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P28838

- AMPL_HUMAN

UniProt

P28838 - AMPL_HUMAN

Protein

Cytosol aminopeptidase

Gene

LAP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.

    Catalytic activityi

    Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
    Release of N-terminal proline from a peptide.

    Cofactori

    Binds 2 zinc ions per subunit. One zinc ion is tightly bound and essential for enzyme activity, while the second metal coordination site can be occupied by zinc, magnesium or manganese to give enzymes of different activities By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi282 – 2821Zinc 2By similarity
    Metal bindingi287 – 2871Zinc 1By similarity
    Metal bindingi287 – 2871Zinc 2By similarity
    Active sitei294 – 2941By similarity
    Metal bindingi305 – 3051Zinc 2By similarity
    Metal bindingi364 – 3641Zinc 1By similarity
    Metal bindingi366 – 3661Zinc 1By similarity
    Metal bindingi366 – 3661Zinc 2By similarity
    Active sitei368 – 3681By similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. manganese ion binding Source: InterPro
    3. metalloexopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM17.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosol aminopeptidase (EC:3.4.11.1)
    Alternative name(s):
    Leucine aminopeptidase 3
    Short name:
    LAP-3
    Leucyl aminopeptidase
    Peptidase S
    Proline aminopeptidase (EC:3.4.11.5)
    Prolyl aminopeptidase
    Gene namesi
    Name:LAP3
    Synonyms:LAPEP, PEPS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:18449. LAP3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrion Source: Ensembl
    4. nucleus Source: UniProt
    5. trans-Golgi network Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38537.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 519519Cytosol aminopeptidasePRO_0000165825Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei45 – 451N6-succinyllysineBy similarity
    Modified residuei61 – 611N6-succinyllysineBy similarity
    Modified residuei103 – 1031N6-succinyllysineBy similarity
    Modified residuei180 – 1801PhosphoserineBy similarity
    Modified residuei221 – 2211N6-acetyllysine; alternate1 Publication
    Modified residuei221 – 2211N6-succinyllysine; alternateBy similarity
    Modified residuei238 – 2381Phosphoserine1 Publication
    Modified residuei455 – 4551N6-acetyllysine; alternateBy similarity
    Modified residuei455 – 4551N6-succinyllysine; alternateBy similarity
    Modified residuei476 – 4761N6-succinyllysineBy similarity
    Modified residuei489 – 4891N6-acetyllysine; alternateBy similarity
    Modified residuei489 – 4891N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP28838.
    PaxDbiP28838.
    PRIDEiP28838.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00789806.
    P28838.
    UCD-2DPAGEP28838.

    PTM databases

    PhosphoSiteiP28838.

    Expressioni

    Gene expression databases

    ArrayExpressiP28838.
    BgeeiP28838.
    CleanExiHS_LAP3.
    GenevestigatoriP28838.

    Organism-specific databases

    HPAiHPA029606.
    HPA029607.

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    BioGridi119248. 19 interactions.
    IntActiP28838. 7 interactions.
    MINTiMINT-2802173.
    STRINGi9606.ENSP00000226299.

    Structurei

    3D structure databases

    ProteinModelPortaliP28838.
    SMRiP28838. Positions 33-516.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M17 family.Curated

    Phylogenomic databases

    eggNOGiCOG0260.
    HOGENOMiHOG000243129.
    HOVERGENiHBG003320.
    InParanoidiP28838.
    KOiK11142.
    OMAiGMDAMRA.
    OrthoDBiEOG7F24SG.
    PhylomeDBiP28838.
    TreeFamiTF314954.

    Family and domain databases

    HAMAPiMF_00181. Cytosol_peptidase_M17.
    InterProiIPR011356. Leucine_aapep/pepB.
    IPR000819. Peptidase_M17_C.
    IPR023042. Peptidase_M17_leu_NH2_pept.
    IPR008283. Peptidase_M17_N.
    [Graphical view]
    PfamiPF00883. Peptidase_M17. 1 hit.
    PF02789. Peptidase_M17_N. 1 hit.
    [Graphical view]
    PRINTSiPR00481. LAMNOPPTDASE.
    PROSITEiPS00631. CYTOSOL_AP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: P28838-1) [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

    MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP    50
    QFTSAGENFD KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG 100
    LGKKAAGIDE QENWHEGKEN IRAAVAAGCR QIQDLELSSV EVDPCGDAQA 150
    AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS GDQEAWQKGV LFASGQNLAR 200
    QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI EEQAMGSFLS 250
    VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD 300
    LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV 350
    RAKNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL 400
    GSGATGVFTN SSWLWNKLFE ASIETGDRVW RMPLFEHYTR QVVDCQLADV 450
    NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL DIAGVMTNKD EVPYLRKGMT 500
    GRPTRTLIEF LLRFSQDNA 519
    Length:519
    Mass (Da):56,166
    Last modified:January 23, 2007 - v3
    Checksum:iD960F8F5B9024585
    GO
    Isoform 2 (identifier: P28838-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: Missing.

    Note: Initiator Met-1 is removed.

    Show »
    Length:488
    Mass (Da):52,771
    Checksum:i0CADB3E07FD10B8B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201R → V in AAD17527. 1 PublicationCurated
    Sequence conflicti22 – 221F → S in AAD17527. 1 PublicationCurated
    Sequence conflicti29 – 291T → A in CAG33409. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3131Missing in isoform 2. 1 PublicationVSP_022631Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061738 mRNA. Translation: AAD17527.1.
    CR457128 mRNA. Translation: CAG33409.1.
    AK022055 mRNA. Translation: BAG51065.1.
    AK298613 mRNA. Translation: BAG60795.1.
    BC065564 mRNA. Translation: AAH65564.1.
    BC006199 mRNA. Translation: AAH06199.3.
    CCDSiCCDS3422.1. [P28838-1]
    PIRiPT0431.
    RefSeqiNP_056991.2. NM_015907.2. [P28838-1]
    UniGeneiHs.570791.

    Genome annotation databases

    EnsembliENST00000226299; ENSP00000226299; ENSG00000002549. [P28838-1]
    ENST00000606142; ENSP00000476028; ENSG00000002549. [P28838-2]
    GeneIDi51056.
    KEGGihsa:51056.
    UCSCiuc003gph.1. human. [P28838-1]

    Polymorphism databases

    DMDMi124028615.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061738 mRNA. Translation: AAD17527.1 .
    CR457128 mRNA. Translation: CAG33409.1 .
    AK022055 mRNA. Translation: BAG51065.1 .
    AK298613 mRNA. Translation: BAG60795.1 .
    BC065564 mRNA. Translation: AAH65564.1 .
    BC006199 mRNA. Translation: AAH06199.3 .
    CCDSi CCDS3422.1. [P28838-1 ]
    PIRi PT0431.
    RefSeqi NP_056991.2. NM_015907.2. [P28838-1 ]
    UniGenei Hs.570791.

    3D structure databases

    ProteinModelPortali P28838.
    SMRi P28838. Positions 33-516.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119248. 19 interactions.
    IntActi P28838. 7 interactions.
    MINTi MINT-2802173.
    STRINGi 9606.ENSP00000226299.

    Chemistry

    BindingDBi P28838.
    ChEMBLi CHEMBL3965.

    Protein family/group databases

    MEROPSi M17.001.

    PTM databases

    PhosphoSitei P28838.

    Polymorphism databases

    DMDMi 124028615.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00789806.
    P28838.
    UCD-2DPAGE P28838.

    Proteomic databases

    MaxQBi P28838.
    PaxDbi P28838.
    PRIDEi P28838.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000226299 ; ENSP00000226299 ; ENSG00000002549 . [P28838-1 ]
    ENST00000606142 ; ENSP00000476028 ; ENSG00000002549 . [P28838-2 ]
    GeneIDi 51056.
    KEGGi hsa:51056.
    UCSCi uc003gph.1. human. [P28838-1 ]

    Organism-specific databases

    CTDi 51056.
    GeneCardsi GC04P017578.
    H-InvDB HIX0004121.
    HGNCi HGNC:18449. LAP3.
    HPAi HPA029606.
    HPA029607.
    MIMi 170250. gene.
    neXtProti NX_P28838.
    PharmGKBi PA38537.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0260.
    HOGENOMi HOG000243129.
    HOVERGENi HBG003320.
    InParanoidi P28838.
    KOi K11142.
    OMAi GMDAMRA.
    OrthoDBi EOG7F24SG.
    PhylomeDBi P28838.
    TreeFami TF314954.

    Miscellaneous databases

    ChiTaRSi LAP3. human.
    GenomeRNAii 51056.
    NextBioi 53624.
    PROi P28838.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28838.
    Bgeei P28838.
    CleanExi HS_LAP3.
    Genevestigatori P28838.

    Family and domain databases

    HAMAPi MF_00181. Cytosol_peptidase_M17.
    InterProi IPR011356. Leucine_aapep/pepB.
    IPR000819. Peptidase_M17_C.
    IPR023042. Peptidase_M17_leu_NH2_pept.
    IPR008283. Peptidase_M17_N.
    [Graphical view ]
    Pfami PF00883. Peptidase_M17. 1 hit.
    PF02789. Peptidase_M17_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00481. LAMNOPPTDASE.
    PROSITEi PS00631. CYTOSOL_AP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Mao M., Liu T., Zhang J., Wu J., Zhang Q., Fu G., Shen Y., Zhou J., Yu Y., Wang Z., Chen S., Chen Z.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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).
    3. "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 2).
      Tissue: Embryo.
    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] (ISOFORM 1).
      Tissue: Eye and Lung.
    5. "Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase."
      Matsushima M., Takahashi T., Ichinose M., Miki K., Kurokawa K., Takahashi K.
      Biochem. Biophys. Res. Commun. 178:1459-1464(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 33-54.
      Tissue: Liver.
    6. "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-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAMPL_HUMAN
    AccessioniPrimary (citable) accession number: P28838
    Secondary accession number(s): B3KMQ3
    , Q6IAM6, Q6P0L6, Q9UQE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 150 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3