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Details on Person UniProt:Q9H792 PEAK1
| Class:Id | ReferenceGeneProduct:248091 |
|---|---|
| _chainChangeLog | chain:1-1746 added on Fri February 6 2015 |
| _displayName | UniProt:Q9H792 PEAK1 |
| _timestamp | 2024-11-03 19:53:09 |
| chain | chain:1-1746 |
| checksum | 7C9A9F60BBCF6C61 |
| comment | FUNCTION Probable catalytically inactive kinase. Scaffolding protein that regulates the cytoskeleton to control cell spreading and migration by modulating focal adhesion dynamics (PubMed:20534451, PubMed:23105102, PubMed:35687021). Acts as a scaffold for mediating EGFR signaling (PubMed:23846654).SUBUNIT Homodimer (PubMed:29212708). Interacts with BCAR1 and CRK (PubMed:20534451). Interacts with PRAG1 (PubMed:29079850). Interacts (when phosphorylated at Tyr-1188) with SHC1 (via PID domain) (PubMed:23846654, PubMed:35687021). Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1. Interacts (when phosphorylated at Tyr-635) with tensin TNS3 (when phosphorylated on the SH2 domain); TNS3 also interacts with integrins ITGB1, ITGB3 and ITGB5 and mediates their association with PEAK1 (PubMed:35687021). Interacts with RASAL2 and GRB2 (PubMed:35687021).INTERACTION Colocalizes with F-actin in serum-rich medium (PubMed:20534451). Actin colocalization is reduced during serum starvation (PubMed:20534451).DOMAIN The dimerization region encompasses helices both from the N- and C-terminal of the protein kinase domain.PTM Phosphorylated on tyrosine in a CSK-dependent manner in response to adhesion to fibronectin and to EGF stimulation (PubMed:20534451). Phosphorylation at Tyr-665 by a Src family kinase controls subcellular localization to focal adhesion and focal adhesion dynamics (PubMed:20534451). Phosphorylation at Tyr-1188 is essential for binding to SHC1 (PubMed:23846654). Phosphorylation at Tyr-635 promotes interaction with tensin TNS3 (PubMed:35687021).SIMILARITY Belongs to the protein kinase superfamily.CAUTION Has been the subject of controversy surrounding its catalytic capabilities. Early characterization of PEAK1 gave a weak in vitro tyrosine kinase activity (PubMed:20534451). The crystal structure indicates that the kinase-domain contains a closed nucleotide-binding cleft that in this conformation may deleteriously affect nucleotide binding (PubMed:29212708). Furthermore PEAK1 is devoid of nucleotide binding activity, as detected by a thermal-shift assay (PubMed:24107129). So it seems probable that PEAK1 is an inactive kinase. |
| created | [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 |
| description | recommendedName: fullName evidence="14"Inactive tyrosine-protein kinase PEAK1 alternativeName: fullName evidence="12"Pseudopodium-enriched atypical kinase 1 alternativeName: fullName evidence="13"Sugen kinase 269 alternativeName: Tyrosine-protein kinase SgK269 |
| geneName | PEAK1 KIAA2002 |
| identifier | Q9H792 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Cell junction Cytoplasm Cytoskeleton Phosphoprotein Proteomics identification Reference proteome |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | PEAK1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8988574] ENSEMBL:ENSG00000173517 PEAK1 [Homo sapiens] |
| secondaryIdentifier | PEAK1_HUMAN Q6ZS78 Q8NAZ4 Q8NCM3 Q8TEG7 |
| sequenceLength | 1746 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:9715162] PEAK1 [cytosol] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:Q9H792 PEAK1 (248091)
