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LIM domain kinase 2; LIMK-2 (LIMK2)
Function:
- serine/threonine kinase
- phosphorylates myelin basic protein & histones in vitro
- binds ROCK1; ROCK1 links Rho GTPases to LIMK2
- phosphorylated on Ser &/or Thr by ROCK1
- activation of TGFBR1 leads to regulation of actin assembly, via LIMK2
- binds LKAP
- interacts with PARD3
- interacts with NISCH (putative)
ATP + a protein ADP + a phosphoprotein
Structure:
- belongs to the protein kinase superfamily, TKL Ser/Thr protein kinase family
- contains 2 LIM Zn+2-binding domains
- contains 1 PDZ domain (DHR domain)
- contains 1 protein kinase domain
Compartment:
- isoform LIMK2a: cytoplasm, nucleus
- isoform LIMK2b: mainly in the cytoplasm, infrequently translocated to the nucleus
Alternative splicing: named isoforms=2, LIMK2a, LIMK2b
Expression:
- expressed in placenta > liver, lung, kidney, & pancreas
- LIMK2a is more abundant then LIMK2b in liver, colon, stomach, & spleen
- in brain, kidney, & placenta LIMK2b is the dominant form
- in adult lung, both LIMK2a & LIMK2b is nearly equally observed
General
LIM domain protein
serine/threonine kinase
Properties
SIZE: entity length = 638 aa
MW = 72 kD
COMPARTMENT: cytoplasm
cell nucleus
STATE: active state
MOTIF: LIM domain {12-63}
MOTIF: cysteine residue (6)
histidine residue
Zn+2-binding site
LIM domain {72-124}
MOTIF: cysteine residue (6)
histidine residue
Zn+2-binding site
PDZ domain
NAME: PDZ domain
SITE: 152-239
MOTIF: Ser phosphorylation site {S191}
Thr phosphorylation site {T210}
Ser phosphorylation site {S287}
Ser phosphorylation site {S289}
Ser phosphorylation site {S291}
Ser phosphorylation site {S293}
Ser phosphorylation site {S298}
kinase domain
SITE: 331-608
MOTIF: ATP-binding site
NAME: ATP-binding site
SITE: 337-345
ATP-binding site
NAME: ATP-binding site
SITE: 360-360
aspartate residue {D451}
Thr phosphorylation site {T505}
Database Correlations
OMIM 601988
UniProt P53671
PFAM correlations
Entrez Gene 3985
ENZYME 2.7.11.
References
- Vardouli L, Moustakas A, Stournaras C.
LIM-kinase 2 and cofilin phosphorylation mediate actin
cytoskeleton reorganization induced by transforming growth
factor-beta.
J Biol Chem. 2005 Mar 25;280(12):11448-57. Epub 2005 Jan 11.
PMID: 15647284
- UniProt :accession P53671