ID ELOA1_HUMAN Reviewed; 772 AA. AC Q14241; B2R7Q8; Q8IXH1; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 3. DT 27-MAR-2024, entry version 206. DE RecName: Full=Elongin-A {ECO:0000305}; DE Short=EloA; DE AltName: Full=Elongin 110 kDa subunit; DE AltName: Full=RNA polymerase II transcription factor SIII subunit A1; DE AltName: Full=SIII p110; DE AltName: Full=Transcription elongation factor B polypeptide 3; GN Name=ELOA {ECO:0000312|HGNC:HGNC:11620}; Synonyms=TCEB3; GN ORFNames=MSTP059; 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] (ISOFORM 2), AND FUNCTION. RC TISSUE=Umbilical vein; RX PubMed=8654961; DOI=10.1016/0378-1119(95)00750-4; RA Aso T., Haque D., Fukudome K., Brower C.S., Conaway J.W., Conaway R.C.; RT "A human cDNA encoding the 110-kDa A subunit of RNA polymerase II RT transcription factor elongin."; RL Gene 168:277-278(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-772 (ISOFORMS 1/2). RC TISSUE=Heart; RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L., Zhao Y., RA Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, AND IDENTIFICATION IN COMPLEX WITH CUL5; ELOB; ELOC AND RBX1. RX PubMed=19920177; DOI=10.1073/pnas.0907052106; RA Harreman M., Taschner M., Sigurdsson S., Anindya R., Reid J., Somesh B., RA Kong S.E., Banks C.A., Conaway R.C., Conaway J.W., Svejstrup J.Q.; RT "Distinct ubiquitin ligases act sequentially for RNA polymerase II RT polyubiquitylation."; RL Proc. Natl. Acad. Sci. U.S.A. 106:20705-20710(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND THR-394, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND SER-387, AND RP IDENTIFICATION BY 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 [10] 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND SER-516, 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 [13] RP SUBCELLULAR LOCATION. RX PubMed=35633597; DOI=10.1016/j.dnarep.2022.103343; RA Herlihy A.E., Boeing S., Weems J.C., Walker J., Dirac-Svejstrup A.B., RA Lehner M.H., Conaway R.C., Conaway J.W., Svejstrup J.Q.; RT "UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA polymerase II and RT are the human orthologues of yeast Def1."; RL DNA Repair 115:103343-103343(2022). CC -!- FUNCTION: SIII, also known as elongin, is a general transcription CC elongation factor that increases the RNA polymerase II transcription CC elongation past template-encoded arresting sites. Subunit A is CC transcriptionally active and its transcription activity is strongly CC enhanced by binding to the dimeric complex of the SIII regulatory CC subunits B and C (elongin BC complex). {ECO:0000269|PubMed:8654961}. CC -!- FUNCTION: As part of a multisubunit complex composed of elongin BC CC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; CC polyubiquitinates monoubiquitinated POLR2A. CC {ECO:0000269|PubMed:19920177}. CC -!- SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC CC subunit (By similarity). Part of a multisubunit ubiquitin ligase CC complex consisting of elongin BC complex (ELOB and ELOC), elongin CC A/ELOA, RBX1 and CUL5 (PubMed:19920177). Interacts with ERCC6; the CC interaction is induced by DNA damaging agents or inhibitors of RNA CC polymerase II elongation (By similarity). Interacts (via BC-box) with CC CUL5 (By similarity). {ECO:0000250|UniProtKB:Q63187, CC ECO:0000269|PubMed:19920177}. CC -!- INTERACTION: CC Q14241; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-742350, EBI-4400025; CC Q14241; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-742350, EBI-1642333; CC Q14241; Q8NA61: CBY2; NbExp=3; IntAct=EBI-742350, EBI-741724; CC Q14241; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-742350, EBI-10961624; CC Q14241; Q86X02: CDR2L; NbExp=3; IntAct=EBI-742350, EBI-11063830; CC Q14241; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-742350, EBI-10181988; CC Q14241; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-742350, EBI-739624; CC Q14241; Q8N137: CNTROB; NbExp=3; IntAct=EBI-742350, EBI-947360; CC Q14241; O60447: EVI5; NbExp=3; IntAct=EBI-742350, EBI-852291; CC Q14241; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-742350, EBI-10175124; CC Q14241; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-742350, EBI-11977403; CC Q14241; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-742350, EBI-10172181; CC Q14241; P51114-2: FXR1; NbExp=3; IntAct=EBI-742350, EBI-11022345; CC Q14241; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-742350, EBI-2548508; CC Q14241; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-742350, EBI-11163335; CC Q14241; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-742350, EBI-717919; CC Q14241; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-742350, EBI-10172004; CC Q14241; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-742350, EBI-752007; CC Q14241; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-742350, EBI-2556193; CC Q14241; O95198: KLHL2; NbExp=3; IntAct=EBI-742350, EBI-746999; CC Q14241; Q6A162: KRT40; NbExp=3; IntAct=EBI-742350, EBI-10171697; CC Q14241; Q9BQD3: KXD1; NbExp=3; IntAct=EBI-742350, EBI-739657; CC Q14241; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-742350, EBI-1216080; CC Q14241; P23508: MCC; NbExp=3; IntAct=EBI-742350, EBI-307531; CC Q14241; Q99750: MDFI; NbExp=6; IntAct=EBI-742350, EBI-724076; CC Q14241; O15344: MID1; NbExp=3; IntAct=EBI-742350, EBI-2340316; CC Q14241; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-742350, EBI-10172526; CC Q14241; Q15742: NAB2; NbExp=3; IntAct=EBI-742350, EBI-8641936; CC Q14241; Q96RE7: NACC1; NbExp=3; IntAct=EBI-742350, EBI-7950997; CC Q14241; Q96HR8: NAF1; NbExp=3; IntAct=EBI-742350, EBI-2515597; CC Q14241; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-742350, EBI-10271199; CC Q14241; O15055: PER2; NbExp=3; IntAct=EBI-742350, EBI-1054296; CC Q14241; O00444: PLK4; NbExp=6; IntAct=EBI-742350, EBI-746202; CC Q14241; Q13136: PPFIA1; NbExp=3; IntAct=EBI-742350, EBI-745426; CC Q14241; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-742350, EBI-11320284; CC Q14241; O14744: PRMT5; NbExp=3; IntAct=EBI-742350, EBI-351098; CC Q14241; Q15276: RABEP1; NbExp=3; IntAct=EBI-742350, EBI-447043; CC Q14241; Q69YQ0: SPECC1L; NbExp=3; IntAct=EBI-742350, EBI-351113; CC Q14241; Q15025: TNIP1; NbExp=3; IntAct=EBI-742350, EBI-357849; CC Q14241; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-742350, EBI-11952721; CC Q14241; O94972: TRIM37; NbExp=3; IntAct=EBI-742350, EBI-741602; CC Q14241; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-742350, EBI-2130429; CC Q14241; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-742350, EBI-10240849; CC Q14241; P0DTC9: N; Xeno; NbExp=3; IntAct=EBI-742350, EBI-25475856; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35633597}. CC Note=Localizes to sites of DNA damage. {ECO:0000269|PubMed:35633597}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=2; CC IsoId=Q14241-2; Sequence=Displayed; CC Name=1; CC IsoId=Q14241-1; Sequence=VSP_062177; CC -!- DOMAIN: The BC-box, which mediates binding to the elongin BC complex, CC has the consensus sequence [APST]-L-x(3)-C-x(3)-[AILV]. CC {ECO:0000250|UniProtKB:Q63187}. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative initiation CC (Probable). Based on proteomic data (Probable). {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO15305.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; L47345; AAA75492.1; -; mRNA. DR EMBL; AK313079; BAG35905.1; -; mRNA. DR EMBL; AL031295; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471134; EAW95070.1; -; Genomic_DNA. DR EMBL; BC002883; AAH02883.1; -; mRNA. DR EMBL; AF116729; AAO15305.1; ALT_INIT; mRNA. DR PIR; JC4636; JC4636. DR RefSeq; NP_003189.2; NM_003198.2. [Q14241-2] DR PDB; 4HFX; X-ray; 2.54 A; A/B/C/D=571-656. DR PDB; 6ZUZ; NMR; -; A=1-82. DR PDB; 8OEV; EM; 2.86 A; M=1-772. DR PDB; 8OEW; EM; 2.80 A; M=1-772. DR PDB; 8OF0; EM; 3.05 A; M=1-772. DR PDBsum; 4HFX; -. DR PDBsum; 6ZUZ; -. DR PDBsum; 8OEV; -. DR PDBsum; 8OEW; -. DR PDBsum; 8OF0; -. DR AlphaFoldDB; Q14241; -. DR EMDB; EMD-16832; -. DR EMDB; EMD-16833; -. DR EMDB; EMD-16837; -. DR EMDB; EMD-16838; -. DR EMDB; EMD-16840; -. DR SMR; Q14241; -. DR BioGRID; 112786; 232. DR IntAct; Q14241; 69. DR MINT; Q14241; -. DR STRING; 9606.ENSP00000395574; -. DR GlyCosmos; Q14241; 1 site, 1 glycan. DR GlyGen; Q14241; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q14241; -. DR PhosphoSitePlus; Q14241; -. DR BioMuta; ELOA; -. DR DMDM; 294862430; -. DR EPD; Q14241; -. DR jPOST; Q14241; -. DR MassIVE; Q14241; -. DR MaxQB; Q14241; -. DR PaxDb; 9606-ENSP00000395574; -. DR PeptideAtlas; Q14241; -. DR ProteomicsDB; 59938; -. DR Pumba; Q14241; -. DR Antibodypedia; 1742; 414 antibodies from 32 providers. DR DNASU; 6924; -. DR Ensembl; ENST00000613537.5; ENSP00000484196.2; ENSG00000011007.13. [Q14241-2] DR GeneID; 6924; -. DR KEGG; hsa:6924; -. DR MANE-Select; ENST00000613537.5; ENSP00000484196.2; NM_003198.3; NP_003189.3. DR UCSC; uc001bho.4; human. [Q14241-2] DR AGR; HGNC:11620; -. DR CTD; 6924; -. DR DisGeNET; 6924; -. DR GeneCards; ELOA; -. DR HGNC; HGNC:11620; ELOA. DR HPA; ENSG00000011007; Low tissue specificity. DR MIM; 600786; gene. DR neXtProt; NX_Q14241; -. DR OpenTargets; ENSG00000011007; -. DR PharmGKB; PA36379; -. DR VEuPathDB; HostDB:ENSG00000011007; -. DR eggNOG; KOG2821; Eukaryota. DR GeneTree; ENSGT00390000002428; -. DR InParanoid; Q14241; -. DR OMA; RKHEFVG; -. DR OrthoDB; 4793at2759; -. DR PhylomeDB; Q14241; -. DR TreeFam; TF317259; -. DR PathwayCommons; Q14241; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat. DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat. DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation. DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery. DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript. DR Reactome; R-HSA-167287; HIV elongation arrest and recovery. DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR SignaLink; Q14241; -. DR BioGRID-ORCS; 6924; 63 hits in 1215 CRISPR screens. DR ChiTaRS; TCEB3; human. DR GeneWiki; TCEB3; -. DR GenomeRNAi; 6924; -. DR Pharos; Q14241; Tbio. DR PRO; PR:Q14241; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q14241; Protein. DR Bgee; ENSG00000011007; Expressed in buccal mucosa cell and 214 other cell types or tissues. DR ExpressionAtlas; Q14241; baseline and differential. DR GO; GO:0070449; C:elongin complex; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:InterPro. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:UniProtKB. DR CDD; cd00183; TFIIS_I; 1. DR Gene3D; 6.10.250.3180; -; 1. DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR010684; RNA_pol_II_trans_fac_SIII_A. DR InterPro; IPR003617; TFIIS/CRSP70_N_sub. DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf. DR InterPro; IPR017923; TFIIS_N. DR PANTHER; PTHR15141:SF75; ELONGIN-A; 1. DR PANTHER; PTHR15141; TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 3; 1. DR Pfam; PF06881; Elongin_A; 1. DR Pfam; PF08711; Med26; 1. DR SMART; SM00509; TFS2N; 1. DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1. DR PROSITE; PS50181; FBOX; 1. DR PROSITE; PS51319; TFIIS_N; 1. DR Genevisible; Q14241; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..772 FT /note="Elongin-A" FT /id="PRO_0000086960" FT DOMAIN 4..79 FT /note="TFIIS N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649" FT DOMAIN 566..610 FT /note="F-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080" FT REGION 79..403 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 418..466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 522..681 FT /note="Activation domain" FT /evidence="ECO:0000250|UniProtKB:Q63187" FT REGION 550..559 FT /note="BC-box" FT /evidence="ECO:0000250|UniProtKB:Q63187" FT REGION 674..732 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 79..113 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 131..163 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 164..186 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 192..207 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 225..311 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 322..346 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 366..393 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63187" FT MOD_RES 384 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 387 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 394 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 434 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CB77" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1 FT /note="M -> MHGGRSCGPRTRREPSSGEEAAPVTAM (in isoform 1)" FT /id="VSP_062177" FT VARIANT 119 FT /note="T -> M (in dbSNP:rs2235541)" FT /id="VAR_020104" FT VARIANT 298 FT /note="V -> I (in dbSNP:rs520713)" FT /id="VAR_033850" FT VARIANT 490 FT /note="A -> V (in dbSNP:rs550252)" FT /id="VAR_033851" FT HELIX 32..44 FT /evidence="ECO:0007829|PDB:6ZUZ" FT HELIX 49..60 FT /evidence="ECO:0007829|PDB:6ZUZ" FT HELIX 66..72 FT /evidence="ECO:0007829|PDB:6ZUZ" FT HELIX 74..81 FT /evidence="ECO:0007829|PDB:6ZUZ" FT HELIX 85..98 FT /evidence="ECO:0007829|PDB:6ZUZ" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:6ZUZ" FT HELIX 607..609 FT /evidence="ECO:0007829|PDB:4HFX" FT HELIX 612..619 FT /evidence="ECO:0007829|PDB:4HFX" FT HELIX 623..625 FT /evidence="ECO:0007829|PDB:4HFX" FT HELIX 630..636 FT /evidence="ECO:0007829|PDB:4HFX" FT STRAND 648..650 FT /evidence="ECO:0007829|PDB:4HFX" FT HELIX 652..671 FT /evidence="ECO:0007829|PDB:4HFX" SQ SEQUENCE 772 AA; 87230 MW; 0D2C93B1D54EB09A CRC64; MAAESALQVV EKLQARLAAN PDPKKLLKYL KKLSTLPITV DILAETGVGK TVNSLRKHEH VGSFARDLVA QWKKLVPVER NAEPDEQDFE KSNSRKRPRD ALQKEEEMEG DYQETWKATG SRSYSPDHRQ KKHRKLSELE RPHKVSHGHE RRDERKRCHR MSPTYSSDPE SSDYGHVQSP PSCTSPHQMY VDHYRSLEED QEPIVSHQKP GKGHSNAFQD RLGASQERHL GEPHGKGVVS QNKEHKSSHK DKRPVDAKSD EKASVVSREK SHKALSKEEN RRPPSGDNAR EKPPSSGVKK EKDREGSSLK KKCLPPSEAA SDNHLKKPKH RDPEKAKLDK SKQGLDSFDT GKGAGDLLPK VKEKGSNNLK TPEGKVKTNL DRKSLGSLPK VEETDMEDEF EQPTMSFESY LSYDQPRKKK KKIVKTSATA LGDKGLKKND SKSTGKNLDS VQKLPKVNKT KSEKPAGADL AKLRKVPDVL PVLPDLPLPA IQANYRPLPS LELISSFQPK RKAFSSPQEE EEAGFTGRRM NSKMQVYSGS KCAYLPKMMT LHQQCIRVLK NNIDSIFEVG GVPYSVLEPV LERCTPDQLY RIEEYNHVLI EETDQLWKVH CHRDFKEERP EEYESWREMY LRLQDAREQR LRVLTKNIQF AHANKPKGRQ AKMAFVNSVA KPPRDVRRRQ EKFGTGGAAV PEKIKIKPAP YPMGSSHASA SSISFNPSPE EPAYDGPSTS SAHLAPVVSS TVSYDPRKPT VKKIAPMMAK TIKAFKNRFS RR //