ID   ELP1_RAT                Reviewed;        1331 AA.
AC   Q8VHU4;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 102.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
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 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; AF388201; AAL40926.1; -; mRNA.
DR   RefSeq; NP_543175.1; NM_080899.1.
DR   AlphaFoldDB; Q8VHU4; -.
DR   SMR; Q8VHU4; -.
DR   BioGRID; 250868; 1.
DR   STRING; 10116.ENSRNOP00000022836; -.
DR   iPTMnet; Q8VHU4; -.
DR   PhosphoSitePlus; Q8VHU4; -.
DR   jPOST; Q8VHU4; -.
DR   PaxDb; Q8VHU4; -.
DR   PRIDE; Q8VHU4; -.
DR   GeneID; 140934; -.
DR   KEGG; rno:140934; -.
DR   CTD; 8518; -.
DR   RGD; 620072; Elp1.
DR   eggNOG; KOG1920; Eukaryota.
DR   InParanoid; Q8VHU4; -.
DR   OrthoDB; 180136at2759; -.
DR   PhylomeDB; Q8VHU4; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q8VHU4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033588; C:elongator holoenzyme complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0004672; F:protein kinase activity; IDA:RGD.
DR   GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0007252; P:I-kappaB phosphorylation; IDA:RGD.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; ISO:RGD.
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..1331
FT                   /note="Elongator complex protein 1"
FT                   /id="PRO_0000283997"
FT   REGION          884..1331
FT                   /note="Mediates dimerization"
FT                   /evidence="ECO:0000250|UniProtKB:O95163"
FT   REGION          1167..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1190..1208
FT                   /note="Required for binding to tRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q06706"
FT   COMPBIAS        1167..1189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         803
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95163"
FT   MOD_RES         1170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95163"
FT   MOD_RES         1173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95163"
SQ   SEQUENCE   1331 AA;  149171 MW;  6B33E22387495543 CRC64;
     MRNLKLHQTL EFRDIQAPGK PQCFCLRAEQ GTVLIGSERG LTEVDPVKKE VKTEISLVAE
     GFLPEDGSGC IVGIQDLLDQ ESVCVATASG DVIVCNVSTQ QLECVGNVAS GISVMSWSPD
     QELLLLATAQ QTLIMMTRDY EVITEQQIHQ DDFGEGKFIT VGWGSKDTQF HGSEGRPITF
     PVQMHESALS WDDHRPQITW RGDGQFFAVS VVCSQTGARK IRVWNREFAL QSTSESVPGL
     GPSLAWKPSG SLIASTQDKP NQQDVVFFEK NGLLHGYFTL PFLKDEVKVN DLLWNADSSV
     LAVWLEDLPK EGSSTLKSYV QLWTVGNYHW YLKQSLPFST TGKNQIVSLL WDPVTPGRLH
     VLCQGWRYLC CDWHWTTDRS SGNSADDLAN VAVIDGNKVL VTVFQRTVTP PPMCTYRLLI
     PHPVNQVMSS AHLGNDLAVL DASNQISVYK CDDKPDMDST VKLGAVGGTG FKVPLRTPHL
     EKRYRIQFGN KEEEEDVSPL QFRFLTWIEG DAFLAISHSH SSPQSIIHHL TMAGSEGDEE
     QGQLNVSSSV TVDGVVIGLC CCSKTKSSAV QLADGQVLKY LWESPSSAVE PWKNSEGRPV
     RFARPCTQME AAAIGGEECV LGLTDRCRFF INDTEVASNI TSFAVCDDFL LVTTHSHTCQ
     CFSLSGASLK MLQAGLCGSQ VPSGEILRKV ERGSRIVTVV PQDTKLILQM PRGNLEVVHH
     RALVLAQIRK WLDKLMFKEA FECMRKLRIN LNLIHDHNPK VFLENVETFI KQIDSVNHLN
     LFFTELKEED VTKTMYPPPV TKSVQVSTNP DGKKVDLICD AMRVAMETIN PRKFCLSILT
     SHVKKTTPEL DIVLQKVHEL QGKIPFVPES VSAEEALKYL LLLVDVNELF NHSLGTYDFD
     LVLMVAEKSQ KDPKEYLPFL NTLKKMETNY QRFTIDKYLK RYEKALGHLS KCGPEYFTEC
     LNLIKDKNLY KEALKLYRPD SPQYQAVSVA YGEHLVQELL YEPAGLVFAR CGAHEKALEA
     FLACGSWQQA LCMAAQLQMA KDKVAGLART LAGKLVEQRK HSEAATVLEQ YALDYEEAVL
     LLLEGSAWEE ALRLVYKYDR VDIIETSVKP SILEAQKNYM DFLDSQTATF IRHKNRLKVV
     RELKSQRPRV HVDHEVAHGR ETDLFSETSS IRSGSEMSGR YSHSNSRISA RSSKNRRKAE
     RKKHSLKEGS PLEGLALLEA LSEVVQSIEK LKDEVHAILK VLFLFEFEEQ ARELQRAFES
     TLQLMGTALP DIWTLTGQQS SSTPVLGPSS TVNSIMASYQ QQKTCVPVLD AWACLPPKID
     QRSQWKLSLL E