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Protein

LIM domain kinase 1

Gene

LIMK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. 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. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1).8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei368ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei460By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi345 – 353ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • heat shock protein binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: Ensembl
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-416572 Sema4D induced cell migration and growth-cone collapse
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5627123 RHO GTPases activate PAKs

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P53667

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P53667

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
LIM domain kinase 1 (EC:2.7.11.1)
Short name:
LIMK-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LIMK1
Synonyms:LIMK
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000106683.14

Human Gene Nomenclature Database

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HGNCi
HGNC:6613 LIMK1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601329 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P53667

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi84C → S: Enhances actin aggregation. 1 Publication1
Mutagenesisi177 – 178GL → EA: Enhances actin aggregation. 1 Publication2
Mutagenesisi460D → N: Abrogates kinase activity. 1 Publication1
Mutagenesisi496 – 506Missing : Reduces actin aggregation. 1 PublicationAdd BLAST11
Mutagenesisi503 – 505RKK → GAA: Abolishes kinase activity. 1 Publication3
Mutagenesisi508T → A: Abolishes activation by ROCK1. 2 Publications1
Mutagenesisi508T → EE: Enhances kinase activity. 2 Publications1
Mutagenesisi508T → V or E: Reduces kinase activity. 2 Publications1

Keywords - Diseasei

Williams-Beuren syndrome

Organism-specific databases

DisGeNET

More...
DisGeNETi
3984

MalaCards human disease database

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MalaCardsi
LIMK1

Open Targets

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OpenTargetsi
ENSG00000106683

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
904 Williams syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30386

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3836

Drug and drug target database

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DrugBanki
DB08912 Dabrafenib

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2054

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
LIMK1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
90185240

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000758031 – 647LIM domain kinase 1Add BLAST647

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei210PhosphoserineCombined sources1
Modified residuei229PhosphothreonineCombined sources1
Modified residuei298PhosphoserineCombined sources1
Modified residuei302PhosphoserineCombined sources1
Modified residuei307PhosphoserineCombined sources1
Modified residuei310PhosphoserineCombined sources1
Modified residuei323Phosphoserine; by MAPKAPK21 Publication1
Modified residuei337PhosphoserineCombined sources1
Modified residuei508Phosphothreonine; by ROCK1 and PAK14 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated (By similarity). 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.By similarity7 Publications
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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P53667

MaxQB - The MaxQuant DataBase

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MaxQBi
P53667

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P53667

PeptideAtlas

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PeptideAtlasi
P53667

PRoteomics IDEntifications database

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PRIDEi
P53667

ProteomicsDB human proteome resource

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ProteomicsDBi
56598
56599 [P53667-2]
56600 [P53667-3]
56601 [P53667-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P53667

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P53667

SwissPalm database of S-palmitoylation events

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SwissPalmi
P53667

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000106683 Expressed in 125 organ(s), highest expression level in anterior cingulate cortex

CleanEx database of gene expression profiles

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CleanExi
HS_LIMK1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P53667 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P53667 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA028064
HPA028516

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110172, 41 interactors

Database of interacting proteins

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DIPi
DIP-31605N

Protein interaction database and analysis system

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IntActi
P53667, 41 interactors

Molecular INTeraction database

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MINTi
P53667

STRING: functional protein association networks

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STRINGi
9606.ENSP00000336740

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P53667

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1647
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P53667

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P53667

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P53667

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini25 – 75LIM zinc-binding 1PROSITE-ProRule annotationAdd BLAST51
Domaini84 – 137LIM zinc-binding 2PROSITE-ProRule annotationAdd BLAST54
Domaini165 – 258PDZPROSITE-ProRule annotationAdd BLAST94
Domaini339 – 604Protein kinasePROSITE-ProRule annotationAdd BLAST266

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IEZ9 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156345

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000013121

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052328

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P53667

KEGG Orthology (KO)

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KOi
K05743

Database for complete collections of gene phylogenies

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PhylomeDBi
P53667

TreeFam database of animal gene trees

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TreeFami
TF318014

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001478 PDZ
IPR036034 PDZ_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR001781 Znf_LIM

