Q8WND5 · ELP1_RABIT

Function

function

Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity).
The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (By similarity).
ELP1 binds to tRNA, mediating interaction of the elongator complex with tRNA (By similarity).
May act as a scaffold protein that assembles active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK) (By similarity).

Caution

The elongator complex was originally thought to play a role in transcription elongation. However, it is no longer thought to play a direct role in this process and its primary function is thought to be in tRNA modification.

Pathway

tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentelongator holoenzyme complex
Cellular Componentnucleus
Molecular FunctiontRNA binding
Biological ProcesstRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Elongator complex protein 1
  • Short names
    ELP1
  • Alternative names
    • IkappaB kinase complex-associated protein (IKK complex-associated protein)

Gene names

    • Name
      ELP1
    • Synonyms
      IKAP, IKBKAP

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    Q8WND5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00002839961-1333Elongator complex protein 1
Modified residue805Phosphoserine
Modified residue868Phosphoserine
Modified residue1172Phosphoserine
Modified residue1175Phosphoserine

Post-translational modification

Phosphorylated.

Keywords

Proteomic databases

Interaction

Subunit

Homodimer; dimerization promotes ELP1 stability and elongator complex formation. Component of the elongator complex which consists of ELP1, ELP2, ELP3, ELP4, ELP5 and ELP6. Interacts preferentially with MAP3K14/NIK followed by IKK-alpha and IKK-beta.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region886-1333Mediates dimerization
Compositional bias1177-1191Polar residues
Region1177-1209Disordered
Region1192-1210Required for binding to tRNA

Sequence similarities

Belongs to the ELP1/IKA1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,333
  • Mass (Da)
    150,794
  • Last updated
    2002-03-01 v1
  • Checksum
    00FA2FEE7046CC5F
MRNLKLLQTLEFKDIQAPGKPQCFSLRTEPGTVLIGSEHGLIEVDPVTREVKNEIPLVAEGFLPEDKSGCIVGIQDLLDQESVCIATASGDVILCNLSTHQLECVGSVASGISVMSWSPDQELVLLATGQQTLIMMTKDFEPIMEQQIHQDDFGESKFITVGWGKKETQFHGSEGRQAAFQIQTHESALPWDDHRPRVTWRGDGQFFAVSVVCPETGARKVRVWNREFALQSTSEPVPGLGPALAWKPSGSLIASTQNKPNQQDVVFFEKNGLLHGQFTLPFLKDEVKVNDLLWNADSSVLAVWLEDLQREEDSVLKTYVQLWTVGNYHWYLNECLPFSTYGKSKIVSLMWDPVIPYRLHVLCQGWHYLCYDWRWTTDRSSGDNESDLANVAVIDGNRILVTVFQQTVVPPPMCTYRLLLPHPVNQVTFCALPKKSNDLAVLDASNQISVYKCGDSPSMDPTVKLGAVGGNGFKVSLRTPHLEKRYKIQFESNEDQETNPLKLSLLSWIEEDIFLAICHSQCSPQQSVIHRLTVVPCEVDEEQGQLSVSSSISVDGIIISMCCNSKTKSVALQLADGQILKYIWESPSLAVEPWKNPGGFPIQFPYPCIQTELAMIGGEECVLGLTDRCRFFINDTEVASNITSFAVYDEFLLLTTHSHTCQCYCLKDASIKTLQAGLSSSHVSNGEILRKVERGSRIVTVVPQDTKLILQMPRGNLEVVHHRALVLAQIRKWLDKIMFKEAFECMRKLRINLNLIHDHNPEVFLQNVETFIRQIDCVNHINLFFTELKEEDVTKTMYPPPVPSSVQQSRDPGGTKLDLICDALRVAMENINPHKYCLPILTSHVKKTTPELEIVLQKVHELQGNAPSDPDAVSAEEALKYLLLLVDVNELYDHSLGTYDFDLVLMVAEKSQKDPKEYLPFLNTLKKMETNYQRFTIDKYLKRYEKAIGHLSKCGPEYFSECLNLIKDKNLYNEALKLYPPTSQEYKDISIAYGEHLMEEHQYEPAGLVFARCGAHEKALSAFLTCGSWQQTLCMAAQLNMTEEQLAGLGRTLAGKLAEQRKHSDAAIVLEQYTQDYEEAVLLLLEGAAWEEALRLVYKYNRLDIIETNIKPSILEAYKNYMAFLESQSATFSRHKERLLEVRELKERAQQVDLDDEMPHGQEADLFSETSSIVSGSEMSSKYSHSNSRISARSSKNRRKAERKKHSLKEGSPLEDLALLEALNEVVQSLDKLKDEVYRILKVLFLFEFDEQGRELQKTFQDTLQLVERSLPEIWTLTYQQNSAMPVLGPSSTANSIMASYQQQKTSVPVLDAELFVPPKINRKTQWKLSLLE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1177-1191Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF388202
EMBL· GenBank· DDBJ
AAL40927.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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