Q8TE02 · ELP5_HUMAN
- ProteinElongator complex protein 5
- GeneELP5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids300 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:29332244).
The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244).
Involved in cell migration (By similarity).
The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244).
Involved in cell migration (By similarity).
Pathway
tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | elongator holoenzyme complex | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Biological Process | positive regulation of cell migration | |
Biological Process | regulation of translation | |
Biological Process | tRNA modification | |
Biological Process | tRNA wobble uridine modification |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongator complex protein 5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TE02
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_088548 | 14 | In isoform Q8TE02-1; in dbSNP:rs2521988 | |||
Sequence: E → K | ||||||
Natural variant | VAR_031205 | 287 | in dbSNP:rs17849664 | |||
Sequence: D → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 420 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000280817 | 1-300 | UniProt | Elongator complex protein 5 | |||
Sequence: MLDSLLALGGLVLLRDSVEWEGRSLLKALVKKSALCGEQVHILGCEVSEEEFREGFDSDINNRLVYHDFFRDPLNWSKTEEAFPGGPLGALRAMCKRTDPVPVTIALDSLSWLLLRLPCTTLCQVLHAVSHQDSCPGDSSSVGKVSVLGLLHEELHGPGPVGALSSLAQTEVTLGGTMGQASAHILCRRPRQRPTDQTQWFSILPDFSLDLQEGPSVESQPYSDPHIPPVDPTTHLTFNLHLSKKEREARDSLILPFQFSSEKQQALLRPRPGQATSHIFYEPDAYDDLDQEDPDDDLDI | |||||||
Modified residue | 252 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Tyrosine-phosphorylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed with high levels in heart, brain, liver, skeletal muscle and testis.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the elongator complex which consists of ELP1, ELP2, ELP3, ELP4, ELP5 and ELP6; in the complex, is required for optimal binding of ELP3 to ELP4.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TE02 | ATXN1 P54253 | 8 | EBI-946189, EBI-930964 | |
BINARY | Q8TE02 | ELP4 Q96EB1 | 6 | EBI-946189, EBI-3951755 | |
BINARY | Q8TE02 | ELP6 Q0PNE2 | 4 | EBI-946189, EBI-2932659 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 264-300 | Disordered | ||||
Sequence: QQALLRPRPGQATSHIFYEPDAYDDLDQEDPDDDLDI | ||||||
Compositional bias | 286-300 | Acidic residues | ||||
Sequence: YDDLDQEDPDDDLDI |
Sequence similarities
Belongs to the ELP5 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing & Alternative initiation.
Q8TE02-5
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.
- Name5
- NoteMajor isoform.
- Length300
- Mass (Da)33,197
- Last updated2024-01-24 v3
- Checksum2443B829343D72EF
Q8TE02-1
- Name1
- NoteProduced by alternative initiation at Met-1 of isoform 5.
- Differences from canonical
- 1-1: M → MTPSEGARAGTGRELEM
Q8TE02-2
- Name2
Q8TE02-3
- Name3
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAG2TUP7 | A0AAG2TUP7_HUMAN | ELP5 | 245 | ||
A0AAG2TUE0 | A0AAG2TUE0_HUMAN | ELP5 | 230 | ||
A0AAG2TUE2 | A0AAG2TUE2_HUMAN | ELP5 | 279 | ||
A0AAG2TUG6 | A0AAG2TUG6_HUMAN | ELP5 | 95 | ||
A0AAG2TUH6 | A0AAG2TUH6_HUMAN | ELP5 | 209 | ||
A0AAG2TTU6 | A0AAG2TTU6_HUMAN | ELP5 | 179 | ||
I3NI50 | I3NI50_HUMAN | ELP5 | 43 | ||
I3L437 | I3L437_HUMAN | ELP5 | 236 | ||
I3L2T0 | I3L2T0_HUMAN | ELP5 | 193 | ||
I3L2A9 | I3L2A9_HUMAN | ELP5 | 117 | ||
I3L1Q3 | I3L1Q3_HUMAN | ELP5 | 262 | ||
I3L200 | I3L200_HUMAN | ELP5 | 108 | ||
I3L1A8 | I3L1A8_HUMAN | ELP5 | 79 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_062149 | 1 | in isoform 1 | |||
Sequence: M → MTPSEGARAGTGRELEM | ||||||
Sequence conflict | 135 | in Ref. 3; AAM10496 | ||||
Sequence: C → R | ||||||
Alternative sequence | VSP_062150 | 138-163 | in isoform 3 | |||
Sequence: DSSSVGKVSVLGLLHEELHGPGPVGA → ETPPSLFPLIHLPLPRSVPLFLSTLE | ||||||
Sequence conflict | 159 | in Ref. 3; AAM10496 | ||||
Sequence: G → S | ||||||
Alternative sequence | VSP_062151 | 164-300 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 165 | in Ref. 3; AAM10496 | ||||
Sequence: S → N | ||||||
Sequence conflict | 212 | in Ref. 3; AAM10496 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 229 | in Ref. 3; AAM10496 | ||||
Sequence: P → R | ||||||
Alternative sequence | VSP_062152 | 231-263 | in isoform 2 | |||
Sequence: DPTTHLTFNLHLSKKEREARDSLILPFQFSSEK → SKNAKARTRKCSLVSGHGRENKSCRGWGWGQGF | ||||||
Sequence conflict | 247 | In isoform Q8TE02-2; in Ref. 9; AAQ13591 | ||||
Sequence: H → Q | ||||||
Alternative sequence | VSP_062153 | 264-300 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 286-300 | Acidic residues | ||||
Sequence: YDDLDQEDPDDDLDI |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB013910 EMBL· GenBank· DDBJ | BAB87800.1 EMBL· GenBank· DDBJ | mRNA | ||
AF087868 EMBL· GenBank· DDBJ | AAM10496.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK289940 EMBL· GenBank· DDBJ | BAF82629.1 EMBL· GenBank· DDBJ | mRNA | ||
AC003688 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471108 EMBL· GenBank· DDBJ | EAW90230.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90231.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002762 EMBL· GenBank· DDBJ | AAH02762.2 EMBL· GenBank· DDBJ | mRNA | ||
AF070658 EMBL· GenBank· DDBJ | AAD20964.1 EMBL· GenBank· DDBJ | mRNA | ||
AF163262 EMBL· GenBank· DDBJ | AAQ13591.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL713741 EMBL· GenBank· DDBJ | CAH56280.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |