ELOC_HUMAN
ID ELOC_HUMAN Reviewed; 112 AA.
AC Q15369; E5RGD9; Q567Q6;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Elongin-C;
DE Short=EloC;
DE AltName: Full=Elongin 15 kDa subunit;
DE AltName: Full=RNA polymerase II transcription factor SIII subunit C;
DE AltName: Full=SIII p15;
DE AltName: Full=Transcription elongation factor B polypeptide 1;
GN Name=ELOC {ECO:0000312|HGNC:HGNC:11617};
GN Synonyms=TCEB1 {ECO:0000312|HGNC:HGNC:11617};
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.
RC TISSUE=Peripheral blood;
RX PubMed=7821821; DOI=10.1016/0378-1119(94)90467-7;
RA Garrett K.P., Haque D., Conaway R.C., Conaway J.W.;
RT "A human cDNA encoding the small subunit of RNA polymerase II transcription
RT factor SIII.";
RL Gene 150:413-414(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [5]
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12004003; DOI=10.1038/labinvest.3780457;
RA Porkka K., Saramaeki O., Tanner M., Visakorpi T.;
RT "Amplification and overexpression of Elongin C gene discovered in prostate
RT cancer by cDNA microarrays.";
RL Lab. Invest. 82:629-637(2002).
RN [7]
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 [8]
RP INTERACTION WITH TMF1.
RX PubMed=15467733; DOI=10.1038/sj.onc.1208149;
RA Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S.,
RA Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.;
RT "TMF/ARA160 is a BC-box-containing protein that mediates the degradation of
RT Stat3.";
RL Oncogene 23:8908-8919(2004).
RN [9]
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 [10]
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 [11]
RP IDENTIFICATION IN COMPLEX WITH CUL2 AND ZYG11B, AND IDENTIFICATION IN
RP COMPLEX WITH ELOB; ZER1 AND CUL2.
RX PubMed=17304241; DOI=10.1038/sj.embor.7400895;
RA Vasudevan S., Starostina N.G., Kipreos E.T.;
RT "The Caenorhabditis elegans cell-cycle regulator ZYG-11 defines a conserved
RT family of CUL-2 complex components.";
RL EMBO Rep. 8:279-286(2007).
RN [12]
RP INTERACTION WITH HRSV PROTEIN NS1 (MICROBIAL INFECTION).
RX PubMed=17251292; DOI=10.1128/jvi.02303-06;
RA Elliott J., Lynch O.T., Suessmuth Y., Qian P., Boyd C.R., Burrows J.F.,
RA Buick R., Stevenson N.J., Touzelet O., Gadina M., Power U.F.,
RA Johnston J.A.;
RT "Respiratory syncytial virus NS1 protein degrades STAT2 by using the
RT Elongin-Cullin E3 ligase.";
RL J. Virol. 81:3428-3436(2007).
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 NOS2.
RX PubMed=21199876; DOI=10.1074/jbc.m110.190678;
RA Nishiya T., Matsumoto K., Maekawa S., Kajita E., Horinouchi T.,
RA Fujimuro M., Ogasawara K., Uehara T., Miwa S.;
RT "Regulation of inducible nitric-oxide synthase by the SPRY domain- and SOCS
RT box-containing proteins.";
RL J. Biol. Chem. 286:9009-9019(2011).
RN [16]
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 [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 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 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 [22]
RP FUNCTION, PATHWAY, AND UBIQUITINATION.
RX PubMed=30166453; DOI=10.15252/embj.201797508;
RA Chen S.H., Jang G.M., Huettenhain R., Gordon D.E., Du D., Newton B.W.,
RA Johnson J.R., Hiatt J., Hultquist J.F., Johnson T.L., Liu Y.L.,
RA Burton L.A., Ye J., Reichermeier K.M., Stroud R.M., Marson A., Debnath J.,
RA Gross J.D., Krogan N.J.;
RT "CRL4AMBRA1 targets Elongin C for ubiquitination and degradation to
RT modulate CRL5 signaling.";
RL EMBO J. 37:0-0(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) OF 17-112 IN COMPLEX WITH 1-120 OF
RP ELOB AND 54-213 OF VHL, AND 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) OF 17-112 IN COMPLEX WITH ELOB;
RP 52-113 OF VHL AND 549-582 OF HIF1A, AND 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 ELOB; 54-113 OF VHL AND
RP 556-575 OF HIF1A, 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) OF 17-112 IN COMPLEX WITH ELOB ANS
RP SOX4, AND 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:7821821). 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:P83940, ECO:0000269|PubMed:7821821}.
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:30166453, PubMed:29775578). This includes the
CC von Hippel-Lindau ubiquitination complex CBC(VHL) (PubMed:10205047,
CC PubMed:12004076, PubMed:12050673, PubMed:15590694). By binding to BC-
CC box 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 (PubMed:10205047, PubMed:12004076,
CC PubMed:12050673, PubMed:15590694). A number of ECS complexes
CC (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or
CC FEM1C as substrate-recognition component) are part of the DesCEND
CC (destruction via C-end degrons) pathway, which recognizes a C-degron
CC located at the extreme C terminus of target proteins, leading to their
CC ubiquitination and degradation (PubMed:26138980, PubMed:29779948,
CC PubMed:29775578). {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 ECO:0000269|PubMed:30166453}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578,
CC ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453}.
CC -!- SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC
CC subunit (PubMed:17997974). 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 (By similarity). Part of E3 ubiquitin ligase complexes
CC with CUL5 or CUL2, RBX1 and a substrate adapter protein that can be
CC either ASB2, KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B, FEM1C,
CC SOCS1, SOCS5, ELOA, VHL or WSB1 (PubMed:15590694, PubMed:21119685,
CC PubMed:26138980, PubMed:29779948, PubMed:29775578). The elongin BC
CC complex is part of a complex with VHL and hydroxylated HIF1A
CC (PubMed:12050673, PubMed:12004076). Part of an E3 ubiquitin-protein
CC ligase complex including ZYG11B, CUL2 and Elongin BC. Part of an E3
CC ubiquitin-protein ligase complex including ZER1, CUL2 and Elongin BC
CC (PubMed:17304241). Interacts with VHL (PubMed:10205047,
CC PubMed:12050673, PubMed:11006129). Interacts with TMF1
CC (PubMed:15467733). Interacts with SPSB1 (PubMed:17189197). Interacts
CC with SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase
CC complex substrate recognition component (PubMed:23102700). Interacts
CC with NOS2 in the presence of SPSB1 or SPSB2 or SPSB4 (PubMed:21199876).
CC {ECO:0000250|UniProtKB:P83940, ECO:0000269|PubMed:10205047,
CC ECO:0000269|PubMed:11006129, ECO:0000269|PubMed:12004076,
CC ECO:0000269|PubMed:12050673, ECO:0000269|PubMed:15467733,
CC ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:17189197,
CC ECO:0000269|PubMed:17304241, ECO:0000269|PubMed:17997974,
CC ECO:0000269|PubMed:21199876, ECO:0000269|PubMed:23102700,
CC ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578,
CC 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 human respiratory
CC syncytial virus (HRSV) protein NS1. {ECO:0000269|PubMed:17251292}.
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 Q15369; Q96DX5: ASB9; NbExp=3; IntAct=EBI-301231, EBI-745641;
CC Q15369; Q8N668: COMMD1; NbExp=2; IntAct=EBI-301231, EBI-1550112;
CC Q15369; Q13617: CUL2; NbExp=10; IntAct=EBI-301231, EBI-456179;
CC Q15369; Q13618: CUL3; NbExp=3; IntAct=EBI-301231, EBI-456129;
CC Q15369; Q15370: ELOB; NbExp=20; IntAct=EBI-301231, EBI-301238;
CC Q15369; Q96G25: MED8; NbExp=3; IntAct=EBI-301231, EBI-394405;
CC Q15369; Q5VZV1: METTL21C; NbExp=9; IntAct=EBI-301231, EBI-10236049;
CC Q15369; O15524: SOCS1; NbExp=4; IntAct=EBI-301231, EBI-968198;
CC Q15369; O14508: SOCS2; NbExp=2; IntAct=EBI-301231, EBI-617737;
CC Q15369; Q99619: SPSB2; NbExp=3; IntAct=EBI-301231, EBI-2323209;
CC Q15369; Q96A44: SPSB4; NbExp=2; IntAct=EBI-301231, EBI-2323233;
CC Q15369; O41974: GAMMAHV.ORF73; Xeno; NbExp=2; IntAct=EBI-301231, EBI-6933128;
CC Q15369; P12504: vif; Xeno; NbExp=5; IntAct=EBI-301231, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15369-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15369-2; Sequence=VSP_045955;
CC -!- TISSUE SPECIFICITY: Overexpressed in prostate cancer cell line PC-3 and
CC breast cancer cell line SK-BR-3. {ECO:0000269|PubMed:12004003}.
CC -!- PTM: Ubiquitinated by the DCX(AMBRA1) complex, leading to its
CC degradation by the proteasome. {ECO:0000269|PubMed:30166453}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR EMBL; L34587; AAA67650.1; -; mRNA.
