ID ELOB_HUMAN Reviewed; 118 AA. AC Q15370; B7WPD3; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 221. 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|HGNC:HGNC:11619}; Synonyms=TCEB2; 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 1), AND FUNCTION. RX PubMed=7638163; DOI=10.1073/pnas.92.16.7172; RA Garrett K.P., Aso T., Bradsher J.N., Foundling S.I., Lane W.S., RA Conaway R.C., Conaway J.W.; RT "Positive regulation of general transcription factor SIII by a tailed RT ubiquitin homolog."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7172-7176(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Bonaldo M.F., Lennon G., Soares M.B.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas, and Placenta; 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 PROTEIN SEQUENCE OF 1-8 AND 44-80, ACETYLATION AT MET-1, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [7] RP INTERACTION WITH VHL. RX PubMed=11006129; DOI=10.1006/bbrc.2000.3451; RA Aso T., Yamazaki K., Aigaki T., Kitajima S.; RT "Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 RT ubiquitin ligase activity."; RL Biochem. Biophys. Res. Commun. 276:355-361(2000). RN [8] RP INTERACTION WITH HIV VIF (MICROBIAL INFECTION). RX PubMed=15574592; DOI=10.1101/gad.1249904; RA Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.; RT "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif- RT Cul5 complex that promotes APOBEC3G degradation."; RL Genes Dev. 18:2861-2866(2004). RN [9] RP INTERACTION WITH SPSB1. RX PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009; RA Woo J.S., Suh H.Y., Park S.Y., Oh B.H.; RT "Structural basis for protein recognition by B30.2/SPRY domains."; RL Mol. Cell 24:967-976(2006). RN [10] RP FUNCTION IN EGFR DEGRADATION, AND INTERACTION WITH SOCS5. RX PubMed=15590694; DOI=10.1074/jbc.m408575200; RA Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N., RA Rechavi G., Yarden Y.; RT "Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor RT receptor signaling."; RL J. Biol. Chem. 280:7038-7048(2005). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP FUNCTION, AND IDENTIFICATION IN COMPLEX WITH CUL5; ELOA; 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 [13] 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 [14] RP INTERACTION WITH ASB2. RX PubMed=21119685; DOI=10.1038/cr.2010.165; RA Nie L., Zhao Y., Wu W., Yang Y.Z., Wang H.C., Sun X.H.; RT "Notch-induced Asb2 expression promotes protein ubiquitination by forming RT non-canonical E3 ligase complexes."; RL Cell Res. 21:754-769(2011). RN [15] RP INTERACTION WITH HERPES VIRUS 8 PROTEIN LANA1 (MICROBIAL INFECTION). RX PubMed=21697472; DOI=10.1128/jvi.00733-11; RA Li X., Liang D., Lin X., Robertson E.S., Lan K.; RT "Kaposi's sarcoma-associated herpesvirus-encoded latency-associated nuclear RT antigen reduces interleukin-8 expression in endothelial cells and impairs RT neutrophil chemotaxis by degrading nuclear p65."; RL J. Virol. 85:8606-8615(2011). RN [16] RP INTERACTION WITH NRBP1. RX PubMed=22510880; DOI=10.1038/emboj.2012.91; RA Wilson C.H., Crombie C., van der Weyden L., Poulogiannis G., Rust A.G., RA Pardo M., Gracia T., Yu L., Choudhary J., Poulin G.B., McIntyre R.E., RA Winton D.J., March H.N., Arends M.J., Fraser A.G., Adams D.J.; RT "Nuclear receptor binding protein 1 regulates intestinal progenitor cell RT homeostasis and tumour formation."; RL EMBO J. 31:2486-2497(2012). RN [17] RP INTERACTION WITH KLHDC10. RX PubMed=23102700; DOI=10.1016/j.molcel.2012.09.018; RA Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., RA Kuranaga E., Miura M., Takeda K., Ichijo H.; RT "The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 RT activation by suppressing PP5."; RL Mol. Cell 48:692-704(2012). RN [18] RP IDENTIFICATION IN A COMPLEX WITH LIMD1; EGLN1/PHD2; VHL AND CUL2. RX PubMed=22286099; DOI=10.1038/ncb2424; RA Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C., Feng Y., RA Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J., Ingvarsson S., RA Ratcliffe P.J., Longmore G.D., Sharp T.V.; RT "The LIMD1 protein bridges an association between the prolyl hydroxylases RT and VHL to repress HIF-1 activity."; RL Nat. Cell Biol. 14:201-208(2012). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP INTERACTION WITH MOLLUSCUM CONTAGIOSUM VIRUS PROTEIN MC132 (MICROBIAL RP INFECTION). RX PubMed=26041281; DOI=10.1128/jvi.00799-15; RA Brady G., Haas D.A., Farrell P.J., Pichlmair A., Bowie A.G.; RT "Poxvirus protein MC132 from molluscum contagiosum virus inhibits NF-B RT activation by targeting p65 for degradation."; RL J. Virol. 89:8406-8415(2015). RN [22] RP FUNCTION, AND PATHWAY. RX PubMed=26138980; DOI=10.1126/science.aab0515; RA Lin H.C., Ho S.C., Chen Y.Y., Khoo K.H., Hsu P.H., Yen H.C.; RT "SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced RT by failed UGA/Sec decoding."; RL Science 349:91-95(2015). RN [23] RP INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3 AND DCUN1D5. RX PubMed=26906416; DOI=10.1242/jcs.181784; RA Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.; RT "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases."; RL J. Cell Sci. 129:1441-1454(2016). RN [24] RP FUNCTION, AND PATHWAY. RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028; RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.; RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C- RT terminal degrons."; RL Cell 173:1622-1635(2018). RN [25] RP FUNCTION, AND PATHWAY. RX PubMed=29775578; DOI=10.1016/j.molcel.2018.04.006; RA Lin H.C., Yeh C.W., Chen Y.F., Lee T.T., Hsieh P.Y., Rusnac D.V., Lin S.Y., RA Elledge S.J., Zheng N., Yen H.S.; RT "C-terminal end-directed protein elimination by CRL2 ubiquitin ligases."; RL Mol. Cell 70:602-613(2018). RN [26] RP IDENTIFICATION IN A E3 UBIQUITIN-PROTEIN LIGASE COMPLEX CONTAINING PCMTD1, RP AND INTERACTION WITH PCMTD1. RX PubMed=35486881; DOI=10.1021/acs.biochem.2c00130; RA Warmack R.A., Pang E.Z., Peluso E., Lowenson J.D., Ong J.Y., Torres J.Z., RA Clarke S.G.; RT "Human Protein-l-isoaspartate O-Methyltransferase Domain-Containing Protein RT 1 (PCMTD1) Associates with Cullin-RING Ligase Proteins."; RL Biochemistry 61:879-894(2022). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ELOC AND VHL, AND RP FUNCTION. RX PubMed=10205047; DOI=10.1126/science.284.5413.455; RA Stebbins C.E., Kaelin W.G. Jr., Pavletich N.P.; RT "Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor RT suppressor function."; RL Science 284:455-461(1999). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) COMPLEX WITH ELOC; VHL AND HIF1A, AND RP FUNCTION. RX PubMed=12050673; DOI=10.1038/nature00767; RA Hon W.-C., Wilson M.I., Harlos K., Claridge T.D.W., Schofield C.J., RA Pugh C.W., Maxwell P.H., Ratcliffe P.J., Stuart D.I., Jones E.Y.; RT "Structural basis for the recognition of hydroxyproline in HIF-1 alpha by RT pVHL."; RL Nature 417:975-978(2002). RN [29] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH ELOC; VHL AND HIF1A, RP AND FUNCTION. RX PubMed=12004076; DOI=10.1126/science.1073440; RA Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr., Pavletich N.P.; RT "Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in RT signaling."; RL Science 296:1886-1889(2002). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH ELOC AND SOX4, AND RP SUBUNIT. RX PubMed=17997974; DOI=10.1016/j.str.2007.09.016; RA Bullock A.N., Rodriguez M.C., Debreczeni J.E., Songyang Z., Knapp S.; RT "Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box RT interface and the molecular basis for SOCS-dependent EGFR degradation."; RL Structure 15:1493-1504(2007). RN [31] {ECO:0007744|PDB:7PLO} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH REPLISOME RP AND DNA POLYMERASE EPSILON, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=34700328; DOI=10.1038/s41586-021-04145-3; RA Jenkyn-Bedford M., Jones M.L., Baris Y., Labib K.P.M., Cannone G., RA Yeeles J.T.P., Deegan T.D.; RT "A conserved mechanism for regulating replisome disassembly in RT eukaryotes."; RL Nature 600:743-747(2021). 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) (PubMed:7638163). 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 (By similarity). CC {ECO:0000250|UniProtKB:P62869, ECO:0000269|PubMed:7638163}. 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 (PubMed:10205047, CC PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:26138980, CC PubMed:29779948, PubMed:29775578). This includes the von Hippel-Lindau CC ubiquitination complex CBC(VHL) (PubMed:10205047, PubMed:12004076, CC PubMed:12050673, PubMed:15590694). By binding to BC-box motifs it seems CC to link target recruitment subunits, like VHL and members of the SOCS CC box family, to Cullin/RBX1 modules that activate E2 ubiquitination CC enzymes (PubMed:10205047, PubMed:12004076, PubMed:12050673, CC PubMed:15590694). As part of a multisubunit ubiquitin ligase complex CC composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 CC and CUL5; polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177). CC A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, CC APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are CC part of the DesCEND (destruction via C-end degrons) pathway, which CC recognizes a C-degron located at the extreme C terminus of target CC proteins, leading to their ubiquitination and degradation CC (PubMed:26138980, PubMed:29779948, PubMed:29775578). ECS(LRR1) CC ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and CC chromatin extraction during S-phase (By similarity). CC {ECO:0000250|UniProtKB:P62869, ECO:0000269|PubMed:10205047, CC ECO:0000269|PubMed:12004076, ECO:0000269|PubMed:12050673, CC ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:26138980, CC ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578, CC ECO:0000269|PubMed:29779948}. CC -!- SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC CC subunit (PubMed:10205047, PubMed:17997974). The elongin BC complex CC interacts with EPOP; leading to recruit the elongin BC complex to CC Polycomb group (PcG) target genes, thereby restricting excessive CC activity of the PRC2/EED-EZH2 complex (By similarity). Part of E3 CC ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and a substrate CC adapter protein that can be either ASB2, KLHDC2, KLHDC3, KLHDC10, CC APPBP2, FEM1A, FEM1B, FEM1C, LRR1, SOCS1, SOCS5, ELOA, VHL or WSB1 CC (PubMed:15590694, PubMed:19413330, PubMed:22286099, PubMed:26138980, CC PubMed:29779948, PubMed:29775578, PubMed:34700328, PubMed:19920177). CC Interacts with VHL (PubMed:10205047, PubMed:11006129). Found