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Protein

Acylamino-acid-releasing enzyme

Gene

APEH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 systemPROSITE-ProRule annotation1 Publication
Active sitei675 – 6751Charge relay systemPROSITE-ProRule annotation
Active sitei707 – 7071Charge relay systemPROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  • omega peptidase activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • beta-amyloid metabolic process Source: UniProtKB
  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

ESTHERihuman-APEH. ACPH_Peptidase_S9.
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 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:586. APEH.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • nuclear membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24878.

Polymorphism and mutation databases

BioMutaiAPEH.
DMDMi38258902.

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 – 1871Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP13798.
PaxDbiP13798.
PeptideAtlasiP13798.
PRIDEiP13798.

PTM databases

PhosphoSiteiP13798.

Expressioni

Gene expression databases

BgeeiP13798.
CleanExiHS_APEH.
ExpressionAtlasiP13798. baseline and differential.
GenevisibleiP13798. HS.

Organism-specific databases

HPAiHPA029700.
HPA029701.
HPA029702.
HPA029703.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
IST1P539904EBI-723792,EBI-945994
LGALS8O002143EBI-723792,EBI-740058

Protein-protein interaction databases

BioGridi106824. 34 interactions.
IntActiP13798. 4 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.
GeneTreeiENSGT00390000013172.
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

        10         20         30         40         50
MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GQYRTVHTEW
60 70 80 90 100
TQRDLERMEN IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG
110 120 130 140 150
TMKAVLRKAG GTGPGEEKQF LEVWEKNRKL KSFNLSALEK HGPVYEDDCF
160 170 180 190 200
GCLSWSHSET HLLYVAEKKR PKAESFFQTK ALDVSASDDE IARLKKPDQA
210 220 230 240 250
IKGDQFVFYE DWGENMVSKS IPVLCVLDVE SGNISVLEGV PENVSPGQAF
260 270 280 290 300
WAPGDAGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLIGG KCELLSDDSL
310 320 330 340 350
AVSSPRLSPD QCRIVYLQYP SLIPHHQCSQ LCLYDWYTKV TSVVVDVVPR
360 370 380 390 400
QLGENFSGIY CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQVGTVTS
410 420 430 440 450
LTAGGSGGSW KLLTIDQDLM VAQFSTPSLP PTLKVGFLPS AGKEQSVLWV
460 470 480 490 500
SLEEAEPIPD IHWGIRVLQP PPEQENVQYA GLDFEAILLQ PGSPPDKTQV
510 520 530 540 550
PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS TGFGQDSILS
560 570 580 590 600
LPGNVGHQDV KDVQFAVEQV LQEEHFDASH VALMGGSHGG FISCHLIGQY
610 620 630 640 650
PETYRACVAR NPVINIASML GSTDIPDWCV VEAGFPFSSD CLPDLSVWAE
660 670 680 690 700
MLDKSPIRYI PQVKTPLLLM LGQEDRRVPF KQGMEYYRAL KTRNVPVRLL
710 720 730
LYPKSTHALS EVEVESDSFM NAVLWLRTHL GS
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. Curated

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:
EMBLi
GenBanki
DDBJi
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.
XP_011531962.1. XM_011533660.1.
UniGeneiHs.517969.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011531962.1. XM_011533660.1.
UniGeneiHs.517969.

3D structure databases

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

Protein-protein interaction databases

BioGridi106824. 34 interactions.
IntActiP13798. 4 interactions.
MINTiMINT-5004051.
STRINGi9606.ENSP00000296456.

Chemistry

ChEMBLiCHEMBL1741174.

Protein family/group databases

ESTHERihuman-APEH. ACPH_Peptidase_S9.
MEROPSiS09.004.

PTM databases

PhosphoSiteiP13798.

Polymorphism and mutation databases

BioMutaiAPEH.
DMDMi38258902.

Proteomic databases

MaxQBiP13798.
PaxDbiP13798.
PeptideAtlasiP13798.
PRIDEiP13798.

Protocols and materials databases

DNASUi327.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi327.
GeneCardsiGC03P049711.
HGNCiHGNC:586. APEH.
HPAiHPA029700.
HPA029701.
HPA029702.
HPA029703.
MIMi102645. gene.
neXtProtiNX_P13798.
PharmGKBiPA24878.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1506.
GeneTreeiENSGT00390000013172.
HOGENOMiHOG000007443.
HOVERGENiHBG000869.
InParanoidiP13798.
KOiK01303.
OrthoDBiEOG776SPB.
PhylomeDBiP13798.
TreeFamiTF312937.

Miscellaneous databases

ChiTaRSiAPEH. human.
GeneWikiiAPEH_(gene).
GenomeRNAii327.
NextBioi1343.
PROiP13798.
SOURCEiSearch...

Gene expression databases

BgeeiP13798.
CleanExiHS_APEH.
ExpressionAtlasiP13798. baseline and differential.
GenevisibleiP13798. HS.

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]
ProtoNetiSearch...

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. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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 22, 2015
This is version 151 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

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.