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00412 LIM, 2 hits
PF00595 PDZ, 1 hit
PF07714 Pkinase_Tyr, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00132 LIM, 2 hits
SM00228 PDZ, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50156 SSF50156, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00478 LIM_DOMAIN_1, 2 hits
PS50023 LIM_DOMAIN_2, 2 hits
PS50106 PDZ, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P53667-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MRLTLLCCTW REERMGEEGS ELPVCASCGQ RIYDGQYLQA LNADWHADCF
60 70 80 90 100
RCCDCSASLS HQYYEKDGQL FCKKDYWARY GESCHGCSEQ ITKGLVMVAG
110 120 130 140 150
ELKYHPECFI CLTCGTFIGD GDTYTLVEHS KLYCGHCYYQ TVVTPVIEQI
160 170 180 190 200
LPDSPGSHLP HTVTLVSIPA SSHGKRGLSV SIDPPHGPPG CGTEHSHTVR
210 220 230 240 250
VQGVDPGCMS PDVKNSIHVG DRILEINGTP IRNVPLDEID LLIQETSRLL
260 270 280 290 300
QLTLEHDPHD TLGHGLGPET SPLSSPAYTP SGEAGSSARQ KPVLRSCSID
310 320 330 340 350
RSPGAGSLGS PASQRKDLGR SESLRVVCRP HRIFRPSDLI HGEVLGKGCF
360 370 380 390 400
GQAIKVTHRE TGEVMVMKEL IRFDEETQRT FLKEVKVMRC LEHPNVLKFI
410 420 430 440 450
GVLYKDKRLN FITEYIKGGT LRGIIKSMDS QYPWSQRVSF AKDIASGMAY
460 470 480 490 500
LHSMNIIHRD LNSHNCLVRE NKNVVVADFG LARLMVDEKT QPEGLRSLKK
510 520 530 540 550
PDRKKRYTVV GNPYWMAPEM INGRSYDEKV DVFSFGIVLC EIIGRVNADP
560 570 580 590 600
DYLPRTMDFG LNVRGFLDRY CPPNCPPSFF PITVRCCDLD PEKRPSFVKL
610 620 630 640
EHWLETLRMH LAGHLPLGPQ LEQLDRGFWE TYRRGESGLP AHPEVPD
Length:647
Mass (Da):72,585
Last modified:March 7, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9838BEFBE7006447
GO
Isoform 2 (identifier: P53667-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.

Show »
Length:633
Mass (Da):70,793
Checksum:iEAF0A3B93916D9FA
GO
Isoform 3 (identifier: P53667-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     294-305: LRSCSIDRSPGA → FARTWVALSPSA
     306-647: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
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Length:305
Mass (Da):33,373
Checksum:i65FEF49849CCA142
GO
Isoform 4 (identifier: P53667-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: MRLTLLCCTWREERMGEEGSELPVCASCGQRIYDGQYLQALNADWHADCFR → MLLASAPRRRRFLQRAK

Note: No experimental confirmation available.
Show »
Length:613
Mass (Da):68,729
Checksum:iA78F41C1313E9CEE
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PC47E9PC47_HUMAN
LIM domain kinase 1
LIMK1
677Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042246190G → A1 PublicationCorresponds to variant dbSNP:rs35827364Ensembl.1
Natural variantiVAR_042247247S → N1 PublicationCorresponds to variant dbSNP:rs55661242Ensembl.1
Natural variantiVAR_042248422R → Q1 PublicationCorresponds to variant dbSNP:rs55679316Ensembl.1
Natural variantiVAR_050148580F → Y2 PublicationsCorresponds to variant dbSNP:rs178412Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0433311 – 51MRLTL…ADCFR → MLLASAPRRRRFLQRAK in isoform 4. 1 PublicationAdd BLAST51
Alternative sequenceiVSP_0031251 – 14Missing in isoform 2. CuratedAdd BLAST14
Alternative sequenceiVSP_003126294 – 305LRSCS…RSPGA → FARTWVALSPSA in isoform 3. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_003127306 – 647Missing in isoform 3. 1 PublicationAdd BLAST342

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D26309 mRNA Translation: BAA05371.1
U62293 Genomic DNA Translation: AAB17545.1
U62293 Genomic DNA Translation: AAB17546.1
U63721 Genomic DNA Translation: AAC13885.1
U63721 Genomic DNA Translation: AAC13886.1
AF134379 mRNA Translation: AAD25742.1
AK300382 mRNA Translation: BAH13274.1
AC005056 Genomic DNA No translation available.
AC005057 Genomic DNA Translation: AAS07438.1
CH471200 Genomic DNA Translation: EAW69620.1
CH471200 Genomic DNA Translation: EAW69621.1
CH471200 Genomic DNA Translation: EAW69622.1
CH471200 Genomic DNA Translation: EAW69623.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS5563.1 [P53667-1]
CCDS56491.1 [P53667-4]

Protein sequence database of the Protein Information Resource

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PIRi
JP0078

NCBI Reference Sequences

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RefSeqi
NP_001191355.1, NM_001204426.1 [P53667-4]
NP_002305.1, NM_002314.3 [P53667-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.647035

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000336180; ENSP00000336740; ENSG00000106683 [P53667-1]
ENST00000435201; ENSP00000414606; ENSG00000106683 [P53667-3]
ENST00000538333; ENSP00000444452; ENSG00000106683 [P53667-4]

Database of genes from NCBI RefSeq genomes

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GeneIDi
3984

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:3984

UCSC genome browser

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UCSCi
uc003uaa.3 human [P53667-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26309 mRNA Translation: BAA05371.1
U62293 Genomic DNA Translation: AAB17545.1
U62293 Genomic DNA Translation: AAB17546.1
U63721 Genomic DNA Translation: AAC13885.1
U63721 Genomic DNA Translation: AAC13886.1
AF134379 mRNA Translation: AAD25742.1
AK300382 mRNA Translation: BAH13274.1
AC005056 Genomic DNA No translation available.
AC005057 Genomic DNA Translation: AAS07438.1
CH471200 Genomic DNA Translation: EAW69620.1
CH471200 Genomic DNA Translation: EAW69621.1
CH471200 Genomic DNA Translation: EAW69622.1
CH471200 Genomic DNA Translation: EAW69623.1
CCDSiCCDS5563.1 [P53667-1]
CCDS56491.1 [P53667-4]
PIRiJP0078
RefSeqiNP_001191355.1, NM_001204426.1 [P53667-4]
NP_002305.1, NM_002314.3 [P53667-1]
UniGeneiHs.647035

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3S95X-ray1.65A/B330-637[»]
5HVJX-ray2.20A/B329-638[»]
5HVKX-ray3.50A/C329-638[»]
5L6WX-ray2.53L330-637[»]
5NXCX-ray2.25L330-637[»]
ProteinModelPortaliP53667
SMRiP53667
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110172, 41 interactors
DIPiDIP-31605N
IntActiP53667, 41 interactors
MINTiP53667
STRINGi9606.ENSP00000336740

Chemistry databases

BindingDBiP53667
ChEMBLiCHEMBL3836
DrugBankiDB08912 Dabrafenib
GuidetoPHARMACOLOGYi2054

PTM databases

iPTMnetiP53667
PhosphoSitePlusiP53667
SwissPalmiP53667

Polymorphism and mutation databases

BioMutaiLIMK1
DMDMi90185240

Proteomic databases

EPDiP53667
MaxQBiP53667
PaxDbiP53667
PeptideAtlasiP53667
PRIDEiP53667
ProteomicsDBi56598
56599 [P53667-2]
56600 [P53667-3]
56601 [P53667-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3984
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336180; ENSP00000336740; ENSG00000106683 [P53667-1]
ENST00000435201; ENSP00000414606; ENSG00000106683 [P53667-3]
ENST00000538333; ENSP00000444452; ENSG00000106683 [P53667-4]
GeneIDi3984
KEGGihsa:3984
UCSCiuc003uaa.3 human [P53667-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3984
DisGeNETi3984
EuPathDBiHostDB:ENSG00000106683.14

GeneCards: human genes, protein and diseases

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GeneCardsi
LIMK1
HGNCiHGNC:6613 LIMK1
HPAiHPA028064
HPA028516
MalaCardsiLIMK1
MIMi601329 gene
neXtProtiNX_P53667
OpenTargetsiENSG00000106683
Orphaneti904 Williams syndrome
PharmGKBiPA30386

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IEZ9 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000156345
HOGENOMiHOG000013121
HOVERGENiHBG052328
InParanoidiP53667
KOiK05743
PhylomeDBiP53667
TreeFamiTF318014

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-416572 Sema4D induced cell migration and growth-cone collapse
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5627123 RHO GTPases activate PAKs
SignaLinkiP53667
SIGNORiP53667

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
LIMK1 human
EvolutionaryTraceiP53667

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
LIMK1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
3984

Protein Ontology

More...
PROi
PR:P53667

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000106683 Expressed in 125 organ(s), highest expression level in anterior cingulate cortex
CleanExiHS_LIMK1
ExpressionAtlasiP53667 baseline and differential
GenevisibleiP53667 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001478 PDZ
IPR036034 PDZ_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR001781 Znf_LIM
PfamiView protein in Pfam
PF00412 LIM, 2 hits
PF00595 PDZ, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00132 LIM, 2 hits
SM00228 PDZ, 1 hit
SUPFAMiSSF50156 SSF50156, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00478 LIM_DOMAIN_1, 2 hits
PS50023 LIM_DOMAIN_2, 2 hits
PS50106 PDZ, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLIMK1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P53667
Secondary accession number(s): B7Z6I8
, D3DXF4, D3DXF5, O15283, Q15820, Q15821, Q75MU3, Q9Y5Q1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 7, 2006
Last modified: December 5, 2018
This is version 200 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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