ELOB_HUMAN
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 03-AUG-2022, entry version 212.
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 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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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).
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). 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
CC (PubMed:26138980, PubMed:29779948, PubMed:29775578).
CC {ECO:0000269|PubMed:10205047, ECO:0000269|PubMed:12004076,
CC ECO:0000269|PubMed:12050673, ECO:0000269|PubMed:15590694,
CC ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578,
CC 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, SOCS1, SOCS5, ELOA, VHL or WSB1
CC (PubMed:15590694, PubMed:19413330 PubMed:22286099, PubMed:26138980,
CC PubMed:29779948, PubMed:29775578). Interacts with VHL (PubMed:10205047,
CC PubMed:11006129). Found in a complex composed of LIMD1, VHL,
CC EGLN1/PHD2, ELOB and CUL2. Interacts with SPSB1 (PubMed:17189197).
CC Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex
CC substrate recognition component (PubMed:23102700). May also interact
CC with DCUN1D1, DCUN1D2, DCUN1D3 and DCUN1D5 (PubMed:26906416).
CC {ECO:0000250|UniProtKB:P62869, ECO:0000269|PubMed:10205047,
CC ECO:0000269|PubMed:11006129, ECO:0000269|PubMed:15590694,
CC ECO:0000269|PubMed:17189197, ECO:0000269|PubMed:17997974,
CC ECO:0000269|PubMed:22286099, ECO:0000269|PubMed:23102700,
CC ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:26906416,
CC ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948}.
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}.
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};
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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 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 AlphaFoldDB; Q15370; -.
DR BMRB; Q15370; -.
DR SMR; Q15370; -.
DR BioGRID; 112785; 265.
DR CORUM; Q15370; -.
DR DIP; DIP-29570N; -.
DR IntAct; Q15370; 100.
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; Q15370; -.
DR PeptideAtlas; Q15370; -.
DR PRIDE; Q15370; -.
DR ProteomicsDB; 60548; -. [Q15370-1]
DR ProteomicsDB; 6294; -.
DR TopDownProteomics; Q15370-1; -. [Q15370-1]
DR TopDownProteomics; Q15370-2; -. [Q15370-2]
DR Antibodypedia; 23893; 334 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 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; RKKMTIF; -.
DR OrthoDB; 1338040at2759; -.
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 UniPathway; UPA00143; -.
DR BioGRID-ORCS; 6923; 754 hits in 1134 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 209 other tissues.
DR ExpressionAtlas; Q15370; baseline and differential.
DR Genevisible; Q15370; HS.
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:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
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; 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:7JTO"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:7JTO"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:7JTO"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:7JTO"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:7JTO"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3ZRF"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6I4X"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:7JTO"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:7JTO"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6FMK"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:7JTO"
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:4AJY"
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
