CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010873
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
 MAP1 
Gene Synonyms/Alias
 YLR244C; L9672.12 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
36RETSSQMKCPVCLKQubiquitination[1]
81GAYDPFPKFKYSGKVacetylation[2]
131LNNIPIYKKDQIKKIacetylation[2]
278ELGDHIEKHATENKCacetylation[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
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). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val. 
Sequence Annotation
 REGION 22 66 Zinc finger-like; important for proper
 METAL 219 219 Divalent metal cation 1 (By similarity).
 METAL 230 230 Divalent metal cation 1 (By similarity).
 METAL 230 230 Divalent metal cation 2; catalytic (By
 METAL 294 294 Divalent metal cation 2; catalytic; via
 METAL 327 327 Divalent metal cation 2; catalytic (By
 METAL 358 358 Divalent metal cation 1 (By similarity).
 METAL 358 358 Divalent metal cation 2; catalytic (By
 BINDING 202 202 Substrate (By similarity).
 BINDING 301 301 Substrate (By similarity).  
Keyword
 Aminopeptidase; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 387 AA 
Protein Sequence
MSTATTTVTT SDQASHPTKI YCSGLQCGRE TSSQMKCPVC LKQGIVSIFC DTSCYENNYK 60
AHKALHNAKD GLEGAYDPFP KFKYSGKVKA SYPLTPRRYV PEDIPKPDWA ANGLPVSEQR 120
NDRLNNIPIY KKDQIKKIRK ACMLGREVLD IAAAHVRPGI TTDELDEIVH NETIKRGAYP 180
SPLNYYNFPK SLCTSVNEVI CHGVPDKTVL KEGDIVNLDV SLYYQGYHAD LNETYYVGEN 240
ISKEALNTTE TSRECLKLAI KMCKPGTTFQ ELGDHIEKHA TENKCSVVRT YCGHGVGEFF 300
HCSPNIPHYA KNRTPGVMKP GMVFTIEPMI NEGTWKDMTW PDDWTSTTQD GKLSAQFEHT 360
LLVTEHGVEI LTARNKKSPG GPRQRIK 387 
Gene Ontology
 GO:0022626; C:cytosolic ribosome; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0070006; F:metalloaminopeptidase activity; IDA:SGD.
 GO:0003729; F:mRNA binding; IDA:SGD.
 GO:0010629; P:negative regulation of gene expression; IMP:SGD.
 GO:0035551; P:protein initiator methionine removal involved in protein maturation; IMP:SGD.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
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.