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UniProtKB - Q15369 (ELOC_HUMAN)

UniProt

Q15369 - ELOC_HUMAN

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Protein

Transcription elongation factor B polypeptide 1

Gene

TCEB1

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).1 Publication
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.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
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.
SIGNORiQ15369.

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
Gene namesi
Name:TCEB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:11617. TCEB1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36376.

Chemistry

ChEMBLiCHEMBL3301400.

Polymorphism and mutation databases

BioMutaiTCEB1.
DMDMi32699511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112Transcription elongation factor B polypeptide 1PRO_0000187258Add
BLAST

Proteomic databases

EPDiQ15369.
MaxQBiQ15369.
PaxDbiQ15369.
PeptideAtlasiQ15369.
PRIDEiQ15369.
TopDownProteomicsiQ15369-1. [Q15369-1]

PTM databases

iPTMnetiQ15369.
PhosphoSiteiQ15369.
SwissPalmiQ15369.

Expressioni

Tissue specificityi

Overexpressed in prostate cancer cell line PC-3 and breast cancer cell line SK-BR-3.1 Publication

Gene expression databases

BgeeiENSG00000154582.
CleanExiHS_TCEB1.
ExpressionAtlasiQ15369. baseline and differential.
GenevisibleiQ15369. 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. 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.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COMMD1Q8N6682EBI-301231,EBI-1550112
CUL2Q136176EBI-301231,EBI-456179
GAMMAHV.ORF73O419742EBI-301231,EBI-6933128From a different organism.
MED8Q96G253EBI-301231,EBI-394405
METTL21CQ5VZV13EBI-301231,EBI-10236049
SOCS1O155242EBI-301231,EBI-968198
SOCS2O145082EBI-301231,EBI-617737
SPSB2Q996193EBI-301231,EBI-2323209
SPSB4Q96A442EBI-301231,EBI-2323233
TCEB2Q1537013EBI-301231,EBI-301238
vifP125045EBI-301231,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi112783. 145 interactions.
DIPiDIP-29571N.
IntActiQ15369. 56 interactions.
MINTiMINT-1323870.
STRINGi9606.ENSP00000284811.

Chemistry

BindingDBiQ15369.

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 225Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 325Combined sources
Helixi33 – 364Combined sources
Helixi40 – 467Combined sources
Beta strandi47 – 504Combined sources
Turni51 – 544Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 653Combined sources
Helixi67 – 8317Combined sources
Turni84 – 863Combined sources
Helixi97 – 993Combined sources
Helixi100 – 11011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/K18-112[»]
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[»]
4W9CX-ray2.20B/E/H/K17-112[»]
4W9DX-ray2.20B/E/H/K17-112[»]
4W9EX-ray2.60B/E/H/K17-112[»]
4W9FX-ray2.10B/E/H/K17-112[»]
4W9GX-ray2.70B/E/H/K17-112[»]
4W9HX-ray2.10B/E/H/K17-112[»]
4W9IX-ray2.40B/E/H/K17-112[»]
4W9JX-ray2.20B/E/H/K17-112[»]
4W9KX-ray2.10B/E/H/K17-112[»]
4W9LX-ray2.20B/E/H/K17-112[»]
4WQOX-ray3.20C17-112[»]
5BO4X-ray2.90C/F/I/L/O/R17-112[»]
ProteinModelPortaliQ15369.
SMRiQ15369. Positions 17-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15369.

Family & Domainsi

Sequence similaritiesi

Belongs to the SKP1 family.Curated

Phylogenomic databases

eggNOGiKOG3473. Eukaryota.
ENOG41123WR. LUCA.
GeneTreeiENSGT00390000011717.
HOGENOMiHOG000216525.
HOVERGENiHBG007440.
InParanoidiQ15369.
KOiK03872.
OMAiDMDIPVE.
OrthoDBiEOG091G0W26.
PhylomeDBiQ15369.
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.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q15369-1) [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
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:November 1, 1996 - v1
Checksum:i98D88696E883538B
GO
Isoform 2 (identifier: Q15369-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.

Note: No experimental confirmation available.
Show »
Length:96
Mass (Da):10,832
Checksum:i749EC1F8EC3DB62E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616Missing in isoform 2. 1 PublicationVSP_045955Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34910.1. [Q15369-1]
CCDS56539.1. [Q15369-2]
RefSeqiNP_001191786.1. NM_001204857.1. [Q15369-1]
NP_001191787.1. NM_001204858.1. [Q15369-1]
NP_001191788.1. NM_001204859.1. [Q15369-1]
NP_001191789.1. NM_001204860.1. [Q15369-1]
NP_001191790.1. NM_001204861.1. [Q15369-1]
NP_001191791.1. NM_001204862.1. [Q15369-1]
NP_001191792.1. NM_001204863.1. [Q15369-2]
NP_001191793.1. NM_001204864.1. [Q15369-2]
NP_005639.1. NM_005648.3. [Q15369-1]
XP_011515882.1. XM_011517580.2. [Q15369-1]
XP_011515883.1. XM_011517581.2. [Q15369-1]
UniGeneiHs.533437.
Hs.554594.
Hs.731928.

