A2RU30 · TESP1_HUMAN
- ProteinProtein TESPA1
- GeneTESPA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids521 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development (By similarity).
Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca2+ release and mitochondrial Ca2+ uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment.
Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca2+ release and mitochondrial Ca2+ uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment.
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 | COP9 signalosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | TCR signalosome | |
Molecular Function | phospholipase binding | |
Molecular Function | signaling receptor binding | |
Biological Process | COP9 signalosome assembly | |
Biological Process | positive regulation of T cell differentiation in thymus | |
Biological Process | positive regulation of T cell receptor signaling pathway | |
Biological Process | protein localization | |
Biological Process | T cell differentiation in thymus | |
Biological Process | TCR signalosome assembly |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein TESPA1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA2RU30
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: May localize to mitochondria-associated endoplasmic reticulum membrane (MAM).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 185 | Loss of ITPR1-binding. | ||||
Sequence: F → A | ||||||
Mutagenesis | 186 | Strong decrease in ITPR1-binding. Complete loss of ITPR1-binding; when associated with A-185. | ||||
Sequence: F → A | ||||||
Natural variant | VAR_049513 | 496 | in dbSNP:rs997173 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 728 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 (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000315219 | 1-521 | UniProt | Protein TESPA1 | |||
Sequence: MEASVLSPTSWEKRRAWLRQSRNWQTQVLEEEAAAALQDVPDPEPSSLDDVFQEGNPINKIEDWLQDCGYSEEGFSEEAGQFIYNGFCSHGTSFEDDLTLGAEATLLAANGKLFSRSFLETARPCQLLDLGCSLASSSMTGGTNKTSSSISEILDKVQEDAEDVLFSLGFGQEDHKDTSRIPARFFTTPSQAKGIDFQLFLKSQVRRIEMEDPCLMLASRFKQVQTLAVTADAFFCLYSYVSKTPVQKFTPSHMFWNCNHPTDVPSIRILSREPEPQSPRDRLRKAISKMCLYTCPRDRPPPPHNTPKRNSLDQVVLEVMDKVKEEKQFLQQDSDLGQFSQEDPVPPAEGKKLPTSPYPCVFCCEEETQQRMSTVLAPSQTLDSNPKVPCCTHSLPIEDPQWSTDPAQIRRELCSLPATNTETHPAKDETFWKRKSRARKSLFQKNLMGRKVKSLDLSITQQKWKQSVDRPELRRSLSQQPQDTFDLEEVQSNSEEEQSQSRWPSRPRHPHHHQTFAGKDS | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 311 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 334 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 454 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 476 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 478 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
May be phosphorylated in response to store-operated Ca(+2) entry.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with PLCG1 and GRB2; the association is increased with prolonged stimulation of the TCR and may facilitate the assembly of the LAT signalosome. Interacts with ITPR1. Also interacts with ITPR3 (By similarity).
Interacts with HSPA9
Interacts with HSPA9
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 331-351 | Disordered | ||||
Sequence: QQDSDLGQFSQEDPVPPAEGK | ||||||
Region | 461-521 | Disordered | ||||
Sequence: QQKWKQSVDRPELRRSLSQQPQDTFDLEEVQSNSEEEQSQSRWPSRPRHPHHHQTFAGKDS | ||||||
Compositional bias | 473-500 | Polar residues | ||||
Sequence: LRRSLSQQPQDTFDLEEVQSNSEEEQSQ |
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
A2RU30-1
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.
- Name1
- Length521
- Mass (Da)59,213
- Last updated2008-01-15 v2
- ChecksumE10A8FC0056909F3
A2RU30-2
- Name2
- Differences from canonical
- 1-138: Missing
A2RU30-3
- Name3
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_030488 | 1-138 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 473-500 | Polar residues | ||||
Sequence: LRRSLSQQPQDTFDLEEVQSNSEEEQSQ | ||||||
Sequence conflict | 475 | in Ref. 7; AAH44578 | ||||
Sequence: R → Q | ||||||
Alternative sequence | VSP_030489 | 520-521 | in isoform 3 | |||
Sequence: DS → FVKLSPPPQQHVV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018291 EMBL· GenBank· DDBJ | BAA34468.2 EMBL· GenBank· DDBJ | mRNA | ||
AK298405 EMBL· GenBank· DDBJ | BAG60635.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303223 EMBL· GenBank· DDBJ | BAG64310.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315972 EMBL· GenBank· DDBJ | BAH14343.1 EMBL· GenBank· DDBJ | mRNA | ||
AC079842 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471054 EMBL· GenBank· DDBJ | EAW96796.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471054 EMBL· GenBank· DDBJ | EAW96799.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC044578 EMBL· GenBank· DDBJ | AAH44578.1 EMBL· GenBank· DDBJ | mRNA | ||
BC132732 EMBL· GenBank· DDBJ | AAI32733.2 EMBL· GenBank· DDBJ | mRNA | ||
BC132734 EMBL· GenBank· DDBJ | AAI32735.2 EMBL· GenBank· DDBJ | mRNA | ||
AF161375 EMBL· GenBank· DDBJ | AAF28935.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |