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 02-SEP-2026, entry version 170. 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; RC 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, RC 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 [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 ERRATUM OF PUBMED:27863226. RX PubMed=28061330; DOI=10.1016/j.molcel.2016.12.006; RA Liefke R., Karwacki-Neisius V., Shi Y.; RL Mol. Cell 65:202-202(2017). RN [9] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION IN E3 UBIQUITIN RP LIGASE COMPLEX. RX PubMed=33590678; DOI=10.15252/embr.202052164; RA Villa F., Fujisawa R., Ainsworth J., Nishimura K., Lie-A-Ling M., RA Lacaud G., Labib K.P.; RT "CUL2LRR1, TRAIP and p97 control CMG helicase disassembly in the mammalian RT cell cycle."; RL EMBO Rep. 22:e52164-e52164(2021). RN [10] RP FUNCTION, SUBUNIT, AND PATHWAY. RX PubMed=35978186; DOI=10.1038/s41586-022-05067-4; RA Wang Q., Li H., Tajima K., Verkerke A.R.P., Taxin Z.H., Hou Z., Cole J.B., RA Li F., Wong J., Abe I., Pradhan R.N., Yamamuro T., Yoneshiro T., RA Hirschhorn J.N., Kajimura S.; RT "Post-translational control of beige fat biogenesis by PRDM16 RT stabilization."; RL Nature 609:151-158(2022). RN [11] 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). RN [12] {ECO:0007744|PDB:4JGH} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH CUL5; ELOC AND RP SOCS2, AND IDENTIFICATION IN E3 UBIQUITIN LIGASE COMPLEX. RX PubMed=23897481; DOI=10.1107/s0907444913011220; RA Kim Y.K., Kwak M.J., Ku B., Suh H.Y., Joo K., Lee J., Jung J.U., Oh B.H.; RT "Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS RT box ubiquitin-protein ligase complexes."; RL Acta Crystallogr. D 69:1587-1597(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 (By similarity). CC Subunit A is transcriptionally active and its transcription activity is CC strongly enhanced by binding to the dimeric complex of the SIII CC regulatory subunits B and C (elongin BC complex) (By similarity). In CC embryonic stem cells, the elongin BC complex is recruited by EPOP to CC Polycomb group (PcG) target genes in order generate genomic region that CC display both active and repressive chromatin properties, an important CC feature 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-2 and cullin-5-RING E3 CC ubiquitin-protein ligase complexes (ECS complexes), which mediate the CC ubiquitination of target proteins (PubMed:33590678, PubMed:35978186). CC By binding to BC-box motifs it seems to link target recruitment CC subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 CC modules that activate E2 ubiquitination enzymes (By similarity). CC Component the von Hippel-Lindau ubiquitination complex CBC(VHL) (By CC similarity). A number of ECS complexes (containing either KLHDC2, CC KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition CC component) are part of the DesCEND (destruction via C-end degrons) CC pathway, which recognizes a C-degron located at the extreme C terminus CC of target proteins, leading to their ubiquitination and degradation (By CC similarity). The ECS(ASB9) complex mediates ubiquitination and CC degradation of CKB (By similarity). As part of a multisubunit ubiquitin CC ligase complex, polyubiquitinates monoubiquitinated POLR2A (By CC similarity). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome CC disassembly by VCP and chromatin extraction during S-phase CC (PubMed:33590678). As part of the ECS(RAB40C) complex, mediates ANKRD28 CC ubiquitination and degradation, thereby inhibiting protein phosphatase CC 6 (PP6) complex activity and focal adhesion assembly during cell CC migration (By similarity). The ECS(ASB7) complex acts a negative CC regulator of H3K9me3 histone mark by mediating ubiquitination and CC degradation of SUV39H1 (By similarity). As part of the ECS(LRRC58) CC complex, mediates CDO1 ubiquitination and degradation, regulating CC cysteine catabolism (By similarity). {ECO:0000250|UniProtKB:Q15370, CC ECO:0000269|PubMed:33590678, ECO:0000269|PubMed:35978186}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:33590678, ECO:0000269|PubMed:35978186}. 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). Component of multiple CC cullin-RING E3 ubiquitin-protein ligase complexes composed of Elongin CC BC (ELOB and ELOC), a cullin (either CUL2 or CUL5), a catalytic subunit CC (either RBX1 or RNF7/RBX2), as well as a substrate adapter protein that CC can be either ASB2, ASB7, ASB9, ASB11, KLHDC2, KLHDC3, KLHDC10, APPBP2, CC FEM1A, FEM1B, FEM1C, LRR1, LRRC58, PCMTD1, SOCS1, SOCS2, SOCS5, SPSB1, CC SPSB3, ELOA, VHL, WSB1 or RAB40C (PubMed:10051596, PubMed:11384984, CC PubMed:23897481, PubMed:33590678, PubMed:35978186). As part of the CC Elongin BC E3 ubiquitin ligase complex; interacts with NRBP1 (By CC similarity). May also interact with DCUN1D1, DCUN1D2, DCUN1D3 and CC DCUN1D5 (By similarity). May form oligomers as a KLHDC2/KLHDC3-ELOB- CC ELOC complex; this interaction is autoinhibitory for the E3 ligase CC complex as the substrate-binding site of KLHDC2/KLHDC3 is blocked in CC the oligomer (By similarity). {ECO:0000250|UniProtKB:Q15370, CC ECO:0000269|PubMed:10051596, ECO:0000269|PubMed:11384984, CC ECO:0000269|PubMed:16498413, ECO:0000269|PubMed:23897481, CC ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226, CC ECO:0000269|PubMed:33590678, ECO:0000269|PubMed:35978186}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:33590678}. CC -!- SIMILARITY: Belongs to the Elongin B family. {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; 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 PDB; 9RP9; X-ray; 2.10 A; B=1-104. DR AlphaFoldDB; P62869; -. DR BMRB; P62869; -. DR SMR; P62869; -. DR BioGRID; 212356; 28. DR CORUM; P62869; -. DR FunCoup; P62869; 1925. DR IntAct; P62869; 10. DR MINT; P62869; -. DR STRING; 10090.ENSMUSP00000066210; -. DR iPTMnet; P62869; -. DR PhosphoSitePlus; P62869; -. DR SwissPalm; P62869; -. DR REPRODUCTION-2DPAGE; P62869; -. DR jPOST; P62869; -. DR PaxDb; 10090-ENSMUSP00000066210; -. DR PeptideAtlas; P62869; -. DR ProteomicsDB; 275601; -. DR Pumba; P62869; -. DR Antibodypedia; 23893; 344 antibodies from 35 providers. DR DNASU; 67673; -. DR Ensembl; ENSMUST00000069579.7; ENSMUSP00000066210.6; ENSMUSG00000055839.7. DR GeneID; 67673; -. DR KEGG; mmu:67673; -. DR UCSC; uc008atr.1; mouse. DR AGR; MGI:1914923; -. 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; GQEQMDQ; -. DR OrthoDB; 7537057at2759; -. DR PhylomeDB; P62869; -. 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 Reactome; R-MMU-9954709; Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 67673; 31 hits in 72 CRISPR screens. DR EvolutionaryTrace; P62869; -. DR PRO; PR:P62869; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; P62869; protein. DR Bgee; ENSMUSG00000055839; Expressed in neural tube and 78 other cell types or tissues. DR ExpressionAtlas; P62869; baseline and differential. DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISO:GO_Central. DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB. 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:GO_Central. DR GO; GO:0030891; C:VCB complex; ISO:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central. DR GO; GO:0003713; F:transcription coactivator activity; ISO:GO_Central. DR GO; GO:0001222; F:transcription corepressor binding; ISO:GO_Central. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:GO_Central. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR GO; GO:0140958; P:target-directed miRNA degradation; ISO:GO_Central. 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; ISO:GO_Central. DR GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; ISO:GO_Central. DR CDD; cd01788; Ubl_ElonginB; 1. DR FunFam; 3.10.20.90:FF:000108; Elongin-B; 1. DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1. DR IDEAL; IID50216; -. DR InterPro; IPR039049; ELOB. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR13248:SF2; ELONGIN-B; 1. DR PANTHER; PTHR13248; TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2; 1. DR Pfam; PF00240; ubiquitin; 1. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. DR PDBsum; 2FNJ; -. DR PDBsum; 4JGH; -. DR PDBsum; 9RP9; -. 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 COMPBIAS 108..118 FT /note="Polar residues" 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 86..88 FT /evidence="ECO:0007829|PDB:2FNJ" FT HELIX 91..93 FT /evidence="ECO:0007829|PDB:2FNJ" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:9RP9" SQ SEQUENCE 118 AA; 13170 MW; BA702F24CEC0FC02 CRC64; MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPE EQRLYKDDQL LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALRI EPFSSPPELP DVMKPQDSGG SANEQAVQ //