CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017801
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acylamino-acid-releasing enzyme 
Protein Synonyms/Alias
 AARE; Acyl-peptide hydrolase; APH; Acylaminoacyl-peptidase 
Gene Name
 Apeh 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
126QFLEVWEKNRKLKSFubiquitination[1]
131WEKNRKLKSFNLSALubiquitination[1]
180AESFFQTKALDVSASubiquitination[1]
434PNLPPSLKVGFLPPAubiquitination[1]
658MLDKSPIKYIPQVKTubiquitination[1]
664IKYIPQVKTPVLLMLubiquitination[1]
681EDRRVPFKQGLEYYHubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 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 (By similarity). 
Sequence Annotation
 ACT_SITE 587 587 Charge relay system (By similarity).
 ACT_SITE 675 675 Charge relay system (By similarity).
 ACT_SITE 707 707 Charge relay system (By similarity).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 185 185 Phosphoserine (By similarity).
 MOD_RES 187 187 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 732 AA 
Protein Sequence
MERQVLLSEP QEAAALYRGL SRQPSLSAAC LGPEVTTQYG GLYRTVHTEW TQRDLDRMEN 60
IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GAVSGEEKQF 120
LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK 180
ALDVSASDEE MARPKKPDQA IKGDQFVFYE DWGETMVSKS IPVLCVLDIE SGNISVLEGV 240
PENVSPGQAF WAPGDTGVVF VGWWHEPFRL GIRYCTNRRS ALYYVDLSGG KCELLSDESL 300
AVCSPRLSPD QCRVVYLQYP SLAPHHQCSQ LFLYDWYTKV TSLVVDIVPR QLGESFSGIY 360
CSLLPLGCWS ADSQRVVFDS VQRSRQDLFA VDTQTGSVTS LTAGGSAGSW KLLTIDRDLM 420
VAQFSTPNLP PSLKVGFLPP AGKEQSVSWV SLEEAEPIPD IHWGIRVLHP PPDQENVQYA 480
DLDFEAILLQ PSNSPDKSQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS 540
TGFGQDSILS LPGNVGHQDV KDVQFAVQQV LQEEHFDARR VALMGGSHGG FLSCHLIGQY 600
PETYSACIAR NPVINIVSMM GTTDIPDWCM VETGFPYSND YLPDLNVLEE MLDKSPIKYI 660
PQVKTPVLLM LGQEDRRVPF KQGLEYYHAL KARNVPVRLL LYPKSTHALS EVEVESDSFM 720
NTVLWLHTHL GS 732 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0031965; C:nuclear membrane; IEA:Compara.
 GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:InterPro. 
Interpro
 IPR002471; Pept_S9_AS.
 IPR001375; Peptidase_S9.
 IPR004106; Peptidase_S9A_B_C_N.
 IPR015943; WD40/YVTN_repeat-like_dom. 
Pfam
 PF00326; Peptidase_S9 
SMART
  
PROSITE
 PS00708; PRO_ENDOPEP_SER 
PRINTS