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Protein

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1

Gene

Aimp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7 (By similarity).By similarity7 Publications

GO - Molecular functioni

  • cytokine activity Source: HGNC
  • GTPase binding Source: MGI
  • protein homodimerization activity Source: HGNC
  • tRNA binding Source: HGNC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Angiogenesis, Apoptosis, Carbohydrate metabolism, Cell adhesion, Glucose metabolism, Inflammatory response, Protein biosynthesis

Keywords - Ligandi

RNA-binding, tRNA-binding

Protein family/group databases

MoonProtiP31230.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
Alternative name(s):
Multisynthase complex auxiliary component p43
Cleaved into the following chain:
Alternative name(s):
Endothelial monocyte-activating polypeptide II
Short name:
EMAP-II
Small inducible cytokine subfamily E member 1
Gene namesi
Name:Aimp1
Synonyms:Emap2, Scye1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:102774. Aimp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Nucleus, Secreted

Pathology & Biotechi

Disruption phenotypei

Increased Hsp90b1 surface expression, dendritic cell hyperactivation and development of lupus-like autoimmune phenotypes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 310309Aminoacyl tRNA synthase complex-interacting multifunctional protein 1PRO_0000223395Add
BLAST
Chaini145 – 310166Endothelial monocyte-activating polypeptide 2PRO_0000019244Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei267 – 2671N6-succinyllysineCombined sources

Post-translational modificationi

Cleaved by caspase-7 in response to apoptosis to produce EMAP-II.

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP31230.
MaxQBiP31230.
PaxDbiP31230.
PRIDEiP31230.

PTM databases

iPTMnetiP31230.
PhosphoSiteiP31230.
SwissPalmiP31230.

Expressioni

Tissue specificityi

Highly expressed in salivary glands and pancreatic alpha cells in the adult (at protein level). In the embryo, expressed primarily at sites of tissue remodeling such as ganglia, developing bones and teeth.2 Publications

Inductioni

By wounding.1 Publication

Gene expression databases

BgeeiP31230.
CleanExiMM_SCYE1.

Interactioni

Subunit structurei

Homodimer (By similarity). Component of the multisynthase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl and aspartyl-tRNA synthases, and three auxiliary proteins, EEF1E1/p18, AIMP2/p38 and AIMP1/p43. Interacts (via N-terminus) with RARS (via N-terminus). Interacts (via C-terminus) with SMURF2. Interacts (via N-terminus) with HSP90B1/gp96 (via C-terminus). Interacts with PSMA7 (By similarity).By similarity

GO - Molecular functioni

  • cytokine activity Source: HGNC
  • GTPase binding Source: MGI
  • protein homodimerization activity Source: HGNC

Protein-protein interaction databases

IntActiP31230. 3 interactions.
MINTiMINT-1869879.
STRINGi10090.ENSMUSP00000029663.

Structurei

3D structure databases

ProteinModelPortaliP31230.
SMRiP31230. Positions 5-78, 147-310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini149 – 250102tRNA-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 4641Required for fibroblast proliferationBy similarityAdd
BLAST
Regioni54 – 192139Interaction with HSP90B1Add
BLAST
Regioni101 – 11515Required for endothelial cell deathBy similarityAdd
BLAST
Regioni115 – 19076Required for endothelial cell migrationBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 tRNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2241. Eukaryota.
COG0073. LUCA.
InParanoidiP31230.
PhylomeDBiP31230.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR002547. tRNA-bd_dom.
[Graphical view]
PfamiPF01588. tRNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS50886. TRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATNDAVLKR LEQKGAEADQ IIEYLKQQVA LLKEKAILQA TMREEKKLRV
60 70 80 90 100
ENAKLKKEIE ELKQELILAE IHNGVEQVRV RLSTPLQTNC TASESVVQSP
110 120 130 140 150
SVATTASPAT KEQIKAGEEK KVKEKTEKKG EKKEKQQSAA ASTDSKPIDA
160 170 180 190 200
SRLDLRIGCI VTAKKHPDAD SLYVEEVDVG EAAPRTVVSG LVNHVPLEQM
210 220 230 240 250
QNRMVVLLCN LKPAKMRGVL SQAMVMCASS PEKVEILAPP NGSVPGDRIT
260 270 280 290 300
FDAFPGEPDK ELNPKKKIWE QIQPDLHTNA ECVATYKGAP FEVKGKGVCR
310
AQTMANSGIK
Length:310
Mass (Da):33,997
Last modified:October 18, 2001 - v2
Checksum:iA2F8FF52A33D03A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10118 mRNA. Translation: AAA62203.1.
BC002054 mRNA. Translation: AAH02054.1.
PIRiA55053.
UniGeneiMm.235137.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10118 mRNA. Translation: AAA62203.1.
BC002054 mRNA. Translation: AAH02054.1.
PIRiA55053.
UniGeneiMm.235137.

3D structure databases

ProteinModelPortaliP31230.
SMRiP31230. Positions 5-78, 147-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP31230. 3 interactions.
MINTiMINT-1869879.
STRINGi10090.ENSMUSP00000029663.

Protein family/group databases

MoonProtiP31230.

PTM databases

iPTMnetiP31230.
PhosphoSiteiP31230.
SwissPalmiP31230.

Proteomic databases

EPDiP31230.
MaxQBiP31230.
PaxDbiP31230.
PRIDEiP31230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:102774. Aimp1.

Phylogenomic databases

eggNOGiKOG2241. Eukaryota.
COG0073. LUCA.
InParanoidiP31230.
PhylomeDBiP31230.

Miscellaneous databases

ChiTaRSiAimp1. mouse.
PROiP31230.
SOURCEiSearch...

Gene expression databases

BgeeiP31230.
CleanExiMM_SCYE1.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR002547. tRNA-bd_dom.
[Graphical view]
PfamiPF01588. tRNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a novel tumor-derived cytokine. Endothelial-monocyte activating polypeptide II."
    Kao J., Houck K., Fan Y., Haehnel I., Libutti S.K., Kayton M.L., Grikscheit T., Chabot J., Nowygrod R., Greenberg S., Kuang W.J., Leung D.W., Hayward J.R., Kisiel W., Heath M., Brett J., Stern D.M.
    J. Biol. Chem. 269:25106-25119(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Endothelial monocyte-activating polypeptide II. A novel tumor-derived polypeptide that activates host-response mechanisms."
    Kao J., Ryan J., Brett G., Chen J., Shen H., Fan Y.-G., Godman G., Familletti P.C., Wang F., Pan Y.-C.E., Stern D., Clauss M.
    J. Biol. Chem. 267:20239-20247(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 145-164, FUNCTION.
  4. "A peptide derived from the amino terminus of endothelial-monocyte-activating polypeptide II modulates mononuclear and polymorphonuclear leukocyte functions, defines an apparently novel cellular interaction site, and induces an acute inflammatory response."
    Kao J., Fan Y., Haehnel I., Brett J., Greenberg S., Clauss M., Kayton M., Houck K., Kisiel W., Seljelid R., Burnier J., Stern D.
    J. Biol. Chem. 269:9774-9782(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Regulation of endothelial monocyte-activating polypeptide II release by apoptosis."
    Knies U.E., Behrensdorf H.A., Mitchell C.A., Deutsch U., Risau W., Drexler H.C.A., Clauss M.
    Proc. Natl. Acad. Sci. U.S.A. 95:12322-12327(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component."
    Shalak V., Kaminska M., Mitnacht-Kraus R., Vandenabeele P., Clauss M., Mirande M.
    J. Biol. Chem. 276:23769-23776(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE.
  7. "The novel cytokine p43 stimulates dermal fibroblast proliferation and wound repair."
    Park S.G., Shin H., Shin Y.K., Lee Y., Choi E.-C., Park B.-J., Kim S.
    Am. J. Pathol. 166:387-398(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Aminoacyl-tRNA synthetase-interacting multifunctional protein 1/p43 controls endoplasmic reticulum retention of heat shock protein gp96: its pathological implications in lupus-like autoimmune diseases."
    Han J.M., Park S.G., Liu B., Park B.-J., Kim J.Y., Jin C.H., Song Y.W., Li Z., Kim S.
    Am. J. Pathol. 170:2042-2054(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSP90B1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  10. "AIMP1/p43 downregulates TGF-beta signaling via stabilization of smurf2."
    Lee Y.S., Han J.M., Son S.H., Choi J.W., Jeon E.J., Bae S.-C., Park Y.I., Kim S.
    Biochem. Biophys. Res. Commun. 371:395-400(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SMURF2, INDUCTION.
  11. "AIMP1/p43 protein induces the maturation of bone marrow-derived dendritic cells with T helper type 1-polarizing ability."
    Kim E., Kim S.H., Kim S., Cho D., Kim T.S.
    J. Immunol. 180:2894-2902(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAIMP1_MOUSE
AccessioniPrimary (citable) accession number: P31230
Secondary accession number(s): Q60659
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 18, 2001
Last modified: May 11, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.