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Protein

Elongin-C

Gene

ELOC

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) (PubMed:7821821). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity).By similarity1 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.4 Publications

GO - Biological processi

Keywordsi

Biological processHost-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

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-8951664. Neddylation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ15369.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongin-C
Short name:
EloC
Alternative name(s):
Elongin 15 kDa subunit
RNA polymerase II transcription factor SIII subunit C
SIII p15
Transcription elongation factor B polypeptide 1
Gene namesi
Name:ELOCImported
Synonyms:TCEB1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:11617. ELOC.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi6921.
OpenTargetsiENSG00000154582.
PharmGKBiPA36376.

Chemistry databases

ChEMBLiCHEMBL3301400.

Polymorphism and mutation databases

BioMutaiTCEB1.
DMDMi32699511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001872581 – 112Elongin-CAdd BLAST112

Proteomic databases

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

PTM databases

iPTMnetiQ15369.
PhosphoSitePlusiQ15369.
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.

Organism-specific databases

HPAiHPA078113.

Interactioni

Subunit structurei

Heterotrimer of an A (ELOA, ELOA2 or ELOA3), ELOB and ELOC subunit (PubMed:17997974). The elongin BC complex interacts with EPOP; leading to recruit the elongin BC complex to Polycomb group (PcG) target genes, thereby restricting excessive activity of the PRC2/EED-EZH2 complex (By similarity). Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and a substrate adapter protein that can be either SOCS1, SOCS5, ELOA, VHL or WSB1 (PubMed:15590694). The elongin BC complex is part of a complex with hydroxylated HIF1A (PubMed:12050673, PubMed:12004076). Interacts with VHL (PubMed:10205047, PubMed:12050673). Interacts with TMF1 (PubMed:15467733). Interacts with SPSB1 (PubMed:17189197). posed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2 (PubMed:11006129, PubMed:10205047, PubMed:12050673). Interacts with SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component (PubMed:23102700).By similarity9 Publications
(Microbial infection) Substrate adapter protein can be a viral protein such as HIV Vif.1 Publication
(Microbial infection) Interacts with human respiratory syncytial virus (HRSV) protein NS1.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi112783. 151 interactors.
DIPiDIP-29571N.
IntActiQ15369. 58 interactors.
MINTiMINT-1323870.
STRINGi9606.ENSP00000284811.

Chemistry databases

BindingDBiQ15369.

Structurei

Secondary structure

1112
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 22Combined sources5
Beta strandi24 – 26Combined sources3
Beta strandi28 – 32Combined sources5
Helixi33 – 36Combined sources4
Helixi40 – 46Combined sources7
Beta strandi47 – 50Combined sources4
Turni51 – 54Combined sources4
Beta strandi59 – 61Combined sources3
Beta strandi63 – 65Combined sources3
Helixi67 – 83Combined sources17
Turni84 – 86Combined sources3
Helixi97 – 99Combined sources3
Helixi100 – 110Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5LLIX-ray2.40B/E/H/K17-112[»]
5T35X-ray2.70C/G17-112[»]
ProteinModelPortaliQ15369.
SMRiQ15369.
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

InterProiView protein in InterPro
IPR001232. SKP1-like.
IPR011333. SKP1/BTB/POZ.
IPR016073. Skp1_comp_POZ.
PfamiView protein in Pfam
PF03931. Skp1_POZ. 1 hit.
SMARTiView protein in SMART
SM00512. Skp1. 1 hit.
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0459551 – 16Missing in isoform 2. 1 PublicationAdd BLAST16

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

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.

Entry informationi

Entry nameiELOC_HUMAN
AccessioniPrimary (citable) accession number: Q15369
Secondary accession number(s): E5RGD9, Q567Q6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: November 1, 1996
Last modified: July 5, 2017
This is version 174 of the entry and version 1 of the sequence. See 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