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Q15370 (ELOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 2
Alternative name(s):
Elongin 18 kDa subunit
Elongin-B
Short name=EloB
RNA polymerase II transcription factor SIII subunit B
SIII p18
Gene names
Name:TCEB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length118 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.1 Ref.10

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.1 Ref.10

Pathway

Protein modification; protein ubiquitination.

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. Substrate adapter protein can be a viral protein such as HIV Vif. Interacts with VHL. Found in a complex composed 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.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.19

Subcellular location

Nucleus Probable.

Sequence similarities

Contains 1 ubiquitin-like domain.

Sequence caution

The sequence AAC08452.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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 viral transcription

Traceable author statement. Source: Reactome

protein complex assembly

Traceable author statement PubMed 7660129. Source: ProtInc

protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

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

viral process

Traceable author statement. Source: Reactome

   Cellular_componentCul2-RING ubiquitin ligase complex

Inferred from direct assay PubMed 17636018. Source: UniProtKB

Cul5-RING ubiquitin ligase complex

Inferred from direct assay PubMed 17636018. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

elongin complex

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionubiquitin protein ligase binding

Inferred from direct assay PubMed 17636018. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MED8Q96G255EBI-301238,EBI-394405
TCEB1Q153698EBI-301238,EBI-301231
vifP125045EBI-301238,EBI-779991From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15370-1)

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: Q15370-2)

The sequence of this isoform differs from the canonical sequence as follows:
     118-118: Q → HLHVHSQTMAKSRNTSWSQCPGLTACSTREPQDGPTQVHPRWGL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 118118Transcription elongation factor B polypeptide 2
PRO_0000114914

Regions

Domain1 – 6666Ubiquitin-like

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6 Ref.11 Ref.15

Natural variations

Alternative sequence1181Q → HLHVHSQTMAKSRNTSWSQC PGLTACSTREPQDGPTQVHP RWGL in isoform 2.
VSP_045784

Secondary structure

................................ 118
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: C045F58FBED0EC47

FASTA11813,133
        10         20         30         40         50         60 
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC 

        70         80         90        100        110 
GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVQ 

« Hide

Isoform 2 [UniParc].

Checksum: 72277A4ACF21429F
Show »

FASTA16117,911

References

« Hide 'large scale' references
[1]"Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog."
Garrett K.P., Aso T., Bradsher J.N., Foundling S.I., Lane W.S., Conaway R.C., Conaway J.W.
Proc. Natl. Acad. Sci. U.S.A. 92:7172-7176(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]Bonaldo M.F., Lennon G., Soares M.B.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Pancreas and Placenta.
[6]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-8 AND 44-80, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity."
Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C., Feng Y., Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J., Ingvarsson S., Ratcliffe P.J., Longmore G.D., Sharp T.V.
Nat. Cell Biol. 14:201-208(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH LIMD1; EGLN1/PHD2; VHL AND CUL2.
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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) IN COMPLEX WITH TCEB1 AND VHL.
[17]"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) COMPLEX WITH TCEB1; VHL AND HIF1A.
[18]"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 TCEB1; VHL AND HIF1A.
[19]"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) IN COMPLEX WITH TCEB1 ANS SOX4, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42856 mRNA. Translation: AAA75522.1.
BM700019 mRNA. No translation available.
AC004493 Genomic DNA. Translation: AAC08452.1. Sequence problems.
AC092117 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85472.1.
CH471112 Genomic DNA. Translation: EAW85474.1.
BC013306 mRNA. Translation: AAH13306.1.
BC065000 mRNA. Translation: AAH65000.1.
PIRI59405.
RefSeqNP_009039.1. NM_007108.3.
NP_996896.1. NM_207013.2.
UniGeneHs.172772.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LM8X-ray1.85B1-118[»]
1LQBX-ray2.00A1-118[»]
1VCBX-ray2.70A/D/G/J1-118[»]
2C9WX-ray1.90B1-118[»]
2IZVX-ray2.55B1-118[»]
2JZ3NMR-B1-118[»]
2MA9NMR-B1-118[»]
3DCGX-ray2.40A/C1-118[»]
3ZKJX-ray2.58C/F1-118[»]
3ZNGX-ray2.85C/F1-118[»]
3ZRCX-ray2.90A/D/G/J1-118[»]
3ZRFX-ray2.80A/D/G/J1-118[»]
3ZTCX-ray2.65A/D/G/J1-118[»]
3ZTDX-ray2.79A/D/G/J1-118[»]
3ZUNX-ray2.50A/D/G/J1-118[»]
4AJYX-ray1.73B1-118[»]
4AWJX-ray2.50A/D/G/J1-104[»]
4B95X-ray2.80A/D/G/J1-118[»]
4B9KX-ray2.00A/D/G/J1-104[»]
4BKSX-ray2.20A/D/G/J1-104[»]
4BKTX-ray2.35A/D/G/J1-104[»]
4N9FX-ray3.304/D/H/J/P/W/X/e/g/m/s/y1-102[»]
ProteinModelPortalQ15370.
SMRQ15370. Positions 1-118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112785. 88 interactions.
DIPDIP-29570N.
IntActQ15370. 32 interactions.
MINTMINT-1323839.
STRING9606.ENSP00000262306.

PTM databases

PhosphoSiteQ15370.

Polymorphism databases

DMDM32699512.

Proteomic databases

PaxDbQ15370.
PeptideAtlasQ15370.
PRIDEQ15370.

Protocols and materials databases

DNASU6923.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262306; ENSP00000262306; ENSG00000103363. [Q15370-2]
ENST00000409906; ENSP00000386652; ENSG00000103363. [Q15370-1]
GeneID6923.
KEGGhsa:6923.
UCSCuc002crn.3. human. [Q15370-1]

Organism-specific databases

CTD6923.
GeneCardsGC16M002824.
HGNCHGNC:11619. TCEB2.
MIM600787. gene.
neXtProtNX_Q15370.
PharmGKBPA36378.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316144.
HOGENOMHOG000293425.
HOVERGENHBG008581.
KOK03873.
OMATLGDCGF.
OrthoDBEOG7GQXX6.
PhylomeDBQ15370.
TreeFamTF325964.

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.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ15370.
BgeeQ15370.
CleanExHS_TCEB2.
GenevestigatorQ15370.

Family and domain databases

InterProIPR000626. Ubiquitin-like.
[Graphical view]
PfamPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ15370.
GeneWikiTCEB2.
GenomeRNAi6923.
NextBio27083.
PROQ15370.
SOURCESearch...

Entry information

Entry nameELOB_HUMAN
AccessionPrimary (citable) accession number: Q15370
Secondary accession number(s): B7WPD3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 144 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM