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Q15369 (ELOC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:TCEB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length112 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.9

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. Ref.9

Subunit structure

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. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.17

Subcellular location

Nucleus Probable.

Tissue specificity

Overexpressed in prostate cancer cell line PC-3 and breast cancer cell line SK-BR-3. Ref.6

Sequence similarities

Belongs to the SKP1 family.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hypoxia

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of viral transcription

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 7660129. Source: ProtInc

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

viral process

Traceable author statement. Source: Reactome

   Cellular_componentVCB complex

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

elongin complex

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15369-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q15369-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 112112Transcription elongation factor B polypeptide 1
PRO_0000187258

Natural variations

Alternative sequence1 – 1616Missing in isoform 2.
VSP_045955

Secondary structure

.................... 112
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 98D88696E883538B

FASTA11212,473
        10         20         30         40         50         60 
MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV 

        70         80         90        100        110 
NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA LELLMAANFL DC 

« Hide

Isoform 2 [UniParc].

Checksum: 749EC1F8EC3DB62E
Show »

FASTA9610,832

References

« Hide 'large scale' references
[1]"A human cDNA encoding the small subunit of RNA polymerase II transcription factor SIII."
Garrett K.P., Haque D., Conaway R.C., Conaway J.W.
Gene 150:413-414(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Peripheral blood.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Colon.
[3]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1).
Tissue: Skin.
[5]"Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 ubiquitin ligase activity."
Aso T., Yamazaki K., Aigaki T., Kitajima S.
Biochem. Biophys. Res. Commun. 276:355-361(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VHL.
[6]"Amplification and overexpression of Elongin C gene discovered in prostate cancer by cDNA microarrays."
Porkka K., Saramaeki O., Tanner M., Visakorpi T.
Lab. Invest. 82:629-637(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation."
Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.
Genes Dev. 18:2861-2866(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV VIF.
[8]"TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3."
Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.
Oncogene 23:8908-8919(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMF1.
[9]"Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling."
Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N., Rechavi G., Yarden Y.
J. Biol. Chem. 280:7038-7048(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EGFR DEGRADATION, INTERACTION WITH SOCS5.
[10]"Structural basis for protein recognition by B30.2/SPRY domains."
Woo J.S., Suh H.Y., Park S.Y., Oh B.H.
Mol. Cell 24:967-976(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPSB1.
[11]"Respiratory syncytial virus NS1 protein degrades STAT2 by using the Elongin-Cullin E3 ligase."
Elliott J., Lynch O.T., Suessmuth Y., Qian P., Boyd C.R., Burrows J.F., Buick R., Stevenson N.J., Touzelet O., Gadina M., Power U.F., Johnston J.A.
J. Virol. 81:3428-3436(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRSV PROTEIN NS1.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 activation by suppressing PP5."
Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., Kuranaga E., Miura M., Takeda K., Ichijo H.
Mol. Cell 48:692-704(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLHDC10.
[14]"Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function."
Stebbins C.E., Kaelin W.G. Jr., Pavletich N.P.
Science 284:455-461(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 17-112 IN COMPLEX WITH 1-120 OF TCEB2 AND 54-213 OF VHL.
[15]"Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL."
Hon W.-C., Wilson M.I., Harlos K., Claridge T.D.W., Schofield C.J., Pugh C.W., Maxwell P.H., Ratcliffe P.J., Stuart D.I., Jones E.Y.
Nature 417:975-978(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2; 52-113 OF VHL AND 549-582 OF HIF1A.
[16]"Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling."
Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr., Pavletich N.P.
Science 296:1886-1889(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH TCEB2; 54-113 OF VHL AND 556-575 OF HIF1A.
[17]"Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation."
Bullock A.N., Rodriguez M.C., Debreczeni J.E., Songyang Z., Knapp S.
Structure 15:1493-1504(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2 ANS SOX4, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34587 mRNA. Translation: AAA67650.1.
BX649138 mRNA. No translation available.
AC022868 Genomic DNA. No translation available.
BC013809 mRNA. Translation: AAH13809.1.
BC093065 mRNA. Translation: AAH93065.1.
BC100028 mRNA. Translation: AAI00029.1.
BC100283 mRNA. Translation: AAI00284.1.
RefSeqNP_001191786.1. NM_001204857.1.
NP_001191787.1. NM_001204858.1.
NP_001191788.1. NM_001204859.1.
NP_001191789.1. NM_001204860.1.
NP_001191790.1. NM_001204861.1.
NP_001191791.1. NM_001204862.1.
NP_001191792.1. NM_001204863.1.
NP_001191793.1. NM_001204864.1.
NP_005639.1. NM_005648.3.
XP_005251347.1. XM_005251290.2.
UniGeneHs.533437.
Hs.554594.
Hs.731928.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LM8X-ray1.85C17-112[»]
1LQBX-ray2.00B17-112[»]
1VCBX-ray2.70B/E/H/K1-112[»]
2C9WX-ray1.90C17-112[»]
2IZVX-ray2.55C17-112[»]
2MA9NMR-C19-109[»]
3DCGX-ray2.40B/D17-112[»]
3ZKJX-ray2.58B/E17-112[»]
3ZNGX-ray2.85B/E17-112[»]
3ZRCX-ray2.90B/E/H/K17-112[»]
3ZRFX-ray2.80B/E/H/K17-112[»]
3ZTCX-ray2.65B/E/H/K17-112[»]
3ZTDX-ray2.79B/E/H/K17-112[»]
3ZUNX-ray2.50B/E/H/K17-112[»]
4AJYX-ray1.73C17-112[»]
4AWJX-ray2.50B/E/H/K17-112[»]
4B95X-ray2.80B/E/H/K17-112[»]
4B9KX-ray2.00B/E/H/K17-112[»]
4BKSX-ray2.20B/E/H/K17-112[»]
4BKTX-ray2.35B/E/H/K17-112[»]
4N9FX-ray3.305/B/E/K/Q/T/Y/Z/h/n/t/z17-112[»]
ProteinModelPortalQ15369.
SMRQ15369. Positions 17-112.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112783. 103 interactions.
DIPDIP-29571N.
IntActQ15369. 51 interactions.
MINTMINT-1323870.
STRING9606.ENSP00000284811.

PTM databases

PhosphoSiteQ15369.

Polymorphism databases

DMDM32699511.

Proteomic databases

PaxDbQ15369.
PRIDEQ15369.

Protocols and materials databases

DNASU6921.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284811; ENSP00000284811; ENSG00000154582. [Q15369-1]
ENST00000518127; ENSP00000428334; ENSG00000154582. [Q15369-1]
ENST00000519487; ENSP00000429596; ENSG00000154582. [Q15369-1]
ENST00000520210; ENSP00000430224; ENSG00000154582. [Q15369-2]
ENST00000520242; ENSP00000428171; ENSG00000154582. [Q15369-1]
ENST00000522337; ENSP00000429906; ENSG00000154582. [Q15369-1]
ENST00000523815; ENSP00000428074; ENSG00000154582. [Q15369-1]
GeneID6921.
KEGGhsa:6921.
UCSCuc003xzx.2. human. [Q15369-1]

Organism-specific databases

CTD6921.
GeneCardsGC08M074858.
HGNCHGNC:11617. TCEB1.
MIM600788. gene.
neXtProtNX_Q15369.
PharmGKBPA36376.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298860.
HOGENOMHOG000216525.
HOVERGENHBG007440.
InParanoidQ15369.
KOK03872.
OMAYFHYWYR.
OrthoDBEOG77M8QN.
PhylomeDBQ15369.
TreeFamTF300233.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ15369.
BgeeQ15369.
CleanExHS_TCEB1.
GenevestigatorQ15369.

Family and domain databases

Gene3D3.30.710.10. 1 hit.
InterProIPR011333. BTB/POZ_fold.
IPR001232. Skp1_comp.
IPR016073. Skp1_comp_POZ.
[Graphical view]
PfamPF03931. Skp1_POZ. 1 hit.
[Graphical view]
SMARTSM00512. Skp1. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTCEB1. human.
EvolutionaryTraceQ15369.
GeneWikiTCEB1.
GenomeRNAi6921.
NextBio27077.
PROQ15369.
SOURCESearch...

Entry information

Entry nameELOC_HUMAN
AccessionPrimary (citable) accession number: Q15369
Secondary accession number(s): E5RGD9, Q567Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM