Aimp1
entrez
13722
canonical
uniprot
P31230
canonical
ensembl
ENSMUSG00000028029
resolver
ensp
ENSMUSP00000029663
resolver
ensp
ENSMUSP00000142513
resolver
enst
ENSMUST00000029663
resolver
enst
ENSMUST00000198513
resolver
genesymbol
Aimp1
resolver
genesymbol_syn
Emap2
resolver
genesymbol_syn
Scye1
resolver
uniprot
F8WI28
resolver
uniprot
Q3UZG4
resolver
uniprot
Q60659
resolver
uniprot_entry
AIMP1_MOUSE
resolver
uniprot_entry
F8WI28_MOUSE
resolver
uniprot_entry
Q3UZG4_MOUSE
resolver
uniprot_sec
Q60659
resolver
amino_acid_sequence
MATNDAVLKRLEQKGAEADQIIEYLKQQVALLKEKAILQATMREEKKLRVENAKLKKEIEELKQELILAEIHNGVEQVRVRLSTPLQTNCTASESVVQSPSVATTASPATKEQIKAGEEKKVKEKTEKKGEKKEKQQSAAASTDSKPIDASRLDLRIGCIVTAKKHPDADSLYVEEVDVGEAAPRTVVSGLVNHVPLEQMQNRMVVLLCNLKPAKMRGVLSQAMVMCASSPEKVEILAPPNGSVPGDRITFDAFPGEPDKELNPKKKIWEQIQPDLHTNAECVATYKGAPFEVKGKGVCRAQTMANSGIK
uniprot
proteins
function
FUNCTION: Non-catalytic component of the multisynthase complex (PubMed:12060739). Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase (By similarity). Binds tRNA. Possesses inflammatory cytokine activity (PubMed:1400342, PubMed:7545917). Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation (PubMed:18448069). Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels (PubMed:17001013). Promotes dermal fibroblast proliferation and wound repair (PubMed:15681823). Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum (PubMed:17525271). Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelial cell apoptosis at high concentrations (By similarity). Induces maturation of dendritic cells and monocyte cell adhesion (PubMed:18292511). Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7 (By similarity). {ECO:0000250|UniProtKB:Q12904, ECO:0000269|PubMed:12060739, ECO:0000269|PubMed:1400342, ECO:0000269|PubMed:15681823, ECO:0000269|PubMed:17001013, ECO:0000269|PubMed:17525271, ECO:0000269|PubMed:18292511, ECO:0000269|PubMed:18448069, ECO:0000269|PubMed:7545917}.
uniprot
proteins
mass_dalton
33997
uniprot
proteins
post_translational_modification
PTM: Cleaved by caspase-7 in response to apoptosis to produce EMAP-II. {ECO:0000269|PubMed:11306575}.
uniprot
proteins
pubmed
11306575
uniprot
proteins
pubmed
12060739
uniprot
proteins
pubmed
1400342
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15681823
uniprot
proteins
pubmed
17001013
uniprot
proteins
pubmed
17525271
uniprot
proteins
pubmed
18292511
uniprot
proteins
pubmed
18448069
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
7545917
uniprot
proteins
pubmed
7929199
uniprot
proteins
pubmed
9770485
uniprot
proteins
sequence_length
310
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12904}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q12904}. Secreted {ECO:0000269|PubMed:17001013, ECO:0000269|PubMed:9770485}. Endoplasmic reticulum {ECO:0000269|PubMed:17525271}. Golgi apparatus {ECO:0000269|PubMed:17525271}. Note=Enriched in secretory vesicles of pancreatic alpha cells and secreted from the pancreas in response to low glucose levels (PubMed:17001013). Secreted in response to hypoxia (By similarity). Also secreted in response to both apoptotic and necrotic cell death. {ECO:0000250|UniProtKB:Q12904, ECO:0000269|PubMed:17001013}.
uniprot
proteins