AIMP1_HUMAN
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 03-AUG-2022, entry version 201.
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.
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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 CCDS; CCDS47121.1; -. [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. [Q12904-1]
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; 174.
DR CORUM; Q12904; -.
DR IntAct; Q12904; 46.
DR MINT; Q12904; -.
DR STRING; 9606.ENSP00000378191; -.
DR ChEMBL; CHEMBL4295810; -.
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; Q12904; -.
DR PeptideAtlas; Q12904; -.
DR PRIDE; Q12904; -.
DR ProteomicsDB; 59011; -. [Q12904-1]
DR ProteomicsDB; 59012; -. [Q12904-2]
DR ABCD; Q12904; 1 sequenced antibody.
DR Antibodypedia; 4317; 610 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 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; IKMSTPN; -.
DR OrthoDB; 1434247at2759; -.
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; 13 hits in 1086 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 213 other tissues.
DR ExpressionAtlas; Q12904; baseline and differential.
DR Genevisible; Q12904; HS.
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:UniProtKB.
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: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 Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR Pfam; PF01588; tRNA_bind; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50886; TRBD; 1.
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
