ELOB_MOUSE
ID ELOB_MOUSE Reviewed; 118 AA.
AC P62869; Q63529; Q80W20;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Elongin-B;
DE Short=EloB;
DE AltName: Full=Elongin 18 kDa subunit;
DE AltName: Full=RNA polymerase II transcription factor SIII subunit B;
DE AltName: Full=SIII p18;
DE AltName: Full=Transcription elongation factor B polypeptide 2;
GN Name=Elob {ECO:0000312|MGI:MGI:1914923}; Synonyms=Tceb2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Hippocampus, Kidney, and Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP INTERACTION WITH SOCS1.
RX PubMed=10051596; DOI=10.1073/pnas.96.5.2071;
RA Zhang J.-G., Farley A., Nicholson S.E., Willson T.A., Zugaro L.M.,
RA Simpson R.J., Moritz R.L., Cary D., Richardson R., Hausmann G., Kile B.J.,
RA Kent S.B.H., Alexander W.S., Metcalf D., Hilton D.J., Nicola N.A., Baca M.;
RT "The conserved SOCS box motif in suppressors of cytokine signaling binds to
RT elongins B and C and may couple bound proteins to proteasomal
RT degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2071-2076(1999).
RN [4]
RP IDENTIFICATION IN E3 UBIQUITIN LIGASE COMPLEXES.
RX PubMed=11384984; DOI=10.1074/jbc.m103093200;
RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can
RT assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84; SER-108 AND SER-111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [6]
RP FUNCTION, AND INTERACTION WITH EPOP.
RX PubMed=27863225; DOI=10.1016/j.molcel.2016.10.018;
RA Beringer M., Pisano P., Di Carlo V., Blanco E., Chammas P., Vizan P.,
RA Gutierrez A., Aranda S., Payer B., Wierer M., Di Croce L.;
RT "EPOP functionally links elongin and Polycomb in pluripotent stem cells.";
RL Mol. Cell 64:645-658(2016).
RN [7]
RP FUNCTION, AND INTERACTION WITH EPOP.
RX PubMed=27863226; DOI=10.1016/j.molcel.2016.10.019;
RA Liefke R., Karwacki-Neisius V., Shi Y.;
RT "EPOP interacts with elongin BC and USP7 to modulate the chromatin
RT landscape.";
RL Mol. Cell 64:659-672(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ELONGIN C AND
RP DROSOPHILA GUS.
RX PubMed=16498413; DOI=10.1038/sj.emboj.7600994;
RA Woo J.S., Imm J.H., Min C.K., Kim K.J., Cha S.S., Oh B.H.;
RT "Structural and functional insights into the B30.2/SPRY domain.";
RL EMBO J. 25:1353-1363(2006).
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) (By similarity). In embryonic
CC stem cells, the elongin BC complex is recruited by EPOP to Polycomb
CC group (PcG) target genes in order generate genomic region that display
CC both active and repressive chromatin properties, an important feature
CC of pluripotent stem cells (PubMed:27863225, PubMed:27863226).
CC {ECO:0000250|UniProtKB:Q15370, ECO:0000269|PubMed:27863225,
CC ECO:0000269|PubMed:27863226}.
CC -!- FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C-
CC CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which
CC mediate the ubiquitination of target proteins. This includes the von
CC Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box
CC motifs it seems to link target recruitment subunits, like VHL and
CC members of the SOCS box family, to Cullin/RBX1 modules that activate E2
CC ubiquitination enzymes. A number of ECS complexes (containing either
CC KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-
CC recognition component) are part of the DesCEND (destruction via C-end
CC degrons) pathway, which recognizes a C-degron located at the extreme C
CC terminus of target proteins, leading to their ubiquitination and
CC degradation. {ECO:0000250|UniProtKB:Q15370}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q15370}.
CC -!- SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC
CC subunit (PubMed:16498413). The elongin BC complex interacts with EPOP;
CC leading to recruit the elongin BC complex to Polycomb group (PcG)
CC target genes, thereby restricting excessive activity of the PRC2/EED-
CC EZH2 complex (PubMed:27863225, PubMed:27863226). Part of E3 ubiquitin
CC ligase complexes with CUL5 or CUL2, RBX1 and a substrate adapter
CC protein that can be either ASB2, KLHDC2, KLHDC3, KLHDC10, APPBP2,
CC FEM1A, FEM1B, FEM1C, SOCS1, SOCS5, ELOA, VHL or WSB1. Interacts with
CC VHL. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and
CC CUL2. Interacts with SPSB1. Interacts with KLHDC10; which may be an E3
CC ubiquitin ligase complex substrate recognition component. May also
CC interact with DCUN1D1, DCUN1D2, DCUN1D3 and DCUN1D5 (By similarity).
CC {ECO:0000250|UniProtKB:Q15370, ECO:0000269|PubMed:10051596,
CC ECO:0000269|PubMed:11384984, ECO:0000269|PubMed:16498413,
CC ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; AK019358; BAB31677.1; -; mRNA.
DR EMBL; AK002223; BAB21946.1; -; mRNA.
DR EMBL; AK002868; BAB22417.1; -; mRNA.
DR EMBL; AK003277; BAB22684.1; -; mRNA.
DR EMBL; AK008477; BAB25690.1; -; mRNA.
DR EMBL; AK008534; BAB25727.1; -; mRNA.
DR EMBL; AK012254; BAB28121.1; -; mRNA.
DR EMBL; AK019181; BAB31590.1; -; mRNA.
DR EMBL; AK019218; BAB31608.1; -; mRNA.
DR EMBL; BC051927; AAH51927.2; -; mRNA.
DR EMBL; BC056983; AAH56983.1; -; mRNA.
DR CCDS; CCDS57055.1; -.
DR RefSeq; NP_080581.1; NM_026305.2.
DR PDB; 2FNJ; X-ray; 1.80 A; B=1-118.
DR PDB; 4JGH; X-ray; 3.00 A; B=1-118.
DR PDBsum; 2FNJ; -.
DR PDBsum; 4JGH; -.
DR AlphaFoldDB; P62869; -.
DR BMRB; P62869; -.
DR SMR; P62869; -.
DR BioGRID; 212356; 28.
DR CORUM; P62869; -.
DR IntAct; P62869; 9.
DR MINT; P62869; -.
DR STRING; 10090.ENSMUSP00000066210; -.
DR iPTMnet; P62869; -.
DR PhosphoSitePlus; P62869; -.
DR SwissPalm; P62869; -.
DR REPRODUCTION-2DPAGE; P62869; -.
DR EPD; P62869; -.
DR jPOST; P62869; -.
DR MaxQB; P62869; -.
DR PaxDb; P62869; -.
DR PeptideAtlas; P62869; -.
DR PRIDE; P62869; -.
DR ProteomicsDB; 275601; -.
DR Antibodypedia; 23893; 334 antibodies from 32 providers.
DR DNASU; 67673; -.
DR Ensembl; ENSMUST00000069579; ENSMUSP00000066210; ENSMUSG00000055839.
DR GeneID; 67673; -.
DR KEGG; mmu:67673; -.
DR UCSC; uc008atr.1; mouse.
DR CTD; 6923; -.
DR MGI; MGI:1914923; Elob.
DR VEuPathDB; HostDB:ENSMUSG00000055839; -.
DR eggNOG; KOG4495; Eukaryota.
DR GeneTree; ENSGT00390000018316; -.
DR HOGENOM; CLU_139243_0_0_1; -.
DR InParanoid; P62869; -.
DR OMA; RKKMTIF; -.
DR OrthoDB; 1637528at2759; -.
DR PhylomeDB; P62869; -.
DR TreeFam; TF325964; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
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 Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 67673; 31 hits in 67 CRISPR screens.
DR ChiTaRS; Elob; mouse.
DR EvolutionaryTrace; P62869; -.
DR PRO; PR:P62869; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P62869; protein.
DR Bgee; ENSMUSG00000055839; Expressed in neural tube and 76 other tissues.
DR ExpressionAtlas; P62869; baseline and differential.
DR Genevisible; P62869; MM.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070449; C:elongin complex; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0030891; C:VCB complex; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; ISO:MGI.
DR IDEAL; IID50216; -.
DR InterPro; IPR039049; ELOB.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13248; PTHR13248; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1..118
FT /note="Elongin-B"
FT /id="PRO_0000114915"
FT DOMAIN 1..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 91..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15370"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:2FNJ"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2FNJ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2FNJ"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:2FNJ"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 73..83
FT /evidence="ECO:0007829|PDB:2FNJ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4JGH"
SQ SEQUENCE 118 AA; 13170 MW; BA702F24CEC0FC02 CRC64;
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPE EQRLYKDDQL LDDGKTLGEC
GFTSQTARPQ APATVGLAFR ADDTFEALRI EPFSSPPELP DVMKPQDSGG SANEQAVQ
