UniProtKB - Q15369 (ELOC_HUMAN)
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Protein
Elongin-C
Gene
ELOC
Organism
Homo sapiens (Human)
Status
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
- positive regulation of transcription elongation from RNA polymerase II promoter Source: GO_Central
- post-translational protein modification Source: Reactome
- protein ubiquitination Source: Reactome
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: GO_Central
- regulation of transcription by RNA polymerase II Source: ProtInc
- regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
- transcription by RNA polymerase II Source: Reactome
- transcription elongation from RNA polymerase II promoter Source: Reactome
- viral process Source: UniProtKB-KW
Keywordsi
Biological process | Host-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway |
Enzyme and pathway databases
Reactomei | R-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-8951664. Neddylation. R-HSA-9010553. Regulation of expression of SLITs and ROBOs. R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation. |
SIGNORi | Q15369. |
Names & Taxonomyi
Protein namesi | Recommended name: Elongin-CShort 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 | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000154582.16. |
HGNCi | HGNC:11617. ELOC. |
MIMi | 600788. gene. |
neXtProti | NX_Q15369. |
Pathology & Biotechi
Organism-specific databases
DisGeNETi | 6921. |
OpenTargetsi | ENSG00000154582. |
PharmGKBi | PA36376. |
Chemistry databases
ChEMBLi | CHEMBL3301400. |
Polymorphism and mutation databases
BioMutai | TCEB1. |
DMDMi | 32699511. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000187258 | 1 – 112 | Elongin-CAdd BLAST | 112 |
Proteomic databases
EPDi | Q15369. |
MaxQBi | Q15369. |
PaxDbi | Q15369. |
PeptideAtlasi | Q15369. |
PRIDEi | Q15369. |
TopDownProteomicsi | Q15369-1. [Q15369-1] |
PTM databases
iPTMneti | Q15369. |
PhosphoSitePlusi | Q15369. |
SwissPalmi | Q15369. |
Expressioni
Tissue specificityi
Overexpressed in prostate cancer cell line PC-3 and breast cancer cell line SK-BR-3.1 Publication
Gene expression databases
Bgeei | ENSG00000154582. |
CleanExi | HS_TCEB1. |
ExpressionAtlasi | Q15369. baseline and differential. |
Genevisiblei | Q15369. HS. |
Organism-specific databases
HPAi | HPA078113. |
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
Protein-protein interaction databases
BioGridi | 112783. 153 interactors. |
CORUMi | Q15369. |
DIPi | DIP-29571N. |
IntActi | Q15369. 70 interactors. |
MINTi | Q15369. |
STRINGi | 9606.ENSP00000284811. |
Chemistry databases
BindingDBi | Q15369. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 18 – 22 | Combined sources | 5 | |
Beta strandi | 24 – 26 | Combined sources | 3 | |
Beta strandi | 28 – 32 | Combined sources | 5 | |
Helixi | 33 – 36 | Combined sources | 4 | |
Helixi | 40 – 46 | Combined sources | 7 | |
Beta strandi | 47 – 50 | Combined sources | 4 | |
Turni | 51 – 54 | Combined sources | 4 | |
Beta strandi | 59 – 61 | Combined sources | 3 | |
Beta strandi | 63 – 65 | Combined sources | 3 | |
Helixi | 67 – 83 | Combined sources | 17 | |
Turni | 84 – 86 | Combined sources | 3 | |
Helixi | 97 – 99 | Combined sources | 3 | |
Helixi | 100 – 110 | Combined sources | 11 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1LM8 | X-ray | 1.85 | C | 17-112 | [»] | |
1LQB | X-ray | 2.00 | B | 17-112 | [»] | |
1VCB | X-ray | 2.70 | B/E/H/K | 1-112 | [»] | |
2C9W | X-ray | 1.90 | C | 17-112 | [»] | |
2IZV | X-ray | 2.55 | C | 17-112 | [»] | |
