CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008708
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methionine aminopeptidase 1 
Protein Synonyms/Alias
 MAP 1; MetAP 1; Peptidase M 1 
Gene Name
 METAP1 
Gene Synonyms/Alias
 KIAA0094 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
19DGCSSEAKLQCPTCIubiquitination[1]
123SESEQALKGTSQIKLubiquitination[2]
129LKGTSQIKLLSSEDIubiquitination[2, 3]
158DVAAGMIKPGVTTEEubiquitination[1]
278ELGNIIQKHAQANGFubiquitination[1, 2, 3]
311PNVPHYAKNKAVGVMubiquitination[2, 3]
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] 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]
 [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
 Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle. 
Sequence Annotation
 REGION 9 52 Zinc finger-like; important for proper
 METAL 220 220 Divalent metal cation 1.
 METAL 231 231 Divalent metal cation 1.
 METAL 231 231 Divalent metal cation 2; catalytic.
 METAL 294 294 Divalent metal cation 2; catalytic; via
 METAL 327 327 Divalent metal cation 2; catalytic.
 METAL 358 358 Divalent metal cation 1.
 METAL 358 358 Divalent metal cation 2; catalytic.
 BINDING 203 203 Substrate.
 BINDING 301 301 Substrate.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Protease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 386 AA 
Protein Sequence
MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA 60
KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ 120
ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DVAAGMIKPG VTTEEIDHAV HLACIARNCY 180
PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE 240
VDDGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF 300
HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT 360
LLVTDTGCEI LTRRLDSARP HFMSQF 386 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:HGNC.
 GO:0004177; F:aminopeptidase activity; TAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008235; F:metalloexopeptidase activity; TAS:UniProtKB.
 GO:0031365; P:N-terminal protein amino acid modification; TAS:HGNC.
 GO:0018206; P:peptidyl-methionine modification; TAS:HGNC.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0006417; P:regulation of translation; TAS:HGNC. 
Interpro
 IPR001714; Pept_M24_MAP.
 IPR000994; Pept_M24_structural-domain.
 IPR002467; Pept_M24A_MAP1. 
Pfam
 PF00557; Peptidase_M24 
SMART
  
PROSITE
 PS00680; MAP_1 
PRINTS
 PR00599; MAPEPTIDASE.