ELOC_MOUSE
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 03-AUG-2022, entry version 158.
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 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. A number of ECS complexes (containing either
CC KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-
CC recognition component) are part of the DesCEND (destruction via C-end
CC degrons) pathway, which recognizes a C-degron located at the extreme C
CC terminus of target proteins, leading to their ubiquitination and
CC degradation. {ECO:0000250|UniProtKB:Q15369}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q15369}.
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, SOCS1, SOCS5, ELOA, VHL or WSB1 (PubMed:10051596,
CC PubMed:11384984, PubMed:9869640). The elongin BC complex is part of a
CC complex with VHL and hydroxylated HIF1A. Part of an E3 ubiquitin-
CC protein ligase complex including ZYG11B, CUL2 and Elongin BC. Part of
CC an E3 ubiquitin-protein ligase complex including ZER1, CUL2 and Elongin
CC BC. Interacts with VHL. Interacts with TMF1. Interacts with SPSB1.
CC Interacts with SPSB1. Interacts with KLHDC10; which may be an E3
CC ubiquitin ligase complex substrate recognition component. Interacts
CC with NOS2 in the presence of SPSB1 or SPSB2 or SPSB4 (By similarity).
CC {ECO:0000250|UniProtKB:Q15369, 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:9869640}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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}.
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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 iPTMnet; P83940; -.
DR PhosphoSitePlus; P83940; -.
DR EPD; P83940; -.
DR jPOST; P83940; -.
DR MaxQB; P83940; -.
DR PaxDb; P83940; -.
DR PeptideAtlas; P83940; -.
DR PRIDE; P83940; -.
DR ProteomicsDB; 275452; -.
DR Antibodypedia; 12329; 261 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 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; VCEYLYY; -.
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 65 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:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 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; 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; 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
