CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008316
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
58AGEQEPDKESGASVDubiquitination[1]
79ERSALEDKERDEDDEubiquitination[1]
98DGDGATGKKKKKKKKubiquitination[1, 2, 3]
209DCSRKLIKENGLNAGubiquitination[4]
272FTVTFNPKYDTLLKAubiquitination[4]
278PKYDTLLKAVKDATNubiquitination[4]
281DTLLKAVKDATNTGIubiquitination[1, 4]
289DATNTGIKCAGIDVRubiquitination[2, 4]
323DGKTYQVKPIRNLNGubiquitination[4]
342QYRIHAGKTVPIVKGubiquitination[4]
348GKTVPIVKGGEATRMubiquitination[4]
427LDRLGESKYLMALKNacetylation[5]
427LDRLGESKYLMALKNubiquitination[4, 6, 7, 8]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] 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] 
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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo. 
Sequence Annotation
 METAL 251 251 Divalent metal cation 1.
 METAL 262 262 Divalent metal cation 1.
 METAL 262 262 Divalent metal cation 2; catalytic.
 METAL 331 331 Divalent metal cation 2; catalytic; via
 METAL 364 364 Divalent metal cation 2; catalytic.
 METAL 459 459 Divalent metal cation 1.
 METAL 459 459 Divalent metal cation 2; catalytic.
 BINDING 231 231 Substrate.
 BINDING 339 339 Substrate.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 45 45 Phosphoserine.
 MOD_RES 60 60 Phosphoserine; alternate.
 MOD_RES 63 63 Phosphoserine; alternate.
 MOD_RES 74 74 Phosphoserine.
 CARBOHYD 60 60 O-linked (GlcNAc); alternate (By
 CARBOHYD 63 63 O-linked (GlcNAc); alternate (By  
Keyword
 3D-structure; 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
MAGVEEVAAS GSHLNGDLDP DDREEGAAST AEEAAKKKRR KKKKSKGPSA AGEQEPDKES 60
GASVDEVARQ LERSALEDKE RDEDDEDGDG DGDGATGKKK KKKKKKRGPK VQTDPPSVPI 120
CDLYPNGVFP KGQECEYPPT QDGRTAAWRT TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR 180
KYVMSWIKPG MTMIEICEKL EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT 240
VLQYDDICKI DFGTHISGRI IDCAFTVTFN PKYDTLLKAV KDATNTGIKC AGIDVRLCDV 300
GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGQYRIHA GKTVPIVKGG EATRMEEGEV 360
YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK HLLNVINENF GTLAFCRRWL 420
DRLGESKYLM ALKNLCDLGI VDPYPPLCDI KGSYTAQFEH TILLRPTCKE VVSRGDDY 478 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HGNC.
 GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008235; F:metalloexopeptidase activity; IDA:UniProtKB.
 GO:0031365; P:N-terminal protein amino acid modification; IDA:HGNC.
 GO:0018206; P:peptidyl-methionine modification; IDA:HGNC.
 GO:0016485; P:protein processing; IDA: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.