Genome annotation databases

EnsembliENST00000284811; 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]
ENST00000622804; ENSP00000478121; ENSG00000154582. [Q15369-1]
GeneIDi6921.
KEGGihsa:6921.
UCSCiuc003xzx.3. human. [Q15369-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34910.1. [Q15369-1]
CCDS56539.1. [Q15369-2]
RefSeqiNP_001191786.1. NM_001204857.1. [Q15369-1]
NP_001191787.1. NM_001204858.1. [Q15369-1]
NP_001191788.1. NM_001204859.1. [Q15369-1]
NP_001191789.1. NM_001204860.1. [Q15369-1]
NP_001191790.1. NM_001204861.1. [Q15369-1]
NP_001191791.1. NM_001204862.1. [Q15369-1]
NP_001191792.1. NM_001204863.1. [Q15369-2]
NP_001191793.1. NM_001204864.1. [Q15369-2]
NP_005639.1. NM_005648.3. [Q15369-1]
XP_011515882.1. XM_011517580.2. [Q15369-1]
XP_011515883.1. XM_011517581.2. [Q15369-1]
UniGeneiHs.533437.
Hs.554594.
Hs.731928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/K18-112[»]
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[»]
4W9CX-ray2.20B/E/H/K17-112[»]
4W9DX-ray2.20B/E/H/K17-112[»]
4W9EX-ray2.60B/E/H/K17-112[»]
4W9FX-ray2.10B/E/H/K17-112[»]
4W9GX-ray2.70B/E/H/K17-112[»]
4W9HX-ray2.10B/E/H/K17-112[»]
4W9IX-ray2.40B/E/H/K17-112[»]
4W9JX-ray2.20B/E/H/K17-112[»]
4W9KX-ray2.10B/E/H/K17-112[»]
4W9LX-ray2.20B/E/H/K17-112[»]
4WQOX-ray3.20C17-112[»]
5BO4X-ray2.90C/F/I/L/O/R17-112[»]
ProteinModelPortaliQ15369.
SMRiQ15369. Positions 17-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112783. 145 interactions.
DIPiDIP-29571N.
IntActiQ15369. 56 interactions.
MINTiMINT-1323870.
STRINGi9606.ENSP00000284811.

Chemistry

BindingDBiQ15369.
ChEMBLiCHEMBL3301400.

PTM databases

iPTMnetiQ15369.
PhosphoSiteiQ15369.
SwissPalmiQ15369.

Polymorphism and mutation databases

BioMutaiTCEB1.
DMDMi32699511.

Proteomic databases

EPDiQ15369.
MaxQBiQ15369.
PaxDbiQ15369.
PeptideAtlasiQ15369.
PRIDEiQ15369.
TopDownProteomicsiQ15369-1. [Q15369-1]

Protocols and materials databases

DNASUi6921.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284811; 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]
ENST00000622804; ENSP00000478121; ENSG00000154582. [Q15369-1]
GeneIDi6921.
KEGGihsa:6921.
UCSCiuc003xzx.3. human. [Q15369-1]

Organism-specific databases

CTDi6921.
GeneCardsiTCEB1.
HGNCiHGNC:11617. TCEB1.
MIMi600788. gene.
neXtProtiNX_Q15369.
PharmGKBiPA36376.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3473. Eukaryota.
ENOG41123WR. LUCA.
GeneTreeiENSGT00390000011717.
HOGENOMiHOG000216525.
HOVERGENiHBG007440.
InParanoidiQ15369.
KOiK03872.
OMAiDMDIPVE.
OrthoDBiEOG091G0W26.
PhylomeDBiQ15369.
TreeFamiTF300233.

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
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.
SIGNORiQ15369.

Miscellaneous databases

ChiTaRSiTCEB1. human.
EvolutionaryTraceiQ15369.
GeneWikiiTCEB1.
GenomeRNAii6921.
PROiQ15369.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000154582.
CleanExiHS_TCEB1.
ExpressionAtlasiQ15369. baseline and differential.
GenevisibleiQ15369. HS.

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...

Entry informationi

Entry nameiELOC_HUMAN
AccessioniPrimary (citable) accession number: Q15369
Secondary accession number(s): E5RGD9, Q567Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 164 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, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.