General Information |
MoonProt ID | 511 |
First appeared in release | 3.0 |
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 ID | Q12904 (AIMP1_HUMAN) |
GO terms | GO: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 demonstrated | Homo sapiens (Human) |
Sequence length | 312 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 ID | 1E7Z
1EUJ
1FL0
4R3Z |
Quaternary structure | NA |
SCOP | 1 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. |
CATH | 1 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 Prediction | no TM helices |
DisProt Annotation | |
Predicted Disorder Regions | Use 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 ID | 603605 |
Function 1 |
Function description | a proinflammatory cytokine. |
References for function | Shalak 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 function | secreted |
Comments | |
Function 2 |
Function description | Non-catalytic component of tRNA multisynthetase complex in protein translation. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. |
References for function | Park 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 function | cytoplasm |
Comments | |