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Protein

Transcription elongation factor B polypeptide 1

Gene

Tceb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).
The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor B polypeptide 1
Alternative name(s):
Elongin 15 kDa subunit
Elongin-C
Short name:
EloC
RNA polymerase II transcription factor SIII subunit C
SIII p15
Stromal membrane-associated protein SMAP1B homolog
Gene namesi
Name:Tceb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1915173. Tceb1.

Subcellular locationi

GO - Cellular componenti

  • elongin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112Transcription elongation factor B polypeptide 1PRO_0000187259Add
BLAST

Proteomic databases

EPDiP83940.
MaxQBiP83940.
PaxDbiP83940.
PeptideAtlasiP83940.
PRIDEiP83940.

PTM databases

iPTMnetiP83940.
PhosphoSiteiP83940.

Expressioni

Gene expression databases

BgeeiP83940.
ExpressionAtlasiP83940. baseline and differential.
GenevisibleiP83940. MM.

Interactioni

Subunit structurei

Heterotrimer of an A (A1, A2 or A3), B and C subunit. Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and a substrate adapter protein that can be either SOCS1, SOCS5, TCEB3, VHL or WSB1. The elongin BC complex is part of a complex with hydroxylated HIF1A. Substrate adapter protein can be a viral protein such as HIV Vif. Interacts with VHL. Interacts with TMF1. Interacts with human respiratory syncytial virus (HRSV) protein NS1. Interacts with SPSB1. posed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component.4 Publications

Protein-protein interaction databases

BioGridi212537. 22 interactions.
DIPiDIP-42814N.
IntActiP83940. 18 interactions.
MINTiMINT-1851784.
STRINGi10090.ENSMUSP00000111009.

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 225Combined sources
Beta strandi28 – 325Combined sources
Helixi33 – 364Combined sources
Helixi37 – 393Combined sources
Helixi40 – 478Combined sources
Helixi48 – 503Combined sources
Beta strandi54 – 563Combined sources
Beta strandi59 – 613Combined sources
Helixi67 – 8418Combined sources
Beta strandi85 – 895Combined sources
Turni97 – 993Combined sources
Helixi100 – 11011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FNJX-ray1.80C17-112[»]
2JZ3NMR-C17-112[»]
4JGHX-ray3.00C17-112[»]
ProteinModelPortaliP83940.
SMRiP83940. Positions 17-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83940.

Family & Domainsi

Sequence similaritiesi

Belongs to the SKP1 family.Curated

Phylogenomic databases

eggNOGiKOG3473. Eukaryota.
ENOG41123WR. LUCA.
GeneTreeiENSGT00390000011717.
HOGENOMiHOG000216525.
HOVERGENiHBG007440.
InParanoidiP83940.
KOiK03872.
OrthoDBiEOG77M8QN.
PhylomeDBiP83940.
TreeFamiTF300233.

Family and domain databases

InterProiIPR001232. SKP1-like.
IPR011333. SKP1/BTB/POZ.
IPR016073. Skp1_comp_POZ.
[Graphical view]
PfamiPF03931. Skp1_POZ. 1 hit.
[Graphical view]
SMARTiSM00512. Skp1. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

P83940-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG
60 70 80 90 100
QFAENETNEV NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA
110
LELLMAANFL DC
Length:112
Mass (Da):12,473
Last modified:June 7, 2004 - v1
Checksum:i98D88696E883538B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013089 mRNA. Translation: BAB28641.1.
AK011757 mRNA. Translation: BAB27825.1.
AK011958 mRNA. Translation: BAB27939.1.
AK012909 mRNA. Translation: BAB28546.1.
AK039746 mRNA. Translation: BAC30437.1.
BC009104 mRNA. Translation: AAH09104.1.
BC028545 mRNA. Translation: AAH28545.1.
CCDSiCCDS35517.1.
RefSeqiNP_001297399.1. NM_001310470.1.
NP_080732.1. NM_026456.4.
XP_006495624.1. XM_006495561.2.
XP_006495625.1. XM_006495562.1.
XP_006495626.1. XM_006495563.2.
XP_006495627.1. XM_006495564.1.
XP_006543684.1. XM_006543621.1.
UniGeneiMm.289248.

Genome annotation databases

EnsembliENSMUST00000115352; ENSMUSP00000111009; ENSMUSG00000079658.
ENSMUST00000185771; ENSMUSP00000139675; ENSMUSG00000079658.
ENSMUST00000186948; ENSMUSP00000140962; ENSMUSG00000079658.
ENSMUST00000188641; ENSMUSP00000140422; ENSMUSG00000079658.
GeneIDi102642819.
67923.
KEGGimmu:102642819.
mmu:67923.
UCSCiuc007ajv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013089 mRNA. Translation: BAB28641.1.
AK011757 mRNA. Translation: BAB27825.1.
AK011958 mRNA. Translation: BAB27939.1.
AK012909 mRNA. Translation: BAB28546.1.
AK039746 mRNA. Translation: BAC30437.1.
BC009104 mRNA. Translation: AAH09104.1.
BC028545 mRNA. Translation: AAH28545.1.
CCDSiCCDS35517.1.
RefSeqiNP_001297399.1. NM_001310470.1.
NP_080732.1. NM_026456.4.
XP_006495624.1. XM_006495561.2.
XP_006495625.1. XM_006495562.1.
XP_006495626.1. XM_006495563.2.
XP_006495627.1. XM_006495564.1.
XP_006543684.1. XM_006543621.1.
UniGeneiMm.289248.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FNJX-ray1.80C17-112[»]
2JZ3NMR-C17-112[»]
4JGHX-ray3.00C17-112[»]
ProteinModelPortaliP83940.
SMRiP83940. Positions 17-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212537. 22 interactions.
DIPiDIP-42814N.
IntActiP83940. 18 interactions.
MINTiMINT-1851784.
STRINGi10090.ENSMUSP00000111009.

PTM databases

iPTMnetiP83940.
PhosphoSiteiP83940.

Proteomic databases

EPDiP83940.
MaxQBiP83940.
PaxDbiP83940.
PeptideAtlasiP83940.
PRIDEiP83940.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115352; ENSMUSP00000111009; ENSMUSG00000079658.
ENSMUST00000185771; ENSMUSP00000139675; ENSMUSG00000079658.
ENSMUST00000186948; ENSMUSP00000140962; ENSMUSG00000079658.
ENSMUST00000188641; ENSMUSP00000140422; ENSMUSG00000079658.
GeneIDi102642819.
67923.
KEGGimmu:102642819.
mmu:67923.
UCSCiuc007ajv.1. mouse.

Organism-specific databases

CTDi6921.
MGIiMGI:1915173. Tceb1.

Phylogenomic databases

eggNOGiKOG3473. Eukaryota.
ENOG41123WR. LUCA.
GeneTreeiENSGT00390000011717.
HOGENOMiHOG000216525.
HOVERGENiHBG007440.
InParanoidiP83940.
KOiK03872.
OrthoDBiEOG77M8QN.
PhylomeDBiP83940.
TreeFamiTF300233.

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSiTceb1. mouse.
EvolutionaryTraceiP83940.
PROiP83940.
SOURCEiSearch...

Gene expression databases

BgeeiP83940.
ExpressionAtlasiP83940. baseline and differential.
GenevisibleiP83940. MM.

Family and domain databases

InterProiIPR001232. SKP1-like.
IPR011333. SKP1/BTB/POZ.
IPR016073. Skp1_comp_POZ.
[Graphical view]
PfamiPF03931. Skp1_POZ. 1 hit.
[Graphical view]
SMARTiSM00512. Skp1. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Spinal cord.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. "The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families."
    Kamura T., Sato S., Haque D., Liu L., Kaelin W.G. Jr., Conaway R.C., Conaway J.W.
    Genes Dev. 12:3872-3881(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SOCS1.
  4. "The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation."
    Zhang J.-G., Farley A., Nicholson S.E., Willson T.A., Zugaro L.M., Simpson R.J., Moritz R.L., Cary D., Richardson R., Hausmann G., Kile B.J., Kent S.B.H., Alexander W.S., Metcalf D., Hilton D.J., Nicola N.A., Baca M.
    Proc. Natl. Acad. Sci. U.S.A. 96:2071-2076(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SOCS1.
  5. "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase."
    Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E., Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 276:29748-29753(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN E3 UBIQUITIN LIGASE COMPLEXES.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Structural and functional insights into the B30.2/SPRY domain."
    Woo J.S., Imm J.H., Min C.K., Kim K.J., Cha S.S., Oh B.H.
    EMBO J. 25:1353-1363(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 17-112 IN COMPLEX WITH ELONGIN B AND DROSOPHILA GUS.

Entry informationi

Entry nameiELOC_MOUSE
AccessioniPrimary (citable) accession number: P83940
Secondary accession number(s): Q63182
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.