DR EMBL; BX649138; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013809; AAH13809.1; -; mRNA.
DR EMBL; BC093065; AAH93065.1; -; mRNA.
DR EMBL; BC100028; AAI00029.1; -; mRNA.
DR EMBL; BC100283; AAI00284.1; -; mRNA.
DR CCDS; CCDS34910.1; -. [Q15369-1]
DR CCDS; CCDS56539.1; -. [Q15369-2]
DR RefSeq; NP_001191786.1; NM_001204857.1. [Q15369-1]
DR RefSeq; NP_001191787.1; NM_001204858.1. [Q15369-1]
DR RefSeq; NP_001191788.1; NM_001204859.1. [Q15369-1]
DR RefSeq; NP_001191789.1; NM_001204860.1. [Q15369-1]
DR RefSeq; NP_001191790.1; NM_001204861.1. [Q15369-1]
DR RefSeq; NP_001191791.1; NM_001204862.1. [Q15369-1]
DR RefSeq; NP_001191792.1; NM_001204863.1. [Q15369-2]
DR RefSeq; NP_001191793.1; NM_001204864.1. [Q15369-2]
DR RefSeq; NP_005639.1; NM_005648.3. [Q15369-1]
DR RefSeq; XP_011515882.1; XM_011517580.2. [Q15369-1]
DR RefSeq; XP_011515883.1; XM_011517581.2. [Q15369-1]
DR PDB; 1LM8; X-ray; 1.85 A; C=17-112.
DR PDB; 1LQB; X-ray; 2.00 A; B=17-112.
DR PDB; 1VCB; X-ray; 2.70 A; B/E/H/K=1-112.
DR PDB; 2C9W; X-ray; 1.90 A; C=17-112.
DR PDB; 2IZV; X-ray; 2.55 A; C=17-112.
DR PDB; 2MA9; NMR; -; C=19-109.
DR PDB; 3DCG; X-ray; 2.40 A; B/D=17-112.
DR PDB; 3ZKJ; X-ray; 2.58 A; B/E=17-112.
DR PDB; 3ZNG; X-ray; 2.85 A; B/E=17-112.
DR PDB; 3ZRC; X-ray; 2.90 A; B/E/H/K=17-112.
DR PDB; 3ZRF; X-ray; 2.80 A; B/E/H/K=17-112.
DR PDB; 3ZTC; X-ray; 2.65 A; B/E/H/K=17-112.
DR PDB; 3ZTD; X-ray; 2.79 A; B/E/H/K=17-112.
DR PDB; 3ZUN; X-ray; 2.50 A; B/E/H/K=17-112.
DR PDB; 4AJY; X-ray; 1.73 A; C=17-112.
DR PDB; 4AWJ; X-ray; 2.50 A; B/E/H/K=17-112.
DR PDB; 4B95; X-ray; 2.80 A; B/E/H/K=18-112.
DR PDB; 4B9K; X-ray; 2.00 A; B/E/H/K=17-112.
DR PDB; 4BKS; X-ray; 2.20 A; B/E/H/K=17-112.
DR PDB; 4BKT; X-ray; 2.35 A; B/E/H/K=17-112.
DR PDB; 4N9F; X-ray; 3.30 A; 5/B/E/K/Q/T/Y/Z/h/n/t/z=17-112.
DR PDB; 4W9C; X-ray; 2.20 A; B/E/H/K=17-112.
DR PDB; 4W9D; X-ray; 2.20 A; B/E/H/K=17-112.
DR PDB; 4W9E; X-ray; 2.60 A; B/E/H/K=17-112.
DR PDB; 4W9F; X-ray; 2.10 A; B/E/H/K=17-112.
DR PDB; 4W9G; X-ray; 2.70 A; B/E/H/K=17-112.
DR PDB; 4W9H; X-ray; 2.10 A; B/E/H/K=17-112.
DR PDB; 4W9I; X-ray; 2.40 A; B/E/H/K=17-112.
DR PDB; 4W9J; X-ray; 2.20 A; B/E/H/K=17-112.
DR PDB; 4W9K; X-ray; 2.10 A; B/E/H/K=17-112.
DR PDB; 4W9L; X-ray; 2.20 A; B/E/H/K=17-112.
DR PDB; 4WQO; X-ray; 3.20 A; C=17-112.
DR PDB; 5BO4; X-ray; 2.90 A; C/F/I/L/O/R=17-112.
DR PDB; 5LLI; X-ray; 2.40 A; B/E/H/K=17-112.
