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P13798

- ACPH_HUMAN

UniProt

P13798 - ACPH_HUMAN

Protein

Acylamino-acid-releasing enzyme

Gene

APEH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (07 Nov 2003)
      Previous versions | rss
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    Functioni

    This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser.2 Publications

    Catalytic activityi

    Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei587 – 5871Charge relay system1 PublicationPROSITE-ProRule annotation
    Active sitei675 – 6751Charge relay systemPROSITE-ProRule annotation
    Active sitei707 – 7071Charge relay system1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. omega peptidase activity Source: UniProt
    2. poly(A) RNA binding Source: UniProtKB
    3. serine-type endopeptidase activity Source: UniProt

    GO - Biological processi

    1. beta-amyloid metabolic process Source: UniProt
    2. proteolysis Source: UniProt

    Keywords - Molecular functioni

    Hydrolase

    Protein family/group databases

    MEROPSiS09.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acylamino-acid-releasing enzyme (EC:3.4.19.1)
    Short name:
    AARE
    Alternative name(s):
    Acyl-peptide hydrolase
    Short name:
    APH
    Acylaminoacyl-peptidase
    Oxidized protein hydrolase
    Short name:
    OPH
    Gene namesi
    Name:APEH
    Synonyms:D3F15S2, D3S48E, DNF15S2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:586. APEH.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. nuclear membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24878.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 732732Acylamino-acid-releasing enzymePRO_0000122430Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei185 – 1851Phosphoserine1 Publication
    Modified residuei187 – 1871Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP13798.
    PaxDbiP13798.
    PeptideAtlasiP13798.
    PRIDEiP13798.

    PTM databases

    PhosphoSiteiP13798.

    Expressioni

    Gene expression databases

    ArrayExpressiP13798.
    BgeeiP13798.
    CleanExiHS_APEH.
    GenevestigatoriP13798.

    Organism-specific databases

    HPAiHPA029700.
    HPA029701.
    HPA029702.
    HPA029703.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi106824. 32 interactions.
    IntActiP13798. 3 interactions.
    MINTiMINT-5004051.
    STRINGi9606.ENSP00000296456.

    Structurei

    3D structure databases

    ProteinModelPortaliP13798.
    SMRiP13798. Positions 375-729.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9C family.Curated

    Phylogenomic databases

    eggNOGiCOG1506.
    HOGENOMiHOG000007443.
    HOVERGENiHBG000869.
    InParanoidiP13798.
    KOiK01303.
    OrthoDBiEOG776SPB.
    PhylomeDBiP13798.
    TreeFamiTF312937.

    Family and domain databases

    Gene3Di2.120.10.30. 2 hits.
    3.40.50.1820. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    [Graphical view]
    PfamiPF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P13798-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GQYRTVHTEW    50
    TQRDLERMEN IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG 100
    TMKAVLRKAG GTGPGEEKQF LEVWEKNRKL KSFNLSALEK HGPVYEDDCF 150
    GCLSWSHSET HLLYVAEKKR PKAESFFQTK ALDVSASDDE IARLKKPDQA 200
    IKGDQFVFYE DWGENMVSKS IPVLCVLDVE SGNISVLEGV PENVSPGQAF 250
    WAPGDAGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLIGG KCELLSDDSL 300
    AVSSPRLSPD QCRIVYLQYP SLIPHHQCSQ LCLYDWYTKV TSVVVDVVPR 350
    QLGENFSGIY CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQVGTVTS 400
    LTAGGSGGSW KLLTIDQDLM VAQFSTPSLP PTLKVGFLPS AGKEQSVLWV 450
    SLEEAEPIPD IHWGIRVLQP PPEQENVQYA GLDFEAILLQ PGSPPDKTQV 500
    PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS TGFGQDSILS 550
    LPGNVGHQDV KDVQFAVEQV LQEEHFDASH VALMGGSHGG FISCHLIGQY 600
    PETYRACVAR NPVINIASML GSTDIPDWCV VEAGFPFSSD CLPDLSVWAE 650
    MLDKSPIRYI PQVKTPLLLM LGQEDRRVPF KQGMEYYRAL KTRNVPVRLL 700
    LYPKSTHALS EVEVESDSFM NAVLWLRTHL GS 732
    Length:732
    Mass (Da):81,225
    Last modified:November 7, 2003 - v4
    Checksum:iA2C370516324D851
    GO

    Sequence cautioni

    The sequence AAA35769.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011T → S in BAA07476. (PubMed:8724851)Curated
    Sequence conflicti137 – 1371A → V in BAA07476. (PubMed:8724851)Curated
    Sequence conflicti168 – 1681K → R in BAA07476. (PubMed:8724851)Curated
    Sequence conflicti200 – 2001A → P in BAA07476. (PubMed:8724851)Curated
    Sequence conflicti403 – 4031A → V in AAF37321. (PubMed:10719179)Curated

    Mass spectrometryi

    Molecular mass is 81269.9±8.7 Da from positions 1 - 732. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti541 – 5411T → M.
    Corresponds to variant rs3816877 [ dbSNP | Ensembl ].
    VAR_051580

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38441 mRNA. Translation: BAA07476.1.
    AF141383 mRNA. Translation: AAF37321.1.
    BC000362 mRNA. Translation: AAH00362.1.
    BC001499 mRNA. Translation: AAH01499.1.
    BC001826 mRNA. Translation: AAH01826.1.
    J03068 mRNA. Translation: AAA35769.1. Frameshift.
    CCDSiCCDS2801.1.
    PIRiJC4655.
    RefSeqiNP_001631.3. NM_001640.3.
    UniGeneiHs.517969.

    Genome annotation databases

    EnsembliENST00000296456; ENSP00000296456; ENSG00000164062.
    GeneIDi327.
    KEGGihsa:327.
    UCSCiuc003cxf.3. human.

    Polymorphism databases

    DMDMi38258902.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38441 mRNA. Translation: BAA07476.1 .
    AF141383 mRNA. Translation: AAF37321.1 .
    BC000362 mRNA. Translation: AAH00362.1 .
    BC001499 mRNA. Translation: AAH01499.1 .
    BC001826 mRNA. Translation: AAH01826.1 .
    J03068 mRNA. Translation: AAA35769.1 . Frameshift.
    CCDSi CCDS2801.1.
    PIRi JC4655.
    RefSeqi NP_001631.3. NM_001640.3.
    UniGenei Hs.517969.

    3D structure databases

    ProteinModelPortali P13798.
    SMRi P13798. Positions 375-729.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106824. 32 interactions.
    IntActi P13798. 3 interactions.
    MINTi MINT-5004051.
    STRINGi 9606.ENSP00000296456.

    Chemistry

    ChEMBLi CHEMBL1741174.

    Protein family/group databases

    MEROPSi S09.004.

    PTM databases

    PhosphoSitei P13798.

    Polymorphism databases

    DMDMi 38258902.

    Proteomic databases

    MaxQBi P13798.
    PaxDbi P13798.
    PeptideAtlasi P13798.
    PRIDEi P13798.

    Protocols and materials databases

    DNASUi 327.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296456 ; ENSP00000296456 ; ENSG00000164062 .
    GeneIDi 327.
    KEGGi hsa:327.
    UCSCi uc003cxf.3. human.

    Organism-specific databases

    CTDi 327.
    GeneCardsi GC03P049711.
    HGNCi HGNC:586. APEH.
    HPAi HPA029700.
    HPA029701.
    HPA029702.
    HPA029703.
    MIMi 102645. gene.
    neXtProti NX_P13798.
    PharmGKBi PA24878.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1506.
    HOGENOMi HOG000007443.
    HOVERGENi HBG000869.
    InParanoidi P13798.
    KOi K01303.
    OrthoDBi EOG776SPB.
    PhylomeDBi P13798.
    TreeFami TF312937.

    Miscellaneous databases

    ChiTaRSi APEH. human.
    GeneWikii APEH_(gene).
    GenomeRNAii 327.
    NextBioi 1343.
    PROi P13798.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13798.
    Bgeei P13798.
    CleanExi HS_APEH.
    Genevestigatori P13798.

    Family and domain databases

    Gene3Di 2.120.10.30. 2 hits.
    3.40.50.1820. 1 hit.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    [Graphical view ]
    Pfami PF00326. Peptidase_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of human acylamino acid-releasing enzyme."
      Mitta M., Ohnogi H., Mizutani S., Sakiyama F., Kato I., Tsunasawa S.
      DNA Res. 3:31-35(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase."
      Fujino T., Watanabe K., Beppu M., Kikugawa K., Yasuda H.
      Biochim. Biophys. Acta 1478:102-112(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    3. "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: Muscle.
    4. "The DNF15S2 locus at 3p21 is transcribed in normal lung and small cell lung cancer."
      Naylor S.L., Marshall A., Hensel C., Martinez P.F., Holley B., Sakaguchi A.Y.
      Genomics 4:355-361(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 102-732.
    5. "Structural investigations on human erythrocyte acylpeptide hydrolase by mass spectrometric procedures."
      Scaloni A., Ingallinella P., Andolfo A., Jones W., Marino G., Manning J.M.
      J. Protein Chem. 18:349-360(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, ACETYLATION AT MET-1.
    6. "The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase."
      Erlandsson R., Boldog F., Persson B., Zabarovsky E.R., Allikmets R.L., Sumegi J., Klein G., Joernvall H.
      Oncogene 6:1293-1295(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities."
      Jones W.M., Scaloni A., Bossa F., Popowicz A.M., Schneewind O., Manning J.M.
      Proc. Natl. Acad. Sci. U.S.A. 88:2194-2198(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme."
      Scaloni A., Jones W.M., Barra D., Pospischil M., Sassa S., Popowicz A., Manning L.R., Schneewind O., Manning J.M.
      J. Biol. Chem. 267:3811-3818(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITES SER-587 AND HIS-707.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase."
      Feese M., Scaloni A., Jones W.M., Mannig J.M., Remington S.J.
      J. Mol. Biol. 233:546-549(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiACPH_HUMAN
    AccessioniPrimary (citable) accession number: P13798
    Secondary accession number(s): Q9BQ33, Q9P0Y2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 7, 2003
    Last modified: October 1, 2014
    This is version 142 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3