ELP1_HUMAN
ID ELP1_HUMAN Reviewed; 1332 AA.
AC O95163; Q5JSV2; Q9H327; Q9UG87;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Elongator complex protein 1;
DE Short=ELP1;
DE AltName: Full=IkappaB kinase complex-associated protein {ECO:0000303|PubMed:9751059};
DE Short=IKK complex-associated protein {ECO:0000303|PubMed:9751059};
DE AltName: Full=p150;
GN Name=ELP1 {ECO:0000312|HGNC:HGNC:5959};
GN Synonyms=IKAP {ECO:0000303|PubMed:9751059}, IKBKAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND VARIANT
RP LYS-312.
RC TISSUE=Cervix carcinoma;
RX PubMed=9751059; DOI=10.1038/26254;
RA Cohen L., Henzel W.J., Baeuerle P.A.;
RT "IKAP is a scaffold protein of the IkappaB kinase complex.";
RL Nature 395:292-296(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT HSAN3 PRO-696, AND VARIANT SER-1072.
RX PubMed=11179008; DOI=10.1086/318810;
RA Slaugenhaupt S.A., Blumenfeld A., Gill S.P., Leyne M., Mull J.,
RA Cuajungco M.P., Liebert C.B., Chadwick B.P., Idelson M., Reznik L.,
RA Robbins C.M., Makalowska I., Brownstein M.J., Krappmann D., Scheidereit C.,
RA Maayan C., Axelrod F.B., Gusella J.F.;
RT "Tissue-specific expression of a splicing mutation in the IKBKAP gene
RT causes familial dysautonomia.";
RL Am. J. Hum. Genet. 68:598-605(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 961-1332, AND VARIANTS SER-1072
RP AND LEU-1158.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION IN THE ELONGATOR COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11714725; DOI=10.1074/jbc.m110445200;
RA Hawkes N.A., Otero G., Winkler G.S., Marshall N., Dahmus M.E.,
RA Krappmann D., Scheidereit C., Thomas C.L., Schiavo G.,
RA Erdjument-Bromage H., Tempst P., Svejstrup J.Q.;
RT "Purification and characterization of the human elongator complex.";
RL J. Biol. Chem. 277:3047-3052(2002).
RN [8]
RP IDENTIFICATION IN THE ELONGATOR COMPLEX, INTERACTION WITH ELP3, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11818576; DOI=10.1073/pnas.251672198;
RA Kim J.H., Lane W.S., Reinberg D.;
RT "Human Elongator facilitates RNA polymerase II transcription through
RT chromatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1241-1246(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-867; SER-1171 AND SER-1174,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-867, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION IN THE ELONGATOR COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=22854966; DOI=10.1074/jbc.m112.402727;
RA Close P., Gillard M., Ladang A., Jiang Z., Papuga J., Hawkes N., Nguyen L.,
RA Chapelle J.P., Bouillenne F., Svejstrup J., Fillet M., Chariot A.;
RT "DERP6 (ELP5) and C3ORF75 (ELP6) regulate tumorigenicity and migration of
RT melanoma cells as subunits of Elongator.";
RL J. Biol. Chem. 287:32535-32545(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-804 AND SER-867, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INTERACTION WITH ELP2 AND ELP3.
RX PubMed=25960406; DOI=10.1016/j.str.2015.03.018;
RA Dong C., Lin Z., Diao W., Li D., Chu X., Wang Z., Zhou H., Xie Z., Shen Y.,
RA Long J.;
RT "The Elp2 subunit is essential for elongator complex assembly and
RT functional regulation.";
RL Structure 23:1078-1086(2015).
RN [16]
RP REVIEW.
RX PubMed=29332244; DOI=10.1007/s00018-018-2747-6;
RA Dalwadi U., Yip C.K.;
RT "Structural insights into the function of Elongator.";
RL Cell. Mol. Life Sci. 75:1613-1622(2018).
RN [17] {ECO:0007744|PDB:5CQR}
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 715-1332, SUBUNIT, IDENTIFICATION
RP IN THE ELONGATOR COMPLEX, DIMERIZATION REGION, CHARACTERIZATION OF VARIANTS
RP PRO-696; LEU-914; SER-1072 AND LEU-1158, AND MUTAGENESIS OF ARG-1011.