DR PDB; 5N4W; X-ray; 3.90 A; C=17-112.
DR PDB; 5NVV; X-ray; 2.10 A; B/E/H/K=17-112.
DR PDB; 5NVW; X-ray; 2.20 A; B/E/H/K=17-112.
DR PDB; 5NVX; X-ray; 2.20 A; B/E/H/K=17-112.
DR PDB; 5NVY; X-ray; 2.90 A; B/E/H/K=17-112.
DR PDB; 5NVZ; X-ray; 2.70 A; B/E/H/K=17-112.
DR PDB; 5NW0; X-ray; 2.30 A; B/E/H/K=17-112.
DR PDB; 5NW1; X-ray; 2.10 A; B/E/H/K=17-112.
DR PDB; 5NW2; X-ray; 2.20 A; B/E/H/K=17-112.
DR PDB; 5T35; X-ray; 2.70 A; C/G=17-112.
DR PDB; 6BVB; X-ray; 2.00 A; C=17-112.
DR PDB; 6C5X; X-ray; 3.10 A; C/F=17-112.
DR PDB; 6FMI; X-ray; 2.80 A; B/E=17-112.
DR PDB; 6FMJ; X-ray; 2.45 A; B/E/H/K=17-112.
DR PDB; 6FMK; X-ray; 2.75 A; B/E/H/K=17-112.
DR PDB; 6GFX; X-ray; 1.83 A; B=17-112.
DR PDB; 6GFY; X-ray; 2.70 A; B/E/H/K=17-112.
DR PDB; 6GFZ; X-ray; 2.30 A; B/E/H/K=17-112.
DR PDB; 6GMN; X-ray; 1.94 A; B/E/H/K=17-112.
DR PDB; 6GMQ; X-ray; 2.75 A; B/E=17-111, H/K=17-112.
DR PDB; 6GMR; X-ray; 1.75 A; C=17-112.
DR PDB; 6GMX; X-ray; 2.53 A; B/H/K=17-112, E=17-111.
DR PDB; 6HAX; X-ray; 2.35 A; C/G=17-112.
DR PDB; 6HAY; X-ray; 2.24 A; C/G=17-112.
DR PDB; 6HR2; X-ray; 1.76 A; C/G=17-112.
DR PDB; 6I4X; X-ray; 2.69 A; C=17-112.
DR PDB; 6I5J; X-ray; 2.80 A; C/F=17-112.
DR PDB; 6I5N; X-ray; 1.98 A; C/F=17-112.
DR PDB; 6I7R; X-ray; 1.95 A; C=16-112.
DR PDB; 6P59; X-ray; 2.94 A; E/Z=1-112.
DR PDB; 6R7F; EM; 8.20 A; Q=1-112.
DR PDB; 6R7H; EM; 8.80 A; Q=1-112.
DR PDB; 6R7N; EM; 6.50 A; Q=1-112.
DR PDB; 6SIS; X-ray; 3.50 A; C/G=17-112.
DR PDB; 6V9H; EM; 4.10 A; D=17-112.
DR PDB; 6ZHC; X-ray; 1.92 A; CCC=17-112.
DR PDB; 7CJB; X-ray; 2.80 A; C/G/K/O=13-112.
DR PDB; 7JTO; X-ray; 1.70 A; K=17-112.
DR PDB; 7JTP; X-ray; 2.12 A; K=17-112.
DR PDB; 7KHH; X-ray; 2.28 A; B=17-112.
DR PDB; 7M6T; X-ray; 3.19 A; C=17-112.
DR PDB; 7PI4; X-ray; 2.24 A; CCC=17-112.
DR PDB; 7PLO; EM; 2.80 A; R=1-112.
DR PDB; 7Q2J; X-ray; 2.50 A; B=17-112.
DR PDBsum; 1LM8; -.
DR PDBsum; 1LQB; -.
DR PDBsum; 1VCB; -.
DR PDBsum; 2C9W; -.
DR PDBsum; 2IZV; -.
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; 6I7R; -.
DR PDBsum; 6P59; -.
DR PDBsum; 6R7F; -.
DR PDBsum; 6R7H; -.
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; Q15369; -.
DR BMRB; Q15369; -.
DR SMR; Q15369; -.
DR BioGRID; 112783; 222.
DR CORUM; Q15369; -.
DR DIP; DIP-29571N; -.
DR IntAct; Q15369; 91.
DR MINT; Q15369; -.
DR STRING; 9606.ENSP00000478121; -.
DR BindingDB; Q15369; -.
DR ChEMBL; CHEMBL3301400; -.
