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Protein Page:
MetAP2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
MetAP2 Removes the N-terminal methionine from nascent proteins. 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. Interacts strongly with the eIF-2 gamma-subunit EIF2S3. Binds EIF2S1 at low magnesium concentrations. Belongs to the peptidase M24A family. Note: This description may include information from UniProtKB.
Protein type: Protease; EC 3.4.11.18
Cellular Component: cytoplasm; cytosol
Molecular Function: metalloexopeptidase activity; metal ion binding; aminopeptidase activity
Biological Process: rhodopsin mediated signaling; phototransduction, visible light; regulation of rhodopsin mediated signaling; peptidyl-methionine modification; protein processing; N-terminal protein amino acid modification
Reference #:  P50579 (UniProtKB)
Alt. Names/Synonyms: AMPM2; eIF-2-associated p67 homolog; Initiation factor 2-associated 67 kDa glycoprotein; MAP 2; MAP2; MetAP 2; METAP2; Methionine aminopeptidase 2; methionyl aminopeptidase 2; MNPEP; p67; P67EIF2; Peptidase M 2
Gene Symbols: METAP2
Molecular weight: 52,892 Da
Basal Isoelectric point: 5.57  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

MetAP2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 A9 AGVEEVAASGSHLNG
0 2 S29-p DREEGAAsTAEEAAK
0 3 S45-p KRRKKKKsKGPSAAG
0 1 K58-u AGEQEPDkEsGAsVD
0 4 S60-p EQEPDkEsGAsVDEV
0 4 S63-p PDkEsGAsVDEVARQ
0 3 S74-p VARQLERsALEDkER
0 1 K79-u ERsALEDkERDEDDE
0 2 T96-p DGDGDGAtGkkKKKK
0 8 K98-u DGDGAtGkkKKKKKK
0 3 K99-u GDGAtGkkKKKKKKK
0 1 - gap
0 2 K281-u DTLLKAVkDATNTGI
0 2 K289-u DATNTGIkCAGIDVR
0 1 K348 GKTVPIVKGGEATRM
0 1 K427-a LDRLGESkYLMALKN
0 3 K427-u LDRLGESkYLMALKN
  mouse

► Hide Isoforms
 
S9-p AGVEQAAsFGGHLNG
S29 DREEGTSSTAEEAAK
G45 KRRKKKKGKGAVSAV
K58 AVQQELDKESGALVD
S60 QQELDKESGALVDEV
L63 LDKESGALVDEVAKQ
Q74 VAKQLESQALEEKER
K79 ESQALEEKERDDDDE
T96 DGDADGATGKkKKKK
K98 DADGATGKkKKKKKK
K99-u ADGATGKkKKKKKKK
- gap
K281-u DILLTAVkDATNTGI
K289-u DATNTGIkCAGIDVR
K348-u GKTVPIVkGGEATRM
K427 LDRLGESKYLMALKN
K427-u LDRLGESkYLMALKN
  MetAP2 iso2  
S9 AGVEQAASFGGHLNG
S29 DREEGTSSTAEEAAK
G45 KRRKKKKGKGAVSAV
K58 AVQQELDKESGALVD
S60 QQELDKESGALVDEV
L63 LDKESGALVDEVAKQ
Q74 VAKQLESQALEEKER
K79 ESQALEEKERDDDDE
T96 DGDADGATGKKKKKK
K98 DADGATGKKKKKKKK
K99 ADGATGKKKKKKKKK
S110-p KKKKRGHsITEYLYL
K291 DILLTAVKDATNTGI
K299 DATNTGIKCAGIDVR
K358 GKTVPIVKGGEATRM
K437 LDRLGESKYLMALKN
K437 LDRLGESKYLMALKN
  rat

 
S9 AGVEEASSFGGHLNR
S29 DREEGTSSTAEEAAK
G45 KRRKKKKGKGAVSAG
K58 AGQQELDKESGTSVD
S60 QQELDKESGTSVDEV
S63 LDKESGTSVDEVAKQ
Q74 VAKQLERQALEEKEK
K79 ERQALEEKEKDDDDE
A96 DGDGDGAAGKKKKKK
K98 DGDGAAGKKKKKKKK
K99 GDGAAGKKKKKKKKK
- gap
K281 DILLKAVKDATNTGI
K289 DATNTGIKCAGIDVR
K348 GKTVPIVKGGEATRM
K427 LDRLGESKYLMALKN
K427 LDRLGESKYLMALKN
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