ELP1_RABIT
ID ELP1_RABIT Reviewed; 1333 AA.
AC Q8WND5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Elongator complex protein 1;
DE Short=ELP1;
DE AltName: Full=IkappaB kinase complex-associated protein;
DE Short=IKK complex-associated protein;
GN Name=ELP1; Synonyms=IKAP, IKBKAP;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11722848; DOI=10.1016/s0378-1119(01)00737-5;
RA Coli R., Anderson S.L., Volpi S.A., Rubin B.Y.;
RT "Genomic organization and chromosomal localization of the mouse IKBKAP
RT gene.";
RL Gene 279:81-89(2001).
CC -!- FUNCTION: Component of the elongator complex which is required for
CC multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC (5-carbamoylmethyl uridine) (By similarity). The elongator complex
CC catalyzes the formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (By similarity). Regulates the migration and
CC branching of projection neurons in the developing cerebral cortex,
CC through a process depending on alpha-tubulin acetylation (By
CC similarity). ELP1 binds to tRNA, mediating interaction of the elongator
CC complex with tRNA (By similarity). May act as a scaffold protein that
CC assembles active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK) (By
CC similarity). {ECO:0000250|UniProtKB:O95163,
CC ECO:0000250|UniProtKB:Q06706, ECO:0000250|UniProtKB:Q7TT37}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:O95163}.
CC -!- SUBUNIT: Homodimer; dimerization promotes ELP1 stability and elongator
CC complex formation. Component of the elongator complex which consists of
CC ELP1, ELP2, ELP3, ELP4, ELP5 and ELP6. Interacts preferentially with
CC MAP3K14/NIK followed by IKK-alpha and IKK-beta.
CC {ECO:0000250|UniProtKB:O95163}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95163}. Nucleus
CC {ECO:0000250|UniProtKB:O95163}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ELP1/IKA1 family. {ECO:0000305}.
CC -!- CAUTION: The elongator complex was originally thought to play a role in
CC transcription elongation. However, it is no longer thought to play a
CC direct role in this process and its primary function is thought to be
CC in tRNA modification. {ECO:0000250|UniProtKB:O95163}.
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DR EMBL; AF388202; AAL40927.1; -; mRNA.
DR RefSeq; NP_001076124.1; NM_001082655.1.
DR AlphaFoldDB; Q8WND5; -.
DR SMR; Q8WND5; -.
DR STRING; 9986.ENSOCUP00000001614; -.
DR GeneID; 100009360; -.
DR KEGG; ocu:100009360; -.
DR CTD; 8518; -.
DR eggNOG; KOG1920; Eukaryota.
DR InParanoid; Q8WND5; -.
DR OrthoDB; 180136at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0033588; C:elongator holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR006849; Elp1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR12747; PTHR12747; 1.
DR Pfam; PF04762; IKI3; 1.
DR PIRSF; PIRSF017233; IKAP; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..1333
FT /note="Elongator complex protein 1"
FT /id="PRO_0000283996"
FT REGION 886..1333
FT /note="Mediates dimerization"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT REGION 1177..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1210
FT /note="Required for binding to tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06706"
FT COMPBIAS 1177..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95163"
SQ SEQUENCE 1333 AA; 150794 MW; 00FA2FEE7046CC5F CRC64;
MRNLKLLQTL EFKDIQAPGK PQCFSLRTEP GTVLIGSEHG LIEVDPVTRE VKNEIPLVAE
GFLPEDKSGC IVGIQDLLDQ ESVCIATASG DVILCNLSTH QLECVGSVAS GISVMSWSPD
QELVLLATGQ QTLIMMTKDF EPIMEQQIHQ DDFGESKFIT VGWGKKETQF HGSEGRQAAF
QIQTHESALP WDDHRPRVTW RGDGQFFAVS VVCPETGARK VRVWNREFAL QSTSEPVPGL
GPALAWKPSG SLIASTQNKP NQQDVVFFEK NGLLHGQFTL PFLKDEVKVN DLLWNADSSV
LAVWLEDLQR EEDSVLKTYV QLWTVGNYHW YLNECLPFST YGKSKIVSLM WDPVIPYRLH
VLCQGWHYLC YDWRWTTDRS SGDNESDLAN VAVIDGNRIL VTVFQQTVVP PPMCTYRLLL
PHPVNQVTFC ALPKKSNDLA VLDASNQISV YKCGDSPSMD PTVKLGAVGG NGFKVSLRTP
HLEKRYKIQF ESNEDQETNP LKLSLLSWIE EDIFLAICHS QCSPQQSVIH RLTVVPCEVD
EEQGQLSVSS SISVDGIIIS MCCNSKTKSV ALQLADGQIL KYIWESPSLA VEPWKNPGGF
PIQFPYPCIQ TELAMIGGEE CVLGLTDRCR FFINDTEVAS NITSFAVYDE FLLLTTHSHT
CQCYCLKDAS IKTLQAGLSS SHVSNGEILR KVERGSRIVT VVPQDTKLIL QMPRGNLEVV
HHRALVLAQI RKWLDKIMFK EAFECMRKLR INLNLIHDHN PEVFLQNVET FIRQIDCVNH
INLFFTELKE EDVTKTMYPP PVPSSVQQSR DPGGTKLDLI CDALRVAMEN INPHKYCLPI
LTSHVKKTTP ELEIVLQKVH ELQGNAPSDP DAVSAEEALK YLLLLVDVNE LYDHSLGTYD
FDLVLMVAEK SQKDPKEYLP FLNTLKKMET NYQRFTIDKY LKRYEKAIGH LSKCGPEYFS
ECLNLIKDKN LYNEALKLYP PTSQEYKDIS IAYGEHLMEE HQYEPAGLVF ARCGAHEKAL
SAFLTCGSWQ QTLCMAAQLN MTEEQLAGLG RTLAGKLAEQ RKHSDAAIVL EQYTQDYEEA
VLLLLEGAAW EEALRLVYKY NRLDIIETNI KPSILEAYKN YMAFLESQSA TFSRHKERLL
EVRELKERAQ QVDLDDEMPH GQEADLFSET SSIVSGSEMS SKYSHSNSRI SARSSKNRRK
AERKKHSLKE GSPLEDLALL EALNEVVQSL DKLKDEVYRI LKVLFLFEFD EQGRELQKTF
QDTLQLVERS LPEIWTLTYQ QNSAMPVLGP SSTANSIMAS YQQQKTSVPV LDAELFVPPK
INRKTQWKLS LLE
