CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000167
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methionine aminopeptidase 2 
Protein Synonyms/Alias
 MAP 2; MetAP 2; Initiation factor 2-associated 67 kDa glycoprotein; p67; p67eIF2; Peptidase M 
Gene Name
 Metap2 
Gene Synonyms/Alias
 Mnpep; P67eif2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
427LDRLGESKYLMALKNubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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) (By similarity). 
Sequence Annotation
 METAL 251 251 Divalent metal cation 1 (By similarity).
 METAL 262 262 Divalent metal cation 1 (By similarity).
 METAL 262 262 Divalent metal cation 2; catalytic (By
 METAL 331 331 Divalent metal cation 2; catalytic; via
 METAL 364 364 Divalent metal cation 2; catalytic (By
 METAL 459 459 Divalent metal cation 1 (By similarity).
 METAL 459 459 Divalent metal cation 2; catalytic (By
 BINDING 231 231 Substrate (By similarity).
 BINDING 339 339 Substrate (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 60 60 Phosphoserine; alternate (By similarity).
 CARBOHYD 60 60 O-linked (GlcNAc); alternate (By  
Keyword
 Acetylation; Aminopeptidase; Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding; Phosphoprotein; Protease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 478 AA 
Protein Sequence
MAGVEQAASF GGHLNGDLDP DDREEGTSST AEEAAKKKRR KKKKGKGAVS AVQQELDKES 60
GALVDEVAKQ LESQALEEKE RDDDDEDGDG DADGATGKKK KKKKKKRGPK VQTDPPSVPI 120
CDLYPNGVFP KGQECEYPPT QDGRTAAWRT TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR 180
KYVMSWIKPG MTMIEICEKL EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT 240
VLQYDDICKI DFGTHISGRI IDCAFTVTFN PKYDILLTAV KDATNTGIKC AGIDVRLCDV 300
GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGPYRIHA GKTVPIVKGG EATRMEEGEV 360
YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK HLLNVINENF GTLAFCRRWL 420
DRLGESKYLM ALKNLCDLGI VDPYPPLCDI KGSYTAQFEH TILLRPTCKE VVSRGDDY 478 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:HGNC.
 GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008235; F:metalloexopeptidase activity; ISS:UniProtKB.
 GO:0031365; P:N-terminal protein amino acid modification; ISS:HGNC.
 GO:0018206; P:peptidyl-methionine modification; ISS:HGNC.
 GO:0016485; P:protein processing; ISS:HGNC.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR001714; Pept_M24_MAP.
 IPR000994; Pept_M24_structural-domain.
 IPR002468; Pept_M24A_MAP2.
 IPR018349; Pept_M24A_MAP2_BS.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00557; Peptidase_M24 
SMART
  
PROSITE
 PS01202; MAP_2 
PRINTS
 PR00599; MAPEPTIDASE.