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 27-MAR-2024, entry version 204. 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] RP INVOLVEMENT IN MDB. RX PubMed=32296180; DOI=10.1038/s41586-020-2164-5; RA Waszak S.M., Robinson G.W., Gudenas B.L., Smith K.S., Forget A., Kojic M., RA Garcia-Lopez J., Hadley J., Hamilton K.V., Indersie E., Buchhalter I., RA Kerssemakers J., Jaeger N., Sharma T., Rausch T., Kool M., Sturm D., RA Jones D.T.W., Vasilyeva A., Tatevossian R.G., Neale G., Lombard B., RA Loew D., Nakitandwe J., Rusch M., Bowers D.C., Bendel A., Partap S., RA Chintagumpala M., Crawford J., Gottardo N.G., Smith A., Dufour C., RA Rutkowski S., Eggen T., Wesenberg F., Kjaerheim K., Feychting M., RA Lannering B., Schuez J., Johansen C., Andersen T.V., Roeoesli M., RA Kuehni C.E., Grotzer M., Remke M., Puget S., Pajtler K.W., Milde T., RA Witt O., Ryzhova M., Korshunov A., Orr B.A., Ellison D.W., Brugieres L., RA Lichter P., Nichols K.E., Gajjar A., Wainwright B.J., Ayrault O., RA Korbel J.O., Northcott P.A., Pfister S.M.; RT "Germline Elongator mutations in Sonic Hedgehog medulloblastoma."; RL Nature 580:396-401(2020). RN [18] {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 [19] 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 [20] 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 -!- DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive CC embryonal tumor of the cerebellum with a preferential manifestation in CC children. {ECO:0000269|PubMed:32296180}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 175. DR ComplexPortal; CPX-1949; Elongator holoenzyme complex. DR CORUM; O95163; -. DR DIP; DIP-27579N; -. DR IntAct; O95163; 56. 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; 9606-ENSP00000363779; -. DR PeptideAtlas; O95163; -. DR ProteomicsDB; 50677; -. DR Pumba; O95163; -. DR Antibodypedia; 14913; 312 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 AGR; HGNC:5959; -. 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; 155255; phenotype. 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; WRESLYC; -. DR OrthoDB; 316709at2759; -. DR PhylomeDB; O95163; -. DR TreeFam; TF300402; -. DR BioCyc; MetaCyc:ENSG00000070061-MONOMER; -. DR PathwayCommons; O95163; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR SignaLink; O95163; -. DR SIGNOR; O95163; -. DR UniPathway; UPA00988; -. DR BioGRID-ORCS; 8518; 674 hits in 1139 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 205 other cell types or tissues. DR ExpressionAtlas; O95163; baseline and differential. 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; NAS: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; NAS:ComplexPortal. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR IDEAL; IID00644; -. DR InterPro; IPR006849; Elp1. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR PANTHER; PTHR12747; ELONGATOR COMPLEX PROTEIN 1; 1. DR PANTHER; PTHR12747:SF0; ELONGATOR COMPLEX PROTEIN 1; 1. DR Pfam; PF04762; IKI3; 1. DR PIRSF; PIRSF017233; IKAP; 1. DR SUPFAM; SSF69322; Tricorn protease domain 2; 1. DR Genevisible; O95163; HS. 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 //