ID ELOB_MOUSE Reviewed; 118 AA.
AC P62869; Q63529; Q80W20;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 01-MAY-2013, entry version 86.
DE RecName: Full=Transcription elongation factor B polypeptide 2;
DE AltName: Full=Elongin 18 kDa subunit;
DE AltName: Full=Elongin-B;
DE Short=EloB;
DE AltName: Full=RNA polymerase II transcription factor SIII subunit B;
DE AltName: Full=SIII p18;
GN Name=Tceb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Hippocampus, Kidney, and Small intestine;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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/6; TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
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.,
RA Kile B.J., Kent S.B.H., Alexander W.S., Metcalf D., Hilton D.J.,
RA Nicola N.A., Baca M.;
RT "The conserved SOCS box motif in suppressors of cytokine signaling
RT binds to 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 [4]
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
RT can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ELONGIN C AND
RP 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
CC transcription elongation past template-encoded arresting sites.
CC Subunit A is transcriptionally active and its transcription
CC activity is strongly enhanced by binding to the dimeric complex of
CC the SIII regulatory subunits B and C (elongin BC complex).
CC -!- FUNCTION: The elongin BC complex seems to be involved as an
CC adapter protein in the proteasomal degradation of target proteins
CC via different E3 ubiquitin ligase complexes, including the von
CC Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-
CC box motifs it seems to link target recruitment subunits, like VHL
CC and members of the SOCS box family, to Cullin/RBX1 modules that
CC activate E2 ubiquitination enzymes.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Heterotrimer of an A (A1, A2 or A3), B and C subunit.
CC Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and
CC a substrate adapter protein that can be either SOCS1, SOCS5,
CC TCEB3, VHL or WSB1. Interacts with VHL. Found in a complex
CC composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with
CC SPSB1.
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR EMBL; AK019358; BAB31677.1; -; mRNA.
DR EMBL; AK002223; BAB21946.1; -; mRNA.
DR EMBL; AK002868; BAB22417.1; -; mRNA.
DR EMBL; AK003277; BAB22684.1; -; mRNA.
DR EMBL; AK008477; BAB25690.1; -; mRNA.
DR EMBL; AK008534; BAB25727.1; -; mRNA.
DR EMBL; AK012254; BAB28121.1; -; mRNA.
DR EMBL; AK019181; BAB31590.1; -; mRNA.
DR EMBL; AK019218; BAB31608.1; -; mRNA.
DR EMBL; BC051927; AAH51927.2; -; mRNA.
DR EMBL; BC056983; AAH56983.1; -; mRNA.
DR IPI; IPI00131224; -.
DR RefSeq; NP_080581.1; NM_026305.2.
DR UniGene; Mm.153758; -.
DR PDB; 2FNJ; X-ray; 1.80 A; B=1-118.
DR PDBsum; 2FNJ; -.
DR ProteinModelPortal; P62869; -.
DR SMR; P62869; 1-98.
DR IntAct; P62869; 2.
DR MINT; MINT-2789207; -.
DR PhosphoSite; P62869; -.
DR REPRODUCTION-2DPAGE; P62869; -.
DR PaxDb; P62869; -.
DR PRIDE; P62869; -.
DR Ensembl; ENSMUST00000069579; ENSMUSP00000066210; ENSMUSG00000055839.
DR GeneID; 67673; -.
DR KEGG; mmu:67673; -.
DR UCSC; uc008atr.1; mouse.
DR CTD; 6923; -.
DR MGI; MGI:1914923; Tceb2.
DR eggNOG; NOG316144; -.
DR GeneTree; ENSGT00390000018316; -.
DR HOGENOM; HOG000293425; -.
DR HOVERGEN; HBG008581; -.
DR InParanoid; P62869; -.
DR KO; K03873; -.
DR OMA; TLGDCGF; -.
DR OrthoDB; EOG4BG8X6; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P62869; -.
DR NextBio; 325215; -.
DR Bgee; P62869; -.
DR Genevestigator; P62869; -.
DR GermOnline; ENSMUSG00000055839; Mus musculus.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR000626; Ubiquitin.
DR InterPro; IPR019955; Ubiquitin_supergroup.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation pathway.
FT CHAIN 1 118 Transcription elongation factor B
FT polypeptide 2.
FT /FTId=PRO_0000114915.
FT DOMAIN 1 79 Ubiquitin-like.
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT STRAND 2 10
FT STRAND 12 19
FT HELIX 24 35
FT HELIX 39 41
FT STRAND 42 46
FT HELIX 57 60
FT TURN 64 66
FT STRAND 73 83
SQ SEQUENCE 118 AA; 13170 MW; BA702F24CEC0FC02 CRC64;
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPE EQRLYKDDQL LDDGKTLGEC
GFTSQTARPQ APATVGLAFR ADDTFEALRI EPFSSPPELP DVMKPQDSGG SANEQAVQ
//
