CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-033420
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Acylamino-acid-releasing enzyme 
Protein Synonyms/Alias
  
Gene Name
 APEH 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
103ESPSGTMKAVLRKAGubiquitination[1, 2]
108TMKAVLRKAGGTGPGubiquitination[1, 3]
118GTGPGEEKQFLEVWEubiquitination[1, 2, 3]
126QFLEVWEKNRKLKSFubiquitination[1]
129EVWEKNRKLKSFNLSubiquitination[1]
131WEKNRKLKSFNLSALubiquitination[1, 2, 4, 5, 6]
180AESFFQTKALDVSASubiquitination[1, 2, 3, 5, 7, 8]
195DDEIARLKKPDQAIKubiquitination[1, 2, 3, 5]
196DEIARLKKPDQAIKGubiquitination[1]
202KKPDQAIKGDQFVFYubiquitination[5]
291YVDLIGGKCELLSDDubiquitination[2, 5]
669IRYIPQVKTPLLLMLubiquitination[1, 3, 5, 7, 8]
686EDRRVPFKQGMEYYRubiquitination[1, 2, 3, 4, 5, 6, 8, 9]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 737 AA 
Protein Sequence
MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GQYRTVHTEW TQRDLERMEN 60
IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GTGPGEEKQF 120
LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK 180
ALDVSASDDE IARLKKPDQA IKGDQFVFYE DWGENMVSKS IPVLCVLDVE SGNISVLEGV 240
PENVSPGQAF WAPGDAGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLIGG KCELLSDDSL 300
AVSSPRLSPD QCRIVYLQYP SLIPHHQCSQ LCLYDWYTKV TSVVVDVVPR QLGENFSGIY 360
CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQVGTVTS LTAGGSGGSW KLLTIDQDLM 420
VAQFSTPSLP PTLKVGFLPS AGKEQSVLWV SLEEAEPIPD IHWGIRVLQP PPEQENVQYA 480
GLDFEAILLQ PGSPPDKTQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS 540
TGFGQDSILS LPGNVGHQDV KDVQFAVEQV LQEEHFDASH VALMGGSHGG FISCHLIGQY 600
PETYRACVAR NPVINIASML GSTDIPDCSV SCRCVVEAGF PFSSDCLPDL SVWAEMLDKS 660
PIRYIPQVKT PLLLMLGQED RRVPFKQGME YYRALKTRNV PVRLLLYPKS THALSEVEVE 720
SDSFMNAVLW LRTHLGS 737 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:InterPro. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR002471; Pept_S9_AS.
 IPR001375; Peptidase_S9.
 IPR004106; Peptidase_S9A_B_C_N. 
Pfam
 PF00326; Peptidase_S9 
SMART
  
PROSITE
 PS00708; PRO_ENDOPEP_SER 
PRINTS