2MA9 | NMR | - | C | 19-109 | [»] | |
3DCG | X-ray | 2.40 | B/D | 17-112 | [»] | |
3ZKJ | X-ray | 2.58 | B/E | 17-112 | [»] | |
3ZNG | X-ray | 2.85 | B/E | 17-112 | [»] | |
3ZRC | X-ray | 2.90 | B/E/H/K | 17-112 | [»] | |
3ZRF | X-ray | 2.80 | B/E/H/K | 17-112 | [»] | |
3ZTC | X-ray | 2.65 | B/E/H/K | 17-112 | [»] | |
3ZTD | X-ray | 2.79 | B/E/H/K | 17-112 | [»] | |
3ZUN | X-ray | 2.50 | B/E/H/K | 17-112 | [»] | |
4AJY | X-ray | 1.73 | C | 17-112 | [»] | |
4AWJ | X-ray | 2.50 | B/E/H/K | 17-112 | [»] | |
4B95 | X-ray | 2.80 | B/E/H/K | 18-112 | [»] | |
4B9K | X-ray | 2.00 | B/E/H/K | 17-112 | [»] | |
4BKS | X-ray | 2.20 | B/E/H/K | 17-112 | [»] | |
4BKT | X-ray | 2.35 | B/E/H/K | 17-112 | [»] | |
4N9F | X-ray | 3.30 | 5/B/E/K/Q/T/Y/Z/h/n/t/z | 17-112 | [»] | |
4W9C | X-ray | 2.20 | B/E/H/K | 17-112 | [»] | |
4W9D | X-ray | 2.20 | B/E/H/K | 17-112 | [»] | |
4W9E | X-ray | 2.60 | B/E/H/K | 17-112 | [»] | |
4W9F | X-ray | 2.10 | B/E/H/K | 17-112 | [»] | |
4W9G | X-ray | 2.70 | B/E/H/K | 17-112 | [»] | |
4W9H | X-ray | 2.10 | B/E/H/K | 17-112 | [»] | |
4W9I | X-ray | 2.40 | B/E/H/K | 17-112 | [»] | |
4W9J | X-ray | 2.20 | B/E/H/K | 17-112 | [»] | |
4W9K | X-ray | 2.10 | B/E/H/K | 17-112 | [»] | |
4W9L | X-ray | 2.20 | B/E/H/K | 17-112 | [»] | |
4WQO | X-ray | 3.20 | C | 17-112 | [»] | |
5BO4 | X-ray | 2.90 | C/F/I/L/O/R | 17-112 | [»] | |
5LLI | X-ray | 2.40 | B/E/H/K | 17-112 | [»] | |
5N4W | X-ray | 3.90 | C | 17-112 | [»] | |
5NVV | X-ray | 2.10 | B/E/H/K | 17-112 | [»] | |
5NVW | X-ray | 2.20 | B/E/H/K | 17-112 | [»] | |
5NVX | X-ray | 2.20 | B/E/H/K | 17-112 | [»] | |
5NVY | X-ray | 2.90 | B/E/H/K | 17-112 | [»] | |
5NVZ | X-ray | 2.70 | B/E/H/K | 17-112 | [»] | |
5NW0 | X-ray | 2.30 | B/E/H/K | 17-112 | [»] | |
5NW1 | X-ray | 2.10 | B/E/H/K | 17-112 | [»] | |
5NW2 | X-ray | 2.20 | B/E/H/K | 17-112 | [»] | |
5T35 | X-ray | 2.70 | C/G | 17-112 | [»] | |
ProteinModelPortali | Q15369. | |||||
SMRi | Q15369. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q15369. |
Family & Domainsi
Sequence similaritiesi
Belongs to the SKP1 family.Curated
Phylogenomic databases
eggNOGi | KOG3473. Eukaryota. ENOG41123WR. LUCA. |
GeneTreei | ENSGT00390000011717. |
HOGENOMi | HOG000216525. |
HOVERGENi | HBG007440. |
InParanoidi | Q15369. |
KOi | K03872. |
OMAi | DMDIPVE. |
OrthoDBi | EOG091G0W26. |
PhylomeDBi | Q15369. |
TreeFami | TF300233. |
Family and domain databases
InterProi | View protein in InterPro IPR001232. SKP1-like. IPR011333. SKP1/BTB/POZ_sf. IPR016073. Skp1_comp_POZ. |
Pfami | View protein in Pfam PF03931. Skp1_POZ. 1 hit. |
SMARTi | View protein in SMART SM00512. Skp1. 1 hit. |
SUPFAMi | SSF54695. SSF54695. 1 hit. |
s (2)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative 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.
10 20 30 40 50
MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG
60 70 80 90 100
QFAENETNEV NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA
110
LELLMAANFL DC
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_045955 | 1 – 16 | Missing in isoform 2. 1 PublicationAdd BLAST | 16 |
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. |
CCDSi | CCDS34910.1. [Q15369-1] CCDS56539.1. [Q15369-2] |
RefSeqi | NP_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] |
UniGenei | Hs.533437. Hs.554594. Hs.731928. |
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | ELOC_HUMAN | |
Accessioni | Q15369Primary (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: | March 28, 2018 | |
This is version 181 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |