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Q12904

- AIMP1_HUMAN

UniProt

Q12904 - AIMP1_HUMAN

Protein

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1

Gene

AIMP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    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 PSMA7.6 Publications

    GO - Molecular functioni

    1. cytokine activity Source: HGNC
    2. protein binding Source: IntAct
    3. protein homodimerization activity Source: HGNC
    4. tRNA binding Source: HGNC

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. apoptotic process Source: UniProtKB-KW
    3. cell adhesion Source: UniProtKB-KW
    4. cell-cell signaling Source: HGNC
    5. chemotaxis Source: ProtInc
    6. gene expression Source: Reactome
    7. glucose metabolic process Source: UniProtKB-KW
    8. inflammatory response Source: ProtInc
    9. leukocyte migration Source: HGNC
    10. negative regulation of endothelial cell proliferation Source: HGNC
    11. response to wounding Source: ProtInc
    12. signal transduction Source: ProtInc
    13. tRNA aminoacylation for protein translation Source: Reactome

    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

    Enzyme and pathway databases

    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:10648. AIMP1.

    Subcellular locationi

    Nucleus. Cytoplasmcytosol. Cytoplasmic vesiclesecretory vesicle By similarity. Secreted By similarity. Endoplasmic reticulum By similarity. Golgi apparatus By similarity
    Note: Enriched in secretory vesicles of pancreatic alpha cells and secreted from the pancreas in response to low glucose levels By similarity. Also secreted in response to hypoxia and both apoptotic and necrotic cell death.By similarity

    GO - Cellular componenti

    1. aminoacyl-tRNA synthetase multienzyme complex Source: HGNC
    2. cell surface Source: BHF-UCL
    3. cytosol Source: Reactome
    4. endoplasmic reticulum Source: UniProtKB-SubCell
    5. extracellular space Source: ProtInc
    6. Golgi apparatus Source: UniProtKB-SubCell
    7. membrane Source: UniProtKB
    8. nucleus Source: UniProtKB-SubCell
    9. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Leukodystrophy, hypomyelinating, 3 (HLD3) [MIM:260600]: A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Leukodystrophy

    Organism-specific databases

    MIMi260600. phenotype.
    Orphaneti280293. Pelizaeus-Merzbacher-like due to AIMP1 mutation.
    PharmGKBiPA35578.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 312311Aminoacyl tRNA synthase complex-interacting multifunctional protein 1PRO_0000223394Add
    BLAST
    Chaini147 – 312166Endothelial monocyte-activating polypeptide 2PRO_0000019242Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei269 – 2691N6-succinyllysineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ12904.
    PaxDbiQ12904.
    PRIDEiQ12904.

    PTM databases

    PhosphoSiteiQ12904.

    Expressioni

    Gene expression databases

    ArrayExpressiQ12904.
    BgeeiQ12904.
    CleanExiHS_SCYE1.
    GenevestigatoriQ12904.

    Organism-specific databases

    HPAiCAB017618.
    HPA018476.

    Interactioni

    Subunit structurei

    Homodimer. 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 PSMA7.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    gagP045913EBI-1045802,EBI-6179719From a different organism.

    Protein-protein interaction databases

    BioGridi114679. 38 interactions.
    IntActiQ12904. 3 interactions.
    MINTiMINT-5004499.
    STRINGi9606.ENSP00000378191.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi152 – 1543
    Beta strandi157 – 16812
    Beta strandi171 – 18010
    Beta strandi182 – 1854
    Beta strandi187 – 1915
    Turni194 – 1963
    Helixi199 – 2024
    Beta strandi205 – 2106
    Beta strandi216 – 2205
    Beta strandi221 – 2233
    Beta strandi229 – 2324
    Beta strandi235 – 2384
    Beta strandi262 – 2643
    Turni266 – 2683
    Helixi271 – 2744
    Helixi275 – 2773
    Beta strandi278 – 2803
    Beta strandi284 – 2885
    Turni296 – 2983
    Beta strandi310 – 3123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E7ZX-ray2.05A148-312[»]
    1EUJX-ray1.80A/B147-312[»]
    1FL0X-ray1.50A150-312[»]
    ProteinModelPortaliQ12904.
    SMRiQ12904. Positions 149-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12904.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini151 – 252102tRNA-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni6 – 4641Required for fibroblast proliferationAdd
    BLAST
    Regioni54 – 194141Interaction with HSP90B1By similarityAdd
    BLAST
    Regioni101 – 11414Required for endothelial cell deathAdd
    BLAST
    Regioni114 – 19279Required for endothelial cell migrationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 tRNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0073.
    HOGENOMiHOG000230584.
    HOVERGENiHBG019053.
    InParanoidiQ12904.
    KOiK15437.
    OMAiMANNDAV.
    PhylomeDBiQ12904.
    TreeFamiTF324775.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12904-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MANNDAVLKR LEQKGAEADQ IIEYLKQQVS LLKEKAILQA TLREEKKLRV    50
    ENAKLKKEIE ELKQELIQAE IQNGVKQIPF PSGTPLHANS MVSENVIQST 100
    AVTTVSSGTK EQIKGGTGDE KKAKEKIEKK GEKKEKKQQS IAGSADSKPI 150
    DVSRLDLRIG CIITARKHPD ADSLYVEEVD VGEIAPRTVV SGLVNHVPLE 200
    QMQNRMVILL CNLKPAKMRG VLSQAMVMCA SSPEKIEILA PPNGSVPGDR 250
    ITFDAFPGEP DKELNPKKKI WEQIQPDLHT NDECVATYKG VPFEVKGKGV 300
    CRAQTMSNSG IK 312
    Length:312
    Mass (Da):34,353
    Last modified:January 24, 2006 - v2
    Checksum:i5F0BF73E58810C60
    GO
    Isoform 2 (identifier: Q12904-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MLPAVAVSEPVVLRFMIFCRLLAKM

    Show »
    Length:336
    Mass (Da):37,039
    Checksum:iC4D804F0180FD7D4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381Q → R in BAG64889. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791P → A.1 Publication
    Corresponds to variant rs1134648 [ dbSNP | Ensembl ].
    VAR_025212
    Natural varianti104 – 1041T → A.
    Corresponds to variant rs2230254 [ dbSNP | Ensembl ].
    VAR_029156
    Natural varianti117 – 1171T → A.
    Corresponds to variant rs2230255 [ dbSNP | Ensembl ].
    VAR_050124

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MLPAVAVSEPVVLRFMIFCR LLAKM in isoform 2. 1 PublicationVSP_042197

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10117 mRNA. Translation: AAA62202.1.
    CR542281 mRNA. Translation: CAG47076.1.
    AK095951 mRNA. Translation: BAG53174.1.
    AK303965 mRNA. Translation: BAG64889.1.
    BC014051 mRNA. Translation: AAH14051.1.
    CCDSiCCDS3674.1. [Q12904-1]
    CCDS47121.1. [Q12904-2]
    PIRiB55053.
    RefSeqiNP_001135887.1. NM_001142415.1. [Q12904-1]
    NP_001135888.1. NM_001142416.1. [Q12904-2]
    NP_004748.2. NM_004757.3. [Q12904-1]
    UniGeneiHs.591680.

    Genome annotation databases

    EnsembliENST00000358008; ENSP00000350699; ENSG00000164022. [Q12904-1]
    ENST00000394701; ENSP00000378191; ENSG00000164022. [Q12904-2]
    ENST00000442366; ENSP00000405248; ENSG00000164022. [Q12904-1]
    GeneIDi9255.
    KEGGihsa:9255.
    UCSCiuc003hyg.3. human. [Q12904-1]
    uc003hyh.3. human. [Q12904-2]

    Polymorphism databases

    DMDMi85700432.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10117 mRNA. Translation: AAA62202.1 .
    CR542281 mRNA. Translation: CAG47076.1 .
    AK095951 mRNA. Translation: BAG53174.1 .
    AK303965 mRNA. Translation: BAG64889.1 .
    BC014051 mRNA. Translation: AAH14051.1 .
    CCDSi CCDS3674.1. [Q12904-1 ]
    CCDS47121.1. [Q12904-2 ]
    PIRi B55053.
    RefSeqi NP_001135887.1. NM_001142415.1. [Q12904-1 ]
    NP_001135888.1. NM_001142416.1. [Q12904-2 ]
    NP_004748.2. NM_004757.3. [Q12904-1 ]
    UniGenei Hs.591680.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E7Z X-ray 2.05 A 148-312 [» ]
    1EUJ X-ray 1.80 A/B 147-312 [» ]
    1FL0 X-ray 1.50 A 150-312 [» ]
    ProteinModelPortali Q12904.
    SMRi Q12904. Positions 149-312.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114679. 38 interactions.
    IntActi Q12904. 3 interactions.
    MINTi MINT-5004499.
    STRINGi 9606.ENSP00000378191.

    PTM databases

    PhosphoSitei Q12904.

    Polymorphism databases

    DMDMi 85700432.

    Proteomic databases

    MaxQBi Q12904.
    PaxDbi Q12904.
    PRIDEi Q12904.

    Protocols and materials databases

    DNASUi 9255.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358008 ; ENSP00000350699 ; ENSG00000164022 . [Q12904-1 ]
    ENST00000394701 ; ENSP00000378191 ; ENSG00000164022 . [Q12904-2 ]
    ENST00000442366 ; ENSP00000405248 ; ENSG00000164022 . [Q12904-1 ]
    GeneIDi 9255.
    KEGGi hsa:9255.
    UCSCi uc003hyg.3. human. [Q12904-1 ]
    uc003hyh.3. human. [Q12904-2 ]

    Organism-specific databases

    CTDi 9255.
    GeneCardsi GC04P107236.
    HGNCi HGNC:10648. AIMP1.
    HPAi CAB017618.
    HPA018476.
    MIMi 260600. phenotype.
    603605. gene.
    neXtProti NX_Q12904.
    Orphaneti 280293. Pelizaeus-Merzbacher-like due to AIMP1 mutation.
    PharmGKBi PA35578.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0073.
    HOGENOMi HOG000230584.
    HOVERGENi HBG019053.
    InParanoidi Q12904.
    KOi K15437.
    OMAi MANNDAV.
    PhylomeDBi Q12904.
    TreeFami TF324775.

    Enzyme and pathway databases

    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi AIMP1. human.
    EvolutionaryTracei Q12904.
    GeneWikii SCYE1.
    GenomeRNAii 9255.
    NextBioi 34695.
    PROi Q12904.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12904.
    Bgeei Q12904.
    CleanExi HS_SCYE1.
    Genevestigatori Q12904.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR002547. tRNA-bd_dom.
    [Graphical view ]
    Pfami PF01588. tRNA_bind. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    PROSITEi PS50886. TRBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1), VARIANT ALA-79.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    4. "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] (ISOFORM 1).
      Tissue: Pancreas.
    5. "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase."
      Park S.G., Jung K.H., Lee J.S., Jo Y.J., Motegi H., Kim S., Shiba K.
      J. Biol. Chem. 274:16673-16676(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RARS.
    6. "Prostate adenocarcinoma cells release the novel proinflammatory polypeptide EMAP-II in response to stress."
      Barnett G., Jakobsen A.-M., Tas M., Rice K., Carmichael J., Murray J.C.
      Cancer Res. 60:2850-2857(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, CLEAVAGE.
    7. "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: FUNCTION, SUBUNIT.
    8. "Dose-dependent biphasic activity of tRNA synthetase-associating factor, p43, in angiogenesis."
      Park S.G., Kang Y.-S., Ahn Y.H., Lee S.H., Kim K.-R., Kim K.-W., Koh G.Y., Ko Y.-G., Kim S.
      J. Biol. Chem. 277:45243-45248(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Monocyte cell adhesion induced by a human aminoacyl-tRNA synthetase-associated factor, p43: identification of the related adhesion molecules and signal pathways."
      Park H., Park S.G., Lee J.-W., Kim T., Kim G., Ko Y.-G., Kim S.
      J. Leukoc. Biol. 71:223-230(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII."
      Wolfe C.L., Warrington J.A., Davis S., Green S., Norcum M.T.
      Protein Sci. 12:2282-2290(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1."
      Han J.M., Park S.G., Lee Y., Kim S.
      Biochem. Biophys. Res. Commun. 342:113-118(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGIONS INVOLVED IN FIBROBLAST PROLIFERATION; ENDOTHELIAL CELL DEATH AND ENDOTHELIAL MIGRATION.
    12. "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines."
      Bottoni A., Vignali C., Piccin D., Tagliati F., Luchin A., Zatelli M.C., Uberti E.C.
      J. Cell. Physiol. 212:293-297(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RARS.
    13. "Endothelial monocyte activating polypeptide-II modulates endothelial cell responses by degrading hypoxia-inducible factor-1alpha through interaction with PSMA7, a component of the proteasome."
      Tandle A.T., Calvani M., Uranchimeg B., Zahavi D., Melillo G., Libutti S.K.
      Exp. Cell Res. 315:1850-1859(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PSMA7.
    14. Cited for: INVOLVEMENT IN HLD3.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases."
      Kim Y., Shin J., Li R., Cheong C., Kim K., Kim S.
      J. Biol. Chem. 275:27062-27068(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 147-312.
    20. "Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry."
      Renault L., Kerjan P., Pasqualato S., Menetrey J., Robinson J.-C., Kawaguchi S., Vassylyev D.G., Yokoyama S., Mirande M., Cherfils J.
      EMBO J. 20:570-578(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-312, FUNCTION.

    Entry informationi

    Entry nameiAIMP1_HUMAN
    AccessioniPrimary (citable) accession number: Q12904
    Secondary accession number(s): B3KTR2
    , B4E1S7, Q6FG28, Q96CQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3