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Entry: ELOB_MOUSE
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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   16-APR-2014, entry version 94.
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. Substrate adapter protein can be a viral
CC       protein such as HIV Vif. Interacts with VHL. Found in a complex
CC       composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with
CC       SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase
CC       complex substrate recognition component.
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   RefSeq; NP_080581.1; NM_026305.2.
DR   UniGene; Mm.153758; -.
DR   PDB; 2FNJ; X-ray; 1.80 A; B=1-118.
DR   PDB; 4JGH; X-ray; 3.00 A; B=1-118.
DR   PDBsum; 2FNJ; -.
DR   PDBsum; 4JGH; -.
DR   ProteinModelPortal; P62869; -.
DR   SMR; P62869; 1-98.
DR   BioGrid; 212356; 12.
DR   IntAct; P62869; 6.
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; EOG7GQXX6; -.
DR   PhylomeDB; P62869; -.
DR   TreeFam; TF325964; -.
DR   UniPathway; UPA00143; -.
DR   EvolutionaryTrace; P62869; -.
DR   NextBio; 325215; -.
DR   PRO; PR:P62869; -.
DR   Bgee; P62869; -.
DR   Genevestigator; P62869; -.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0070449; C:elongin complex; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR000626; Ubiquitin-like.
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
FT   HELIX       101    103
SQ   SEQUENCE   118 AA;  13170 MW;  BA702F24CEC0FC02 CRC64;
     MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPE EQRLYKDDQL LDDGKTLGEC
     GFTSQTARPQ APATVGLAFR ADDTFEALRI EPFSSPPELP DVMKPQDSGG SANEQAVQ
//
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