UniProtKB - Q15370 (ELOB_HUMAN)
Elongin-B
ELOB
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:7638163).
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 PublicationCore component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:26138980, PubMed:29779948, PubMed:29775578).
This includes the von Hippel-Lindau ubiquitination complex CBC(VHL) (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694).
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 (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694).
A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:26138980, PubMed:29779948, PubMed:29775578).
7 Publications: protein ubiquitination Pathwayi
This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.3 PublicationsView all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.
GO - Molecular functioni
- transcription corepressor binding Source: UniProtKB
- ubiquitin protein ligase binding Source: UniProtKB
GO - Biological processi
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: FlyBase
- protein-containing complex assembly Source: ProtInc
- protein ubiquitination Source: UniProtKB-UniPathway
- transcription elongation from RNA polymerase II promoter Source: ProtInc
- transcription initiation from RNA polymerase II promoter Source: UniProtKB
Keywordsi
Biological process | Host-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway |
Enzyme and pathway databases
PathwayCommonsi | Q15370 |
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-9705462, Inactivation of CSF3 (G-CSF) signaling R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation |
SignaLinki | Q15370 |
UniPathwayi | UPA00143 |
Names & Taxonomyi
Protein namesi | Recommended name: Elongin-BShort name: EloB Alternative name(s): Elongin 18 kDa subunit RNA polymerase II transcription factor SIII subunit B SIII p18 Transcription elongation factor B polypeptide 2 |
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
HGNCi | HGNC:11619, ELOB |
MIMi | 600787, gene |
neXtProti | NX_Q15370 |
VEuPathDBi | HostDB:ENSG00000103363 |
Subcellular locationi
Nucleus
- Nucleus Curated
Cytosol
- cytosol Source: Reactome
Nucleus
- elongin complex Source: UniProtKB
- nucleoplasm Source: Reactome
Other locations
- Cul2-RING ubiquitin ligase complex Source: UniProtKB
- Cul5-RING ubiquitin ligase complex Source: UniProtKB
- VCB complex Source: GO_Central
Keywords - Cellular componenti
NucleusPathology & Biotechi
Organism-specific databases
DisGeNETi | 6923 |
OpenTargetsi | ENSG00000103363 |
PharmGKBi | PA36378 |
Miscellaneous databases
Pharosi | Q15370, Tbio |
Chemistry databases
ChEMBLi | CHEMBL3301400 CHEMBL4296117 |
Genetic variation databases
BioMutai | ELOB |
DMDMi | 32699512 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000114914 | 1 – 118 | Elongin-BAdd BLAST | 118 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineCombined sources1 Publication | 1 | |
Modified residuei | 84 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 108 | PhosphoserineBy similarity | 1 | |
Modified residuei | 111 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | Q15370 |
jPOSTi | Q15370 |
MassIVEi | Q15370 |
MaxQBi | Q15370 |
PaxDbi | Q15370 |
PeptideAtlasi | Q15370 |
PRIDEi | Q15370 |
ProteomicsDBi | 60548 [Q15370-1] 6294 |
TopDownProteomicsi | Q15370-1 [Q15370-1] Q15370-2 [Q15370-2] |
PTM databases
GlyGeni | Q15370, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q15370 |
MetOSitei | Q15370 |
PhosphoSitePlusi | Q15370 |
SwissPalmi | Q15370 |
Expressioni
Gene expression databases
Bgeei | ENSG00000103363, Expressed in left testis and 251 other tissues |
ExpressionAtlasi | Q15370, baseline and differential |
Genevisiblei | Q15370, HS |
Organism-specific databases
HPAi | ENSG00000103363, Low tissue specificity |
Interactioni
Subunit structurei
Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC subunit (PubMed:10205047, 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 ASB2, KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B, FEM1C, SOCS1, SOCS5, ELOA, VHL or WSB1 (PubMed:15590694, PubMed:19413330 PubMed:22286099, PubMed:26138980, PubMed:29779948, PubMed:29775578).
Interacts with VHL (PubMed:10205047, PubMed:11006129).
Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2.
Interacts with SPSB1 (PubMed:17189197).
Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component (PubMed:23102700). May also interact with DCUN1D1, DCUN1D2, DCUN1D3 and DCUN1D5 (PubMed:26906416).
By similarity11 Publications(Microbial infection) Substrate adapter protein can be a viral protein such as HIV Vif.
1 Publication(Microbial infection) Interacts with molluscum contagiosum virus MC132.
1 Publication(Microbial infection) Interacts with herpes virus 8 virus protein LANA1.
1 PublicationBinary interactionsi
Q15370
GO - Molecular functioni
- transcription corepressor binding Source: UniProtKB
- ubiquitin protein ligase binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 112785, 263 interactors |
CORUMi | Q15370 |
DIPi | DIP-29570N |
IntActi | Q15370, 100 interactors |
MINTi | Q15370 |
STRINGi | 9606.ENSP00000262306 |
Chemistry databases
BindingDBi | Q15370 |
Miscellaneous databases
RNActi | Q15370, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q15370 |
BMRBi | Q15370 |
SMRi | Q15370 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q15370 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 66 | Ubiquitin-likePROSITE-ProRule annotationAdd BLAST | 66 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 92 – 118 | DisorderedSequence analysisAdd BLAST | 27 |
Phylogenomic databases
eggNOGi | KOG4495, Eukaryota |
GeneTreei | ENSGT00390000018316 |
HOGENOMi | CLU_139243_1_0_1 |
InParanoidi | Q15370 |
OMAi | RKKMTIF |
OrthoDBi | 1338040at2759 |
PhylomeDBi | Q15370 |
TreeFami | TF325964 |
Family and domain databases
InterProi | View protein in InterPro IPR039049, ELOB IPR000626, Ubiquitin-like_dom IPR029071, Ubiquitin-like_domsf |
PANTHERi | PTHR13248, PTHR13248, 1 hit |
Pfami | View protein in Pfam PF00240, ubiquitin, 1 hit |
SMARTi | View protein in SMART SM00213, UBQ, 1 hit |
SUPFAMi | SSF54236, SSF54236, 1 hit |
PROSITEi | View protein in PROSITE PS50053, UBIQUITIN_2, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL
60 70 80 90 100
LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP
110
DVMKPQDSGS SANEQAVQ
Computationally mapped potential isoform sequencesi
There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketB8ZZU8 | B8ZZU8_HUMAN | Elongin-B | ELOB TCEB2, hCG_1778969 | 113 | Annotation score: | ||
I3L0M9 | I3L0M9_HUMAN | Elongin-B | ELOB | 140 | Annotation score: | ||
A0A0B4J296 | A0A0B4J296_HUMAN | Elongin-B | ELOB | 66 | Annotation score: | ||
A0A8I5KQX6 | A0A8I5KQX6_HUMAN | Elongin-B | ELOB | 55 | Annotation score: | ||
A0A8I5KUS5 | A0A8I5KUS5_HUMAN | Elongin-B | ELOB | 92 | Annotation score: |
Sequence cautioni
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_045784 | 118 | Q → HLHVHSQTMAKSRNTSWSQC PGLTACSTREPQDGPTQVHP RWGL in isoform 2. 1 Publication | 1 |
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 |
CCDSi | CCDS32374.1 [Q15370-2] CCDS45387.1 [Q15370-1] |
PIRi | I59405 |
RefSeqi | NP_009039.1, NM_007108.3 [Q15370-1] NP_996896.1, NM_207013.2 [Q15370-2] |
Genome annotation databases
Ensembli | ENST00000262306.11; ENSP00000262306.7; ENSG00000103363.16 [Q15370-2] ENST00000409906.9; ENSP00000386652.5; ENSG00000103363.16 |
GeneIDi | 6923 |
KEGGi | hsa:6923 |
MANE-Selecti | ENST00000409906.9; ENSP00000386652.5; NM_007108.4; NP_009039.1 |
UCSCi | uc002crm.4, human [Q15370-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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 |
CCDSi | CCDS32374.1 [Q15370-2] CCDS45387.1 [Q15370-1] |
PIRi | I59405 |
RefSeqi | NP_009039.1, NM_007108.3 [Q15370-1] NP_996896.1, NM_207013.2 [Q15370-2] |
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 | B | 1-118 | [»] | |
1LQB | X-ray | 2.00 | A | 1-118 | [»] | |
1VCB | X-ray | 2.70 | A/D/G/J | 1-118 | [»] | |
2C9W | X-ray | 1.90 | B | 1-118 | [»] | |
2IZV | X-ray | 2.55 | B | 1-118 | [»] | |
2JZ3 | NMR | - | B | 1-118 | [»] | |
2MA9 | NMR | - | B | 1-118 | [»] | |
3DCG | X-ray | 2.40 | A/C | 1-118 | [»] | |
3ZKJ | X-ray | 2.58 | C/F | 1-118 | [»] | |
3ZNG | X-ray | 2.85 | C/F | 1-118 | [»] | |
3ZRC | X-ray | 2.90 | A/D/G/J | 1-118 | [»] | |
3ZRF | X-ray | 2.80 | A/D/G/J | 1-118 | [»] | |
3ZTC | X-ray | 2.65 | A/D/G/J | 1-118 | [»] | |
3ZTD | X-ray | 2.79 | A/D/G/J | 1-118 | [»] | |
3ZUN | X-ray | 2.50 | A/D/G/J | 1-118 | [»] | |
4AJY | X-ray | 1.73 | B | 1-118 | [»] | |
4AWJ | X-ray | 2.50 | A/D/G/J | 1-104 | [»] | |
4B95 | X-ray | 2.80 | A/D/G/J | 1-118 | [»] | |
4B9K | X-ray | 2.00 | A/D/G/J | 1-104 | [»] | |
4BKS | X-ray | 2.20 | A/D/G/J | 1-104 | [»] | |
4BKT | X-ray | 2.35 | A/D/G/J | 1-104 | [»] | |
4N9F | X-ray | 3.30 | 4/D/H/J/P/W/X/e/g/m/s/y | 1-102 | [»] | |
4W9C | X-ray | 2.20 | A/D/G/J | 1-104 | [»] | |
4W9D | X-ray | 2.20 | A/D/G/J | 1-104 | [»] | |
4W9E | X-ray | 2.60 | A/D/G/J | 1-104 | [»] | |
4W9F | X-ray | 2.10 | A/D/G/J | 1-104 | [»] | |
4W9G | X-ray | 2.70 | A/D/G/J | 1-104 | [»] | |
4W9H | X-ray | 2.10 | A/D/G/J | 1-104 | [»] | |
4W9I | X-ray | 2.40 | A/D/G/J | 1-104 | [»] | |
4W9J | X-ray | 2.20 | A/D/G/J | 1-104 | [»] | |
4W9K | X-ray | 2.10 | A/D/G/J | 1-104 | [»] | |
4W9L | X-ray | 2.20 | A/D/G/J | 1-104 | [»] | |
4WQO | X-ray | 3.20 | B | 1-118 | [»] | |
5BO4 | X-ray | 2.90 | B/E/H/K/N/Q | 1-104 | [»] | |
5LLI | X-ray | 2.40 | A/D/G/J | 1-104 | [»] | |
5N4W | X-ray | 3.90 | B | 1-104 | [»] | |
5NVV | X-ray | 2.10 | A/D/G/J | 1-104 | [»] | |
5NVW | X-ray | 2.20 | A/D/G/J | 1-104 | [»] | |
5NVX | X-ray | 2.20 | A/D/G/J | 1-104 | [»] | |
5NVY | X-ray | 2.90 | A/D/G/J | 1-104 | [»] | |
5NVZ | X-ray | 2.70 | A/D/G/J | 1-104 | [»] | |
5NW0 | X-ray | 2.30 | A/D/G/J | 1-104 | [»] | |
5NW1 | X-ray | 2.10 | A/D/G/J | 1-104 | [»] | |
5NW2 | X-ray | 2.20 | A/D/G/J | 1-104 | [»] | |
5T35 | X-ray | 2.70 | B/F | 1-104 | [»] | |
6BVB | X-ray | 2.00 | B | 1-118 | [»] | |
6C5X | X-ray | 3.10 | B/E | 1-118 | [»] | |
6FMI | X-ray | 2.80 | A/D | 1-104 | [»] | |
6FMJ | X-ray | 2.45 | A/D/G/J | 1-104 | [»] | |
6FMK | X-ray | 2.75 | A/D/G/J | 1-104 | [»] | |
6GFX | X-ray | 1.83 | A | 1-104 | [»] | |
6GFY | X-ray | 2.70 | A/D/G/J | 1-104 | [»] | |
6GFZ | X-ray | 2.30 | A/D/G/J | 1-104 | [»] | |
6GMN | X-ray | 1.94 | A/D/G/J | 1-104 | [»] | |
6GMQ | X-ray | 2.75 | A/D/G/J | 1-104 | [»] | |
6GMR | X-ray | 1.75 | B | 1-118 | [»] | |
6GMX | X-ray | 2.53 | A/D/G/J | 1-104 | [»] | |
6HAX | X-ray | 2.35 | D/H | 1-104 | [»] | |
6HAY | X-ray | 2.24 | D/H | 1-104 | [»] | |
6HR2 | X-ray | 1.76 | D/H | 1-104 | [»] | |
6I4X | X-ray | 2.69 | B | 1-104 | [»] | |
6I5J | X-ray | 2.80 | B/E | 1-104 | [»] | |
6I5N | X-ray | 1.98 | B/E | 1-104 | [»] | |
6I7Q | X-ray | 1.80 | B | 1-118 | [»] | |
6I7R | X-ray | 1.95 | B | 1-118 | [»] | |
6P59 | X-ray | 2.94 | D/W | 1-118 | [»] | |
6R6H | electron microscopy | 8.40 | P | 1-104 | [»] | |
6R7F | electron microscopy | 8.20 | P | 1-118 | [»] | |
6R7H | electron microscopy | 8.80 | P | 1-104 | [»] | |
6R7I | electron microscopy | 5.90 | P | 1-106 | [»] | |
6R7N | electron microscopy | 6.50 | P | 1-104 | [»] | |
6SIS | X-ray | 3.50 | B/F | 1-104 | [»] | |
6V9H | electron microscopy | 4.10 | E | 1-118 | [»] | |
6ZHC | X-ray | 1.92 | BBB | 1-107 | [»] | |
7CJB | X-ray | 2.80 | B/F/J/N | 1-118 | [»] | |
7JTO | X-ray | 1.70 | J | 1-104 | [»] | |
7JTP | X-ray | 2.12 | J | 1-104 | [»] | |
7KHH | X-ray | 2.28 | A | 1-118 | [»] | |
7M6T | X-ray | 3.19 | B | 1-118 | [»] | |
7PI4 | X-ray | 2.24 | BBB | 1-105 | [»] | |
7PLO | electron microscopy | 2.80 | P | 1-118 | [»] | |
7Q2J | X-ray | 2.50 | A | 1-104 | [»] | |
AlphaFoldDBi | Q15370 | |||||
BMRBi | Q15370 | |||||
SMRi | Q15370 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 112785, 263 interactors |
CORUMi | Q15370 |
DIPi | DIP-29570N |
IntActi | Q15370, 100 interactors |
MINTi | Q15370 |
STRINGi | 9606.ENSP00000262306 |
Chemistry databases
BindingDBi | Q15370 |
ChEMBLi | CHEMBL3301400 CHEMBL4296117 |
PTM databases
GlyGeni | Q15370, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q15370 |
MetOSitei | Q15370 |
PhosphoSitePlusi | Q15370 |
SwissPalmi | Q15370 |
Genetic variation databases
BioMutai | ELOB |
DMDMi | 32699512 |
Proteomic databases
EPDi | Q15370 |
jPOSTi | Q15370 |
MassIVEi | Q15370 |
MaxQBi | Q15370 |
PaxDbi | Q15370 |
PeptideAtlasi | Q15370 |
PRIDEi | Q15370 |
ProteomicsDBi | 60548 [Q15370-1] 6294 |
TopDownProteomicsi | Q15370-1 [Q15370-1] Q15370-2 [Q15370-2] |
Protocols and materials databases
Antibodypediai | 23893, 332 antibodies from 32 providers |
DNASUi | 6923 |
Genome annotation databases
Ensembli | ENST00000262306.11; ENSP00000262306.7; ENSG00000103363.16 [Q15370-2] ENST00000409906.9; ENSP00000386652.5; ENSG00000103363.16 |
GeneIDi | 6923 |
KEGGi | hsa:6923 |
MANE-Selecti | ENST00000409906.9; ENSP00000386652.5; NM_007108.4; NP_009039.1 |
UCSCi | uc002crm.4, human [Q15370-1] |
Organism-specific databases
CTDi | 6923 |
DisGeNETi | 6923 |
GeneCardsi | ELOB |
HGNCi | HGNC:11619, ELOB |
HPAi | ENSG00000103363, Low tissue specificity |
MIMi | 600787, gene |
neXtProti | NX_Q15370 |
OpenTargetsi | ENSG00000103363 |
PharmGKBi | PA36378 |
VEuPathDBi | HostDB:ENSG00000103363 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG4495, Eukaryota |
GeneTreei | ENSGT00390000018316 |
HOGENOMi | CLU_139243_1_0_1 |
InParanoidi | Q15370 |
OMAi | RKKMTIF |
OrthoDBi | 1338040at2759 |
PhylomeDBi | Q15370 |
TreeFami | TF325964 |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
PathwayCommonsi | Q15370 |
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-9705462, Inactivation of CSF3 (G-CSF) signaling R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation |
SignaLinki | Q15370 |
Miscellaneous databases
BioGRID-ORCSi | 6923, 754 hits in 1134 CRISPR screens |
ChiTaRSi | TCEB2, human |
EvolutionaryTracei | Q15370 |
GeneWikii | TCEB2 |
GenomeRNAii | 6923 |
Pharosi | Q15370, Tbio |
PROi | PR:Q15370 |
RNActi | Q15370, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000103363, Expressed in left testis and 251 other tissues |
ExpressionAtlasi | Q15370, baseline and differential |
Genevisiblei | Q15370, HS |
Family and domain databases
InterProi | View protein in InterPro IPR039049, ELOB IPR000626, Ubiquitin-like_dom IPR029071, Ubiquitin-like_domsf |
PANTHERi | PTHR13248, PTHR13248, 1 hit |
Pfami | View protein in Pfam PF00240, ubiquitin, 1 hit |
SMARTi | View protein in SMART SM00213, UBQ, 1 hit |
SUPFAMi | SSF54236, SSF54236, 1 hit |
PROSITEi | View protein in PROSITE PS50053, UBIQUITIN_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ELOB_HUMAN | |
Accessioni | Q15370Primary (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: | May 25, 2022 | |
This is version 211 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 16
Human chromosome 16: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references