RX PubMed=26261306; DOI=10.1073/pnas.1502597112;
RA Xu H., Lin Z., Li F., Diao W., Dong C., Zhou H., Xie X., Wang Z., Shen Y.,
RA Long J.;
RT "Dimerization of elongator protein 1 is essential for Elongator complex
RT assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:10697-10702(2015).
RN [18]
RP VARIANT HSAN3 PRO-696, AND EFFECT ON PHOSPHORYLATION.
RX PubMed=11179021; DOI=10.1086/318808;
RA Anderson S.L., Coli R., Daly I.W., Kichula E.A., Rork M.J., Volpi S.A.,
RA Ekstein J., Rubin B.Y.;
RT "Familial dysautonomia is caused by mutations of the IKAP gene.";
RL Am. J. Hum. Genet. 68:753-758(2001).
RN [19]
RP VARIANT HSAN3 LEU-914.
RX PubMed=12687659; DOI=10.1002/ajmg.a.20052;
RA Leyne M., Mull J., Gill S.P., Cuajungco M.P., Oddoux C., Blumenfeld A.,
RA Maayan C., Gusella J.F., Axelrod F.B., Slaugenhaupt S.A.;
RT "Identification of the first non-Jewish mutation in familial
RT Dysautonomia.";
RL Am. J. Med. Genet. A 118A:305-308(2003).
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) (PubMed:29332244). The elongator complex
CC catalyzes the formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (PubMed:29332244). 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)
CC (PubMed:9751059). {ECO:0000250|UniProtKB:Q06706,
CC ECO:0000250|UniProtKB:Q7TT37, ECO:0000269|PubMed:9751059,
CC ECO:0000303|PubMed:29332244}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000303|PubMed:29332244}.
CC -!- SUBUNIT: Homodimer; dimerization promotes ELP1 stability and elongator
CC complex formation (PubMed:26261306). Component of the elongator complex
CC which consists of ELP1, ELP2, ELP3, ELP4, ELP5 and ELP6
CC (PubMed:11714725, PubMed:11818576, PubMed:22854966, PubMed:11818576,
CC PubMed:26261306, PubMed:25960406). Interacts preferentially with
CC MAP3K14/NIK followed by IKK-alpha and IKK-beta (PubMed:9751059).
CC {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576,
CC ECO:0000269|PubMed:22854966, ECO:0000269|PubMed:26261306,
CC ECO:0000269|PubMed:9751059}.
CC -!- INTERACTION:
CC O95163; Q9H9T3: ELP3; NbExp=8; IntAct=EBI-347559, EBI-355217;
CC O95163; P42858: HTT; NbExp=4; IntAct=EBI-347559, EBI-466029;
CC O95163; Q15306: IRF4; NbExp=2; IntAct=EBI-347559, EBI-751345;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11714725,
CC ECO:0000269|PubMed:11818576, ECO:0000269|PubMed:22854966}. Nucleus
CC {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576}.
CC -!- DISEASE: Neuropathy, hereditary sensory and autonomic, 3 (HSAN3)
CC [MIM:223900]: A form of hereditary sensory and autonomic neuropathy, a
CC genetically and clinically heterogeneous group of disorders
CC characterized by degeneration of dorsal root and autonomic ganglion
CC cells, and by sensory and/or autonomic abnormalities. HSAN3 patients
CC manifest a variety of symptoms such as alacrima, decreased taste,
CC decreased sensitivity to pain and temperature, vasomotor instability,
CC hypoactive or absent deep tendon reflexes, vomiting crises, and
CC gastrointestinal dysfunction. {ECO:0000269|PubMed:11179008,
CC ECO:0000269|PubMed:11179021, ECO:0000269|PubMed:12687659}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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:0000305|PubMed:11714725,
CC ECO:0000305|PubMed:11818576, ECO:0000305|PubMed:29332244}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43219.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF044195; AAC64258.1; -; mRNA.
DR EMBL; AF153419; AAG43369.1; -; mRNA.
DR EMBL; AK001641; BAG50955.1; -; mRNA.
DR EMBL; AK289962; BAF82651.1; -; mRNA.
DR EMBL; AL354797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW59027.1; -; Genomic_DNA.
DR EMBL; AL049945; CAB43219.1; ALT_FRAME; mRNA.
DR CCDS; CCDS6773.1; -.
DR RefSeq; NP_001305289.1; NM_001318360.1.
DR RefSeq; NP_003631.2; NM_003640.4.
DR PDB; 5CQR; X-ray; 3.02 A; A=715-1332.
DR PDBsum; 5CQR; -.
DR AlphaFoldDB; O95163; -.
DR SMR; O95163; -.
DR BioGRID; 114090; 136.
DR ComplexPortal; CPX-1949; Elongator holoenzyme complex.
DR CORUM; O95163; -.
DR DIP; DIP-27579N; -.
DR IntAct; O95163; 54.
DR MINT; O95163; -.
DR STRING; 9606.ENSP00000363779; -.
DR GlyGen; O95163; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95163; -.
DR MetOSite; O95163; -.
DR PhosphoSitePlus; O95163; -.
DR BioMuta; ELP1; -.
DR EPD; O95163; -.
DR jPOST; O95163; -.
DR MassIVE; O95163; -.
DR MaxQB; O95163; -.
DR PaxDb; O95163; -.
DR PeptideAtlas; O95163; -.
DR PRIDE; O95163; -.
DR ProteomicsDB; 50677; -.
DR Antibodypedia; 14913; 273 antibodies from 32 providers.
DR DNASU; 8518; -.
DR Ensembl; ENST00000374647.10; ENSP00000363779.5; ENSG00000070061.16.
DR Ensembl; ENST00000675406.1; ENSP00000501893.1; ENSG00000070061.16.
DR GeneID; 8518; -.
DR KEGG; hsa:8518; -.
DR MANE-Select; ENST00000374647.10; ENSP00000363779.5; NM_003640.5; NP_003631.2.
DR UCSC; uc004bdm.5; human.
DR CTD; 8518; -.
DR DisGeNET; 8518; -.
DR GeneCards; ELP1; -.
DR GeneReviews; ELP1; -.
DR HGNC; HGNC:5959; ELP1.
DR HPA; ENSG00000070061; Low tissue specificity.
DR MalaCards; ELP1; -.
DR MIM; 223900; phenotype.
DR MIM; 603722; gene.
DR neXtProt; NX_O95163; -.
DR OpenTargets; ENSG00000070061; -.
DR Orphanet; 1764; Familial dysautonomia.
DR PharmGKB; PA29775; -.
DR VEuPathDB; HostDB:ENSG00000070061; -.
DR eggNOG; KOG1920; Eukaryota.
DR GeneTree; ENSGT00390000013344; -.
DR HOGENOM; CLU_001477_1_0_1; -.
DR InParanoid; O95163; -.
DR OMA; DMNILHD; -.
DR OrthoDB; 180136at2759; -.
DR PhylomeDB; O95163; -.
DR TreeFam; TF300402; -.
DR PathwayCommons; O95163; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; O95163; -.
DR SIGNOR; O95163; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 8518; 641 hits in 1061 CRISPR screens.
DR ChiTaRS; IKBKAP; human.
DR GenomeRNAi; 8518; -.
DR Pharos; O95163; Tbio.
DR PRO; PR:O95163; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O95163; protein.
DR Bgee; ENSG00000070061; Expressed in adrenal tissue and 203 other tissues.
DR ExpressionAtlas; O95163; baseline and differential.
DR Genevisible; O95163; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IC:ComplexPortal.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 1.
DR IDEAL; IID00644; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Disease variant;
KW Neurodegeneration; Neuropathy; Nucleus; Phosphoprotein; Reference proteome;
KW tRNA processing.
FT CHAIN 1..1332
FT /note="Elongator complex protein 1"
FT /id="PRO_0000084177"
FT REGION 885..1332
FT /note="Mediates dimerization"
FT /evidence="ECO:0000269|PubMed:26261306"
FT REGION 1150..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1209
FT /note="Required for binding to tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06706"
FT COMPBIAS 1163..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 70
FT /note="R -> C (in dbSNP:rs3737311)"
FT /id="VAR_047476"
FT VARIANT 182
FT /note="M -> K (in dbSNP:rs10521092)"
FT /id="VAR_047477"
FT VARIANT 312
FT /note="E -> K (in dbSNP:rs1140064)"
FT /evidence="ECO:0000269|PubMed:9751059"
FT /id="VAR_047478"
FT VARIANT 525
FT /note="R -> Q (in dbSNP:rs838827)"
FT /id="VAR_047479"
FT VARIANT 696
FT /note="R -> P (in HSAN3; mild phenotype; phosphorylation is
FT reduced; does not affect interaction with ELP2; reduced
FT interaction with ELP3; does not affect dimerization;
FT dbSNP:rs137853022)"
FT /evidence="ECO:0000269|PubMed:11179008,
FT ECO:0000269|PubMed:11179021, ECO:0000269|PubMed:26261306"
FT /id="VAR_011327"
FT VARIANT 765
FT /note="G -> E (in dbSNP:rs2230792)"
FT /id="VAR_047480"
FT VARIANT 816
FT /note="I -> L (in dbSNP:rs2230793)"
FT /id="VAR_047481"
FT VARIANT 830
FT /note="I -> M (in dbSNP:rs2230794)"
FT /id="VAR_047482"
FT VARIANT 848
FT /note="T -> N (in dbSNP:rs10979599)"
FT /id="VAR_047483"
FT VARIANT 914
FT /note="P -> L (in HSAN3; reduced interaction with ELP2;
FT does not affect interaction with ELP3; does not affect
FT dimerization)"
FT /evidence="ECO:0000269|PubMed:12687659,
FT ECO:0000269|PubMed:26261306"
FT /id="VAR_085681"
FT VARIANT 952
FT /note="K -> I (in dbSNP:rs2230798)"
FT /id="VAR_047484"
FT VARIANT 1013
FT /note="G -> S (in dbSNP:rs2230795)"
FT /id="VAR_047485"
FT VARIANT 1072
FT /note="C -> S (reduced interaction with ELP2; does not
FT affect interaction with ELP3; does not affect dimerization;
FT dbSNP:rs3204145)"
FT /evidence="ECO:0000269|PubMed:11179008,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:26261306"
FT /id="VAR_047486"
FT VARIANT 1158
FT /note="P -> L (reduced interaction with ELP2; does not
FT affect interaction with ELP3; does not affect dimerization;
FT dbSNP:rs1538660)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:26261306"
FT /id="VAR_047487"
FT MUTAGEN 1011
FT /note="R->A: Disruption of dimer formation, reduced protein
FT stability and reduced interaction with ELP2 and ELP3. Does
FT not affect binding to tRNA."
FT /evidence="ECO:0000269|PubMed:26261306"
FT CONFLICT 304
FT /note="W -> R (in Ref. 1; AAC64258)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="L -> P (in Ref. 1; AAC64258)"
FT /evidence="ECO:0000305"
FT CONFLICT 961
FT /note="C -> G (in Ref. 6; CAB43219)"
FT /evidence="ECO:0000305"
FT CONFLICT 1320
FT /note="I -> V (in Ref. 6; CAB43219)"
FT /evidence="ECO:0000305"
FT HELIX 723..734
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 738..747
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 754..757
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 760..763
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 767..773
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 777..786
FT /evidence="ECO:0007829|PDB:5CQR"
FT TURN 792..796
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 815..830
FT /evidence="ECO:0007829|PDB:5CQR"
FT TURN 832..835
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 836..844
FT /evidence="ECO:0007829|PDB:5CQR"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 851..860
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 868..870
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 874..882
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 887..894
FT /evidence="ECO:0007829|PDB:5CQR"
FT TURN 895..897
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 900..908
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 918..924
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 929..939
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 943..950
FT /evidence="ECO:0007829|PDB:5CQR"
FT STRAND 955..957
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 958..967
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 971..975
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 983..997
FT /evidence="ECO:0007829|PDB:5CQR"
FT TURN 998..1000
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1002..1011
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1015..1024
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1028..1036
FT /evidence="ECO:0007829|PDB:5CQR"
FT TURN 1037..1039
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1042..1057
FT /evidence="ECO:0007829|PDB:5CQR"
FT TURN 1058..1060
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1062..1072
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1076..1085
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1089..1097
FT /evidence="ECO:0007829|PDB:5CQR"
FT TURN 1098..1100
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1103..1107
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1109..1126
FT /evidence="ECO:0007829|PDB:5CQR"
FT TURN 1127..1130
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1233..1245
FT /evidence="ECO:0007829|PDB:5CQR"
FT HELIX 1249..1264
FT /evidence="ECO:0007829|PDB:5CQR"
SQ SEQUENCE 1332 AA; 150254 MW; 5BAC580433CC8641 CRC64;
MRNLKLFRTL EFRDIQGPGN PQCFSLRTEQ GTVLIGSEHG LIEVDPVSRE VKNEVSLVAE
GFLPEDGSGR IVGVQDLLDQ ESVCVATASG DVILCSLSTQ QLECVGSVAS GISVMSWSPD
QELVLLATGQ QTLIMMTKDF EPILEQQIHQ DDFGESKFIT VGWGRKETQF HGSEGRQAAF
QMQMHESALP WDDHRPQVTW RGDGQFFAVS VVCPETGARK VRVWNREFAL QSTSEPVAGL
GPALAWKPSG SLIASTQDKP NQQDIVFFEK NGLLHGHFTL PFLKDEVKVN DLLWNADSSV
LAVWLEDLQR EESSIPKTCV QLWTVGNYHW YLKQSLSFST CGKSKIVSLM WDPVTPYRLH
VLCQGWHYLA YDWHWTTDRS VGDNSSDLSN VAVIDGNRVL VTVFRQTVVP PPMCTYQLLF
PHPVNQVTFL AHPQKSNDLA VLDASNQISV YKCGDCPSAD PTVKLGAVGG SGFKVCLRTP
HLEKRYKIQF ENNEDQDVNP LKLGLLTWIE EDVFLAVSHS EFSPRSVIHH LTAASSEMDE
EHGQLNVSSS AAVDGVIISL CCNSKTKSVV LQLADGQIFK YLWESPSLAI KPWKNSGGFP
VRFPYPCTQT ELAMIGEEEC VLGLTDRCRF FINDIEVASN ITSFAVYDEF LLLTTHSHTC
QCFCLRDASF KTLQAGLSSN HVSHGEVLRK VERGSRIVTV VPQDTKLVLQ MPRGNLEVVH
HRALVLAQIR KWLDKLMFKE AFECMRKLRI NLNLIYDHNP KVFLGNVETF IKQIDSVNHI
NLFFTELKEE DVTKTMYPAP VTSSVYLSRD PDGNKIDLVC DAMRAVMESI NPHKYCLSIL
TSHVKKTTPE LEIVLQKVHE LQGNAPSDPD AVSAEEALKY LLHLVDVNEL YDHSLGTYDF
DLVLMVAEKS QKDPKEYLPF LNTLKKMETN YQRFTIDKYL KRYEKAIGHL SKCGPEYFPE
CLNLIKDKNL YNEALKLYSP SSQQYQDISI AYGEHLMQEH MYEPAGLMFA RCGAHEKALS
AFLTCGNWKQ ALCVAAQLNF TKDQLVGLGR TLAGKLVEQR KHIDAAMVLE ECAQDYEEAV
LLLLEGAAWE EALRLVYKYN RLDIIETNVK PSILEAQKNY MAFLDSQTAT FSRHKKRLLV
VRELKEQAQQ AGLDDEVPHG QESDLFSETS SVVSGSEMSG KYSHSNSRIS ARSSKNRRKA
ERKKHSLKEG SPLEDLALLE ALSEVVQNTE NLKDEVYHIL KVLFLFEFDE QGRELQKAFE
DTLQLMERSL PEIWTLTYQQ NSATPVLGPN STANSIMASY QQQKTSVPVL DAELFIPPKI
NRRTQWKLSL LD