DR ChEMBL; CHEMBL4296117; -.
DR GlyGen; Q15369; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15369; -.
DR MetOSite; Q15369; -.
DR PhosphoSitePlus; Q15369; -.
DR SwissPalm; Q15369; -.
DR BioMuta; ELOC; -.
DR DMDM; 32699511; -.
DR EPD; Q15369; -.
DR jPOST; Q15369; -.
DR MassIVE; Q15369; -.
DR MaxQB; Q15369; -.
DR PaxDb; Q15369; -.
DR PeptideAtlas; Q15369; -.
DR PRIDE; Q15369; -.
DR ProteomicsDB; 15637; -.
DR ProteomicsDB; 60547; -. [Q15369-1]
DR TopDownProteomics; Q15369-1; -. [Q15369-1]
DR Antibodypedia; 12329; 261 antibodies from 29 providers.
DR DNASU; 6921; -.
DR Ensembl; ENST00000284811.12; ENSP00000284811.8; ENSG00000154582.18. [Q15369-1]
DR Ensembl; ENST00000518127.5; ENSP00000428334.1; ENSG00000154582.18. [Q15369-1]
DR Ensembl; ENST00000520210.1; ENSP00000430224.1; ENSG00000154582.18. [Q15369-2]
DR Ensembl; ENST00000520242.6; ENSP00000428171.1; ENSG00000154582.18. [Q15369-1]
DR Ensembl; ENST00000522337.5; ENSP00000429906.1; ENSG00000154582.18. [Q15369-1]
DR Ensembl; ENST00000523815.5; ENSP00000428074.1; ENSG00000154582.18. [Q15369-1]
DR Ensembl; ENST00000622804.2; ENSP00000478121.1; ENSG00000154582.18. [Q15369-1]
DR Ensembl; ENST00000687224.1; ENSP00000509184.1; ENSG00000154582.18. [Q15369-1]
DR Ensembl; ENST00000688584.1; ENSP00000509989.1; ENSG00000154582.18. [Q15369-2]
DR GeneID; 6921; -.
DR KEGG; hsa:6921; -.
DR MANE-Select; ENST00000520242.6; ENSP00000428171.1; NM_005648.4; NP_005639.1.
DR UCSC; uc003xzx.3; human. [Q15369-1]
DR CTD; 6921; -.
DR DisGeNET; 6921; -.
DR GeneCards; ELOC; -.
DR HGNC; HGNC:11617; ELOC.
DR HPA; ENSG00000154582; Low tissue specificity.
DR MIM; 600788; gene.
DR neXtProt; NX_Q15369; -.
DR OpenTargets; ENSG00000154582; -.
DR PharmGKB; PA36376; -.
DR VEuPathDB; HostDB:ENSG00000154582; -.
DR eggNOG; KOG3473; Eukaryota.
DR GeneTree; ENSGT00390000011717; -.
DR HOGENOM; CLU_130038_0_2_1; -.
DR InParanoid; Q15369; -.
DR OMA; VCEYLYY; -.
DR PhylomeDB; Q15369; -.
DR TreeFam; TF300233; -.
DR PathwayCommons; Q15369; -.
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; Q15369; -.
DR SIGNOR; Q15369; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 6921; 534 hits in 1058 CRISPR screens.
DR ChiTaRS; TCEB1; human.
DR EvolutionaryTrace; Q15369; -.
DR GeneWiki; TCEB1; -.
DR GenomeRNAi; 6921; -.
DR Pharos; Q15369; Tbio.
DR PRO; PR:Q15369; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q15369; protein.
DR Bgee; ENSG00000154582; Expressed in oocyte and 202 other tissues.
DR ExpressionAtlas; Q15369; baseline and differential.
DR Genevisible; Q15369; HS.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:FlyBase.
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:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR039948; ELC1.
DR InterPro; IPR001232; SKP1-like.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR016073; Skp1_comp_POZ.
DR PANTHER; PTHR20648; PTHR20648; 1.
DR Pfam; PF03931; Skp1_POZ; 1.
DR SMART; SM00512; Skp1; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Host-virus interaction; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..112
FT /note="Elongin-C"
FT /id="PRO_0000187258"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045955"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:7JTO"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3ZNG"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:7JTO"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:7JTO"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:7JTO"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:6I7R"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6I7R"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7JTO"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6HR2"
FT HELIX 67..83
FT /evidence="ECO:0007829|PDB:7JTO"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6GMQ"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:7JTO"
SQ SEQUENCE 112 AA; 12473 MW; 98D88696E883538B CRC64;
MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV
NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA LELLMAANFL DC
