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Protein

Xaa-Pro aminopeptidase 1

Gene

XPNPEP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mn2+2 PublicationsNote: 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

    • aminopeptidase activity Source: UniProtKB
    • manganese ion binding Source: UniProtKB
    • metalloaminopeptidase activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    • bradykinin catabolic process Source: UniProtKB
    • proteolysis Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.8.1. 2681.
    3.4.11.9. 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 Componenti: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:12822. XPNPEP1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    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.

    Polymorphism and mutation databases

    BioMutaiXPNPEP1.
    DMDMi68566146.

    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

    BgeeiQ9NQW7.
    CleanExiHS_XPNPEP1.
    ExpressionAtlasiQ9NQW7. baseline and differential.
    GenevisibleiQ9NQW7. HS.

    Organism-specific databases

    HPAiCAB025196.
    HPA030419.
    HPA030420.
    HPA030422.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi113346. 42 interactions.
    IntActiQ9NQW7. 7 interactions.
    MINTiMINT-3039782.
    STRINGi9606.ENSP00000421566.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    GeneTreeiENSGT00390000013970.
    HOGENOMiHOG000255713.
    HOVERGENiHBG002934.
    InParanoidiQ9NQW7.
    KOiK01262.
    OMAiYRPGKWG.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MPPKVTSELL RQLRQAMRNS EYVTEPIQAY IIPSGDAHQS EYIAPCDCRR
    60 70 80 90 100
    AFVSGFDGSA GTAIITEEHA AMWTDGRYFL QAAKQMDSNW TLMKMGLKDT
    110 120 130 140 150
    PTQEDWLVSV LPEGSRVGVD PLIIPTDYWK KMAKVLRSAG HHLIPVKENL
    160 170 180 190 200
    VDKIWTDRPE RPCKPLLTLG LDYTGISWKD KVADLRLKMA ERNVMWFVVT
    210 220 230 240 250
    ALDEIAWLFN LRGSDVEHNP VFFSYAIIGL ETIMLFIDGD RIDAPSVKEH
    260 270 280 290 300
    LLLDLGLEAE YRIQVHPYKS ILSELKALCA DLSPREKVWV SDKASYAVSE
    310 320 330 340 350
    TIPKDHRCCM PYTPICIAKA VKNSAESEGM RRAHIKDAVA LCELFNWLEK
    360 370 380 390 400
    EVPKGGVTEI SAADKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYAPVP
    410 420 430 440 450
    ETNRTLSLDE VYLIDSGAQY KDGTTDVTRT MHFGTPTAYE KECFTYVLKG
    460 470 480 490 500
    HIAVSAAVFP TGTKGHLLDS FARSALWDSG LDYLHGTGHG VGSFLNVHEG
    510 520 530 540 550
    PCGISYKTFS DEPLEAGMIV TDEPGYYEDG AFGIRIENVV LVVPVKTKYN
    560 570 580 590 600
    FNNRGSLTFE PLTLVPIQTK MIDVDSLTDK ECDWLNNYHL TCRDVIGKEL
    610 620
    QKQGRQEALE WLIRETQPIS KQH
    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.Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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.
    CCDSiCCDS53576.1. [Q9NQW7-4]
    CCDS7560.2. [Q9NQW7-3]
    RefSeqiNP_001161076.1. NM_001167604.1. [Q9NQW7-4]
    NP_065116.3. NM_020383.3. [Q9NQW7-3]
    UniGeneiHs.390623.

    Genome annotation databases

    EnsembliENST00000322238; ENSP00000324011; ENSG00000108039. [Q9NQW7-4]
    ENST00000502935; ENSP00000421566; ENSG00000108039. [Q9NQW7-3]
    GeneIDi7511.
    KEGGihsa:7511.
    UCSCiuc001kyp.2. human.
    uc001kyq.2. human. [Q9NQW7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.
    CCDSiCCDS53576.1. [Q9NQW7-4]
    CCDS7560.2. [Q9NQW7-3]
    RefSeqiNP_001161076.1. NM_001167604.1. [Q9NQW7-4]
    NP_065116.3. NM_020383.3. [Q9NQW7-3]
    UniGeneiHs.390623.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi113346. 42 interactions.
    IntActiQ9NQW7. 7 interactions.
    MINTiMINT-3039782.
    STRINGi9606.ENSP00000421566.

    Chemistry

    BindingDBiQ9NQW7.
    ChEMBLiCHEMBL3782.

    Protein family/group databases

    MEROPSiM24.009.

    PTM databases

    PhosphoSiteiQ9NQW7.

    Polymorphism and mutation databases

    BioMutaiXPNPEP1.
    DMDMi68566146.

    Proteomic databases

    MaxQBiQ9NQW7.
    PaxDbiQ9NQW7.
    PRIDEiQ9NQW7.

    Protocols and materials databases

    DNASUi7511.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000322238; ENSP00000324011; ENSG00000108039. [Q9NQW7-4]
    ENST00000502935; ENSP00000421566; ENSG00000108039. [Q9NQW7-3]
    GeneIDi7511.
    KEGGihsa:7511.
    UCSCiuc001kyp.2. human.
    uc001kyq.2. human. [Q9NQW7-1]

    Organism-specific databases

    CTDi7511.
    GeneCardsiGC10M111614.
    HGNCiHGNC:12822. XPNPEP1.
    HPAiCAB025196.
    HPA030419.
    HPA030420.
    HPA030422.
    MIMi602443. gene.
    neXtProtiNX_Q9NQW7.
    PharmGKBiPA37415.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0006.
    GeneTreeiENSGT00390000013970.
    HOGENOMiHOG000255713.
    HOVERGENiHBG002934.
    InParanoidiQ9NQW7.
    KOiK01262.
    OMAiYRPGKWG.
    PhylomeDBiQ9NQW7.
    TreeFamiTF314183.

    Enzyme and pathway databases

    BRENDAi3.1.8.1. 2681.
    3.4.11.9. 2681.

    Miscellaneous databases

    ChiTaRSiXPNPEP1. human.
    EvolutionaryTraceiQ9NQW7.
    GeneWikiiXPNPEP1.
    GenomeRNAii7511.
    NextBioi29395.
    PROiQ9NQW7.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NQW7.
    CleanExiHS_XPNPEP1.
    ExpressionAtlasiQ9NQW7. baseline and differential.
    GenevisibleiQ9NQW7. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "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: July 22, 2015
    This is version 131 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.