ELOB_RAT
ID ELOB_RAT Reviewed; 118 AA.
AC P62870; Q63529; Q80W20;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
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; Synonyms=Tceb2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Liver;
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].
RC TISSUE=Pituitary;
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 PROTEIN SEQUENCE OF 1-8; 12-28; 44-55 AND 69-89, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Pheochromocytoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (AUG-2006) to UniProtKB.
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8244996; DOI=10.1016/s0021-9258(19)74431-7;
RA Bradsher J.N., Jackson K.W., Conaway R.C., Conaway J.W.;
RT "RNA polymerase II transcription factor SIII. I. Identification,
RT purification, and properties.";
RL J. Biol. Chem. 268:25587-25593(1993).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P62869, ECO:0000250|UniProtKB:Q15370}.
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:Q15370}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q15370}.
CC -!- SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC
CC subunit. The elongin BC complex interacts with EPOP; leading to recruit
CC the elongin BC complex to Polycomb group (PcG) target genes, thereby
CC restricting excessive activity of the PRC2/EED-EZH2 complex. 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. Interacts
CC with VHL. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB
CC and CUL2. Interacts with SPSB1. Interacts with KLHDC10; which may be an
CC E3 ubiquitin ligase complex substrate recognition component. May also
CC interact with DCUN1D1, DCUN1D2, DCUN1D3 and DCUN1D5 (By similarity).
CC {ECO:0000250|UniProtKB:P62869, ECO:0000250|UniProtKB:Q15370}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; L42855; AAA80968.1; -; mRNA.
DR EMBL; BC058463; AAH58463.1; -; mRNA.
DR RefSeq; NP_112391.1; NM_031129.3.
DR AlphaFoldDB; P62870; -.
DR BMRB; P62870; -.
DR SMR; P62870; -.
DR BioGRID; 249665; 8.
DR CORUM; P62870; -.
DR IntAct; P62870; 7.
DR MINT; P62870; -.
DR STRING; 10116.ENSRNOP00000006892; -.
DR iPTMnet; P62870; -.
DR PhosphoSitePlus; P62870; -.
DR SwissPalm; P62870; -.
DR jPOST; P62870; -.
DR PaxDb; P62870; -.
DR PRIDE; P62870; -.
DR GeneID; 81807; -.
DR KEGG; rno:81807; -.
DR UCSC; RGD:621200; rat.
DR CTD; 6923; -.
DR RGD; 621200; Elob.
DR VEuPathDB; HostDB:ENSRNOG00000004814; -.
DR eggNOG; KOG4495; Eukaryota.
DR HOGENOM; CLU_139243_0_0_1; -.
DR InParanoid; P62870; -.
DR OMA; RKKMTIF; -.
DR OrthoDB; 1637528at2759; -.
DR PhylomeDB; P62870; -.
DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P62870; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000004814; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; P62870; baseline and differential.
DR Genevisible; P62870; RN.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0070449; C:elongin complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; IDA:RGD.
DR GO; GO:0030891; C:VCB complex; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:RGD.
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 Acetylation; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation pathway.
FT CHAIN 1..118
FT /note="Elongin-B"
FT /id="PRO_0000114916"
FT DOMAIN 1..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 91..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.3"
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"
SQ SEQUENCE 118 AA; 13170 MW; BA702F24CEC0FC02 CRC64;
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPE EQRLYKDDQL LDDGKTLGEC
GFTSQTARPQ APATVGLAFR ADDTFEALRI EPFSSPPELP DVMKPQDSGG SANEQAVQ
