METAP2 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0016485Biological processprotein processing
GO_0031365Biological processN-terminal protein amino acid modification
GO_0018206Biological processpeptidyl-methionine modification
GO_0005829Cellular componentcytosol
GO_0005886Cellular componentplasma membrane
GO_0005737Cellular componentcytoplasm
GO_0004239Molecular functioninitiator methionyl aminopeptidase activity
GO_0008235Molecular functionmetalloexopeptidase activity
GO_0005515Molecular functionprotein binding
GO_0070006Molecular functionmetalloaminopeptidase activity
GO_0046872Molecular functionmetal ion binding
GO_0004177Molecular functionaminopeptidase activity
GO_0003723Molecular functionRNA binding

IV. Literature review

[source]
Gene nameMETAP2
Protein nameMethionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Initiation factor 2-associated 67 kDa glycoprotein) (p67) (p67eIF2) (Peptidase M)
Methionyl aminopeptidase 2
Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Initiation factor 2-associated 67 kDa glycoprotein) (Peptidase M) (p67) (p67eIF2)
Alternative protein METAP2
SynonymshCG_2015111
MNPEP
P67EIF2
DescriptionFUNCTION: 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.; FUNCTION: Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.

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). .; FUNCTION: Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis. .

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). .; FUNCTION: Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis. .

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). .; FUNCTION: Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis. .

AccessionsL0R5B9
ENST00000549502.5
ENST00000546753.5 [P50579-3]
ENST00000551840.5
F8VRR3
ENST00000535095.5
F8VY03
P50579
ENST00000323666.10 [P50579-1]
A0A140VJE3
ENST00000549808.1
F8VSC4
ENST00000553151.5
G3V1U3
ENST00000550777.5
F8VQZ7
F8VZX9
ENST00000261220.13 [P50579-2]