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Q12904 (AIMP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
Alternative name(s):
Multisynthase complex auxiliary component p43

Cleaved into the following chain:

  1. Endothelial monocyte-activating polypeptide 2
    Short name=EMAP-2
    Alternative name(s):
    Endothelial monocyte-activating polypeptide II
    Short name=EMAP-II
    Small inducible cytokine subfamily E member 1
Gene names
Name:AIMP1
Synonyms:EMAP2, SCYE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7 Ref.8 Ref.9 Ref.13 Ref.20

Subunit structure

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. Ref.5 Ref.7 Ref.12 Ref.13

Subcellular location

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. Ref.6 Ref.10

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Contains 1 tRNA-binding domain.

Ontologies

Keywords
   Biological processAngiogenesis
Apoptosis
Carbohydrate metabolism
Cell adhesion
Glucose metabolism
Inflammatory response
Protein biosynthesis
   Cellular componentCytoplasm
Cytoplasmic vesicle
Endoplasmic reticulum
Golgi apparatus
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseLeukodystrophy
   LigandRNA-binding
tRNA-binding
   Molecular functionCytokine
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell-cell signaling

Inferred from direct assay PubMed 11741979. Source: HGNC

chemotaxis

Traceable author statement PubMed 7545917. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

glucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Traceable author statement PubMed 7545917. Source: ProtInc

leukocyte migration

Inferred from direct assay Ref.7. Source: HGNC

negative regulation of endothelial cell proliferation

Inferred from direct assay PubMed 11741979. Source: HGNC

response to wounding

Traceable author statement PubMed 7545917. Source: ProtInc

signal transduction

Non-traceable author statement PubMed 9405472. Source: ProtInc

tRNA aminoacylation for protein translation

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

aminoacyl-tRNA synthetase multienzyme complex

Inferred from direct assay Ref.10. Source: HGNC

cell surface

Inferred from direct assay PubMed 11741979. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Traceable author statement PubMed 7545917. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

transport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncytokine activity

Inferred from sequence or structural similarity Ref.7. Source: HGNC

protein homodimerization activity

Inferred from direct assay Ref.7. Source: HGNC

tRNA binding

Inferred from direct assay Ref.7. Source: HGNC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

gagP045913EBI-1045802,EBI-6179719From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12904-1)

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.
Isoform 2 (identifier: Q12904-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 312311Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
PRO_0000223394
Chain147 – 312166Endothelial monocyte-activating polypeptide 2
PRO_0000019242

Regions

Domain151 – 252102tRNA-binding
Region6 – 4641Required for fibroblast proliferation
Region54 – 194141Interaction with HSP90B1 By similarity
Region101 – 11414Required for endothelial cell death
Region114 – 19279Required for endothelial cell migration

Amino acid modifications

Modified residue21N-acetylalanine Ref.17 Ref.18
Modified residue2691N6-succinyllysine By similarity

Natural variations

Alternative sequence11M → MLPAVAVSEPVVLRFMIFCR LLAKM in isoform 2.
VSP_042197
Natural variant791P → A. Ref.1
Corresponds to variant rs1134648 [ dbSNP | Ensembl ].
VAR_025212
Natural variant1041T → A.
Corresponds to variant rs2230254 [ dbSNP | Ensembl ].
VAR_029156
Natural variant1171T → A.
Corresponds to variant rs2230255 [ dbSNP | Ensembl ].
VAR_050124

Experimental info

Sequence conflict1381Q → R in BAG64889. Ref.3

Secondary structure

..................................... 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 5F0BF73E58810C60

FASTA31234,353
        10         20         30         40         50         60 
MANNDAVLKR LEQKGAEADQ IIEYLKQQVS LLKEKAILQA TLREEKKLRV ENAKLKKEIE 

        70         80         90        100        110        120 
ELKQELIQAE IQNGVKQIPF PSGTPLHANS MVSENVIQST AVTTVSSGTK EQIKGGTGDE 

       130        140        150        160        170        180 
KKAKEKIEKK GEKKEKKQQS IAGSADSKPI DVSRLDLRIG CIITARKHPD ADSLYVEEVD 

       190        200        210        220        230        240 
VGEIAPRTVV SGLVNHVPLE QMQNRMVILL CNLKPAKMRG VLSQAMVMCA SSPEKIEILA 

       250        260        270        280        290        300 
PPNGSVPGDR ITFDAFPGEP DKELNPKKKI WEQIQPDLHT NDECVATYKG VPFEVKGKGV 

       310 
CRAQTMSNSG IK 

« Hide

Isoform 2 [UniParc].

Checksum: C4D804F0180FD7D4
Show »

FASTA33637,039

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Pelizaeus-Merzbacher-like disease caused by AIMP1/p43 homozygous mutation."
Feinstein M., Markus B., Noyman I., Shalev H., Flusser H., Shelef I., Liani-Leibson K., Shorer Z., Cohen I., Khateeb S., Sivan S., Birk O.S.
Am. J. Hum. Genet. 87:820-828(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB55053.
RefSeqNP_001135887.1. NM_001142415.1.
NP_001135888.1. NM_001142416.1.
NP_004748.2. NM_004757.3.
UniGeneHs.591680.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7ZX-ray2.05A148-312[»]
1EUJX-ray1.80A/B147-312[»]
1FL0X-ray1.50A150-312[»]
ProteinModelPortalQ12904.
SMRQ12904. Positions 149-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114679. 38 interactions.
IntActQ12904. 3 interactions.
MINTMINT-5004499.
STRING9606.ENSP00000378191.

PTM databases

PhosphoSiteQ12904.

Polymorphism databases

DMDM85700432.

Proteomic databases

PaxDbQ12904.
PRIDEQ12904.

Protocols and materials databases

DNASU9255.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358008; ENSP00000350699; ENSG00000164022. [Q12904-1]
ENST00000394701; ENSP00000378191; ENSG00000164022. [Q12904-2]
ENST00000442366; ENSP00000405248; ENSG00000164022. [Q12904-1]
GeneID9255.
KEGGhsa:9255.
UCSCuc003hyg.3. human. [Q12904-1]
uc003hyh.3. human. [Q12904-2]

Organism-specific databases

CTD9255.
GeneCardsGC04P107236.
HGNCHGNC:10648. AIMP1.
HPACAB017618.
HPA018476.
MIM260600. phenotype.
603605. gene.
neXtProtNX_Q12904.
Orphanet280293. Pelizaeus-Merzbacher-like due to AIMP1 mutation.
PharmGKBPA35578.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0073.
HOGENOMHOG000230584.
HOVERGENHBG019053.
InParanoidQ12904.
KOK15437.
OMAMANNDAV.
PhylomeDBQ12904.
TreeFamTF324775.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ12904.
BgeeQ12904.
CleanExHS_SCYE1.
GenevestigatorQ12904.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR002547. tRNA-bd_dom.
[Graphical view]
PfamPF01588. tRNA_bind. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
PROSITEPS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAIMP1. human.
EvolutionaryTraceQ12904.
GeneWikiSCYE1.
GenomeRNAi9255.
NextBio34695.
PROQ12904.
SOURCESearch...

Entry information

Entry nameAIMP1_HUMAN
AccessionPrimary (citable) accession number: Q12904
Secondary accession number(s): B3KTR2 expand/collapse secondary AC list , B4E1S7, Q6FG28, Q96CQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM