ID ELOC_MOUSE Reviewed; 112 AA. AC P83940; Q63182; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 1. DT 28-JUN-2023, entry version 163. 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=Stromal membrane-associated protein SMAP1B homolog; DE AltName: Full=Transcription elongation factor B polypeptide 1; GN Name=Eloc {ECO:0000312|MGI:MGI:1915173}; GN Synonyms=Tceb1 {ECO:0000312|MGI:MGI:1915173}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Spinal cord; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP INTERACTION WITH SOCS1. RX PubMed=9869640; DOI=10.1101/gad.12.24.3872; RA Kamura T., Sato S., Haque D., Liu L., Kaelin W.G. Jr., Conaway R.C., RA Conaway J.W.; RT "The Elongin BC complex interacts with the conserved SOCS-box motif present RT in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families."; RL Genes Dev. 12:3872-3881(1998). RN [4] RP INTERACTION WITH SOCS1. RX PubMed=10051596; DOI=10.1073/pnas.96.5.2071; RA Zhang J.-G., Farley A., Nicholson S.E., Willson T.A., Zugaro L.M., RA Simpson R.J., Moritz R.L., Cary D., Richardson R., Hausmann G., Kile B.J., RA Kent S.B.H., Alexander W.S., Metcalf D., Hilton D.J., Nicola N.A., Baca M.; RT "The conserved SOCS box motif in suppressors of cytokine signaling binds to RT elongins B and C and may couple bound proteins to proteasomal RT degradation."; RL Proc. Natl. Acad. Sci. U.S.A. 96:2071-2076(1999). RN [5] RP IDENTIFICATION IN E3 UBIQUITIN LIGASE COMPLEXES. RX PubMed=11384984; DOI=10.1074/jbc.m103093200; RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E., RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.; RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can RT assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase."; RL J. Biol. Chem. 276:29748-29753(2001). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP FUNCTION, AND INTERACTION WITH EPOP. RX PubMed=27863225; DOI=10.1016/j.molcel.2016.10.018; RA Beringer M., Pisano P., Di Carlo V., Blanco E., Chammas P., Vizan P., RA Gutierrez A., Aranda S., Payer B., Wierer M., Di Croce L.; RT "EPOP functionally links elongin and Polycomb in pluripotent stem cells."; RL Mol. Cell 64:645-658(2016). RN [8] RP FUNCTION, AND INTERACTION WITH EPOP. RX PubMed=27863226; DOI=10.1016/j.molcel.2016.10.019; RA Liefke R., Karwacki-Neisius V., Shi Y.; RT "EPOP interacts with elongin BC and USP7 to modulate the chromatin RT landscape."; RL Mol. Cell 64:659-672(2016). RN [9] RP ERRATUM OF PUBMED:27863226. RX PubMed=28061330; DOI=10.1016/j.molcel.2016.12.006; RA Liefke R., Karwacki-Neisius V., Shi Y.; RL Mol. Cell 65:202-202(2017). RN [10] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=33590678; DOI=10.15252/embr.202052164; RA Villa F., Fujisawa R., Ainsworth J., Nishimura K., Lie-A-Ling M., RA Lacaud G., Labib K.P.; RT "CUL2LRR1, TRAIP and p97 control CMG helicase disassembly in the mammalian RT cell cycle."; RL EMBO Rep. 22:e52164-e52164(2021). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 17-112 IN COMPLEX WITH ELONGIN B RP AND DROSOPHILA GUS. RX PubMed=16498413; DOI=10.1038/sj.emboj.7600994; RA Woo J.S., Imm J.H., Min C.K., Kim K.J., Cha S.S., Oh B.H.; RT "Structural and functional insights into the B30.2/SPRY domain."; RL EMBO J. 25:1353-1363(2006). CC -!- FUNCTION: SIII, also known as elongin, is a general transcription CC elongation factor that increases the RNA polymerase II transcription CC elongation past template-encoded arresting sites. Subunit A is CC transcriptionally active and its transcription activity is strongly CC enhanced by binding to the dimeric complex of the SIII regulatory CC subunits B and C (elongin BC complex) (By similarity). In embryonic CC stem cells, the elongin BC complex is recruited by EPOP to Polycomb CC group (PcG) target genes in order generate genomic region that display CC both active and repressive chromatin properties, an important feature CC of pluripotent stem cells (PubMed:27863225, PubMed:27863226). CC {ECO:0000250|UniProtKB:Q15369, ECO:0000269|PubMed:27863225, CC ECO:0000269|PubMed:27863226}. CC -!- FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C- CC CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which CC mediate the ubiquitination of target proteins. This includes the von CC Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box CC motifs it seems to link target recruitment subunits, like VHL and CC members of the SOCS box family, to Cullin/RBX1 modules that activate E2 CC ubiquitination enzymes. As part of a multisubunit ubiquitin ligase CC complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, CC RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (By CC similarity). A number of ECS complexes (containing either KLHDC2, CC KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition CC component) are part of the DesCEND (destruction via C-end degrons) CC pathway, which recognizes a C-degron located at the extreme C terminus CC of target proteins, leading to their ubiquitination and degradation (By CC similarity). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome CC disassembly by VCP and chromatin extraction during S-phase CC (PubMed:33590678). {ECO:0000250|UniProtKB:Q15369, CC ECO:0000269|PubMed:33590678}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:33590678}. CC -!- SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC CC subunit (By similarity). The elongin BC complex interacts with EPOP; CC leading to recruit the elongin BC complex to Polycomb group (PcG) CC target genes, thereby restricting excessive activity of the PRC2/EED- CC EZH2 complex (PubMed:27863225, PubMed:27863226). Part of E3 ubiquitin CC ligase complexes with CUL5 or CUL2, RBX1 and a substrate adapter CC protein that can be either ASB2, KLHDC2, KLHDC3, KLHDC10, APPBP2, CC FEM1A, FEM1B, FEM1C, LRR1, SOCS1, SOCS5, ELOA, VHL or WSB1 CC (PubMed:10051596, PubMed:11384984, PubMed:9869640, PubMed:33590678). CC The elongin BC complex is part of a complex with VHL and hydroxylated CC HIF1A. Part of an E3 ubiquitin-protein ligase complex including ZYG11B, CC CUL2 and Elongin BC. Part of an E3 ubiquitin-protein ligase complex CC including ZER1, CUL2 and Elongin BC. Interacts with VHL. Interacts with CC TMF1. Interacts with SPSB1. Interacts with SPSB1. Interacts with CC KLHDC10; which may be an E3 ubiquitin ligase complex substrate CC recognition component. Interacts with NOS2 in the presence of SPSB1 or CC SPSB2 or SPSB4 (By similarity). As part of the Elongin BC E3 ubiquitin CC ligase complex; interacts with NRBP1 (By similarity). Component of the CC ECS(PCMTD1) complex with the substrate recognition subunit PCMTD1. CC Interacts with PCMTD1 (via the BC-box); the interaction is direct and CC stabilizes PCMTD1 (By similarity). {ECO:0000250|UniProtKB:Q15369, CC ECO:0000250|UniProtKB:Q15370, ECO:0000269|PubMed:10051596, CC ECO:0000269|PubMed:11384984, ECO:0000269|PubMed:16498413, CC ECO:0000269|PubMed:27863225, ECO:0000269|PubMed:27863226, CC ECO:0000269|PubMed:33590678, ECO:0000269|PubMed:9869640}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:33590678}. CC -!- PTM: Ubiquitinated by the DCX(AMBRA1) complex, leading to its CC degradation by the proteasome. {ECO:0000250|UniProtKB:Q15369}. CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK013089; BAB28641.1; -; mRNA. DR EMBL; AK011757; BAB27825.1; -; mRNA. DR EMBL; AK011958; BAB27939.1; -; mRNA. DR EMBL; AK012909; BAB28546.1; -; mRNA. DR EMBL; AK039746; BAC30437.1; -; mRNA. DR EMBL; BC009104; AAH09104.1; -; mRNA. DR EMBL; BC028545; AAH28545.1; -; mRNA. DR CCDS; CCDS35517.1; -. DR RefSeq; NP_001297399.1; NM_001310470.1. DR RefSeq; NP_080732.1; NM_026456.4. DR RefSeq; XP_006495624.1; XM_006495561.2. DR RefSeq; XP_006495625.1; XM_006495562.1. DR RefSeq; XP_006495626.1; XM_006495563.3. DR RefSeq; XP_006495627.1; XM_006495564.1. DR PDB; 2FNJ; X-ray; 1.80 A; C=17-112. DR PDB; 2JZ3; NMR; -; C=17-112. DR PDB; 4JGH; X-ray; 3.00 A; C=17-112. DR PDBsum; 2FNJ; -. DR PDBsum; 2JZ3; -. DR PDBsum; 4JGH; -. DR AlphaFoldDB; P83940; -. DR BMRB; P83940; -. DR SMR; P83940; -. DR BioGRID; 212537; 39. DR CORUM; P83940; -. DR DIP; DIP-42814N; -. DR IntAct; P83940; 19. DR MINT; P83940; -. DR STRING; 10090.ENSMUSP00000140422; -. DR GlyGen; P83940; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P83940; -. DR PhosphoSitePlus; P83940; -. DR SwissPalm; P83940; -. DR EPD; P83940; -. DR jPOST; P83940; -. DR MaxQB; P83940; -. DR PaxDb; P83940; -. DR PeptideAtlas; P83940; -. DR ProteomicsDB; 275452; -. DR Antibodypedia; 12329; 278 antibodies from 29 providers. DR DNASU; 67923; -. DR Ensembl; ENSMUST00000115352; ENSMUSP00000111009; ENSMUSG00000079658. DR Ensembl; ENSMUST00000185771; ENSMUSP00000139675; ENSMUSG00000079658. DR Ensembl; ENSMUST00000186948; ENSMUSP00000140962; ENSMUSG00000079658. DR Ensembl; ENSMUST00000188641; ENSMUSP00000140422; ENSMUSG00000079658. DR GeneID; 67923; -. DR KEGG; mmu:67923; -. DR UCSC; uc007ajv.1; mouse. DR AGR; MGI:1915173; -. DR CTD; 6921; -. DR MGI; MGI:1915173; Eloc. DR VEuPathDB; HostDB:ENSMUSG00000079658; -. DR eggNOG; KOG3473; Eukaryota. DR GeneTree; ENSGT00390000011717; -. DR HOGENOM; CLU_130038_0_2_1; -. DR InParanoid; P83940; -. DR OMA; AMVSPII; -. DR OrthoDB; 5030121at2759; -. DR PhylomeDB; P83940; -. DR TreeFam; TF300233; -. DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation. DR Reactome; R-MMU-8951664; Neddylation. DR Reactome; R-MMU-9705462; Inactivation of CSF3 (G-CSF) signaling. DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 67923; 26 hits in 70 CRISPR screens. DR ChiTaRS; Tceb1; mouse. DR EvolutionaryTrace; P83940; -. DR PRO; PR:P83940; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P83940; protein. DR Bgee; ENSMUSG00000079658; Expressed in morula and 283 other tissues. DR ExpressionAtlas; P83940; baseline and differential. DR Genevisible; P83940; MM. DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070449; C:elongin complex; IDA:UniProtKB. DR GO; GO:0030891; C:VCB complex; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central. DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR GO; GO:0140958; P:target-directed miRNA degradation; ISO:MGI. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; ISO:MGI. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR CDD; cd18321; BTB_POZ_EloC; 1. DR IDEAL; IID50219; -. 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; ELONGIN-C; 1. DR PANTHER; PTHR20648:SF0; ELONGIN-C; 1. DR Pfam; PF03931; Skp1_POZ; 1. DR SMART; SM00512; Skp1; 1. DR SUPFAM; SSF54695; POZ domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Nucleus; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..112 FT /note="Elongin-C" FT /id="PRO_0000187259" FT STRAND 18..22 FT /evidence="ECO:0007829|PDB:2FNJ" FT STRAND 28..32 FT /evidence="ECO:0007829|PDB:2FNJ" FT HELIX 33..36 FT /evidence="ECO:0007829|PDB:2FNJ" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:2JZ3" FT HELIX 40..47 FT /evidence="ECO:0007829|PDB:2FNJ" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:4JGH" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:4JGH" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:2FNJ" FT HELIX 67..84 FT /evidence="ECO:0007829|PDB:2FNJ" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:4JGH" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:2FNJ" FT HELIX 100..110 FT /evidence="ECO:0007829|PDB:2FNJ" SQ SEQUENCE 112 AA; 12473 MW; 98D88696E883538B CRC64; MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA LELLMAANFL DC //