Search Results

Overview

Uniprot ID	P50579
Protein Name	Methionine aminopeptidase 2
Gene Name	METAP2
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
348	GKTVPIVKGGEATRM
46	RRKKKKSKGPSAAGE

Function

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

Protein Sequence

10 MAGVEEVAAS 20 GSHLNGDLDP 30 DDREEGAAST 40 AEEAAKKKRR 50 KKKKSKGPSA 60 AGEQEPDKES 70 GASVDEVARQ 80 LERSALEDKE 90 RDEDDEDGDG 100 DGDGATGKKK 110 KKKKKKRGPK 120 VQTDPPSVPI 130 CDLYPNGVFP 140 KGQECEYPPT 150 QDGRTAAWRT 160 TSEEKKALDQ 170 ASEEIWNDFR 180 EAAEAHRQVR 190 KYVMSWIKPG 200 MTMIEICEKL 210 EDCSRKLIKE 220 NGLNAGLAFP 230 TGCSLNNCAA 240 HYTPNAGDTT 250 VLQYDDICKI 260 DFGTHISGRI 270 IDCAFTVTFN 280 PKYDTLLKAV 290 KDATNTGIKC 300 AGIDVRLCDV 310 GEAIQEVMES 320 YEVEIDGKTY 330 QVKPIRNLNG 340 HSIGQYRIHA 350 GKTVPIVKGG 360 EATRMEEGEV 370 YAIETFGSTG 380 KGVVHDDMEC 390 SHYMKNFDVG 400 HVPIRLPRTK 410 HLLNVINENF 420 GTLAFCRRWL 430 DRLGESKYLM 440 ALKNLCDLGI 450 VDPYPPLCDI 460 KGSYTAQFEH 470 TILLRPTCKE VVSRGDDY

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Molecular Function	GO:0004177	aminopeptidase activity
Molecular Function	GO:0004239	initiator methionyl aminopeptidase activity
Molecular Function	GO:0046872	metal ion binding
Molecular Function	GO:0070006	metalloaminopeptidase activity
Molecular Function	GO:0008235	metalloexopeptidase activity
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0016485	protein processing
Biological Process	GO:0006446	regulation of translational initiation

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.