ELOA1_MOUSE
ID ELOA1_MOUSE Reviewed; 773 AA.
AC Q8CB77; Q3UI38; Q80VB2; Q9R0Q5;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 162.
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|MGI:MGI:1351315}; Synonyms=Tceb3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10575222; DOI=10.1159/000015355;
RA Aso T., Amimoto K., Takebayashi S., Okumura K., Hatakeyama M.;
RT "Structural organization and chromosome location of the mouse elongin A
RT gene (Tceb3).";
RL Cytogenet. Cell Genet. 86:259-262(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-309 AND THR-390, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(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:0000250|UniProtKB:Q63187}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}.
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}.
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DR EMBL; AB025015; BAA84994.1; -; mRNA.
DR EMBL; AK036592; BAC29497.1; -; mRNA.
DR EMBL; AK145994; BAE26815.1; -; mRNA.
DR EMBL; AK147088; BAE27668.1; -; mRNA.
DR EMBL; AL672076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL29954.1; -; Genomic_DNA.
DR EMBL; BC049885; AAH49885.1; -; mRNA.
DR CCDS; CCDS18798.1; -.
DR RefSeq; NP_038764.2; NM_013736.4.
DR AlphaFoldDB; Q8CB77; -.
DR SMR; Q8CB77; -.
DR BioGRID; 205145; 7.
DR IntAct; Q8CB77; 3.
DR MINT; Q8CB77; -.
DR STRING; 10090.ENSMUSP00000030427; -.
DR iPTMnet; Q8CB77; -.
DR PhosphoSitePlus; Q8CB77; -.
DR EPD; Q8CB77; -.
DR jPOST; Q8CB77; -.
DR MaxQB; Q8CB77; -.
DR PaxDb; Q8CB77; -.
DR PeptideAtlas; Q8CB77; -.
DR PRIDE; Q8CB77; -.
DR ProteomicsDB; 275744; -.
DR Antibodypedia; 1742; 385 antibodies from 32 providers.
DR DNASU; 27224; -.
DR Ensembl; ENSMUST00000030427; ENSMUSP00000030427; ENSMUSG00000028668.
DR GeneID; 27224; -.
DR KEGG; mmu:27224; -.
DR UCSC; uc008vhp.1; mouse.
DR CTD; 6924; -.
DR MGI; MGI:1351315; Eloa.
DR VEuPathDB; HostDB:ENSMUSG00000028668; -.
DR eggNOG; KOG2821; Eukaryota.
DR GeneTree; ENSGT00390000002428; -.
DR HOGENOM; CLU_021679_1_0_1; -.
DR InParanoid; Q8CB77; -.
DR OMA; MYIDHYR; -.
DR OrthoDB; 1174517at2759; -.
DR PhylomeDB; Q8CB77; -.
DR TreeFam; TF317259; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 27224; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Eloa; mouse.
DR PRO; PR:Q8CB77; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CB77; protein.
DR Bgee; ENSMUSG00000028668; Expressed in molar tooth and 258 other tissues.
DR Genevisible; Q8CB77; MM.
DR GO; GO:0070449; C:elongin complex; ISO:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:Ensembl.
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 Acetylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..773
FT /note="Elongin-A"
FT /id="PRO_0000086961"
FT DOMAIN 4..79
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 565..609
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 81..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..680
FT /note="Activation domain"
FT /evidence="ECO:0000250|UniProtKB:Q63187"
FT REGION 549..558
FT /note="BC-box"
FT /evidence="ECO:0000250|UniProtKB:Q63187"
FT REGION 671..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..112
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 165..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63187"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14241"
FT MOD_RES 390
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 430
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14241"
FT CONFLICT 35
FT /note="I -> V (in Ref. 1; BAA84994)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="P -> R (in Ref. 1; BAA84994)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="H -> Q (in Ref. 1; BAA84994)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="H -> Q (in Ref. 1; BAA84994)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="P -> L (in Ref. 1; BAA84994 and 5; AAH49885)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="H -> P (in Ref. 1; BAA84994)"
FT /evidence="ECO:0000305"
FT CONFLICT 625..626
FT /note="WR -> LE (in Ref. 1; BAA84994)"
FT /evidence="ECO:0000305"
FT CONFLICT 633..635
FT /note="QDA -> SER (in Ref. 1; BAA84994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 87161 MW; 7F5B33C4B6E87561 CRC64;
MAAESALQVV EKLQARLAAN PDPKKLLKYL KKLSILPITV DILVETGVGK TVNSFRKHEQ
VGNFARDLVA QWKKLVPVER NSEAEDQDFE KNNSRKRPRD ALQREEELEG NYQESWKPSG
SRSYSPEHRQ KKHKKLSEPE RPHKVAHSHE KRDERKRCHK VSPPYSSDPE SSDYGHVQSP
PPSSPHQMYT DLSRSPEEDQ EPIISHQKPG KVHSNTFQDR LGVSHLGEQG KGAVSHHKQH
RSSHKEKHPA DAREDEKISA VSREKSHKAS SKEESRRLLS GDSAKEKLPS SVVKKDKDRE
GSSLKKKFSP ALDVASDNHF KKPKHKDSEK AKSDKNKQSV DGVDSGRGTG DPLPKAKEKV
PNHLKAQEGK VRTNADGKSA GPLHPKAEET DVDDEFERPT MSFESYLSYD QPRKKKKKVV
KTSSTALGEK GLKKKDSKST SKNLNSAQKL PKVNENKSEK LQPAGAEPTR PRKVPTDVLP
ALPDIPLPAI HANYRPLPSL ELIPSFQPKR KAFSSPQEEE EAGFTGRRMN SKMQVYSGSK
CAYLPKMMTL HQQCIRVLKN NIDSIFEVGG VPYSVLEPVL ERCTPDQLYR IEECNHVLIE
ETDQLWKVHC HRDFKEERPE EYESWREMYL RLQDAREQRL RLLTNNIRSA HANKPKGRQA
KMAFVNSVAK PPRDVRRRQE KFGTGGAAVP EKVRIKPAPY TTGSSHVPAS NSSSNFHSSP
EELAYDGPST SSAHLAPVAS SSVSYDPRKP AVKKIAPMMA KTIKAFKNRF SRR
