform 3 (identifier: Q9NQW7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAASRKPPRVRVNHQDFQLRNLRIIEPNEVTHSGDTGVETDGRM

    Note: No experimental confirmation available.

    Show »
    Length:666
    Mass (Da):74,798
    Checksum:i59D0596A49C93B17
    GO
    Isoform 4 (identifier: Q9NQW7-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAASRKPPRVRVNHQDFQLRNLRIIEPNEVTHSGDTGVETDGRM
         398-421: Missing.

    Show »
    Length:642
    Mass (Da):72,107
    Checksum:i0119CDC61051D1C2
    GO

    Sequence cautioni

    The sequence CAD38640.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901W → C in AAH13417. (PubMed:15489334)Curated
    Sequence conflicti131 – 1311K → R in BAF82125. (PubMed:14702039)Curated
    Sequence conflicti332 – 3321R → P in CAA65068. (PubMed:9465902)Curated
    Sequence conflicti332 – 3321R → P in AAF97866. (PubMed:10871044)Curated
    Sequence conflicti496 – 4961N → D in BAD97233. (PubMed:17974005)Curated
    Sequence conflicti498 – 4981H → R in BAD97233. (PubMed:17974005)Curated
    Sequence conflicti572 – 5721I → T in BAF82125. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAASRKPPRVRVNHQDFQLR NLRIIEPNEVTHSGDTGVET DGRM in isoform 3 and isoform 4. 1 PublicationVSP_045250
    Alternative sequencei398 – 42124Missing in isoform 2 and isoform 4. 1 PublicationVSP_051752Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95762 mRNA. Translation: CAA65068.1.
    AF195530 mRNA. Translation: AAF97866.1.
    AF272981 mRNA. Translation: AAF75795.1.
    AK289436 mRNA. Translation: BAF82125.1.
    CR456922 mRNA. Translation: CAG33203.1.
    AK223513 mRNA. Translation: BAD97233.1.
    AL833411 mRNA. Translation: CAD38640.1. Different initiation.
    AL354951 Genomic DNA. Translation: CAI14248.1.
    CH471066 Genomic DNA. Translation: EAW49577.1.
    BC005126 mRNA. Translation: AAH05126.1.
    BC007579 mRNA. Translation: AAH07579.1.
    BC013417 mRNA. Translation: AAH13417.4.
    CCDSiCCDS7560.2. [Q9NQW7-3]
    RefSeqiNP_001161076.1. NM_001167604.1.
    NP_065116.3. NM_020383.3. [Q9NQW7-3]
    UniGeneiHs.390623.

    Genome annotation databases

    EnsembliENST00000322238; ENSP00000324011; ENSG00000108039.
    ENST00000502935; ENSP00000421566; ENSG00000108039. [Q9NQW7-3]
    GeneIDi7511.
    KEGGihsa:7511.
    UCSCiuc001kyp.2. human.
    uc001kyq.2. human. [Q9NQW7-1]
    uc009xxt.2. human.

    Polymorphism databases

    DMDMi68566146.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95762 mRNA. Translation: CAA65068.1 .
    AF195530 mRNA. Translation: AAF97866.1 .
    AF272981 mRNA. Translation: AAF75795.1 .
    AK289436 mRNA. Translation: BAF82125.1 .
    CR456922 mRNA. Translation: CAG33203.1 .
    AK223513 mRNA. Translation: BAD97233.1 .
    AL833411 mRNA. Translation: CAD38640.1 . Different initiation.
    AL354951 Genomic DNA. Translation: CAI14248.1 .
    CH471066 Genomic DNA. Translation: EAW49577.1 .
    BC005126 mRNA. Translation: AAH05126.1 .
    BC007579 mRNA. Translation: AAH07579.1 .
    BC013417 mRNA. Translation: AAH13417.4 .
    CCDSi CCDS7560.2. [Q9NQW7-3 ]
    RefSeqi NP_001161076.1. NM_001167604.1.
    NP_065116.3. NM_020383.3. [Q9NQW7-3 ]
    UniGenei Hs.390623.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CTZ X-ray 1.60 A 1-623 [» ]
    ProteinModelPortali Q9NQW7.
    SMRi Q9NQW7. Positions 3-619.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113346. 39 interactions.
    IntActi Q9NQW7. 7 interactions.
    MINTi MINT-3039782.
    STRINGi 9606.ENSP00000358694.

    Chemistry

    BindingDBi Q9NQW7.
    ChEMBLi CHEMBL3782.

    Protein family/group databases

    MEROPSi M24.009.

    PTM databases

    PhosphoSitei Q9NQW7.

    Polymorphism databases

    DMDMi 68566146.

    Proteomic databases

    MaxQBi Q9NQW7.
    PaxDbi Q9NQW7.
    PRIDEi Q9NQW7.

    Protocols and materials databases

    DNASUi 7511.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322238 ; ENSP00000324011 ; ENSG00000108039 .
    ENST00000502935 ; ENSP00000421566 ; ENSG00000108039 . [Q9NQW7-3 ]
    GeneIDi 7511.
    KEGGi hsa:7511.
    UCSCi uc001kyp.2. human.
    uc001kyq.2. human. [Q9NQW7-1 ]
    uc009xxt.2. human.

    Organism-specific databases

    CTDi 7511.
    GeneCardsi GC10M111614.
    HGNCi HGNC:12822. XPNPEP1.
    HPAi CAB025196.
    HPA030419.
    HPA030420.
    HPA030422.
    MIMi 602443. gene.
    neXtProti NX_Q9NQW7.
    PharmGKBi PA37415.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0006.
    HOGENOMi HOG000255713.
    HOVERGENi HBG002934.
    InParanoidi Q9NQW7.
    KOi K01262.
    OMAi KWLEREC.
    PhylomeDBi Q9NQW7.
    TreeFami TF314183.

    Enzyme and pathway databases

    BRENDAi 3.4.11.9. 2681.

    Miscellaneous databases

    ChiTaRSi XPNPEP1. human.
    EvolutionaryTracei Q9NQW7.
    GeneWikii XPNPEP1.
    GenomeRNAii 7511.
    NextBioi 29395.
    PROi Q9NQW7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQW7.
    Bgeei Q9NQW7.
    CleanExi HS_XPNPEP1.
    Genevestigatori Q9NQW7.

    Family and domain databases

    Gene3Di 3.40.350.10. 2 hits.
    3.90.230.10. 1 hit.
    InterProi IPR029149. Creatin/AminoP/Spt16_NTD.
    IPR028980. Creatinase/Aminopeptidase_P_N.
    IPR000587. Creatinase_N.
    IPR000994. Pept_M24_structural-domain.
    IPR001131. Peptidase_M24B_aminopep-P_CS.
    [Graphical view ]
    Pfami PF01321. Creatinase_N. 1 hit.
    PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53092. SSF53092. 1 hit.
    SSF55920. SSF55920. 1 hit.
    PROSITEi PS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)."
      Vanhoof G., Goossens F., Juliano M.A., Juliano L., Hendriks D., Schatteman K., Lin A.H., Scharpe S.
      Cytogenet. Cell Genet. 78:275-280(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Lymphocyte.
    2. "Cloning, chromosomal sublocalization of the human soluble aminopeptidase P gene (XPNPEP1) to 10q25.3 and conservation of the putative proton shuttle and metal ligand binding sites with XPNPEP2."
      Sprinkle T.J., Caldwell C., Ryan J.W.
      Arch. Biochem. Biophys. 378:51-56(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme."
      Cottrell G.S., Hooper N.M., Turner A.J.
      Biochemistry 39:15121-15128(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Tissue: Pancreatic adenocarcinoma1 Publication.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Adipose tissue.
    8. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: ColonImported, OvaryImported and PlacentaImported.
    11. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Tissue: Platelet1 Publication.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit."
      Li X., Lou Z., Li X., Zhou W., Ma M., Cao Y., Geng Y., Bartlam M., Zhang X.C., Rao Z.
      J. Biol. Chem. 283:22858-22866(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-41 AND TRP-477, SUBUNIT.

    Entry informationi

    Entry nameiXPP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQW7
    Secondary accession number(s): A8K071
    , G5E9Y2, G8JLB2, O15250, Q53EX6, Q8N3Q0, Q96D23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3