Q8N103 · TAGAP_HUMAN
- ProteinT-cell activation Rho GTPase-activating protein
- GeneTAGAP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids731 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
May function as a GTPase-activating protein and may play important roles during T-cell activation.
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 | cytosol | |
Molecular Function | GTPase activator activity | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Biological Process | regulation of Rho protein signal transduction | |
Biological Process | regulation of small GTPase mediated signal transduction | |
Biological Process | signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameT-cell activation Rho GTPase-activating protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8N103
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_049146 | 346 | in dbSNP:rs35263580 | |||
Sequence: G → D |
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_0000056719 | 1-731 | UniProt | T-cell activation Rho GTPase-activating protein | |||
Sequence: MKLRSSHNASKTLNANNMETLIECQSEGDIKEHPLLASCESEDSICQLIEVKKRKKVLSWPFLMRRLSPASDFSGALETDLKASLFDQPLSIICGDSDTLPRPIQDILTILCLKGPSTEGIFRRAANEKARKELKEELNSGDAVDLERLPVHLLAVVFKDFLRSIPRKLLSSDLFEEWMGALEMQDEEDRIEALKQVADKLPRPNLLLLKHLVYVLHLISKNSEVNRMDSSNLAICIGPNMLTLENDQSLSFEAQKDLNNKVKTLVEFLIDNCFEIFGENIPVHSSITSDDSLEHTDSSDVSTLQNDSAYDSNDPDVESNSSSGISSPSRQPQVPMATAAGLDSAGPQDAREVSPEPIVSTVARLKSSLAQPDRRYSEPSMPSSQECLESRVTNQTLTKSEGDFPVPRVGSRLESEEAEDPFPEEVFPAVQGKTKRPVDLKIKNLAPGSVLPRALVLKAFSSSSLDASSDSSPVASPSSPKRNFFSRHQSFTTKTEKGKPSREIKKHSMSFTFAPHKKVLTKNLSAGSGKSQDFTRDHVPRGVRKESQLAGRIVQENGCETHNQTARGFCLRPHALSVDDVFQGADWERPGSPPSYEEAMQGPAARLVASESQTVGSMTVGSMRARMLEAHCLLPPLPPAHHVEDSRHRGSKEPLPGHGLSPLPERWKQSRTVHASGDSLGHVSGPGRPELLPLRTVSESVQRNKRDCLVRRCSQPVFEADQFQYAKESYI | |||||||
Modified residue (large scale data) | 68 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 71 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 354 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 377 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 400 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 714 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8N103 | HSF2BP O75031 | 3 | EBI-12136823, EBI-7116203 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 88-277 | Rho-GAP | ||||
Sequence: QPLSIICGDSDTLPRPIQDILTILCLKGPSTEGIFRRAANEKARKELKEELNSGDAVDLERLPVHLLAVVFKDFLRSIPRKLLSSDLFEEWMGALEMQDEEDRIEALKQVADKLPRPNLLLLKHLVYVLHLISKNSEVNRMDSSNLAICIGPNMLTLENDQSLSFEAQKDLNNKVKTLVEFLIDNCFEIF | ||||||
Region | 288-421 | Disordered | ||||
Sequence: TSDDSLEHTDSSDVSTLQNDSAYDSNDPDVESNSSSGISSPSRQPQVPMATAAGLDSAGPQDAREVSPEPIVSTVARLKSSLAQPDRRYSEPSMPSSQECLESRVTNQTLTKSEGDFPVPRVGSRLESEEAEDP | ||||||
Compositional bias | 298-334 | Polar residues | ||||
Sequence: SSDVSTLQNDSAYDSNDPDVESNSSSGISSPSRQPQV | ||||||
Compositional bias | 373-401 | Polar residues | ||||
Sequence: DRRYSEPSMPSSQECLESRVTNQTLTKSE | ||||||
Compositional bias | 464-491 | Polar residues | ||||
Sequence: SLDASSDSSPVASPSSPKRNFFSRHQSF | ||||||
Region | 464-507 | Disordered | ||||
Sequence: SLDASSDSSPVASPSSPKRNFFSRHQSFTTKTEKGKPSREIKKH | ||||||
Compositional bias | 492-507 | Basic and acidic residues | ||||
Sequence: TTKTEKGKPSREIKKH | ||||||
Region | 641-662 | Disordered | ||||
Sequence: HHVEDSRHRGSKEPLPGHGLSP |
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q8N103-1
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
- Length731
- Mass (Da)80,703
- Last updated2002-10-01 v1
- Checksum9D8768258A0A681E
Q8N103-2
- Name2
- Differences from canonical
- 1-178: Missing
Q8N103-3
- Name3
- SynonymsFKSG15
- NoteDubious isoform. The N-terminus appears to be derived from exons of the CEP43 locus which is located on the opposing strand of chromosome 6 at a distance of several Mb.
Q8N103-4
- Name4
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAQ5BID7 | A0AAQ5BID7_HUMAN | TAGAP | 67 | ||
A0A2R8YEB9 | A0A2R8YEB9_HUMAN | TAGAP | 57 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_015869 | 1-178 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015868 | 1-209 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015870 | 210-261 | in isoform 3 | |||
Sequence: KHLVYVLHLISKNSEVNRMDSSNLAICIGPNMLTLENDQSLSFEAQKDLNNK → MAATAAAVVAEEDTELRDLLVQTLENSGVLNRIKAELRAAVFLALEEQEKVE | ||||||
Alternative sequence | VSP_015871 | 263-266 | in isoform 4 | |||
Sequence: KTLV → CSAY | ||||||
Alternative sequence | VSP_015872 | 267-731 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 298-334 | Polar residues | ||||
Sequence: SSDVSTLQNDSAYDSNDPDVESNSSSGISSPSRQPQV | ||||||
Compositional bias | 373-401 | Polar residues | ||||
Sequence: DRRYSEPSMPSSQECLESRVTNQTLTKSE | ||||||
Compositional bias | 464-491 | Polar residues | ||||
Sequence: SLDASSDSSPVASPSSPKRNFFSRHQSF | ||||||
Compositional bias | 492-507 | Basic and acidic residues | ||||
Sequence: TTKTEKGKPSREIKKH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF385429 EMBL· GenBank· DDBJ | AAM43830.1 EMBL· GenBank· DDBJ | mRNA | ||
AF385430 EMBL· GenBank· DDBJ | AAM43831.1 EMBL· GenBank· DDBJ | mRNA | ||
AF314817 EMBL· GenBank· DDBJ | AAL16675.1 EMBL· GenBank· DDBJ | mRNA | ||
AK097090 EMBL· GenBank· DDBJ | BAC04947.1 EMBL· GenBank· DDBJ | mRNA | ||
AL035530 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC015859 EMBL· GenBank· DDBJ | AAH15859.1 EMBL· GenBank· DDBJ | mRNA | ||
BC111731 EMBL· GenBank· DDBJ | AAI11732.1 EMBL· GenBank· DDBJ | mRNA |