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P13798

- ACPH_HUMAN

UniProt

P13798 - ACPH_HUMAN

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Protein
Acylamino-acid-releasing enzyme
Gene
APEH, D3F15S2, D3S48E, DNF15S2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publication
Active sitei675 – 6751Charge relay system By similarity
Active sitei707 – 7071Charge relay system1 Publication

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24878.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732Acylamino-acid-releasing enzyme
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9C family.

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011T → S in BAA07476. 1 Publication
Sequence conflicti137 – 1371A → V in BAA07476. 1 Publication
Sequence conflicti168 – 1681K → R in BAA07476. 1 Publication
Sequence conflicti200 – 2001A → P in BAA07476. 1 Publication
Sequence conflicti403 – 4031A → V in AAF37321. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 141 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

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