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Q9ULA0

- DNPEP_HUMAN

UniProt

Q9ULA0 - DNPEP_HUMAN

Protein

Aspartyl aminopeptidase

Gene

DNPEP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism.

    Catalytic activityi

    Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.

    Cofactori

    Binds 2 zinc ions per subunit.

    Enzyme regulationi

    One of the zinc ions is readily exchangeable with other divalent cations such as manganese, which strongly stimulates the enzymatic activity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi94 – 941Zinc 1
    Binding sitei170 – 1701Substrate
    Metal bindingi264 – 2641Zinc 1
    Metal bindingi264 – 2641Zinc 2
    Binding sitei301 – 3011Substrate
    Metal bindingi302 – 3021Zinc 2
    Metal bindingi346 – 3461Zinc 1
    Binding sitei346 – 3461Substrate
    Binding sitei349 – 3491Substrate
    Binding sitei374 – 3741Substrate
    Binding sitei381 – 3811Substrate
    Metal bindingi440 – 4401Zinc 2

    GO - Molecular functioni

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

    GO - Biological processi

    1. peptide metabolic process Source: ProtInc

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM18.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartyl aminopeptidase (EC:3.4.11.21)
    Gene namesi
    Name:DNPEP
    Synonyms:ASPEP, DAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2981. DNPEP.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytoplasm Source: ProtInc
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27448.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 475475Aspartyl aminopeptidasePRO_0000173451Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9ULA0.
    PaxDbiQ9ULA0.
    PRIDEiQ9ULA0.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9ULA0.
    BgeeiQ9ULA0.
    CleanExiHS_DAP.
    HS_DNPEP.
    GenevestigatoriQ9ULA0.

    Organism-specific databases

    HPAiHPA036398.
    HPA044860.

    Interactioni

    Subunit structurei

    Tetrahedron-shaped homododecamer built from six homodimers.1 Publication

    Protein-protein interaction databases

    BioGridi117093. 22 interactions.
    IntActiQ9ULA0. 3 interactions.
    STRINGi9606.ENSP00000273075.

    Structurei

    Secondary structure

    1
    475
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 2619
    Helixi31 – 4414
    Beta strandi63 – 686
    Turni69 – 713
    Beta strandi72 – 787
    Beta strandi88 – 947
    Beta strandi99 – 11012
    Beta strandi113 – 12311
    Helixi126 – 1294
    Beta strandi134 – 14310
    Turni145 – 1473
    Beta strandi150 – 1567
    Helixi169 – 1713
    Turni173 – 1775
    Turni183 – 1864
    Beta strandi190 – 1934
    Helixi194 – 2007
    Helixi218 – 22811
    Helixi232 – 2343
    Beta strandi235 – 24410
    Beta strandi249 – 2513
    Turni252 – 2554
    Beta strandi257 – 2604
    Helixi263 – 27917
    Turni283 – 2886
    Beta strandi291 – 2999
    Helixi301 – 3033
    Helixi315 – 32410
    Helixi332 – 3365
    Helixi337 – 3393
    Beta strandi341 – 3455
    Helixi356 – 3583
    Beta strandi372 – 3743
    Turni377 – 3804
    Helixi385 – 39814
    Beta strandi403 – 4053
    Helixi417 – 4259
    Beta strandi428 – 4336
    Beta strandi435 – 4384
    Beta strandi441 – 4488
    Helixi449 – 46820

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DYOX-ray2.20A1-468[»]
    ProteinModelPortaliQ9ULA0.
    SMRiQ9ULA0. Positions 7-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M18 family.Curated

    Phylogenomic databases

    eggNOGiCOG1362.
    HOVERGENiHBG051386.
    InParanoidiQ9ULA0.
    KOiK01267.
    OrthoDBiEOG789CB1.
    PhylomeDBiQ9ULA0.
    TreeFamiTF300487.

    Family and domain databases

    Gene3Di2.30.250.10. 1 hit.
    InterProiIPR001948. Peptidase_M18.
    IPR023358. Peptidase_M18_dom2.
    [Graphical view]
    PfamiPF02127. Peptidase_M18. 1 hit.
    [Graphical view]
    PRINTSiPR00932. AMINO1PTASE.

    Sequencei

    Sequence statusi: Complete.

    Q9ULA0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQVAMNGKAR KEAVQTAAKE LLKFVNRSPS PFHAVAECRN RLLQAGFSEL    50
    KETEKWNIKP ESKYFMTRNS STIIAFAVGG QYVPGNGFSL IGAHTDSPCL 100
    RVKRRSRRSQ VGFQQVGVET YGGGIWSTWF DRDLTLAGRV IVKCPTSGRL 150
    EQQLVHVERP ILRIPHLAIH LQRNINENFG PNTEMHLVPI LATAIQEELE 200
    KGTPEPGPLN AVDERHHSVL MSLLCAHLGL SPKDIVEMEL CLADTQPAVL 250
    GGAYDEFIFA PRLDNLHSCF CALQALIDSC AGPGSLATEP HVRMVTLYDN 300
    EEVGSESAQG AQSLLTELVL RRISASCQHP TAFEEAIPKS FMISADMAHA 350
    VHPNYLDKHE ENHRPLFHKG PVIKVNSKQR YASNAVSEAL IREVANKVKV 400
    PLQDLMVRND TPCGTTIGPI LASRLGLRVL DLGSPQLAMH SIREMACTTG 450
    VLQTLTLFKG FFELFPSLSH NLLVD 475
    Length:475
    Mass (Da):52,428
    Last modified:May 1, 2000 - v1
    Checksum:iA02BDCFB516BD081
    GO

    Sequence cautioni

    The sequence BAA92014.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191E → V in BAA92014. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005050 mRNA. Translation: AAD01211.2.
    AK001977 mRNA. Translation: BAA92014.1. Different initiation.
    AC053503 Genomic DNA. No translation available.
    BC000653 mRNA. Translation: AAH00653.2.
    RefSeqiNP_036232.2. NM_012100.2.
    UniGeneiHs.258551.

    Genome annotation databases

    EnsembliENST00000273075; ENSP00000273075; ENSG00000123992.
    GeneIDi23549.
    KEGGihsa:23549.
    UCSCiuc002vle.2. human.

    Polymorphism databases

    DMDMi17367145.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005050 mRNA. Translation: AAD01211.2 .
    AK001977 mRNA. Translation: BAA92014.1 . Different initiation.
    AC053503 Genomic DNA. No translation available.
    BC000653 mRNA. Translation: AAH00653.2 .
    RefSeqi NP_036232.2. NM_012100.2.
    UniGenei Hs.258551.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DYO X-ray 2.20 A 1-468 [» ]
    ProteinModelPortali Q9ULA0.
    SMRi Q9ULA0. Positions 7-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117093. 22 interactions.
    IntActi Q9ULA0. 3 interactions.
    STRINGi 9606.ENSP00000273075.

    Chemistry

    BindingDBi Q9ULA0.
    ChEMBLi CHEMBL2761.
    DrugBanki DB00142. L-Glutamic Acid.

    Protein family/group databases

    MEROPSi M18.002.

    Polymorphism databases

    DMDMi 17367145.

    Proteomic databases

    MaxQBi Q9ULA0.
    PaxDbi Q9ULA0.
    PRIDEi Q9ULA0.

    Protocols and materials databases

    DNASUi 23549.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273075 ; ENSP00000273075 ; ENSG00000123992 .
    GeneIDi 23549.
    KEGGi hsa:23549.
    UCSCi uc002vle.2. human.

    Organism-specific databases

    CTDi 23549.
    GeneCardsi GC02M220238.
    HGNCi HGNC:2981. DNPEP.
    HPAi HPA036398.
    HPA044860.
    MIMi 611367. gene.
    neXtProti NX_Q9ULA0.
    PharmGKBi PA27448.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1362.
    HOVERGENi HBG051386.
    InParanoidi Q9ULA0.
    KOi K01267.
    OrthoDBi EOG789CB1.
    PhylomeDBi Q9ULA0.
    TreeFami TF300487.

    Miscellaneous databases

    GeneWikii DNPEP.
    GenomeRNAii 23549.
    NextBioi 46092.
    PROi Q9ULA0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ULA0.
    Bgeei Q9ULA0.
    CleanExi HS_DAP.
    HS_DNPEP.
    Genevestigatori Q9ULA0.

    Family and domain databases

    Gene3Di 2.30.250.10. 1 hit.
    InterProi IPR001948. Peptidase_M18.
    IPR023358. Peptidase_M18_dom2.
    [Graphical view ]
    Pfami PF02127. Peptidase_M18. 1 hit.
    [Graphical view ]
    PRINTSi PR00932. AMINO1PTASE.
    ProtoNeti Search...

    Publicationsi

    1. "Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase."
      Wilk S., Wilk E., Magnusson R.P.
      J. Biol. Chem. 273:15961-15970(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    2. "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].
      Tissue: Placenta.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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: Eye.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family."
      Chaikuad A., Pilka E.S., Riso A.D., Delft F.V., Kavanagh K.L., Venien-Bryan C., Oppermann U., Yue W.W.
      BMC Struct. Biol. 12:14-14(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-468 IN COMPLEX WITH SUBSTRATE ANALOG, ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, SUBUNIT.

    Entry informationi

    Entry nameiDNPEP_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULA0
    Secondary accession number(s): Q9BW44, Q9NUV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    It is uncertain whether Met-1 or Met-5 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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