in a CC complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2. Interacts CC with SPSB1 (PubMed:17189197). Interacts with KLHDC10; which may be an CC E3 ubiquitin ligase complex substrate recognition component CC (PubMed:23102700). May also interact with DCUN1D1, DCUN1D2, DCUN1D3 and CC DCUN1D5 (PubMed:26906416). As part of the Elongin BC E3 ubiquitin CC ligase complex; interacts with NRBP1 (PubMed:22510880, PubMed:11006129, CC PubMed:15590694, PubMed:17189197, PubMed:19920177, PubMed:22286099, CC PubMed:23102700, PubMed:26138980, PubMed:26906416, PubMed:29775578, CC PubMed:29779948, PubMed:10205047, PubMed:17997974, PubMed:34700328) (By CC similarity). Component of the ECS(PCMTD1) complex with the substrate CC recognition subunit PCMTD1 (PubMed:35486881). Interacts with PCMTD1 CC (via the BC-box); the interaction is direct and stabilizes PCMTD1 CC (PubMed:35486881). {ECO:0000250|UniProtKB:P62869, CC ECO:0000269|PubMed:10205047, ECO:0000269|PubMed:11006129, CC ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:17189197, CC ECO:0000269|PubMed:17997974, ECO:0000269|PubMed:19920177, CC ECO:0000269|PubMed:22286099, ECO:0000269|PubMed:22510880, CC ECO:0000269|PubMed:23102700, ECO:0000269|PubMed:26138980, CC ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:29775578, CC ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:34700328, CC ECO:0000269|PubMed:35486881}. CC -!- SUBUNIT: (Microbial infection) Substrate adapter protein can be a viral CC protein such as HIV Vif. {ECO:0000269|PubMed:15574592}. CC -!- SUBUNIT: (Microbial infection) Interacts with molluscum contagiosum CC virus MC132. {ECO:0000269|PubMed:26041281}. CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 virus CC protein LANA1. {ECO:0000269|PubMed:21697472}. CC -!- INTERACTION: CC Q15370; Q15369: ELOC; NbExp=20; IntAct=EBI-301238, EBI-301231; CC Q15370; Q96G25: MED8; NbExp=5; IntAct=EBI-301238, EBI-394405; CC Q15370; Q96EL3: MRPL53; NbExp=5; IntAct=EBI-301238, EBI-2513715; CC Q15370; P12504: vif; Xeno; NbExp=5; IntAct=EBI-301238, EBI-779991; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:34700328}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15370-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15370-2; Sequence=VSP_045784; CC -!- SEQUENCE CAUTION: CC Sequence=AAC08452.1; Type=Erroneous gene model prediction; 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; L42856; AAA75522.1; -; mRNA. DR EMBL; BM700019; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC004493; AAC08452.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC092117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471112; EAW85472.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85474.1; -; Genomic_DNA. DR EMBL; BC013306; AAH13306.1; -; mRNA. DR EMBL; BC065000; AAH65000.1; -; mRNA. DR CCDS; CCDS32374.1; -. [Q15370-2] DR CCDS; CCDS45387.1; -. [Q15370-1] DR PIR; I59405; I59405. DR RefSeq; NP_009039.1; NM_007108.3. [Q15370-1] DR RefSeq; NP_996896.1; NM_207013.2. [Q15370-2] DR PDB; 1LM8; X-ray; 1.85 A; B=1-118. DR PDB; 1LQB; X-ray; 2.00 A; A=1-118. DR PDB; 1VCB; X-ray; 2.70 A; A/D/G/J=1-118. DR PDB; 2C9W; X-ray; 1.90 A; B=1-118. DR PDB; 2IZV; X-ray; 2.55 A; B=1-118. DR PDB; 2JZ3; NMR; -; B=1-118. DR PDB; 2MA9; NMR; -; B=1-118. DR PDB; 3DCG; X-ray; 2.40 A; A/C=1-118. DR PDB; 3ZKJ; X-ray; 2.58 A; C/F=1-118. DR PDB; 3ZNG; X-ray; 2.85 A; C/F=1-118. DR PDB; 3ZRC; X-ray; 2.90 A; A/D/G/J=1-118. DR PDB; 3ZRF; X-ray; 2.80 A; A/D/G/J=1-118. DR PDB; 3ZTC; X-ray; 2.65 A; A/D/G/J=1-118. DR PDB; 3ZTD; X-ray; 2.79 A; A/D/G/J=1-118. DR PDB; 3ZUN; X-ray; 2.50 A; A/D/G/J=1-118. DR PDB; 4AJY; X-ray; 1.73 A; B=1-118. DR PDB; 4AWJ; X-ray; 2.50 A; A/D/G/J=1-104. DR PDB; 4B95; X-ray; 2.80 A; A/D/G/J=1-118. DR PDB; 4B9K; X-ray; 2.00 A; A/D/G/J=1-104. DR PDB; 4BKS; X-ray; 2.20 A; A/D/G/J=1-104. DR PDB; 4BKT; X-ray; 2.35 A; A/D/G/J=1-104. DR PDB; 4N9F; X-ray; 3.30 A; 4/D/H/J/P/W/X/e/g/m/s/y=1-102. DR PDB; 4W9C; X-ray; 2.20 A; A/D/G/J=1-104. DR PDB; 4W9D; X-ray; 2.20 A; A/D/G/J=1-104. DR PDB; 4W9E; X-ray; 2.60 A; A/D/G/J=1-104. DR PDB; 4W9F; X-ray; 2.10 A; A/D/G/J=1-104. DR PDB; 4W9G; X-ray; 2.70 A; A/D/G/J=1-104. DR PDB; 4W9H; X-ray; 2.10 A; A/D/G/J=1-104. DR PDB; 4W9I; X-ray; 2.40 A; A/D/G/J=1-104. DR PDB; 4W9J; X-ray; 2.20 A; A/D/G/J=1-104. DR PDB; 4W9K; X-ray; 2.10 A; A/D/G/J=1-104. DR PDB; 4W9L; X-ray; 2.20 A; A/D/G/J=1-104. DR PDB; 4WQO; X-ray; 3.20 A; B=1-118. DR PDB; 5BO4; X-ray; 2.90 A; B/E/H/K/N/Q=1-104. DR PDB; 5LLI; X-ray; 2.40 A; A/D/G/J=1-104. DR PDB; 5N4W; X-ray; 3.90 A; B=1-104. DR PDB; 5NVV; X-ray; 2.10 A; A/D/G/J=1-104. DR PDB; 5NVW; X-ray; 2.20 A; A/D/G/J=1-104. DR PDB; 5NVX; X-ray; 2.20 A; A/D/G/J=1-104. DR PDB; 5NVY; X-ray; 2.90 A; A/D/G/J=1-104. DR PDB; 5NVZ; X-ray; 2.70 A; A/D/G/J=1-104. DR PDB; 5NW0; X-ray; 2.30 A; A/D/G/J=1-104. DR PDB; 5NW1; X-ray; 2.10 A; A/D/G/J=1-104. DR PDB; 5NW2; X-ray; 2.20 A; A/D/G/J=1-104. DR PDB; 5T35; X-ray; 2.70 A; B/F=1-104. DR PDB; 6BVB; X-ray; 2.00 A; B=1-118. DR PDB; 6C5X; X-ray; 3.10 A; B/E=1-118. DR PDB; 6FMI; X-ray; 2.80 A; A/D=1-104. DR PDB; 6FMJ; X-ray; 2.45 A; A/D/G/J=1-104. DR PDB; 6FMK; X-ray; 2.75 A; A/D/G/J=1-104. DR PDB; 6GFX; X-ray; 1.83 A; A=1-104. DR PDB; 6GFY; X-ray; 2.70 A; A/D/G/J=1-104. DR PDB; 6GFZ; X-ray; 2.30 A; A/D/G/J=1-104. DR PDB; 6GMN; X-ray; 1.94 A; A/D/G/J=1-104. DR PDB; 6GMQ; X-ray; 2.75 A; A/D/G/J=1-104. DR PDB; 6GMR; X-ray; 1.75 A; B=1-118. DR PDB; 6GMX; X-ray; 2.53 A; A/D/G/J=1-104. DR PDB; 6HAX; X-ray; 2.35 A; D/H=1-104. DR PDB; 6HAY; X-ray; 2.24 A; D/H=1-104. DR PDB; 6HR2; X-ray; 1.76 A; D/H=1-104. DR PDB; 6I4X; X-ray; 2.69 A; B=1-104. DR PDB; 6I5J; X-ray; 2.80 A; B/E=1-104. DR PDB; 6I5N; X-ray; 1.98 A; B/E=1-104. DR PDB; 6I7Q; X-ray; 1.80 A; B=1-118. DR PDB; 6I7R; X-ray; 1.95 A; B=1-118. DR PDB; 6P59; X-ray; 2.94 A; D/W=1-118. DR PDB; 6R6H; EM; 8.40 A; P=1-104. DR PDB; 6R7F; EM; 8.20 A; P=1-118. DR PDB; 6R7H; EM; 8.80 A; P=1-104. DR PDB; 6R7I; EM; 5.90 A; P=1-106. DR PDB; 6R7N; EM; 6.50 A; P=1-104. DR PDB; 6SIS; X-ray; 3.50 A; B/F=1-104. DR PDB; 6V9H; EM; 4.10 A; E=1-118. DR PDB; 6ZHC; X-ray; 1.92 A; BBB=1-107. DR PDB; 7CJB; X-ray; 2.80 A; B/F/J/N=1-118. DR PDB; 7JTO; X-ray; 1.70 A; J=1-104. DR PDB; 7JTP; X-ray; 2.12 A; J=1-104. DR PDB; 7KHH; X-ray; 2.28 A; A=1-118. DR PDB; 7M6T; X-ray; 3.19 A; B=1-118. DR PDB; 7PI4; X-ray; 2.24 A; BBB=1-105. DR PDB; 7PLO; EM; 2.80 A; P=1-118. DR PDB; 7Q2J; X-ray; 2.50 A; A=1-104. DR PDB; 7S4E; X-ray; 2.25 A; D/H=1-104. DR PDB; 7UPN; EM; 3.50 A; H/I=1-118. DR PDB; 7Z6L; X-ray; 2.24 A; D=1-104. DR PDB; 7Z76; X-ray; 1.32 A; A=1-104. DR PDB; 7Z77; X-ray; 1.97 A; A=1-104. DR PDB; 7ZLM; X-ray; 1.79 A; B/E/H/K=1-118. DR PDB; 7ZLN; X-ray; 2.60 A; B=1-118. DR PDB; 7ZLO; X-ray; 2.22 A; B=1-118. DR PDB; 7ZLP; X-ray; 1.94 A; B=1-118. DR PDB; 7ZLR; X-ray; 2.01 A; B=1-118. DR PDB; 7ZLS; X-ray; 1.92 A; B/E/H/K=1-118. DR PDB; 7ZNT; X-ray; 3.00 A; A/D=1-104. DR PDB; 8BB2; X-ray; 2.05 A; J=1-104. DR PDB; 8BB3; X-ray; 1.80 A; J=1-104. DR PDB; 8BB4; X-ray; 2.80 A; I=1-104. DR PDB; 8BB5; X-ray; 2.20 A; A=1-104. DR PDB; 8BDI; X-ray; 2.11 A; A/D/G/J=1-104. DR PDB; 8BDJ; X-ray; 2.02 A; A/D/G/J=1-104. DR PDB; 8BDL; X-ray; 2.29 A; A/D/G/J=1-104. DR PDB; 8BDM; X-ray; 2.02 A; A/D/G/J=1-104. DR PDB; 8BDN; X-ray; 2.76 A; A/D/G/J=1-104. DR PDB; 8BDO; X-ray; 2.80 A; A/D=1-104. DR PDB; 8BDS; X-ray; 1.72 A; A=1-104. DR PDB; 8BDT; X-ray; 2.70 A; B/F=1-104. DR PDB; 8BDX; X-ray; 2.93 A; B/F=1-104. DR PDB; 8BEB; X-ray; 3.18 A; A=1-104. DR PDB; 8C13; X-ray; 2.30 A; J=1-118. DR PDB; 8CQE; X-ray; 2.85 A; A/D/G/J=1-104. DR PDB; 8CQK; X-ray; 2.62 A; A/D/G/J=1-104. DR PDB; 8CQL; X-ray; 2.38 A; A/D/G/J=1-104. DR PDB; 8CX0; EM; 2.70 A; D=1-118. DR PDB; 8CX1; EM; 3.30 A; D/I=1-118. DR PDB; 8CX2; EM; 3.20 A; D/I=1-118. DR PDB; 8EBN; X-ray; 2.60 A; C/E=1-104. DR PDB; 8EI3; X-ray; 3.49 A; A/D=1-118. DR PDB; 8EWV; X-ray; 3.40 A; A/E/I/M/Q/U=1-118. DR PDB; 8FVI; EM; 3.24 A; y=1-102. DR PDB; 8FVJ; EM; 3.54 A; 3/8=1-102. DR PDB; 8G1P; X-ray; 2.70 A; A/D=1-118. DR PDB; 8G1Q; X-ray; 3.73 A; A=1-104. DR PDB; 8JAL; EM; 3.30 A; C/G=1-118. DR PDB; 8JAQ; EM; 3.26 A; C/G/M/Q=1-118. DR PDB; 8JAR; EM; 3.30 A; C/G=1-118. DR PDB; 8JAS; EM; 3.54 A; C/G/M/Q=1-118. DR PDB; 8JAU; EM; 3.22 A; C/G=1-118. DR PDB; 8JAV; EM; 3.44 A; C/G/M/Q=1-118. DR PDB; 8OEV; EM; 2.86 A; Q=1-118. DR PDB; 8OEW; EM; 2.80 A; Q=1-118. DR PDB; 8OF0; EM; 3.05 A; Q=1-118. DR PDB; 8P0F; X-ray; 1.98 A; C/F=1-104. DR PDB; 8PC2; X-ray; 2.80 A; D/F=1-104. DR PDB; 8QU8; EM; 3.50 A; B=2-118. DR PDB; 8QVU; X-ray; 2.24 A; D/H=1-104. DR PDB; 8QW6; X-ray; 2.20 A; D/H=1-104. DR PDB; 8QW7; X-ray; 2.36 A; D/H=1-104. DR PDBsum; 1LM8; -. DR PDBsum; 1LQB; -. DR PDBsum; 1VCB; -. DR PDBsum; 2C9W; -. DR PDBsum; 2IZV; -. DR PDBsum; 2JZ3; -. DR PDBsum; 2MA9; -. DR PDBsum; 3DCG; -. DR PDBsum; 3ZKJ; -. DR PDBsum; 3ZNG; -. DR PDBsum; 3ZRC; -. DR PDBsum; 3ZRF; -. DR PDBsum; 3ZTC; -. DR PDBsum; 3ZTD; -. DR PDBsum; 3ZUN; -. DR PDBsum; 4AJY; -. DR PDBsum; 4AWJ; -. DR PDBsum; 4B95; -. DR PDBsum; 4B9K; -. DR PDBsum; 4BKS; -. DR PDBsum; 4BKT; -. DR PDBsum; 4N9F; -. DR PDBsum; 4W9C; -. DR PDBsum; 4W9D; -. DR PDBsum; 4W9E; -. DR PDBsum; 4W9F; -. DR PDBsum; 4W9G; -. DR PDBsum; 4W9H; -. DR PDBsum; 4W9I; -. DR PDBsum; 4W9J; -. DR PDBsum; 4W9K; -. DR PDBsum; 4W9L; -. DR PDBsum; 4WQO; -. DR PDBsum; 5BO4; -. DR PDBsum; 5LLI; -. DR PDBsum; 5N4W; -. DR PDBsum; 5NVV; -. DR PDBsum; 5NVW; -. DR PDBsum; 5NVX; -. DR PDBsum; 5NVY; -. DR PDBsum; 5NVZ; -. DR PDBsum; 5NW0; -. DR PDBsum; 5NW1; -. DR PDBsum; 5NW2; -. DR PDBsum; 5T35; -. DR PDBsum; 6BVB; -. DR PDBsum; 6C5X; -. DR PDBsum; 6FMI; -. DR PDBsum; 6FMJ; -. DR PDBsum; 6FMK; -. DR PDBsum; 6GFX; -. DR PDBsum; 6GFY; -. DR PDBsum; 6GFZ; -. DR PDBsum; 6GMN; -. DR PDBsum; 6GMQ; -. DR PDBsum; 6GMR; -. DR PDBsum; 6GMX; -. DR PDBsum; 6HAX; -. DR PDBsum; 6HAY; -. DR PDBsum; 6HR2; -. DR PDBsum; 6I4X; -. DR PDBsum; 6I5J; -. DR PDBsum; 6I5N; -. DR PDBsum; 6I7Q; -. DR PDBsum; 6I7R; -. DR PDBsum; 6P59; -. DR PDBsum; 6R6H; -. DR PDBsum; 6R7F; -. DR PDBsum; 6R7H; -. DR PDBsum; 6R7I; -. DR PDBsum; 6R7N; -. DR PDBsum; 6SIS; -. DR PDBsum; 6V9H; -. DR PDBsum; 6ZHC; -. DR PDBsum; 7CJB; -. DR PDBsum; 7JTO; -. DR PDBsum; 7JTP; -. DR PDBsum; 7KHH; -. DR PDBsum; 7M6T; -. DR PDBsum; 7PI4; -. DR PDBsum; 7PLO; -. DR PDBsum; 7Q2J; -. DR PDBsum; 7S4E; -. DR PDBsum; 7UPN; -. DR PDBsum; 7Z6L; -. DR PDBsum; 7Z76; -. DR PDBsum; 7Z77; -. DR PDBsum; 7ZLM; -. DR PDBsum; 7ZLN; -. DR PDBsum; 7ZLO; -. DR PDBsum; 7ZLP; -. DR PDBsum; 7ZLR; -. DR PDBsum; 7ZLS; -. DR PDBsum; 7ZNT; -. DR PDBsum; 8BB2; -. DR PDBsum; 8BB3; -. DR PDBsum; 8BB4; -. DR PDBsum; 8BB5; -. DR PDBsum; 8BDI; -. DR PDBsum; 8BDJ; -. DR PDBsum; 8BDL; -. DR PDBsum; 8BDM; -. DR PDBsum; 8BDN; -. DR PDBsum; 8BDO; -. DR PDBsum; 8BDS; -. DR PDBsum; 8BDT; -. DR PDBsum; 8BDX; -. DR PDBsum; 8BEB; -. DR PDBsum; 8C13; -. DR PDBsum; 8CQE; -. DR PDBsum; 8CQK; -. DR PDBsum; 8CQL; -. DR PDBsum; 8CX0; -. DR PDBsum; 8CX1; -. DR PDBsum; 8CX2; -. DR PDBsum; 8EBN; -. DR PDBsum; 8EI3; -. DR PDBsum; 8EWV; -. DR PDBsum; 8FVI; -. DR PDBsum; 8FVJ; -. DR PDBsum; 8G1P; -. DR PDBsum; 8G1Q; -. DR PDBsum; 8JAL; -. DR PDBsum; 8JAQ; -. DR PDBsum; 8JAR; -. DR PDBsum; 8JAS; -. DR PDBsum; 8JAU; -. DR PDBsum; 8JAV; -. DR PDBsum; 8OEV; -. DR PDBsum; 8OEW; -. DR PDBsum; 8OF0; -. DR PDBsum; 8P0F; -. DR PDBsum; 8PC2; -. DR PDBsum; 8QU8; -. DR PDBsum; 8QVU; -. DR PDBsum; 8QW6; -. DR PDBsum; 8QW7; -. DR AlphaFoldDB; Q15370; -. DR BMRB; Q15370; -. DR EMDB; EMD-13494; -. DR EMDB; EMD-16832; -. DR EMDB; EMD-16833; -. DR EMDB; EMD-16837; -. DR EMDB; EMD-16838; -. DR EMDB; EMD-16840; -. DR EMDB; EMD-26673; -. DR EMDB; EMD-27032; -. DR EMDB; EMD-27033; -. DR EMDB; EMD-27034; -. DR EMDB; EMD-27885; -. DR EMDB; EMD-29488; -. DR EMDB; EMD-29489; -. DR EMDB; EMD-29490; -. DR EMDB; EMD-36129; -. DR EMDB; EMD-36131; -. DR EMDB; EMD-36132; -. DR EMDB; EMD-36133; -. DR EMDB; EMD-36134; -. DR EMDB; EMD-36135; -. DR EMDB; EMD-4736; -. DR EMDB; EMD-4742; -. DR SASBDB; Q15370; -. DR SMR; Q15370; -. DR BioGRID; 112785; 336. DR ComplexPortal; CPX-2214; LRR1-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2217; FEM1A-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2218; FEB1B-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2219; FEB1C-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2220; ZYG11B-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2221; APPBP2-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2222; ZER1-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2223; KLHDC10-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2226; KLHDC2-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2228; KLHDC3-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2229; PRAME-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2250; VHL-Elongin C-Elongin B E3 ubiquitin ligase complex. DR CORUM; Q15370; -. DR DIP; DIP-29570N; -. DR IntAct; Q15370; 102. DR MINT; Q15370; -. DR STRING; 9606.ENSP00000262306; -. DR BindingDB; Q15370; -. DR ChEMBL; CHEMBL3301400; -. DR ChEMBL; CHEMBL4296117; -. DR GlyGen; Q15370; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q15370; -. DR MetOSite; Q15370; -. DR PhosphoSitePlus; Q15370; -. DR SwissPalm; Q15370; -. DR BioMuta; ELOB; -. DR DMDM; 32699512; -. DR EPD; Q15370; -. DR jPOST; Q15370; -. DR MassIVE; Q15370; -. DR MaxQB; Q15370; -. DR PaxDb; 9606-ENSP00000262306; -. DR PeptideAtlas; Q15370; -. DR ProteomicsDB; 60548; -. [Q15370-1] DR ProteomicsDB; 6294; -. DR Pumba; Q15370; -. DR TopDownProteomics; Q15370-1; -. [Q15370-1] DR TopDownProteomics; Q15370-2; -. [Q15370-2] DR Antibodypedia; 23893; 370 antibodies from 32 providers. DR DNASU; 6923; -. DR Ensembl; ENST00000262306.11; ENSP00000262306.7; ENSG00000103363.16. [Q15370-2] DR Ensembl; ENST00000409906.9; ENSP00000386652.5; ENSG00000103363.16. [Q15370-1] DR GeneID; 6923; -. DR KEGG; hsa:6923; -. DR MANE-Select; ENST00000409906.9; ENSP00000386652.5; NM_007108.4; NP_009039.1. DR UCSC; uc002crm.4; human. [Q15370-1] DR AGR; HGNC:11619; -. DR CTD; 6923; -. DR DisGeNET; 6923; -. DR GeneCards; ELOB; -. DR HGNC; HGNC:11619; ELOB. DR HPA; ENSG00000103363; Low tissue specificity. DR MIM; 600787; gene. DR neXtProt; NX_Q15370; -. DR OpenTargets; ENSG00000103363; -. DR PharmGKB; PA36378; -. DR VEuPathDB; HostDB:ENSG00000103363; -. DR eggNOG; KOG4495; Eukaryota. DR GeneTree; ENSGT00390000018316; -. DR HOGENOM; CLU_139243_1_0_1; -. DR InParanoid; Q15370; -. DR OMA; GQEQMDQ; -. DR OrthoDB; 2909995at2759; -. DR PhylomeDB; Q15370; -. DR TreeFam; TF325964; -. DR PathwayCommons; Q15370; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. 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-180585; Vif-mediated degradation of APOBEC3G. 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 Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q15370; -. DR SIGNOR; Q15370; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 6923; 795 hits in 1215 CRISPR screens. DR ChiTaRS; TCEB2; human. DR EvolutionaryTrace; Q15370; -. DR GeneWiki; TCEB2; -. DR GenomeRNAi; 6923; -. DR Pharos; Q15370; Tbio. DR PRO; PR:Q15370; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q15370; Protein. DR Bgee; ENSG00000103363; Expressed in left testis and 211 other cell types or tissues. DR ExpressionAtlas; Q15370; baseline and differential. DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB. 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:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0030891; C:VCB complex; IBA:GO_Central. DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:FlyBase. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc. DR GO; GO:0140958; P:target-directed miRNA degradation; IMP:FlyBase. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; TAS:ProtInc. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:UniProtKB. DR CDD; cd01788; Ubl_ElonginB; 1. DR InterPro; IPR039049; ELOB. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR13248:SF4; 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 Genevisible; Q15370; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation pathway. FT CHAIN 1..118 FT /note="Elongin-B" FT /id="PRO_0000114914" FT DOMAIN 1..66 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT REGION 92..118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 84 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P62869" FT MOD_RES 108 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62869" FT MOD_RES 111 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62869" FT VAR_SEQ 118 FT /note="Q -> HLHVHSQTMAKSRNTSWSQCPGLTACSTREPQDGPTQVHPRWGL FT (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_045784" FT STRAND 2..10 FT /evidence="ECO:0007829|PDB:7Z76" FT STRAND 12..19 FT /evidence="ECO:0007829|PDB:7Z76" FT HELIX 24..35 FT /evidence="ECO:0007829|PDB:7Z76" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:7Z76" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:7Z76" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:3ZRF" FT STRAND 53..56 FT /evidence="ECO:0007829|PDB:8EBN" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:7Z76" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:7Z76" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:8C13" FT STRAND 73..81 FT /evidence="ECO:0007829|PDB:7Z76" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:1LM8" FT HELIX 86..89 FT /evidence="ECO:0007829|PDB:2MA9" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:2MA9" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:2JZ3" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:7Z76" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:2JZ3" SQ SEQUENCE 118 AA; 13133 MW; C045F58FBED0EC47 CRC64; MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVQ //