ID AIMP1_HUMAN Reviewed; 312 AA. AC Q12904; B3KTR2; B4E1S7; Q6FG28; Q96CQ9; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 2. DT 27-MAR-2024, entry version 210. DE RecName: Full=Aminoacyl tRNA synthase complex-interacting multifunctional protein 1; DE AltName: Full=Multisynthase complex auxiliary component p43; DE Contains: DE RecName: Full=Endothelial monocyte-activating polypeptide 2; DE Short=EMAP-2; DE AltName: Full=Endothelial monocyte-activating polypeptide II; DE Short=EMAP-II; DE AltName: Full=Small inducible cytokine subfamily E member 1; GN Name=AIMP1; Synonyms=EMAP2, SCYE1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-79. RX PubMed=7929199; DOI=10.1016/s0021-9258(17)31505-3; RA Kao J., Houck K., Fan Y., Haehnel I., Libutti S.K., Kayton M.L., RA Grikscheit T., Chabot J., Nowygrod R., Greenberg S., Kuang W.J., RA Leung D.W., Hayward J.R., Kisiel W., Heath M., Brett J., Stern D.M.; RT "Characterization of a novel tumor-derived cytokine. Endothelial-monocyte RT activating polypeptide II."; RL J. Biol. Chem. 269:25106-25119(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 1-9, ALTERNATIVE SPLICING, IDENTIFICATION IN THE MSC RP COMPLEX, INTERACTION WITH TARS3, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY (ISOFORMS 1 RP AND 2). RX PubMed=24312579; DOI=10.1371/journal.pone.0081734; RA Kim K., Park S.J., Na S., Kim J.S., Choi H., Kim Y.K., Paek E., Lee C.; RT "Reinvestigation of aminoacyl-tRNA synthetase core complex by affinity RT purification-mass spectrometry reveals TARSL2 as a potential member of the RT complex."; RL PLoS ONE 8:E81734-E81734(2013). RN [6] RP FUNCTION, AND INTERACTION WITH RARS1. RX PubMed=10358004; DOI=10.1074/jbc.274.24.16673; RA Park S.G., Jung K.H., Lee J.S., Jo Y.J., Motegi H., Kim S., Shiba K.; RT "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of RT tRNA synthetase."; RL J. Biol. Chem. 274:16673-16676(1999). RN [7] RP SUBCELLULAR LOCATION, AND CLEAVAGE. RX PubMed=10850427; RA Barnett G., Jakobsen A.-M., Tas M., Rice K., Carmichael J., Murray J.C.; RT "Prostate adenocarcinoma cells release the novel proinflammatory RT polypeptide EMAP-II in response to stress."; RL Cancer Res. 60:2850-2857(2000). RN [8] RP FUNCTION, SUBUNIT, AND CLEAVAGE. RX PubMed=11306575; DOI=10.1074/jbc.m100489200; RA Shalak V., Kaminska M., Mitnacht-Kraus R., Vandenabeele P., Clauss M., RA Mirande M.; RT "The EMAPII cytokine is released from the mammalian multisynthetase complex RT after cleavage of its p43/proEMAPII component."; RL J. Biol. Chem. 276:23769-23776(2001). RN [9] RP FUNCTION. RX PubMed=12237313; DOI=10.1074/jbc.m207934200; RA Park S.G., Kang Y.-S., Ahn Y.H., Lee S.H., Kim K.-R., Kim K.-W., Koh G.Y., RA Ko Y.-G., Kim S.; RT "Dose-dependent biphasic activity of tRNA synthetase-associating factor, RT p43, in angiogenesis."; RL J. Biol. Chem. 277:45243-45248(2002). RN [10] RP FUNCTION. RX PubMed=11818442; RA Park H., Park S.G., Lee J.-W., Kim T., Kim G., Ko Y.-G., Kim S.; RT "Monocyte cell adhesion induced by a human aminoacyl-tRNA synthetase- RT associated factor, p43: identification of the related adhesion molecules RT and signal pathways."; RL J. Leukoc. Biol. 71:223-230(2002). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=14500886; DOI=10.1110/ps.03147903; RA Wolfe C.L., Warrington J.A., Davis S., Green S., Norcum M.T.; RT "Isolation and characterization of human nuclear and cytosolic RT multisynthetase complexes and the intracellular distribution of RT p43/EMAPII."; RL Protein Sci. 12:2282-2290(2003). RN [12] RP REGIONS INVOLVED IN FIBROBLAST PROLIFERATION; ENDOTHELIAL CELL DEATH AND RP ENDOTHELIAL MIGRATION. RX PubMed=16472771; DOI=10.1016/j.bbrc.2006.01.117; RA Han J.M., Park S.G., Lee Y., Kim S.; RT "Structural separation of different extracellular activities in aminoacyl- RT tRNA synthetase-interacting multi-functional protein, p43/AIMP1."; RL Biochem. Biophys. Res. Commun. 342:113-118(2006). RN [13] RP INTERACTION WITH RARS1. RX PubMed=17443684; DOI=10.1002/jcp.21083; RA Bottoni A., Vignali C., Piccin D., Tagliati F., Luchin A., Zatelli M.C., RA Uberti E.C.; RT "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell RT lines."; RL J. Cell. Physiol. 212:293-297(2007). RN [14] RP FUNCTION, AND INTERACTION WITH PSMA7. RX PubMed=19362550; DOI=10.1016/j.yexcr.2009.03.021; RA Tandle A.T., Calvani M., Uranchimeg B., Zahavi D., Melillo G., RA Libutti S.K.; RT "Endothelial monocyte activating polypeptide-II modulates endothelial cell RT responses by degrading hypoxia-inducible factor-1alpha through interaction RT with PSMA7, a component of the proteasome."; RL Exp. Cell Res. 315:1850-1859(2009). RN [15] RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19131329; DOI=10.1074/jbc.m809636200; RA Kaminska M., Havrylenko S., Decottignies P., Gillet S., Le Marechal P., RA Negrutskii B., Mirande M.; RT "Dissection of the structural organization of the aminoacyl-tRNA synthetase RT complex."; RL J. Biol. Chem. 284:6053-6060(2009). RN [16] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=19289464; DOI=10.1074/jbc.m900480200; RA Kaminska M., Havrylenko S., Decottignies P., Le Marechal P., Negrutskii B., RA Mirande M.; RT "Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the RT Cytoplasm of Human Cells."; RL J. Biol. Chem. 284:13746-13754(2009). RN [17] RP INVOLVEMENT IN HLD3. RX PubMed=21092922; DOI=10.1016/j.ajhg.2010.10.016; RA Feinstein M., Markus B., Noyman I., Shalev H., Flusser H., Shelef I., RA Liani-Leibson K., Shorer Z., Cohen I., Khateeb S., Sivan S., Birk O.S.; RT "Pelizaeus-Merzbacher-like disease caused by AIMP1/p43 homozygous RT mutation."; RL Am. J. Hum. Genet. 87:820-828(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 147-312. RX PubMed=10852899; DOI=10.1074/jbc.c000216200; RA Kim Y., Shin J., Li R., Cheong C., Kim K., Kim S.; RT "A novel anti-tumor cytokine contains an RNA binding motif present in RT aminoacyl-tRNA synthetases."; RL J. Biol. Chem. 275:27062-27068(2000). RN [27] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-312, AND FUNCTION. RX PubMed=11157763; DOI=10.1093/emboj/20.3.570; RA Renault L., Kerjan P., Pasqualato S., Menetrey J., Robinson J.-C., RA Kawaguchi S., Vassylyev D.G., Yokoyama S., Mirande M., Cherfils J.; RT "Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex RT reveals evolutionary dimer mimicry."; RL EMBO J. 20:570-578(2001). RN [28] {ECO:0007744|PDB:4R3Z} RP X-RAY CRYSTALLOGRAPHY (4.03 ANGSTROMS) IN COMPLEX WITH QARS1 AND RARS1. RX PubMed=25288775; DOI=10.1073/pnas.1408836111; RA Fu Y., Kim Y., Jin K.S., Kim H.S., Kim J.H., Wang D., Park M., Jo C.H., RA Kwon N.H., Kim D., Kim M.H., Jeon Y.H., Hwang K.Y., Kim S., Cho Y.; RT "Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for RT mammalian translation."; RL Proc. Natl. Acad. Sci. U.S.A. 111:15084-15089(2014). CC -!- FUNCTION: Non-catalytic component of the multisynthase complex. CC Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase CC (PubMed:10358004). Binds tRNA. Possesses inflammatory cytokine activity CC (PubMed:11306575). Negatively regulates TGF-beta signaling through CC stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7- CC mediated degradation (By similarity). Involved in glucose homeostasis CC through induction of glucagon secretion at low glucose levels (By CC similarity). Promotes dermal fibroblast proliferation and wound repair CC (PubMed:16472771). Regulates KDELR1-mediated retention of HSP90B1/gp96 CC in the endoplasmic reticulum (By similarity). Plays a role in CC angiogenesis by inducing endothelial cell migration at low CC concentrations and endothelian cell apoptosis at high concentrations CC (PubMed:12237313). Induces maturation of dendritic cells and monocyte CC cell adhesion (PubMed:11818442). Modulates endothelial cell responses CC by degrading HIF-1A through interaction with PSMA7 (PubMed:19362550). CC {ECO:0000250|UniProtKB:P31230, ECO:0000269|PubMed:10358004, CC ECO:0000269|PubMed:11157763, ECO:0000269|PubMed:11306575, CC ECO:0000269|PubMed:11818442, ECO:0000269|PubMed:12237313, CC ECO:0000269|PubMed:19362550}. CC -!- SUBUNIT: Homodimer. Part of the multisynthetase complex (MSC), a CC multisubunit complex that groups tRNA ligases for Arg (RARS1), Asp CC (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met CC (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the CC auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 CC (PubMed:24312579, PubMed:19131329, PubMed:19289464). Interacts (via N- CC terminus) with RARS1 (via N-terminus) (PubMed:10358004, CC PubMed:17443684). Part of a complex composed of RARS1, QARS1 and AIMP1 CC (PubMed:25288775). Interacts (via C-terminus) with SMURF2. Interacts CC (via N-terminus) with HSP90B1/gp96 (via C-terminus) (By similarity). CC Interacts with PSMA7 (PubMed:19362550). Interacts with TARS3 CC (PubMed:24312579). {ECO:0000250|UniProtKB:P31230, CC ECO:0000269|PubMed:10358004, ECO:0000269|PubMed:11306575, CC ECO:0000269|PubMed:17443684, ECO:0000269|PubMed:19131329, CC ECO:0000269|PubMed:19289464, ECO:0000269|PubMed:19362550, CC ECO:0000269|PubMed:24312579, ECO:0000269|PubMed:25288775}. CC -!- INTERACTION: CC Q12904; Q13155: AIMP2; NbExp=4; IntAct=EBI-1045802, EBI-745226; CC Q12904; Q99598: TSNAX; NbExp=3; IntAct=EBI-1045802, EBI-742638; CC Q12904; PRO_0000038593 [P04591]: gag; Xeno; NbExp=3; IntAct=EBI-1045802, EBI-6179719; CC Q12904-2; Q13155: AIMP2; NbExp=5; IntAct=EBI-12412735, EBI-745226; CC Q12904-2; Q86YM7: HOMER1; NbExp=3; IntAct=EBI-12412735, EBI-746815; CC Q12904-2; Q96CV9: OPTN; NbExp=6; IntAct=EBI-12412735, EBI-748974; CC Q12904-2; P54136: RARS1; NbExp=3; IntAct=EBI-12412735, EBI-355482; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14500886}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:19289464}. Secreted CC {ECO:0000269|PubMed:10850427}. Endoplasmic reticulum CC {ECO:0000250|UniProtKB:P31230}. Golgi apparatus CC {ECO:0000250|UniProtKB:P31230}. Note=Enriched in secretory vesicles of CC pancreatic alpha cells and secreted from the pancreas in response to CC low glucose levels (By similarity). Secreted in response to hypoxia CC (PubMed:10850427). Also secreted in response to both apoptotic and CC necrotic cell death. {ECO:0000250|UniProtKB:P31230, CC ECO:0000269|PubMed:10850427}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q12904-1; Sequence=Displayed; CC Name=2; CC IsoId=Q12904-2; Sequence=VSP_042197; CC -!- PTM: Cleaved by caspase-7 in response to apoptosis to produce EMAP-II. CC {ECO:0000269|PubMed:10850427, ECO:0000269|PubMed:11306575}. CC -!- DISEASE: Leukodystrophy, hypomyelinating, 3 (HLD3) [MIM:260600]: A CC severe autosomal recessive hypomyelinating leukodystrophy characterized CC by early infantile onset of global developmental delay, lack of CC development, lack of speech acquisition, and peripheral spasticity CC associated with decreased myelination in the central nervous system. CC {ECO:0000269|PubMed:21092922}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U10117; AAA62202.1; -; mRNA. DR EMBL; CR542281; CAG47076.1; -; mRNA. DR EMBL; AK095951; BAG53174.1; -; mRNA. DR EMBL; AK303965; BAG64889.1; -; mRNA. DR EMBL; BC014051; AAH14051.1; -; mRNA. DR CCDS; CCDS3674.1; -. [Q12904-1] DR PIR; B55053; B55053. DR RefSeq; NP_001135887.1; NM_001142415.1. [Q12904-1] DR RefSeq; NP_001135888.1; NM_001142416.1. [Q12904-1] DR RefSeq; NP_004748.2; NM_004757.3. [Q12904-1] DR RefSeq; XP_016864324.1; XM_017008835.1. [Q12904-1] DR RefSeq; XP_016864325.1; XM_017008836.1. DR PDB; 1E7Z; X-ray; 2.05 A; A=148-312. DR PDB; 1EUJ; X-ray; 1.80 A; A/B=147-312. DR PDB; 1FL0; X-ray; 1.50 A; A=150-312. DR PDB; 4R3Z; X-ray; 4.03 A; A=1-312. DR PDBsum; 1E7Z; -. DR PDBsum; 1EUJ; -. DR PDBsum; 1FL0; -. DR PDBsum; 4R3Z; -. DR AlphaFoldDB; Q12904; -. DR BMRB; Q12904; -. DR SMR; Q12904; -. DR BioGRID; 114679; 255. DR ComplexPortal; CPX-2469; Multiaminoacyl-tRNA synthetase complex. DR CORUM; Q12904; -. DR IntAct; Q12904; 52. DR MINT; Q12904; -. DR STRING; 9606.ENSP00000378191; -. DR ChEMBL; CHEMBL4295810; -. DR MoonProt; Q12904; -. DR GlyGen; Q12904; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q12904; -. DR PhosphoSitePlus; Q12904; -. DR SwissPalm; Q12904; -. DR BioMuta; AIMP1; -. DR DMDM; 85700432; -. DR EPD; Q12904; -. DR jPOST; Q12904; -. DR MassIVE; Q12904; -. DR MaxQB; Q12904; -. DR PaxDb; 9606-ENSP00000378191; -. DR PeptideAtlas; Q12904; -. DR ProteomicsDB; 59011; -. [Q12904-1] DR ProteomicsDB; 59012; -. [Q12904-2] DR Pumba; Q12904; -. DR ABCD; Q12904; 1 sequenced antibody. DR Antibodypedia; 4317; 678 antibodies from 46 providers. DR DNASU; 9255; -. DR Ensembl; ENST00000358008.7; ENSP00000350699.3; ENSG00000164022.18. [Q12904-1] DR Ensembl; ENST00000671868.1; ENSP00000499850.1; ENSG00000164022.18. [Q12904-1] DR Ensembl; ENST00000671960.1; ENSP00000500025.1; ENSG00000164022.18. [Q12904-1] DR Ensembl; ENST00000672285.1; ENSP00000500668.1; ENSG00000164022.18. [Q12904-1] DR Ensembl; ENST00000672328.1; ENSP00000500159.1; ENSG00000164022.18. [Q12904-1] DR Ensembl; ENST00000672337.1; ENSP00000499921.1; ENSG00000164022.18. [Q12904-1] DR Ensembl; ENST00000672341.1; ENSP00000500620.1; ENSG00000164022.18. [Q12904-1] DR Ensembl; ENST00000672911.1; ENSP00000500170.1; ENSG00000164022.18. [Q12904-1] DR Ensembl; ENST00000673018.1; ENSP00000500732.1; ENSG00000164022.18. [Q12904-1] DR Ensembl; ENST00000673123.1; ENSP00000500794.1; ENSG00000164022.18. [Q12904-1] DR GeneID; 9255; -. DR KEGG; hsa:9255; -. DR MANE-Select; ENST00000672341.1; ENSP00000500620.1; NM_001142416.2; NP_001135888.2. DR UCSC; uc003hyg.4; human. [Q12904-1] DR AGR; HGNC:10648; -. DR CTD; 9255; -. DR DisGeNET; 9255; -. DR GeneCards; AIMP1; -. DR HGNC; HGNC:10648; AIMP1. DR HPA; ENSG00000164022; Low tissue specificity. DR MalaCards; AIMP1; -. DR MIM; 260600; phenotype. DR MIM; 603605; gene. DR neXtProt; NX_Q12904; -. DR OpenTargets; ENSG00000164022; -. DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability. DR Orphanet; 280293; Pelizaeus-Merzbacher-like disease due to AIMP1 mutation. DR PharmGKB; PA35578; -. DR VEuPathDB; HostDB:ENSG00000164022; -. DR eggNOG; KOG2241; Eukaryota. DR GeneTree; ENSGT00940000154950; -. DR HOGENOM; CLU_009710_6_1_1; -. DR InParanoid; Q12904; -. DR OMA; FTNDECV; -. DR OrthoDB; 1341752at2759; -. DR PhylomeDB; Q12904; -. DR TreeFam; TF324775; -. DR PathwayCommons; Q12904; -. DR Reactome; R-HSA-2408522; Selenoamino acid metabolism. DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation. DR SignaLink; Q12904; -. DR SIGNOR; Q12904; -. DR BioGRID-ORCS; 9255; 14 hits in 1163 CRISPR screens. DR ChiTaRS; AIMP1; human. DR EvolutionaryTrace; Q12904; -. DR GeneWiki; SCYE1; -. DR GenomeRNAi; 9255; -. DR Pharos; Q12904; Tbio. DR PRO; PR:Q12904; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q12904; Protein. DR Bgee; ENSG00000164022; Expressed in calcaneal tendon and 215 other cell types or tissues. DR ExpressionAtlas; Q12904; baseline and differential. DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005125; F:cytokine activity; ISS:HGNC-UCL. DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC-UCL. DR GO; GO:0000049; F:tRNA binding; IDA:HGNC-UCL. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007267; P:cell-cell signaling; IDA:HGNC-UCL. DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0050900; P:leukocyte migration; IDA:HGNC-UCL. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:HGNC-UCL. DR GO; GO:0070094; P:positive regulation of glucagon secretion; ISS:UniProtKB. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR CDD; cd02799; tRNA_bind_EMAP-II_like; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR002547; tRNA-bd_dom. DR PANTHER; PTHR11586:SF46; AMINOACYL TRNA SYNTHASE COMPLEX-INTERACTING MULTIFUNCTIONAL PROTEIN 1; 1. DR PANTHER; PTHR11586; TRNA-AMINOACYLATION COFACTOR ARC1 FAMILY MEMBER; 1. DR Pfam; PF01588; tRNA_bind; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50886; TRBD; 1. DR Genevisible; Q12904; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Angiogenesis; Apoptosis; KW Cytokine; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; KW Golgi apparatus; Inflammatory response; Isopeptide bond; Leukodystrophy; KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome; KW RNA-binding; Secreted; tRNA-binding; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:24312579, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..312 FT /note="Aminoacyl tRNA synthase complex-interacting FT multifunctional protein 1" FT /id="PRO_0000223394" FT CHAIN 147..312 FT /note="Endothelial monocyte-activating polypeptide 2" FT /id="PRO_0000019242" FT DOMAIN 151..252 FT /note="tRNA-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209" FT REGION 6..46 FT /note="Required for fibroblast proliferation" FT REGION 54..194 FT /note="Interaction with HSP90B1" FT /evidence="ECO:0000250" FT REGION 101..114 FT /note="Required for endothelial cell death" FT REGION 107..147 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 114..192 FT /note="Required for endothelial cell migration" FT COMPBIAS 114..141 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:24312579, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 269 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P31230" FT CROSSLNK 137 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0007744|PubMed:25114211" FT VAR_SEQ 1 FT /note="M -> MLPAVAVSEPVVLRFMIFCRLLAKM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000305|PubMed:24312579" FT /id="VSP_042197" FT VARIANT 79 FT /note="P -> A (in dbSNP:rs1134648)" FT /evidence="ECO:0000269|PubMed:7929199" FT /id="VAR_025212" FT VARIANT 104 FT /note="T -> A (in dbSNP:rs113844295)" FT /id="VAR_029156" FT VARIANT 117 FT /note="T -> A (in dbSNP:rs2230255)" FT /id="VAR_050124" FT CONFLICT 138 FT /note="Q -> R (in Ref. 3; BAG64889)" FT /evidence="ECO:0000305" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 157..168 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 171..180 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 182..185 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:1FL0" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:1FL0" FT HELIX 199..202 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 216..220 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 221..223 FT /evidence="ECO:0007829|PDB:1EUJ" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:1EUJ" FT TURN 266..268 FT /evidence="ECO:0007829|PDB:1FL0" FT HELIX 271..274 FT /evidence="ECO:0007829|PDB:1FL0" FT HELIX 275..277 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:1FL0" FT TURN 296..298 FT /evidence="ECO:0007829|PDB:1FL0" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:1E7Z" SQ SEQUENCE 312 AA; 34353 MW; 5F0BF73E58810C60 CRC64; MANNDAVLKR LEQKGAEADQ IIEYLKQQVS LLKEKAILQA TLREEKKLRV ENAKLKKEIE ELKQELIQAE IQNGVKQIPF PSGTPLHANS MVSENVIQST AVTTVSSGTK EQIKGGTGDE KKAKEKIEKK GEKKEKKQQS IAGSADSKPI DVSRLDLRIG CIITARKHPD ADSLYVEEVD VGEIAPRTVV SGLVNHVPLE QMQNRMVILL CNLKPAKMRG VLSQAMVMCA SSPEKIEILA PPNGSVPGDR ITFDAFPGEP DKELNPKKKI WEQIQPDLHT NDECVATYKG VPFEVKGKGV CRAQTMSNSG IK //