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P13798 (ACPH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acylamino-acid-releasing enzyme

Short name=AARE
EC=3.4.19.1
Alternative name(s):
Acyl-peptide hydrolase
Short name=APH
Acylaminoacyl-peptidase
Oxidized protein hydrolase
Short name=OPH
Gene names
Name:APEH
Synonyms:D3F15S2, D3S48E, DNF15S2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length732 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7

Catalytic activity

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase S9C family.

Mass spectrometry

Molecular mass is 81269.9±8.7 Da from positions 1 - 732. Determined by ESI. Ref.5

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 732732Acylamino-acid-releasing enzyme
PRO_0000122430

Sites

Active site5871Charge relay system Ref.8
Active site6751Charge relay system By similarity
Active site7071Charge relay system Ref.8

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5
Modified residue1851Phosphoserine Ref.10
Modified residue1871Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13

Natural variations

Natural variant5411T → M.
Corresponds to variant rs3816877 [ dbSNP | Ensembl ].
VAR_051580

Experimental info

Sequence conflict1011T → S in BAA07476. Ref.1
Sequence conflict1371A → V in BAA07476. Ref.1
Sequence conflict1681K → R in BAA07476. Ref.1
Sequence conflict2001A → P in BAA07476. Ref.1
Sequence conflict4031A → V in AAF37321. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P13798 [UniParc].

Last modified November 7, 2003. Version 4.
Checksum: A2C370516324D851

FASTA73281,225
        10         20         30         40         50         60 
MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GQYRTVHTEW TQRDLERMEN 

        70         80         90        100        110        120 
IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GTGPGEEKQF 

       130        140        150        160        170        180 
LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK 

       190        200        210        220        230        240 
ALDVSASDDE IARLKKPDQA IKGDQFVFYE DWGENMVSKS IPVLCVLDVE SGNISVLEGV 

       250        260        270        280        290        300 
PENVSPGQAF WAPGDAGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLIGG KCELLSDDSL 

       310        320        330        340        350        360 
AVSSPRLSPD QCRIVYLQYP SLIPHHQCSQ LCLYDWYTKV TSVVVDVVPR QLGENFSGIY 

       370        380        390        400        410        420 
CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQVGTVTS LTAGGSGGSW KLLTIDQDLM 

       430        440        450        460        470        480 
VAQFSTPSLP PTLKVGFLPS AGKEQSVLWV SLEEAEPIPD IHWGIRVLQP PPEQENVQYA 

       490        500        510        520        530        540 
GLDFEAILLQ PGSPPDKTQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS 

       550        560        570        580        590        600 
TGFGQDSILS LPGNVGHQDV KDVQFAVEQV LQEEHFDASH VALMGGSHGG FISCHLIGQY 

       610        620        630        640        650        660 
PETYRACVAR NPVINIASML GSTDIPDWCV VEAGFPFSSD CLPDLSVWAE MLDKSPIRYI 

       670        680        690        700        710        720 
PQVKTPLLLM LGQEDRRVPF KQGMEYYRAL KTRNVPVRLL LYPKSTHALS EVEVESDSFM 

       730 
NAVLWLRTHL GS 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC4655.
RefSeqNP_001631.3. NM_001640.3.
UniGeneHs.517969.

3D structure databases

ProteinModelPortalP13798.
SMRP13798. Positions 375-729.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106824. 32 interactions.
IntActP13798. 3 interactions.
MINTMINT-5004051.
STRING9606.ENSP00000296456.

Chemistry

ChEMBLCHEMBL1741174.

Protein family/group databases

MEROPSS09.004.

PTM databases

PhosphoSiteP13798.

Polymorphism databases

DMDM38258902.

Proteomic databases

PaxDbP13798.
PeptideAtlasP13798.
PRIDEP13798.

Protocols and materials databases

DNASU327.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296456; ENSP00000296456; ENSG00000164062.
GeneID327.
KEGGhsa:327.
UCSCuc003cxf.3. human.

Organism-specific databases

CTD327.
GeneCardsGC03P049711.
HGNCHGNC:586. APEH.
HPAHPA029700.
HPA029701.
HPA029702.
HPA029703.
MIM102645. gene.
neXtProtNX_P13798.
PharmGKBPA24878.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1506.
HOGENOMHOG000007443.
HOVERGENHBG000869.
InParanoidP13798.
KOK01303.
OrthoDBEOG776SPB.
PhylomeDBP13798.
TreeFamTF312937.

Gene expression databases

ArrayExpressP13798.
BgeeP13798.
CleanExHS_APEH.
GenevestigatorP13798.

Family and domain databases

Gene3D2.120.10.30. 2 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
[Graphical view]
PfamPF00326. Peptidase_S9. 1 hit.
[Graphical view]
PROSITEPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPEH. human.
GeneWikiAPEH_(gene).
GenomeRNAi327.
NextBio1343.
PROP13798.
SOURCESearch...

Entry information

Entry nameACPH_HUMAN
AccessionPrimary (citable) accession number: P13798
Secondary accession number(s): Q9BQ33, Q9P0Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 7, 2003
Last modified: April 16, 2014
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM