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UniProtKB - P53667 (LIMK1_HUMAN)

UniProt

P53667 - LIMK1_HUMAN

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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-Experimental evidence at protein leveli

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

  • ATP binding Source: UniProtKB-KW
  • heat shock protein binding Source: BHF-UCL
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activity Source: Reactome
  • zinc ion binding Source: InterPro

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • negative regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  • nervous system development Source: ProtInc
  • positive regulation of actin filament bundle assembly Source: BHF-UCL
  • positive regulation of axon extension Source: UniProtKB
  • positive regulation of stress fiber assembly Source: Ensembl
  • protein phosphorylation Source: UniProtKB
  • Rho protein signal transduction Source: ProtInc
  • 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.
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.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:6613. LIMK1.

Subcellular locationi

GO - Cellular componenti

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

MalaCardsiLIMK1.
Orphaneti904. Williams syndrome.
PharmGKBiPA30386.

Chemistry

ChEMBLiCHEMBL3836.
DrugBankiDB08912. Dabrafenib.
GuidetoPHARMACOLOGYi2054.

Polymorphism and mutation databases

BioMutaiLIMK1.
DMDMi90185240.

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 – 2101PhosphoserineCombined sources
Modified residuei229 – 2291PhosphothreonineCombined sources
Modified residuei298 – 2981PhosphoserineCombined sources
Modified residuei302 – 3021PhosphoserineCombined sources
Modified residuei307 – 3071PhosphoserineCombined sources
Modified residuei310 – 3101PhosphoserineCombined sources
Modified residuei323 – 3231Phosphoserine; by MAPKAPK21 Publication
Modified residuei337 – 3371PhosphoserineCombined sources
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 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

EPDiP53667.
MaxQBiP53667.
PaxDbiP53667.
PeptideAtlasiP53667.
PRIDEiP53667.

PTM databases

iPTMnetiP53667.
PhosphoSiteiP53667.
SwissPalmiP53667.

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

BgeeiENSG00000106683.
CleanExiHS_LIMK1.
ExpressionAtlasiP53667. baseline and differential.
GenevisibleiP53667. HS.

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.
CFL1P235282EBI-444403,EBI-352733
LATS1O958355EBI-444403,EBI-444209
MMP14P502814EBI-444403,EBI-992788
PAK1Q131535EBI-444403,EBI-1307
PAK2Q131772EBI-444403,EBI-1045887
SSH1Q8WYL57EBI-444403,EBI-1222387

GO - Molecular functioni

  • heat shock protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110172. 39 interactions.
DIPiDIP-31605N.
IntActiP53667. 32 interactions.
MINTiMINT-2833166.
STRINGi9606.ENSP00000336740.

Chemistry

BindingDBiP53667.

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[»]
5HVJX-ray2.20A/B329-638[»]
5HVKX-ray3.50A/C329-638[»]
5L6WX-ray2.53L330-637[»]
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

eggNOGiENOG410IEZ9. Eukaryota.
COG0515. LUCA.
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. AlignAdd to basket

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.3. human. [P53667-1]

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.
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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S95X-ray1.65A/B330-637[»]
5HVJX-ray2.20A/B329-638[»]
5HVKX-ray3.50A/C329-638[»]
5L6WX-ray2.53L330-637[»]
ProteinModelPortaliP53667.
SMRiP53667. Positions 22-145, 158-258, 330-637.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110172. 39 interactions.
DIPiDIP-31605N.
IntActiP53667. 32 interactions.
MINTiMINT-2833166.
STRINGi9606.ENSP00000336740.

Chemistry

BindingDBiP53667.
ChEMBLiCHEMBL3836.
DrugBankiDB08912. Dabrafenib.
GuidetoPHARMACOLOGYi2054.

PTM databases

iPTMnetiP53667.
PhosphoSiteiP53667.
SwissPalmiP53667.

Polymorphism and mutation databases

BioMutaiLIMK1.
DMDMi90185240.

Proteomic databases

EPDiP53667.
MaxQBiP53667.
PaxDbiP53667.
PeptideAtlasiP53667.
PRIDEiP53667.

Protocols and materials databases

DNASUi3984.
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

CTDi3984.
GeneCardsiLIMK1.
HGNCiHGNC:6613. LIMK1.
HPAiHPA028064.
HPA028516.
MalaCardsiLIMK1.
MIMi601329. gene.
neXtProtiNX_P53667.
Orphaneti904. Williams syndrome.
PharmGKBiPA30386.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEZ9. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00530000063025.
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

ChiTaRSiLIMK1. human.
EvolutionaryTraceiP53667.
GeneWikiiLIMK1.
GenomeRNAii3984.
PROiP53667.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106683.
CleanExiHS_LIMK1.
ExpressionAtlasiP53667. baseline and differential.
GenevisibleiP53667. HS.

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]
ProtoNetiSearch...

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: September 7, 2016
This is version 182 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

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 one 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.