CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020381
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Neurolysin, mitochondrial 
Protein Synonyms/Alias
 Angiotensin-binding protein; Microsomal endopeptidase; MEP; Mitochondrial oligopeptidase M; Neurotensin endopeptidase 
Gene Name
 NLN 
Gene Synonyms/Alias
 AGTBP; KIAA1226 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
58DLSPEQIKTRTEELIubiquitination[1, 2]
116PQHVSSDKEVRAASTubiquitination[2]
157QETCDLGKIKPEARRubiquitination[2]
254HYFPVMKKCCIPETRubiquitination[2]
327DDLSQKLKPLGEAERubiquitination[2]
562IADDLLEKLVASRLVubiquitination[1]
664MNPEVGMKYRNLILKacetylation[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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
 Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A (By similarity). 
Sequence Annotation
 ACT_SITE 498 498 By similarity.
 METAL 497 497 Zinc; catalytic (By similarity).
 METAL 501 501 Zinc; catalytic (By similarity).
 METAL 504 504 Zinc; catalytic (By similarity).
 MOD_RES 664 664 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Polymorphism; Protease; Reference proteome; Transit peptide; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 704 AA 
Protein Sequence
MIARCLLAVR SLRRVGGSRI LLRMTLGREV MSPLQAMSSY TVAGRNVLRW DLSPEQIKTR 60
TEELIVQTKQ VYDAVGMLGI EEVTYENCLQ ALADVEVKYI VERTMLDFPQ HVSSDKEVRA 120
ASTEADKRLS RFDIEMSMRG DIFERIVHLQ ETCDLGKIKP EARRYLEKSI KMGKRNGLHL 180
PEQVQNEIKS MKKRMSELCI DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKTDDDKYK 240
ITLKYPHYFP VMKKCCIPET RRRMEMAFNT RCKEENTIIL QQLLPLRTKV AKLLGYSTHA 300
DFVLEMNTAK STSRVTAFLD DLSQKLKPLG EAEREFILNL KKKECKDRGF EYDGKINAWD 360
LYYYMTQTEE LKYSIDQEFL KEYFPIEVVT EGLLNTYQEL LGLSFEQMTD AHVWNKSVTL 420
YTVKDKATGE VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMMAVA ALVVNFSQPV 480
AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD 540
SLRRLSKHYK DGSPIADDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NTSLDAASEY 600
AKYCSEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC FKKEGIMNPE 660
VGMKYRNLIL KPGGSLDGMD MLHNFLKREP NQKAFLMSRG LHAP 704 
Gene Ontology
 GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR024079; MetalloPept_cat_dom.
 IPR024077; Neurolysin/TOP_dom2.
 IPR024080; Neurolysin/TOP_N.
 IPR001567; Pept_M3A_M3B. 
Pfam
 PF01432; Peptidase_M3 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS