Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P53667

- LIMK1_HUMAN

UniProt

P53667 - LIMK1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

LIM domain kinase 1

Gene

LIMK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (4)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei368 – 3681ATPPROSITE-ProRule annotation
Active sitei460 – 4601By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi345 – 3539ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. heat shock protein binding Source: BHF-UCL
  3. protein kinase activity Source: ProtInc
  4. protein serine/threonine kinase activity Source: Reactome
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. actin cytoskeleton organization Source: ProtInc
  2. axon guidance Source: Reactome
  3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  4. innate immune response Source: Reactome
  5. negative regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  6. nervous system development Source: ProtInc
  7. positive regulation of actin filament bundle assembly Source: BHF-UCL
  8. positive regulation of axon extension Source: UniProtKB
  9. positive regulation of stress fiber assembly Source: Ensembl
  10. protein phosphorylation Source: UniProtKB
  11. Rho protein signal transduction Source: ProtInc
  12. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_228085. EPHB-mediated forward signaling.
SignaLinkiP53667.

Names & Taxonomyi

Protein namesi
Recommended name:
LIM domain kinase 1 (EC:2.7.11.1)
Short name:
LIMK-1
Gene namesi
Name:LIMK1
Synonyms:LIMK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:6613. LIMK1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Predominantly found in the cytoplasm.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
  3. focal adhesion Source: Ensembl
  4. neuron projection Source: UniProtKB
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi84 – 841C → S: Enhances actin aggregation. 1 Publication
Mutagenesisi177 – 1782GL → EA: Enhances actin aggregation. 1 Publication
Mutagenesisi460 – 4601D → N: Abrogates kinase activity. 1 Publication
Mutagenesisi496 – 50611Missing: Reduces actin aggregation. 1 PublicationAdd
BLAST
Mutagenesisi503 – 5053RKK → GAA: Abolishes kinase activity. 1 Publication
Mutagenesisi508 – 5081T → A: Abolishes activation by ROCK1. 2 Publications
Mutagenesisi508 – 5081T → EE: Enhances kinase activity. 2 Publications
Mutagenesisi508 – 5081T → V or E: Reduces kinase activity. 2 Publications

Keywords - Diseasei

Williams-Beuren syndrome

Organism-specific databases

Orphaneti904. Williams syndrome.
PharmGKBiPA30386.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 647647LIM domain kinase 1PRO_0000075803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101Phosphoserine2 Publications
Modified residuei229 – 2291Phosphothreonine2 Publications
Modified residuei302 – 3021Phosphoserine1 Publication
Modified residuei307 – 3071Phosphoserine1 Publication
Modified residuei310 – 3101Phosphoserine3 Publications
Modified residuei323 – 3231Phosphoserine; by MAPKAPK21 Publication
Modified residuei337 – 3371Phosphoserine1 Publication
Modified residuei508 – 5081Phosphothreonine; by ROCK1 and PAK14 Publications

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 similarity10 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

MaxQBiP53667.
PaxDbiP53667.
PRIDEiP53667.

PTM databases

PhosphoSiteiP53667.

Expressioni

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

BgeeiP53667.
CleanExiHS_LIMK1.
ExpressionAtlasiP53667. baseline and differential.
GenevestigatoriP53667.

Organism-specific databases

HPAiHPA028064.
HPA028516.

Interactioni

Subunit structurei

Interacts (via LIM domain) with the cytoplasmic domain of NRG1 (By similarity). Interacts with NISCH (By similarity). Interacts with RLIM and RNF6 (By similarity). Self-associates to form homodimers. Interacts with HSP90AA1; this interaction promotes LIMK1 dimerization and subsequent transphosphorylation. Interacts with CDN1C. Interacts with SSH1. Interacts with ROCK1.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Arrb1P290662EBI-444403,EBI-4303019From a different organism.
Arrb2P290672EBI-444403,EBI-1636616From a different organism.
LATS1O958355EBI-444403,EBI-444209
MMP14P502814EBI-444403,EBI-992788
PAK1Q131535EBI-444403,EBI-1307
PAK2Q131772EBI-444403,EBI-1045887
SSH1Q8WYL57EBI-444403,EBI-1222387

Protein-protein interaction databases

BioGridi110172. 24 interactions.
DIPiDIP-31605N.
IntActiP53667. 16 interactions.
MINTiMINT-2833166.
STRINGi9606.ENSP00000336740.

Structurei

Secondary structure

1
647
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi332 – 3343Combined sources
Helixi336 – 3383Combined sources
Beta strandi339 – 3468Combined sources
Beta strandi349 – 35810Combined sources
Turni359 – 3613Combined sources
Beta strandi364 – 3718Combined sources
Helixi375 – 38814Combined sources
Beta strandi399 – 4057Combined sources
Beta strandi408 – 4147Combined sources
Helixi421 – 4277Combined sources
Helixi434 – 45320Combined sources
Beta strandi465 – 4684Combined sources
Beta strandi474 – 4763Combined sources
Helixi513 – 5153Combined sources
Helixi518 – 5214Combined sources
Helixi529 – 54416Combined sources
Turni550 – 5523Combined sources
Beta strandi559 – 5613Combined sources
Helixi563 – 5697Combined sources
Helixi579 – 5868Combined sources
Helixi591 – 5933Combined sources
Helixi597 – 61317Combined sources
Helixi618 – 63417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S95X-ray1.65A/B330-637[»]
ProteinModelPortaliP53667.
SMRiP53667. Positions 22-145, 158-258, 330-637.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53667.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 7551LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini84 – 13754LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini165 – 25894PDZPROSITE-ProRule annotationAdd
BLAST
Domaini339 – 604266Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.Curated
Contains 2 LIM zinc-binding domains.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063025.
HOGENOMiHOG000013121.
HOVERGENiHBG052328.
InParanoidiP53667.
KOiK05743.
PhylomeDBiP53667.
TreeFamiTF318014.

Family and domain databases

Gene3Di2.10.110.10. 2 hits.
2.30.42.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR001478. PDZ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 2 hits.
PF00595. PDZ. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00132. LIM. 2 hits.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00478. 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.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

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
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.

Show »
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti190 – 1901G → A.1 Publication
Corresponds to variant rs35827364 [ dbSNP | Ensembl ].		VAR_042246
Natural varianti247 – 2471S → N.1 Publication
Corresponds to variant rs55661242 [ dbSNP | Ensembl ].		VAR_042247
Natural varianti422 – 4221R → Q.1 Publication
Corresponds to variant rs55679316 [ dbSNP | Ensembl ].		VAR_042248
Natural varianti580 – 5801F → Y.2 Publications
Corresponds to variant rs178412 [ dbSNP | Ensembl ].		VAR_050148

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151MRLTL…ADCFR → MLLASAPRRRRFLQRAK in isoform 4. 1 PublicationVSP_043331Add
BLAST
Alternative sequencei1 – 1414Missing in isoform 2. CuratedVSP_003125Add
BLAST
Alternative sequencei294 – 30512LRSCS…RSPGA → FARTWVALSPSA in isoform 3. 1 PublicationVSP_003126Add
BLAST
Alternative sequencei306 – 647342Missing in isoform 3. 1 PublicationVSP_003127Add
BLAST

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.

Genome annotation databases

EnsembliENST00000336180; ENSP00000336740; ENSG00000106683. [P53667-1]
ENST00000435201; ENSP00000414606; ENSG00000106683. [P53667-3]
ENST00000538333; ENSP00000444452; ENSG00000106683. [P53667-4]
GeneIDi3984.
KEGGihsa:3984.
UCSCiuc003uaa.2. human. [P53667-1]
uc003uab.3. human. [P53667-4]

Polymorphism databases

DMDMi90185240.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

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 .
CCDSi CCDS5563.1. [P53667-1 ]
CCDS56491.1. [P53667-4 ]
PIRi JP0078.
RefSeqi NP_001191355.1. NM_001204426.1. [P53667-4 ]
NP_002305.1. NM_002314.3. [P53667-1 ]
UniGenei Hs.647035.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3S95 X-ray 1.65 A/B 330-637 [» ]
ProteinModelPortali P53667.
SMRi P53667. Positions 22-145, 158-258, 330-637.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110172. 24 interactions.
DIPi DIP-31605N.
IntActi P53667. 16 interactions.
MINTi MINT-2833166.
STRINGi 9606.ENSP00000336740.

Chemistry

BindingDBi P53667.
ChEMBLi CHEMBL3836.
DrugBanki DB08912. Dabrafenib.
GuidetoPHARMACOLOGYi 2054.

PTM databases

PhosphoSitei P53667.

Polymorphism databases

DMDMi 90185240.

Proteomic databases

MaxQBi P53667.
PaxDbi P53667.
PRIDEi P53667.

Protocols and materials databases

DNASUi 3984.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336180 ; ENSP00000336740 ; ENSG00000106683 . [P53667-1 ]
ENST00000435201 ; ENSP00000414606 ; ENSG00000106683 . [P53667-3 ]
ENST00000538333 ; ENSP00000444452 ; ENSG00000106683 . [P53667-4 ]
GeneIDi 3984.
KEGGi hsa:3984.
UCSCi uc003uaa.2. human. [P53667-1 ]
uc003uab.3. human. [P53667-4 ]

Organism-specific databases

CTDi 3984.
GeneCardsi GC07P073497.
HGNCi HGNC:6613. LIMK1.
HPAi HPA028064.
HPA028516.
MIMi 601329. gene.
neXtProti NX_P53667.
Orphaneti 904. Williams syndrome.
PharmGKBi PA30386.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063025.
HOGENOMi HOG000013121.
HOVERGENi HBG052328.
InParanoidi P53667.
KOi K05743.
PhylomeDBi P53667.
TreeFami TF318014.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_228085. EPHB-mediated forward signaling.
SignaLinki P53667.

Miscellaneous databases

ChiTaRSi LIMK1. human.
EvolutionaryTracei P53667.
GeneWikii LIMK1.
GenomeRNAii 3984.
NextBioi 15626.
PROi P53667.
SOURCEi Search...

Gene expression databases

Bgeei P53667.
CleanExi HS_LIMK1.
ExpressionAtlasi P53667. baseline and differential.
Genevestigatori P53667.

Family and domain databases

Gene3Di 2.10.110.10. 2 hits.
2.30.42.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR001478. PDZ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR001781. Znf_LIM.
[Graphical view ]
Pfami PF00412. LIM. 2 hits.
PF00595. PDZ. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00132. LIM. 2 hits.
SM00228. PDZ. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human cDNA encoding a novel protein kinase with two repeats of the LIM/double zinc finger motif."
    Mizuno K., Okano I., Ohashi K., Nunoue K., Kuma K., Miyata T., Nakamura T.
    Oncogene 9:1605-1612(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), VARIANT TYR-580.
    Tissue: Hippocampus and Placenta.
  3. "Identification of genes from a 500-kb region at 7q11.23 that is commonly deleted in Williams syndrome patients."
    Osborne L.R., Martindale D.W., Scherer S.W., Shi X.-M., Huizenga J., Heng H.H.Q., Costa T., Pober B., Lew L., Brinkman J., Rommens J., Koop B.F., Tsui L.-C.
    Genomics 36:328-336(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-580, GENE DELETION IN WILLIAMS-BEUREN SYNDROME.
  4. "Structural features of LIM kinase that control effects on the actin cytoskeleton."
    Edwards D.C., Gill G.N.
    J. Biol. Chem. 274:11352-11361(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-84; 177-GLY-LEU-178; ASP-460; 496-ARG--ARG-506; 503-ARG--GLY-505 AND THR-508.
    Tissue: Epidermal carcinoma.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Placenta.
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics."
    Edwards D.C., Sanders L.C., Bokoch G.M., Gill G.N.
    Nat. Cell Biol. 1:253-259(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-508 BY PAK1.
  9. "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase."
    Maekawa M., Ishizaki T., Boku S., Watanabe N., Fujita A., Iwamatsu A., Obinata T., Ohashi K., Mizuno K., Narumiya S.
    Science 285:895-898(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ROCK1.
  10. "Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop."
    Ohashi K., Nagata K., Maekawa M., Ishizaki T., Narumiya S., Mizuno K.
    J. Biol. Chem. 275:3577-3582(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-508, MUTAGENESIS OF THR-508, INTERACTION WITH ROCK1.
  11. "Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha."
    Sumi T., Matsumoto K., Shibuya A., Nakamura T.
    J. Biol. Chem. 276:23092-23096(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDC42BP.
  12. "Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin."
    Dan C., Kelly A., Bernard O., Minden A.
    J. Biol. Chem. 276:32115-32121(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PAK4.
  13. "Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin."
    Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.
    Cell 108:233-246(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Cell cycle-associated changes in Slingshot phosphatase activity and roles in cytokinesis in animal cells."
    Kaji N., Ohashi K., Shuin M., Niwa R., Uemura T., Mizuno K.
    J. Biol. Chem. 278:33450-33455(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "p57Kip2 regulates actin dynamics by binding and translocating LIM-kinase 1 to the nucleus."
    Yokoo T., Toyoshima H., Miura M., Wang Y., Iida K.T., Suzuki H., Sone H., Shimano H., Gotoda T., Nishimori S., Tanaka K., Yamada N.
    J. Biol. Chem. 278:52919-52923(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDKN1C.
  16. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  17. "Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
    Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
    EMBO J. 24:473-486(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SSH1, PHOSPHORYLATION AT THR-508, DEPHOSPHORYLATION.
  18. "Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration."
    Nishita M., Tomizawa C., Yamamoto M., Horita Y., Ohashi K., Mizuno K.
    J. Cell Biol. 171:349-359(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  19. "MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration."
    Kobayashi M., Nishita M., Mishima T., Ohashi K., Mizuno K.
    EMBO J. 25:713-726(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-323 BY MAPKAPK2.
  20. "Hsp90 increases LIM kinase activity by promoting its homo-dimerization."
    Li R., Soosairajah J., Harari D., Citri A., Price J., Ng H.L., Morton C.J., Parker M.W., Yarden Y., Bernard O.
    FASEB J. 20:1218-1220(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90AA1.
  21. "The phosphorylation of p25/TPPP by LIM kinase 1 inhibits its ability to assemble microtubules."
    Acevedo K., Li R., Soo P., Suryadinata R., Sarcevic B., Valova V.A., Graham M.E., Robinson P.J., Bernard O.
    Exp. Cell Res. 313:4091-4106(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TPPP.
  22. Cited for: REVIEW ON FUNCTION.
  23. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; THR-229; SER-310 AND SER-337, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; THR-229; SER-302 AND SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "LIM kinases are attractive targets with many macromolecular partners and only a few small molecule regulators."
    Manetti F.
    Med. Res. Rev. 32:968-998(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  28. "Nuclear and cytoplasmic LIMK1 enhances human breast cancer progression."
    McConnell B.V., Koto K., Gutierrez-Hartmann A.
    Mol. Cancer 10:75-75(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  29. "Beta-arrestin-dependent activation of the cofilin pathway is required for the scavenging activity of the atypical chemokine receptor D6."
    Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B., Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A., Bonecchi R., Locati M.
    Sci. Signal. 6:RA30-RA30(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-508.
  30. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-190; ASN-247 AND GLN-422.
  31. "Crystal structure of the human limk1 kinase domain in complex with staurosporine."
    Structural genomics consortium (SGC)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 330-637.
+Additional computationally mapped references.

Entry informationi

Entry nameiLIMK1_HUMAN
AccessioniPrimary (citable) accession number: P53667
Secondary accession number(s): B7Z6I8
, D3DXF4, D3DXF5, O15283, Q15820, Q15821, Q75MU3, Q9Y5Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 7, 2006
Last modified: January 7, 2015
This is version 163 of the entry and version 3 of the sequence. [Complete history]
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.

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
© 2002– 2015 UniProt Consortium | License & Disclaimer