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There are several matches for 'aminopeptidase 2'.
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3216 matches
showing page 1 of 161
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protein
1)
Saccharomyces cerevisiae
AAP1 - Alanine/arginine aminopeptidase; Arginine/alanine amino peptidase; overproduction stimulates glycogen accumulation; AAP1 has a paralog, APE2, that arose from the whole genome duplication.
[a.k.a. YHR047C, EC 3.4.11.-, S000001089,
Aminopeptidase 2
]
2)
Saccharomyces cerevisiae
APE2 -
Aminopeptidase
2
, mitochondrial;
Aminopeptidase
yscII; may have a role in obtaining leucine from dipeptide substrates; APE2 has a paralog, AAP1, that arose from the whole genome duplication; Belongs to the peptidase M1 family.
[a.k.a. YKL157W, YKL158W, AP-II,
Aminopeptidase 2
]
3)
Homo sapiens
ERAP2 - Endoplasmic reticulum
aminopeptidase
2
;
Aminopeptidase
that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys.
[a.k.a. NX_Q6P179, CCDS87316, XM_011543544.2]
4)
Homo sapiens
METAP2 - Methionine
aminopeptidase
2
; 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; Belongs to the peptidase M24A family. Methionine
aminopeptidase
eukaryotic typ [...]
[a.k.a. R-HSA-388396, ENST00000549502, BAC03733.1]
5)
Homo sapiens
XPNPEP2 - Xaa-Pro
aminopeptidase
2
; Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin; Belongs to the peptidase M24B family.
[a.k.a. ENST00000371106.3, U90724, Xaa-Pro aminopeptidase 2]
6)
Homo sapiens
SLC15A2 - Solute carrier family 15 member
2
; Proton-coupled intake of oligopeptides of
2
to 4 amino acids with a preference for dipeptides. Transports the dipeptide-like
aminopeptidase
inhibitor bestatin (By similarity). Can also transport the aminocephalosporin antibiotic cefadroxil (By similarity); Belongs to the PTR2/POT transporter (TC
2
.A.17) family.
[a.k.a. Q16348, ENSP00000295605, ENSG00000163406]
7)
Homo sapiens
JMJD7 - Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7; Bifunctional enzyme that acts both as an endopeptidase and
2
- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its
aminopeptidase
activity. Additionally, may play a role in [...]
[a.k.a. UPI000173A692, HGNC:34397, ENST00000408047.5]
8)
Homo sapiens
KDM8 - Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and
2
- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its
aminopeptidase
activity. Upon DNA damage, cleaves the N-term [...]
[a.k.a. NM_024773.2, ENSP00000455463, ENST00000564961]
9)
Mus musculus
Metap2 - Methionine
aminopeptidase
2
; 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).
[a.k.a. ENSMUSP00000048285, XP_017169521.1, NP_062622.1]
10)
Mus musculus
Xpnpep2 - Xaa-Pro
aminopeptidase
2
; Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin; Belongs to the peptidase M24B family.
[a.k.a. XP_006541495.1, NP_573476, Xpnpep2-204]
11)
Mus musculus
Slc15a2 - Solute carrier family 15 member
2
; Proton-coupled intake of oligopeptides of
2
to 4 amino acids with a preference for dipeptides. Transports the dipeptide-like
aminopeptidase
inhibitor bestatin (By similarity). Can also transport the aminocephalosporin antibiotic cefadroxil (By similarity); Belongs to the PTR2/POT transporter (TC
2
.A.17) family.
[a.k.a. Slc15a2-212, Slc15a2-211, NM_021301]
12)
Mus musculus
Kdm8 - Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and
2
- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its
aminopeptidase
activity. Upon DNA damage, cleaves the N-term [...]
[a.k.a. 77035, NP_084118, AC125187]
13)
Mus musculus
Jmjd7 - Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7; Bifunctional enzyme that acts both as an endopeptidase and
2
- oxoglutarate-dependent monoxygenase (By similarity). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its
aminopeptidase
activity. Additionally, m [...]
[a.k.a. F6SBG7, ENSMUSP00000041220, 433466]
14)
Drosophila melanogaster
S-Lap2 - Sperm-Leucylaminopeptidase
2
;
Aminopeptidase
activity; metalloexopeptidase activity; manganese ion binding. It is involved in the biological process described with: proteolysis.
[a.k.a. FBgn0052351, S-Lap2-PA, NM_168282.2]
15)
Drosophila melanogaster
und - Methionine
aminopeptidase
2
; 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).
[a.k.a. FBgn0283478, und-PA, und-PB]
16)
Caenorhabditis elegans
map-2 - Methionine
aminopeptidase
2
; 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). Required for germ cell proliferation and/or differentiation.
[a.k.a. Y116A8A.9b, Y116A8A.9a.1, Y116A8A.9a.2]
17)
Saccharomyces cerevisiae
LAP2 - Leucine
aminopeptidase
2
; Leucyl
aminopeptidase
yscIV with epoxide hydrolase activity; metalloenzyme containing one zinc atom; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm and nucleus; also known as leukotriene A4 hydrolase.
[a.k.a. YNL045W, 2XQ0, CAA64237.1]
18)
Saccharomyces cerevisiae
MAP2 - Methionine
aminopeptidase
; catalyzes the cotranslational removal of N-terminal methionine from nascent polypeptides; function is partially redundant with that of Map1p; Belongs to the peptidase M24A family. Methionine
aminopeptidase
eukaryotic type
2
subfamily.
[a.k.a. YBL091C, D6VPR3, 852187]
19)
Escherichia coli K12
iap -
Aminopeptidase
in alkaline phosphatase isozyme conversion; This protein, presumably an
aminopeptidase
, mediates the conversion of E.coli alkaline phosphatase isozyme 1, to isozymes
2
and 3 by removing, one by one, the two N-terminal arginine residues.
[a.k.a. AAC75795.1, b2753, EC 3.4.11.-]
20)
Acetobacterium wieringae
ACWI_03940 -
Aminopeptidase
2
.
[a.k.a. OFV72144.1, NZ_VSLA01000024.1, OFV72144,
Aminopeptidase 2
,
aminopeptidase 2
, ...]
3216 matches
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