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Details on Person UniProt:P53667 LIMK1

Class:Id	ReferenceGeneProduct:58571
_chainChangeLog	chain:1-647 added on Sat February 7 2015
_displayName	UniProt:P53667 LIMK1
_timestamp	2025-02-21 19:39:32
chain	chain:1-647
checksum	9838BEFBE7006447
comment	FUNCTION Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways (PubMed:10436159, PubMed:11832213, PubMed:12807904, PubMed:15660133, PubMed:16230460, PubMed:18028908, PubMed:22328514, PubMed:23633677). Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop (PubMed:10436159). LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton (PubMed:11832213, PubMed:15660133, PubMed:16230460, PubMed:23633677). In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation (PubMed:11832213, PubMed:15660133, PubMed:16230460, PubMed:23633677). Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly (PubMed:18028908). Stimulates axonal outgrowth and may be involved in brain development (PubMed:18028908).FUNCTION Has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1).CATALYTIC ACTIVITY L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)CATALYTIC ACTIVITY L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)SUBUNIT Interacts (via LIM domain) with the cytoplasmic domain of NRG1. Interacts with NISCH. Interacts with RLIM and RNF6 (By similarity). Self-associates to form homodimers (PubMed:10196227). Interacts with HSP90AA1; this interaction promotes LIMK1 dimerization and subsequent transphosphorylation (PubMed:16641196). Interacts with CDKN1C (PubMed:14530263). Interacts with SSH1 (PubMed:15660133). Interacts with ROCK1 (PubMed:10436159, PubMed:10652353). Interacts (via LIM zinc-binding domains) with FAM89B/LRAP25 (via LRR repeat). Forms a tripartite complex with CDC42BPA, CDC42BPB and FAM89B/LRAP25 (By similarity).INTERACTION Predominantly found in the cytoplasm. Localizes in the lamellipodium in a CDC42BPA, CDC42BPB and FAM89B/LRAP25-dependent manner.ALTERNATIVE PRODUCTS Highest expression in both adult and fetal nervous system. Detected ubiquitously throughout the different regions of adult brain, with highest levels in the cerebral cortex. Expressed to a lesser extent in heart and skeletal muscle.PTM Autophosphorylated. Phosphorylated on Thr-508 by ROCK1 and PAK1, resulting in activation. Phosphorylated by PAK4 which increases the ability of LIMK1 to phosphorylate cofilin. Phosphorylated at Ser-323 by MAPKAPK2 during activation of VEGFA-induced signaling, which results in activation of LIMK1 and promotion of actin reorganization, cell migration, and tubule formation of endothelial cells. Dephosphorylated and inactivated by SSH1. Phosphorylated by CDC42BP.PTM Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF6 leads to proteasomal degradation through the 26S proteasome, modulating LIMK1 levels in the growth cone and its effect on axonal outgrowth. Also polyubiquitinated by RLIM (By similarity).DISEASE LIMK1 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.MISCELLANEOUS May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.SIMILARITY Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
description	recommendedName: LIM domain kinase 1 shortName: LIMK-1 ecNumber evidence="23"2.7.11.1
geneName	LIMK1 LIMK
identifier	P53667
isSequenceChanged	FALSE
keyword	3D-structure Alternative splicing ATP-binding Cell projection Cytoplasm Cytoskeleton Kinase LIM domain Metal-binding Nucleotide-binding Nucleus Phosphoprotein Proteomics identification Reference proteome Repeat Serine/threonine-protein kinase Transferase Ubl conjugation Williams-Beuren syndrome Zinc
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21
name	LIMK1
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8994313] ENSEMBL:ENSG00000106683 LIMK1 [Homo sapiens]
secondaryIdentifier	LIMK1_HUMAN B7Z6I8 D3DXF4 D3DXF5 O15283 Q15820 Q15821 Q75MU3 Q9Y5Q1
sequenceLength	647
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:149715] UniProt:P53667-2 LIMK1 [Homo sapiens] [ReferenceIsoform:149716] UniProt:P53667-3 LIMK1 [Homo sapiens] [ReferenceIsoform:404362] UniProt:P53667-1 LIMK1 [Homo sapiens] [ReferenceIsoform:8968854] UniProt:P53667-4 LIMK1 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:397785] LIMK1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:399816] p-T508-LIMK1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:419610] p-S,T508-LIMK1 [cytosol] [Homo sapiens]
(referenceSequence)	[ModifiedResidue:399817] O-phospho-L-threonine at 508 [ModifiedResidue:419615] O-phospho-L-serine at unknown position
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