ID   ELOB_HUMAN              Reviewed;         118 AA.
AC   Q15370;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   26-FEB-2008, entry version 78.
DE   Transcription elongation factor B polypeptide 2 (RNA polymerase II
DE   transcription factor SIII subunit B) (SIII p18) (Elongin B) (EloB)
DE   (Elongin 18 kDa subunit).
GN   Name=TCEB2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   MEDLINE=95365330; PubMed=7638163;
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 GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas, and Placenta;
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   [4]
RP   INTERACTION WITH VHL.
RX   PubMed=11006129; DOI=10.1006/bbrc.2000.3451;
RA   Aso T., Yamazaki K., Aigaki T., Kitajima S.;
RT   "Drosophila von Hippel-Lindau tumor suppressor complex possesses E3
RT   ubiquitin ligase activity.";
RL   Biochem. Biophys. Res. Commun. 276:355-361(2000).
RN   [5]
RP   INTERACTION WITH HIV VIF.
RX   PubMed=15574592; DOI=10.1101/gad.1249904;
RA   Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.;
RT   "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1
RT   Vif-Cul5 complex that promotes APOBEC3G degradation.";
RL   Genes Dev. 18:2861-2866(2004).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH TCEB1 AND VHL.
RX   MEDLINE=99221829; PubMed=10205047; DOI=10.1126/science.284.5413.455;
RA   Stebbins C.E., Kaelin W.G. Jr., Pavletich N.P.;
RT   "Structure of the VHL-ElonginC-ElonginB complex: implications for VHL
RT   tumor suppressor function.";
RL   Science 284:455-461(1999).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) COMPLEX WITH TCEB1; VHL AND
RP   HIF1A.
RX   MEDLINE=22082290; PubMed=12050673; DOI=10.1038/nature00767;
RA   Hon W.-C., Wilson M.I., Harlos K., Claridge T.D.W., Schofield C.J.,
RA   Pugh C.W., Maxwell P.H., Ratcliffe P.J., Stuart D.I., Jones E.Y.;
RT   "Structural basis for the recognition of hydroxyproline in HIF-1 alpha
RT   by pVHL.";
RL   Nature 417:975-978(2002).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH TCEB1; VHL AND
RP   HIF1A.
RX   MEDLINE=22048364; PubMed=12004076; DOI=10.1126/science.1073440;
RA   Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr.,
RA   Pavletich N.P.;
RT   "Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition
RT   in signaling.";
RL   Science 296:1886-1889(2002).
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 degradation; 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, TCEB3, VHL
CC       or WSB1 (By similarity). Substrate adapter protein can be a viral
CC       protein such as HIV Vif. Interacts with VHL.
CC   -!- INTERACTION:
CC       P40337:VHL; NbExp=1; IntAct=EBI-301238, EBI-301246;
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC08452.1; Type=Erroneous gene model prediction;
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; L42856; AAA75522.1; -; mRNA.
DR   EMBL; AC004493; AAC08452.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC013306; AAH13306.1; -; mRNA.
DR   EMBL; BC065000; AAH65000.1; -; mRNA.
DR   PIR; I59405; I59405.
DR   RefSeq; NP_009039.1; -.
DR   UniGene; Hs.172772; -.
DR   PDB; 1LM8; X-ray; 1.85 A; B=1-118.
DR   PDB; 1LQB; X-ray; 2.00 A; A=1-118.
DR   PDB; 1VCB; X-ray; 2.70 A; A/D/G/J=1-118.
DR   PDB; 2C9W; X-ray; 1.90 A; B=1-118.
DR   PDB; 2IZV; X-ray; 2.55 A; B=1-118.
DR   PDBsum; 1LM8; -.
DR   PDBsum; 1LQB; -.
DR   PDBsum; 1VCB; -.
DR   PDBsum; 2C9W; -.
DR   PDBsum; 2IZV; -.
DR   IntAct; Q15370; -.
DR   TRANSFAC; T02268; -.
DR   PeptideAtlas; Q15370; -.
DR   Ensembl; ENSG00000103363; Homo sapiens.
DR   GeneID; 6923; -.
DR   KEGG; hsa:6923; -.
DR   H-InvDB; HIX0036589; -.
DR   H-InvDB; HIX0038597; -.
DR   HGNC; HGNC:11619; TCEB2.
DR   MIM; 600787; gene.
DR   PharmGKB; PA36378; -.
DR   Reactome; REACT_1788; Transcription.
DR   Reactome; REACT_1892; Elongation arrest and recovery.
DR   Reactome; REACT_6143; Pausing and recovery of Tat-mediated HIV-1 elongation.
DR   Reactome; REACT_6185; HIV Infection.
DR   Reactome; REACT_6244; Pausing and recovery of HIV-1 elongation.
DR   Reactome; REACT_6259; HIV-1 elongation arrest and recovery.
DR   Reactome; REACT_6344; Tat-mediated HIV-1 elongation arrest and recovery.
DR   Reactome; REACT_71; Gene Expression.
DR   Reactome; REACT_769; Pausing and recovery of elongation.
DR   LinkHub; Q15370; -.
DR   ArrayExpress; Q15370; -.
DR   CleanEx; HS_TCEB2; -.
DR   GermOnline; ENSG00000103363; Homo sapiens.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR   GO; GO:0006368; P:RNA elongation from RNA polymerase II promoter; TAS:ProtInc.
DR   InterPro; IPR000626; Ubiquitin.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Nucleus; Transcription;
KW   Transcription regulation; Ubl conjugation pathway.
FT   CHAIN         1    118       Transcription elongation factor B
FT                                polypeptide 2.
FT                                /FTId=PRO_0000114914.
FT   DOMAIN        1     66       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   TURN         57     61
FT   TURN         64     66
FT   STRAND       73     79
FT   STRAND       82     84
FT   HELIX       101    103
SQ   SEQUENCE   118 AA;  13133 MW;  C045F58FBED0EC47 CRC64;
     MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC
     GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVQ
//