CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019793
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mitochondrial intermediate peptidase 
Protein Synonyms/Alias
 MIP 
Gene Name
 MIPEP 
Gene Synonyms/Alias
 MIP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
126ADLADFVKIAHPEPAacetylation[1]
126ADLADFVKIAHPEPAubiquitination[2]
601NSTTDILKETQEKFYubiquitination[3]
Reference
 [1] 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]
 [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] 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] 
Functional Description
 Cleaves proteins, imported into the mitochondrion, to their mature size. 
Sequence Annotation
 ACT_SITE 496 496 By similarity.
 METAL 495 495 Zinc; catalytic (By similarity).
 METAL 499 499 Zinc; catalytic (By similarity).
 METAL 502 502 Zinc; catalytic (By similarity).
 MOD_RES 126 126 N6-acetyllysine.  
Keyword
 Acetylation; Calcium; Cobalt; Complete proteome; Hydrolase; Iron; Magnesium; Manganese; Metal-binding; Metalloprotease; Mitochondrion; Polymorphism; Protease; Reference proteome; Transit peptide; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 713 AA 
Protein Sequence
MLCVGRLGGL GARAAALPPR RAGRGSLEAG IRARRVSTSW SPVGAAFNVK PQGSRLDLFG 60
ERRGLFGVPE LSAPEGFHIA QEKALRKTEL LVDRACSTPP GPQTVLIFDE LSDSLCRVAD 120
LADFVKIAHP EPAFREAAEE ACRSIGTMVE KLNTNVDLYQ SLQKLLADKK LVDSLDPETR 180
RVAELFMFDF EISGIHLDKE KRKRAVDLNV KILDLSSTFL MGTNFPNKIE KHLLPEHIRR 240
NFTSAGDHII IDGLHAESPD DLVREAAYKI FLYPNAGQLK CLEELLSSRD LLAKLVGYST 300
FSHRALQGTI AKNPETVMQF LEKLSDKLSE RTLKDFEMIR GMKMKLNPQN SEVMPWDPPY 360
YSGVIRAERY NIEPSLYCPF FSLGACMEGL NILLNRLLGI SLYAEQPAKG EVWSEDVRKL 420
AVVHESEGLL GYIYCDFFQR ADKPHQDCHF TIRGGRLKED GDYQLPVVVL MLNLPRSSRS 480
SPTLLTPSMM ENLFHEMGHA MHSMLGRTRY QHVTGTRCPT DFAEVPSILM EYFANDYRVV 540
NQFARHYQTG QPLPKNMVSR LCESKKVCAA ADMQLQVFYA TLDQIYHGKH PLRNSTTDIL 600
KETQEKFYGL PYVPNTAWQL RFSHLVGYGA RYYSYLMSRA VASMVWKECF LQDPFNRAAG 660
ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD LDLDFETFLM DSE 713 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; TAS:ProtInc.
 GO:0006627; P:protein processing involved in protein targeting to mitochondrion; TAS:ProtInc.
 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