Protein Information

General Information
MoonProt ID511
First appeared in release3.0
Name(s)Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 Gene:AIMP1 Synonyms:EMAP2, SCYE1 Recommended name: Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 Alternative name(s): Multisynthase complex auxiliary component p43 Cleaved into the following chain: Endothelial monocyte-activating polypeptide 2 Short name: EMAP-2 Alternative name(s): Endothelial monocyte-activating polypeptide II Short name: EMAP-II Small inducible cytokine subfamily E member 1
UniProt IDQ12904 (AIMP1_HUMAN)
GO termsGO:0005829 cytosol GO:0017101 aminoacyl-tRNA synthetase multienzyme complex GO:0005615 extracellular space GO:0001525 angiogenesis GO:0006412 translation GO:0005125 cytokine activity GO:0000049 tRNA binding GO:0005794 Golgi apparatus GO:0005576 extracellular region GO:0005737 cytoplasm GO:0005634 nucleus GO:0006915 apoptotic process GO:0006954 inflammatory response GO:0003723 RNA binding GO:0005783 endoplasmic reticulum GO:0005515 protein binding GO:0051020 GTPase binding GO:0070094 positive regulation of glucagon secretion GO:0016020 membrane
Organisms for which functions have been demonstratedHomo sapiens (Human)
Sequence length312 amino acids
FASTA sequence>sp|Q12904|AIMP1_HUMAN Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 OS=Homo sapiens OX=9606 GN=AIMP1 PE=1 SV=2 MANNDAVLKRLEQKGAEADQIIEYLKQQVSLLKEKAILQATLREEKKLRVENAKLKKEIEELKQELIQAEIQNGVKQIPFPSGTPLHANSMVSENVIQSTAVTTVSSGTKEQIKGGTGDEKKAKEKIEKKGEKKEKKQQSIAGSADSKPIDVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCASSPEKIEILAPPNGSVPGDRITFDAFPGEPDKELNPKKKIWEQIQPDLHTNDECVATYKGVPFEVKGKGVCRAQTMSNSGIK
Structure Information
PDB ID1E7Z 1EUJ 1FL0 4R3Z
Quaternary structureNA
SCOP1 domain. class 1000001 All beta proteins fold 2000100 OB-fold superfamily 3000135 Nucleic acid-binding proteins family 4001906 Myf domain domain 8029555 1FL0 A:150-312 Aminoacyl tRNA synthase complex-interacting multifunctional protein 1. Species Homo sapiens.
CATH1 Matching CATH Superfamily. Superfamily: 2.40.50.140 Nucleic acid-binding proteins. 1 Matching CATH Domain. Domain: PDB code 1e7z, chain A, domain 00 Superfamily: 2.40.50.140.
TM Helix Predictionno TM helices
DisProt Annotation
Predicted Disorder RegionsUse FASTA sequence on the MFDp2 webserver. spQ12904AIMP1_HUMAN_Amin is 312 residues long, with 109 residues (34.94 %) predicted as disordered. The protein has 3 short (< 30 residues) disorder segments and 1 long (>= 30 residues) disorder segment. Segment 1 - Short (< 30 residues) disordered segment Segment is located between positions 1 and 9 in the sequence. The segment is 9 residues long (2.88 % of the total sequence length). Segment 2 - Long (>= 30 residues) disordered segment Segment is located between positions 82 and 152 in the sequence. The segment is 71 residues long (22.76 % of the total sequence length). Segment 3 - Short (< 30 residues) disordered segment Segment is located between positions 252 and 273 in the sequence. The segment is 22 residues long (7.05 % of the total sequence length). Segment 4 - Short (< 30 residues) disordered segment Segment is located between positions 306 and 312 in the sequence. The segment is 7 residues long (2.24 % of the total sequence length).
Connections to Disease
OMIM ID603605
Function 1
Function descriptiona proinflammatory cytokine.
References for functionShalak V, Kaminska M, Mitnacht-Kraus R, Vandenabeele P, Clauss M, Mirande M. The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component. J Biol Chem. 2001 Jun 29;276(26):23769-76. doi: 10.1074/jbc.M100489200. Epub 2001 Apr 16. PMID: 11306575. Barnett G, Jakobsen AM, Tas M, Rice K, Carmichael J, Murray JC. Prostate adenocarcinoma cells release the novel proinflammatory polypeptide EMAP-II in response to stress. Cancer Res. 2000 Jun 1;60(11):2850-7. PMID: 10850427.
E.C. number
Location of functional site(s)
Cellular location of functionsecreted
Comments
Function 2
Function descriptionNon-catalytic component of tRNA multisynthetase complex in protein translation. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase.
References for functionPark SG, Jung KH, Lee JS, Jo YJ, Motegi H, Kim S, Shiba K. Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase. J Biol Chem. 1999 Jun 11;274(24):16673-6. doi: 10.1074/jbc.274.24.16673. PMID: 10358004. Kaminska M, Havrylenko S, Decottignies P, Le Maréchal P, Negrutskii B, Mirande M. Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the Cytoplasm of Human Cells. J Biol Chem. 2009 May 15;284(20):13746-54. doi: 10.1074/jbc.M900480200. Epub 2009 Mar 16. PMID: 19289464; PMCID: PMC2679476.
E.C. number
Location of functional site(s)
Cellular location of functioncytoplasm
Comments