Tag | Content |
---|
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 |
---|
427 | LDRLGESKYLMALKN | ubiquitination | [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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |