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Protein

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1

Gene

AIMP1

Organism
Homo sapiens (Human)
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 PSMA7.6 Publications

GO - Molecular functioni

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

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • apoptotic process Source: UniProtKB-KW
  • cell adhesion Source: UniProtKB-KW
  • cell-cell signaling Source: HGNC
  • chemotaxis Source: ProtInc
  • gene expression Source: Reactome
  • glucose metabolic process Source: UniProtKB-KW
  • inflammatory response Source: ProtInc
  • leukocyte migration Source: HGNC
  • negative regulation of endothelial cell proliferation Source: HGNC
  • response to wounding Source: ProtInc
  • signal transduction Source: ProtInc
  • tRNA aminoacylation for protein translation Source: Reactome
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

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 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:10648. AIMP1.

Subcellular locationi

GO - Cellular componenti

  • aminoacyl-tRNA synthetase multienzyme complex Source: HGNC
  • cell surface Source: BHF-UCL
  • cytoplasm Source: HPA
  • cytosol Source: GO_Central
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • extracellular space Source: ProtInc
  • Golgi apparatus Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Leukodystrophy, hypomyelinating, 3 (HLD3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:260600

Keywords - Diseasei

Leukodystrophy

Organism-specific databases

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

Polymorphism and mutation databases

BioMutaiAIMP1.
DMDMi85700432.

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

BgeeiQ12904.
CleanExiHS_SCYE1.
ExpressionAtlasiQ12904. baseline and differential.
GenevisibleiQ12904. HS.

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
AIMP2Q131553EBI-1045802,EBI-745226
gagP045913EBI-1045802,EBI-6179719From a different organism.
TSNAXQ995983EBI-1045802,EBI-742638

Protein-protein interaction databases

BioGridi114679. 46 interactions.
IntActiQ12904. 5 interactions.
MINTiMINT-5004499.
STRINGi9606.ENSP00000378191.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7ZX-ray2.05A148-312[»]
1EUJX-ray1.80A/B147-312[»]
1FL0X-ray1.50A150-312[»]
4R3ZX-ray4.03A1-312[»]
ProteinModelPortaliQ12904.
SMRiQ12904. Positions 5-80, 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.
GeneTreeiENSGT00790000123080.
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. AlignAdd to basket

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

        10         20         30         40         50
MANNDAVLKR LEQKGAEADQ IIEYLKQQVS LLKEKAILQA TLREEKKLRV
60 70 80 90 100
ENAKLKKEIE ELKQELIQAE IQNGVKQIPF PSGTPLHANS MVSENVIQST
110 120 130 140 150
AVTTVSSGTK EQIKGGTGDE KKAKEKIEKK GEKKEKKQQS IAGSADSKPI
160 170 180 190 200
DVSRLDLRIG CIITARKHPD ADSLYVEEVD VGEIAPRTVV SGLVNHVPLE
210 220 230 240 250
QMQNRMVILL CNLKPAKMRG VLSQAMVMCA SSPEKIEILA PPNGSVPGDR
260 270 280 290 300
ITFDAFPGEP DKELNPKKKI WEQIQPDLHT NDECVATYKG VPFEVKGKGV
310
CRAQTMSNSG IK
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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7ZX-ray2.05A148-312[»]
1EUJX-ray1.80A/B147-312[»]
1FL0X-ray1.50A150-312[»]
4R3ZX-ray4.03A1-312[»]
ProteinModelPortaliQ12904.
SMRiQ12904. Positions 5-80, 149-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114679. 46 interactions.
IntActiQ12904. 5 interactions.
MINTiMINT-5004499.
STRINGi9606.ENSP00000378191.

PTM databases

PhosphoSiteiQ12904.

Polymorphism and mutation databases

BioMutaiAIMP1.
DMDMi85700432.

Proteomic databases

MaxQBiQ12904.
PaxDbiQ12904.
PRIDEiQ12904.

Protocols and materials databases

DNASUi9255.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi9255.
GeneCardsiGC04P107236.
HGNCiHGNC:10648. AIMP1.
HPAiCAB017618.
HPA018476.
MIMi260600. phenotype.
603605. gene.
neXtProtiNX_Q12904.
Orphaneti280293. Pelizaeus-Merzbacher-like disease due to AIMP1 mutation.
PharmGKBiPA35578.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0073.
GeneTreeiENSGT00790000123080.
HOGENOMiHOG000230584.
HOVERGENiHBG019053.
InParanoidiQ12904.
KOiK15437.
OMAiMANNDAV.
PhylomeDBiQ12904.
TreeFamiTF324775.

Enzyme and pathway databases

ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSiAIMP1. human.
EvolutionaryTraceiQ12904.
GeneWikiiSCYE1.
GenomeRNAii9255.
NextBioi34695.
PROiQ12904.
SOURCEiSearch...

Gene expression databases

BgeeiQ12904.
CleanExiHS_SCYE1.
ExpressionAtlasiQ12904. baseline and differential.
GenevisibleiQ12904. HS.

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] (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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "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.
  21. "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: June 24, 2015
This is version 147 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

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 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.