ELOA1_HUMAN
ID ELOA1_HUMAN Reviewed; 798 AA.
AC Q14241; B2R7Q8; Q8IXH1;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Elongin-A;
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; 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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-798, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-798.
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 32-798.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND THR-420, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND SER-413, 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 [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND SER-542, 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).
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 -!- SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC
CC subunit (By similarity). Interacts with ERCC6; the interaction is
CC induced by DNA damaging agents or inhibitors of RNA polymerase II
CC elongation (By similarity). Interacts (via BC-box) with CUL5 (By
CC similarity). {ECO:0000250|UniProtKB:Q63187}.
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:0000305}.
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 -!- CAUTION: It is uncertain whether Met-1 or Met-27 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA75492.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH02883.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO15305.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG35905.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW95070.1; 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; AK313079; BAG35905.1; ALT_INIT; mRNA.
DR EMBL; DA333869; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL031295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW95070.1; ALT_INIT; Genomic_DNA.
DR EMBL; L47345; AAA75492.1; ALT_INIT; mRNA.
DR EMBL; BC002883; AAH02883.1; ALT_INIT; mRNA.
DR EMBL; AF116729; AAO15305.1; ALT_INIT; mRNA.
DR PIR; JC4636; JC4636.
DR RefSeq; NP_003189.2; NM_003198.2.
DR PDB; 4HFX; X-ray; 2.54 A; A/B/C/D=597-682.
DR PDB; 6ZUZ; NMR; -; A=26-108.
DR PDBsum; 4HFX; -.
DR PDBsum; 6ZUZ; -.
DR AlphaFoldDB; Q14241; -.
DR SMR; Q14241; -.
DR BioGRID; 112786; 195.
DR IntAct; Q14241; 68.
DR MINT; Q14241; -.
DR STRING; 9606.ENSP00000395574; -.
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; Q14241; -.
DR PeptideAtlas; Q14241; -.
DR PRIDE; Q14241; -.
DR ProteomicsDB; 59938; -.
DR Antibodypedia; 1742; 385 antibodies from 32 providers.
DR DNASU; 6924; -.
DR Ensembl; ENST00000418390.7; ENSP00000395574.3; ENSG00000011007.13.
DR Ensembl; ENST00000613537.5; ENSP00000484196.2; ENSG00000011007.13.
DR GeneID; 6924; -.
DR KEGG; hsa:6924; -.
DR UCSC; uc001bho.4; human.
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 PharmGKB; PA36379; -.
DR VEuPathDB; HostDB:ENSG00000011007; -.
DR eggNOG; KOG2821; Eukaryota.
DR InParanoid; Q14241; -.
DR OMA; MYIDHYR; -.
DR OrthoDB; 1174517at2759; -.
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; 58 hits in 1127 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 212 other tissues.
DR ExpressionAtlas; Q14241; baseline and differential.
DR Genevisible; Q14241; HS.
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 from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR Gene3D; 1.20.930.10; -; 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 Pfam; PF06881; Elongin_A; 1.
DR Pfam; PF08711; Med26; 1.
DR SMART; SM00509; TFS2N; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..798
FT /note="Elongin-A"
FT /id="PRO_0000086960"
FT DOMAIN 30..105
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 592..636
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..707
FT /note="Activation domain"
FT /evidence="ECO:0000250|UniProtKB:Q63187"
FT REGION 576..585
FT /note="BC-box"
FT /evidence="ECO:0000250|UniProtKB:Q63187"
FT REGION 700..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63187"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 420
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 460
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CB77"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 145
FT /note="T -> M (in dbSNP:rs2235541)"
FT /id="VAR_020104"
FT VARIANT 324
FT /note="V -> I (in dbSNP:rs520713)"
FT /id="VAR_033850"
FT VARIANT 516
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 798 AA; 89909 MW; 2C8FD8710E27EE46 CRC64;
MHGGRSCGPR TRREPSSGEE AAPVTAMAAE SALQVVEKLQ ARLAANPDPK KLLKYLKKLS
TLPITVDILA ETGVGKTVNS LRKHEHVGSF ARDLVAQWKK LVPVERNAEP DEQDFEKSNS
RKRPRDALQK EEEMEGDYQE TWKATGSRSY SPDHRQKKHR KLSELERPHK VSHGHERRDE
RKRCHRMSPT YSSDPESSDY GHVQSPPSCT SPHQMYVDHY RSLEEDQEPI VSHQKPGKGH
SNAFQDRLGA SQERHLGEPH GKGVVSQNKE HKSSHKDKRP VDAKSDEKAS VVSREKSHKA
LSKEENRRPP SGDNAREKPP SSGVKKEKDR EGSSLKKKCL PPSEAASDNH LKKPKHRDPE
KAKLDKSKQG LDSFDTGKGA GDLLPKVKEK GSNNLKTPEG KVKTNLDRKS LGSLPKVEET
DMEDEFEQPT MSFESYLSYD QPRKKKKKIV KTSATALGDK GLKKNDSKST GKNLDSVQKL
PKVNKTKSEK PAGADLAKLR KVPDVLPVLP DLPLPAIQAN YRPLPSLELI SSFQPKRKAF
SSPQEEEEAG FTGRRMNSKM QVYSGSKCAY LPKMMTLHQQ CIRVLKNNID SIFEVGGVPY
SVLEPVLERC TPDQLYRIEE YNHVLIEETD QLWKVHCHRD FKEERPEEYE SWREMYLRLQ
DAREQRLRVL TKNIQFAHAN KPKGRQAKMA FVNSVAKPPR DVRRRQEKFG TGGAAVPEKI
KIKPAPYPMG SSHASASSIS FNPSPEEPAY DGPSTSSAHL APVVSSTVSY DPRKPTVKKI
APMMAKTIKA FKNRFSRR
