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Protein

Transcription elongation factor B polypeptide 2

Gene

TCEB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000103363-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TCEB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:11619. TCEB2.

Subcellular locationi

GO - Cellular componenti

  • Cul2-RING ubiquitin ligase complex Source: UniProtKB
  • Cul5-RING ubiquitin ligase complex Source: UniProtKB
  • cytosol Source: Reactome
  • elongin complex Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • VCB complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi6923.
OpenTargetsiENSG00000103363.
PharmGKBiPA36378.

Chemistry databases

ChEMBLiCHEMBL3301400.

Polymorphism and mutation databases

BioMutaiTCEB2.
DMDMi32699512.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001149141 – 118Transcription elongation factor B polypeptide 2Add BLAST118

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei84PhosphothreonineBy similarity1
Modified residuei108PhosphoserineBy similarity1
Modified residuei111PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15370.
MaxQBiQ15370.
PaxDbiQ15370.
PeptideAtlasiQ15370.
PRIDEiQ15370.
TopDownProteomicsiQ15370-1. [Q15370-1]
Q15370-2. [Q15370-2]

PTM databases

iPTMnetiQ15370.
PhosphoSitePlusiQ15370.

Expressioni

Gene expression databases

BgeeiENSG00000103363.
CleanExiHS_TCEB2.
ExpressionAtlasiQ15370. baseline and differential.
GenevisibleiQ15370. HS.

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. 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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MED8Q96G255EBI-301238,EBI-394405
TCEB1Q1536915EBI-301238,EBI-301231
vifP125045EBI-301238,EBI-779991From a different organism.

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112785. 122 interactors.
DIPiDIP-29570N.
IntActiQ15370. 49 interactors.
MINTiMINT-1323839.
STRINGi9606.ENSP00000262306.

Chemistry databases

BindingDBiQ15370.

Structurei

Secondary structure

1118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 10Combined sources9
Beta strandi12 – 19Combined sources8
Helixi24 – 35Combined sources12
Helixi39 – 41Combined sources3
Beta strandi42 – 46Combined sources5
Beta strandi49 – 51Combined sources3
Turni57 – 61Combined sources5
Helixi64 – 66Combined sources3
Beta strandi69 – 71Combined sources3
Beta strandi73 – 79Combined sources7
Beta strandi82 – 84Combined sources3
Helixi86 – 89Combined sources4
Turni92 – 94Combined sources3
Beta strandi96 – 98Combined sources3
Helixi101 – 103Combined sources3
Beta strandi110 – 112Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W9CX-ray2.20A/D/G/J1-104[»]
4W9DX-ray2.20A/D/G/J1-104[»]
4W9EX-ray2.60A/D/G/J1-104[»]
4W9FX-ray2.10A/D/G/J1-104[»]
4W9GX-ray2.70A/D/G/J1-104[»]
4W9HX-ray2.10A/D/G/J1-104[»]
4W9IX-ray2.40A/D/G/J1-104[»]
4W9JX-ray2.20A/D/G/J1-104[»]
4W9KX-ray2.10A/D/G/J1-104[»]
4W9LX-ray2.20A/D/G/J1-104[»]
4WQOX-ray3.20B1-118[»]
5BO4X-ray2.90B/E/H/K/N/Q1-104[»]
ProteinModelPortaliQ15370.
SMRiQ15370.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15370.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 66Ubiquitin-likePROSITE-ProRule annotationAdd BLAST66

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4495. Eukaryota.
ENOG4111UGJ. LUCA.
GeneTreeiENSGT00390000018316.
HOGENOMiHOG000293425.
HOVERGENiHBG008581.
InParanoidiQ15370.
KOiK03873.
OrthoDBiEOG091G10A8.
PhylomeDBiQ15370.
TreeFamiTF325964.

Family and domain databases

InterProiIPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15370-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL
60 70 80 90 100
LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP
110
DVMKPQDSGS SANEQAVQ
Length:118
Mass (Da):13,133
Last modified:November 1, 1996 - v1
Checksum:iC045F58FBED0EC47
GO
Isoform 2 (identifier: Q15370-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     118-118: Q → HLHVHSQTMAKSRNTSWSQCPGLTACSTREPQDGPTQVHPRWGL

Note: No experimental confirmation available.
Show »
Length:161
Mass (Da):17,911
Checksum:i72277A4ACF21429F
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_045784118Q → HLHVHSQTMAKSRNTSWSQC PGLTACSTREPQDGPTQVHP RWGL in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32374.1. [Q15370-2]
CCDS45387.1. [Q15370-1]
PIRiI59405.
RefSeqiNP_009039.1. NM_007108.3. [Q15370-1]
NP_996896.1. NM_207013.2. [Q15370-2]
UniGeneiHs.172772.

Genome annotation databases

EnsembliENST00000262306; ENSP00000262306; ENSG00000103363. [Q15370-2]
ENST00000409906; ENSP00000386652; ENSG00000103363. [Q15370-1]
GeneIDi6923.
KEGGihsa:6923.
UCSCiuc002crm.4. human. [Q15370-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32374.1. [Q15370-2]
CCDS45387.1. [Q15370-1]
PIRiI59405.
RefSeqiNP_009039.1. NM_007108.3. [Q15370-1]
NP_996896.1. NM_207013.2. [Q15370-2]
UniGeneiHs.172772.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W9CX-ray2.20A/D/G/J1-104[»]
4W9DX-ray2.20A/D/G/J1-104[»]
4W9EX-ray2.60A/D/G/J1-104[»]
4W9FX-ray2.10A/D/G/J1-104[»]
4W9GX-ray2.70A/D/G/J1-104[»]
4W9HX-ray2.10A/D/G/J1-104[»]
4W9IX-ray2.40A/D/G/J1-104[»]
4W9JX-ray2.20A/D/G/J1-104[»]
4W9KX-ray2.10A/D/G/J1-104[»]
4W9LX-ray2.20A/D/G/J1-104[»]
4WQOX-ray3.20B1-118[»]
5BO4X-ray2.90B/E/H/K/N/Q1-104[»]
ProteinModelPortaliQ15370.
SMRiQ15370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112785. 122 interactors.
DIPiDIP-29570N.
IntActiQ15370. 49 interactors.
MINTiMINT-1323839.
STRINGi9606.ENSP00000262306.

Chemistry databases

BindingDBiQ15370.
ChEMBLiCHEMBL3301400.

PTM databases

iPTMnetiQ15370.
PhosphoSitePlusiQ15370.

Polymorphism and mutation databases

BioMutaiTCEB2.
DMDMi32699512.

Proteomic databases

EPDiQ15370.
MaxQBiQ15370.
PaxDbiQ15370.
PeptideAtlasiQ15370.
PRIDEiQ15370.
TopDownProteomicsiQ15370-1. [Q15370-1]
Q15370-2. [Q15370-2]

Protocols and materials databases

DNASUi6923.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262306; ENSP00000262306; ENSG00000103363. [Q15370-2]
ENST00000409906; ENSP00000386652; ENSG00000103363. [Q15370-1]
GeneIDi6923.
KEGGihsa:6923.
UCSCiuc002crm.4. human. [Q15370-1]

Organism-specific databases

CTDi6923.
DisGeNETi6923.
GeneCardsiTCEB2.
HGNCiHGNC:11619. TCEB2.
MIMi600787. gene.
neXtProtiNX_Q15370.
OpenTargetsiENSG00000103363.
PharmGKBiPA36378.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4495. Eukaryota.
ENOG4111UGJ. LUCA.
GeneTreeiENSGT00390000018316.
HOGENOMiHOG000293425.
HOVERGENiHBG008581.
InParanoidiQ15370.
KOiK03873.
OrthoDBiEOG091G10A8.
PhylomeDBiQ15370.
TreeFamiTF325964.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000103363-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiQ15370.
GeneWikiiTCEB2.
GenomeRNAii6923.
PROiQ15370.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103363.
CleanExiHS_TCEB2.
ExpressionAtlasiQ15370. baseline and differential.
GenevisibleiQ15370. HS.

Family and domain databases

InterProiIPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiELOB_HUMAN
AccessioniPrimary (citable) accession number: Q15370
Secondary accession number(s): B7WPD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.