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Acylamino-acid-releasing enzyme (AARE) (EC 3.4.19.1) (Acyl-peptide hydrolase) (APH) (Acylaminoacyl-peptidase) (Oxidized protein hydrolase) (OPH)

 ACPH_HUMAN              Reviewed;         732 AA.
P13798; Q9BQ33; Q9P0Y2;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
07-NOV-2003, sequence version 4.
08-MAY-2019, entry version 185.
RecName: Full=Acylamino-acid-releasing enzyme;
Short=AARE;
EC=3.4.19.1;
AltName: Full=Acyl-peptide hydrolase;
Short=APH;
AltName: Full=Acylaminoacyl-peptidase;
AltName: Full=Oxidized protein hydrolase;
Short=OPH;
Name=APEH; Synonyms=D3F15S2, D3S48E, DNF15S2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8724851; DOI=10.1093/dnares/3.1.31;
Mitta M., Ohnogi H., Mizutani S., Sakiyama F., Kato I., Tsunasawa S.;
"The nucleotide sequence of human acylamino acid-releasing enzyme.";
DNA Res. 3:31-35(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=10719179; DOI=10.1016/S0167-4838(00)00004-2;
Fujino T., Watanabe K., Beppu M., Kikugawa K., Yasuda H.;
"Identification of oxidized protein hydrolase of human erythrocytes as
acylpeptide hydrolase.";
Biochim. Biophys. Acta 1478:102-112(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PRELIMINARY NUCLEOTIDE SEQUENCE OF 102-732.
PubMed=2565880; DOI=10.1016/0888-7543(89)90342-X;
Naylor S.L., Marshall A., Hensel C., Martinez P.F., Holley B.,
Sakaguchi A.Y.;
"The DNF15S2 locus at 3p21 is transcribed in normal lung and small
cell lung cancer.";
Genomics 4:355-361(1989).
[5]
PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND ACETYLATION AT MET-1.
PubMed=10395453; DOI=10.1023/A:1021047730831;
Scaloni A., Ingallinella P., Andolfo A., Jones W., Marino G.,
Manning J.M.;
"Structural investigations on human erythrocyte acylpeptide hydrolase
by mass spectrometric procedures.";
J. Protein Chem. 18:349-360(1999).
[6]
FUNCTION.
PubMed=1861871;
Erlandsson R., Boldog F., Persson B., Zabarovsky E.R., Allikmets R.L.,
Sumegi J., Klein G., Joernvall H.;
"The gene from the short arm of chromosome 3, at D3F15S2, frequently
deleted in renal cell carcinoma, encodes acylpeptide hydrolase.";
Oncogene 6:1293-1295(1991).
[7]
FUNCTION.
PubMed=2006156; DOI=10.1073/pnas.88.6.2194;
Jones W.M., Scaloni A., Bossa F., Popowicz A.M., Schneewind O.,
Manning J.M.;
"Genetic relationship between acylpeptide hydrolase and acylase, two
hydrolytic enzymes with similar binding but different catalytic
specificities.";
Proc. Natl. Acad. Sci. U.S.A. 88:2194-2198(1991).
[8]
ACTIVE SITES SER-587 AND HIS-707.
PubMed=1740429;
Scaloni A., Jones W.M., Barra D., Pospischil M., Sassa S.,
Popowicz A., Manning L.R., Schneewind O., Manning J.M.;
"Acylpeptide hydrolase: inhibitors and some active site residues of
the human enzyme.";
J. Biol. Chem. 267:3811-3818(1992).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=8411161; DOI=10.1006/jmbi.1993.1531;
Feese M., Scaloni A., Jones W.M., Mannig J.M., Remington S.J.;
"Crystallization and preliminary X-ray studies of human erythrocyte
acylpeptide hydrolase.";
J. Mol. Biol. 233:546-549(1993).
-!- 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.
{ECO:0000269|PubMed:1861871, ECO:0000269|PubMed:2006156}.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the
N-terminus of a polypeptide.; EC=3.4.19.1;
-!- SUBUNIT: Homotetramer.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-723792, EBI-723792;
P53990:IST1; NbExp=4; IntAct=EBI-723792, EBI-945994;
O00214:LGALS8; NbExp=3; IntAct=EBI-723792, EBI-740058;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MASS SPECTROMETRY: Mass=81269.9; Mass_error=8.7;
Method=Electrospray; Range=1-732;
Evidence={ECO:0000269|PubMed:10395453};
-!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35769.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; D38441; BAA07476.1; -; mRNA.
EMBL; AF141383; AAF37321.1; -; mRNA.
EMBL; BC000362; AAH00362.1; -; mRNA.
EMBL; BC001499; AAH01499.1; -; mRNA.
EMBL; BC001826; AAH01826.1; -; mRNA.
EMBL; J03068; AAA35769.1; ALT_FRAME; mRNA.
CCDS; CCDS2801.1; -.
PIR; JC4655; JC4655.
RefSeq; NP_001631.3; NM_001640.3.
RefSeq; XP_011531962.1; XM_011533660.2.
BioGrid; 106824; 42.
IntAct; P13798; 5.
STRING; 9606.ENSP00000296456; -.
ChEMBL; CHEMBL1741174; -.
GuidetoPHARMACOLOGY; 2328; -.
ESTHER; human-APEH; ACPH_Peptidase_S9.
MEROPS; S09.004; -.
iPTMnet; P13798; -.
PhosphoSitePlus; P13798; -.
SwissPalm; P13798; -.
BioMuta; APEH; -.
DMDM; 38258902; -.
EPD; P13798; -.
jPOST; P13798; -.
MaxQB; P13798; -.
PaxDb; P13798; -.
PeptideAtlas; P13798; -.
PRIDE; P13798; -.
ProteomicsDB; 52988; -.
DNASU; 327; -.
Ensembl; ENST00000296456; ENSP00000296456; ENSG00000164062.
GeneID; 327; -.
KEGG; hsa:327; -.
UCSC; uc003cxf.4; human.
CTD; 327; -.
DisGeNET; 327; -.
GeneCards; APEH; -.
HGNC; HGNC:586; APEH.
HPA; HPA029700; -.
HPA; HPA029701; -.
HPA; HPA029702; -.
HPA; HPA029703; -.
MIM; 102645; gene.
neXtProt; NX_P13798; -.
OpenTargets; ENSG00000164062; -.
PharmGKB; PA24878; -.
eggNOG; KOG2100; Eukaryota.
eggNOG; COG1506; LUCA.
GeneTree; ENSGT00390000013172; -.
HOGENOM; HOG000007443; -.
InParanoid; P13798; -.
KO; K01303; -.
OrthoDB; 265965at2759; -.
PhylomeDB; P13798; -.
TreeFam; TF312937; -.
BioCyc; MetaCyc:HS08997-MONOMER; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
ChiTaRS; APEH; human.
GeneWiki; APEH_(gene); -.
GenomeRNAi; 327; -.
PRO; PR:P13798; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000164062; Expressed in 211 organ(s), highest expression level in mucosa of transverse colon.
ExpressionAtlas; P13798; baseline and differential.
Genevisible; P13798; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008242; F:omega peptidase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0050435; P:amyloid-beta metabolic process; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0006415; P:translational termination; TAS:Reactome.
Gene3D; 2.120.10.30; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002471; Pept_S9_AS.
InterPro; IPR001375; Peptidase_S9.
Pfam; PF00326; Peptidase_S9; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Phosphoprotein; Polymorphism; Reference proteome.
C