CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005728
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytosol aminopeptidase 
Protein Synonyms/Alias
 Leucine aminopeptidase 3; LAP-3; Leucyl aminopeptidase; Peptidase S; Proline aminopeptidase; Prolyl aminopeptidase 
Gene Name
 LAP3 
Gene Synonyms/Alias
 LAPEP; PEPS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
79NISGPPLKAGKTRTFubiquitination[1]
118QENWHEGKENIRAAVubiquitination[1, 2]
188GDQEAWQKGVLFASGubiquitination[1, 3, 4, 5, 6]
221RFAEIIEKNLKSASSacetylation[7]
221RFAEIIEKNLKSASSubiquitination[1, 3, 6]
224EIIEKNLKSASSKTEubiquitination[1]
345MPSGKANKPGDVVRAubiquitination[1]
356VVRAKNGKTIQVDNTubiquitination[1]
455ADVNNIGKYRSAGACubiquitination[1, 4]
469CTAAAFLKEFVTHPKubiquitination[1]
476KEFVTHPKWAHLDIAubiquitination[3, 6]
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] 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]
 [4] 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]
 [5] 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]
 [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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. 
Sequence Annotation
 ACT_SITE 294 294 By similarity.
 ACT_SITE 368 368 By similarity.
 METAL 282 282 Zinc 2 (By similarity).
 METAL 287 287 Zinc 1 (By similarity).
 METAL 287 287 Zinc 2 (By similarity).
 METAL 305 305 Zinc 2 (By similarity).
 METAL 364 364 Zinc 1 (By similarity).
 METAL 366 366 Zinc 1 (By similarity).
 METAL 366 366 Zinc 2 (By similarity).
 MOD_RES 221 221 N6-acetyllysine.
 MOD_RES 238 238 Phosphoserine.  
Keyword
 Acetylation; Alternative initiation; Aminopeptidase; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 519 AA 
Protein Sequence
MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD 60
KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN 120
IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS 180
GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI 240
EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD 300
LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV 360
DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE 420
ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL 480
DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA 519 
Gene Ontology
 GO:0005737; C:cytoplasm; NAS:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005802; C:trans-Golgi network; IEA:Compara.
 GO:0004177; F:aminopeptidase activity; NAS:UniProtKB.
 GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
 GO:0030145; F:manganese ion binding; NAS:UniProtKB.
 GO:0008235; F:metalloexopeptidase activity; NAS:UniProtKB.
 GO:0008270; F:zinc ion binding; NAS:UniProtKB.
 GO:0006508; P:proteolysis; NAS:UniProtKB. 
Interpro
 IPR011356; Leucine_aapep/pepB.
 IPR000819; Peptidase_M17_C.
 IPR023042; Peptidase_M17_leu_NH2_pept.
 IPR008283; Peptidase_M17_N. 
Pfam
 PF00883; Peptidase_M17
 PF02789; Peptidase_M17_N 
SMART
  
PROSITE
 PS00631; CYTOSOL_AP 
PRINTS
 PR00481; LAMNOPPTDASE.