Reviewed, UniProtKB/Swiss-Prot P53667 (LIMK1_HUMAN)

Names and origin

Protein names

Recommended name:
    LIM domain kinase 1
      Short name=LIMK-1
    EC=2.7.11.1

Gene names

Name:	LIMK1
Synonyms:	LIMK

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	647 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Protein kinase which regulates actin filament dynamics. Phosphorylates and inactivates the actin binding/depolymerizing factor cofilin, thereby stabilizing the actin cytoskeleton. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. May be involved in brain development. Ref.4 Ref.6 Ref.8 Ref.9 Ref.11 Ref.12
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Self-associates. The LIM domain interacts with the cytoplasmic domain of NRG1. Binds ROCK1. Interacts with SSH1. Interacts with NISCH By similarity. Interacts with TPPP. Ref.6 Ref.11 Ref.7 Ref.13
Subcellular location	Cytoplasm Ref.4 Ref.12.
Tissue specificity	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.
Post-translational modification	Autophosphorylated By similarity. Phosphorylated on serine and/or threonine residues by ROCK1. May be dephosphorylated and inactivated by SSH1.
Involvement in disease	Haploinsufficiency of LIMK1 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in Williams-Beuren syndrome (WBS), a rare developmental disorder. It is a contiguous gene deletion syndrome involving genes from chromosome band 7q11.23.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Contains 2 LIM zinc-binding domains. Contains 1 PDZ (DHR) domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Williams-Beuren syndrome
Domain	LIM domain Repeat
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	Rho protein signal transduction Ref.6 Traceable author statement. Source: ProtInc actin cytoskeleton organization Traceable author statement. Source: ProtInc negative regulation of ubiquitin-protein ligase activity Inferred from direct assay. Source: UniProtKB nervous system development Ref.2 Traceable author statement. Source: ProtInc positive regulation of actin filament bundle assembly Inferred from direct assay. Source: UniProtKB protein amino acid phosphorylation Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW heat shock protein binding Inferred from direct assay. Source: UniProtKB protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Traceable author statement. Source: ProtInc protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LATS1	O95835	3	EBI-444403,EBI-444209
PAK2	Q13177	2	EBI-444403,EBI-1045887
YWHAZ	P63104	1	EBI-444403,EBI-347088

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P53667-1)

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.

Isoform 2 (identifier: P53667-2)

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

Isoform 3 (identifier: P53667-3)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 647	647	LIM domain kinase 1		PRO_0000075803
Regions
	Domain	25 – 75	51	LIM zinc-binding 1
	Domain	84 – 137	54	LIM zinc-binding 2
	Domain	165 – 258	94	PDZ
	Domain	339 – 604	266	Protein kinase
	Nucleotide binding	345 – 353	9	ATP By similarity
Sites
	Active site	460	1	By similarity
	Binding site	368	1	ATP By similarity
Amino acid modifications
	Modified residue	210	1	Phosphoserine Ref.15
	Modified residue	229	1	Phosphothreonine Ref.15
	Modified residue	261	1	Phosphothreonine
	Modified residue	270	1	Phosphothreonine
	Modified residue	296	1	Phosphoserine
	Modified residue	298	1	Phosphoserine Ref.14 Ref.15 Ref.17
	Modified residue	302	1	Phosphoserine Ref.16
	Modified residue	307	1	Phosphoserine Ref.16
	Modified residue	310	1	Phosphoserine Ref.14 Ref.15 Ref.16 Ref.17
	Modified residue	313	1	Phosphoserine
	Modified residue	337	1	Phosphoserine Ref.15
	Modified residue	508	1	Phosphothreonine; by ROCK1 Ref.11 Ref.7
Natural variations
	Alternative sequence	1 – 14	14	Missing in isoform 2.		VSP_003125
	Alternative sequence	294 – 305	12	LRSCS…RSPGA → FARTWVALSPSA in isoform 3.		VSP_003126
	Alternative sequence	306 – 647	342	Missing in isoform 3.		VSP_003127
	Natural variant	190	1	G → A: dbSNP rs35827364. Ref.19		VAR_042246
	Natural variant	247	1	S → N: dbSNP rs55661242. Ref.19		VAR_042247
	Natural variant	422	1	R → Q: dbSNP rs55679316. Ref.19		VAR_042248
	Natural variant	580	1	F → Y: dbSNP rs178412. Ref.2 Ref.3		VAR_050148
Experimental info
	Mutagenesis	84	1	C → S: Enhances actin aggregation. Ref.4
	Mutagenesis	177 – 178	2	GL → EA: Enhances actin aggregation.
	Mutagenesis	460	1	D → N: Abrogates kinase activity. Ref.4
	Mutagenesis	496 – 506	11	Missing: Reduces actin aggregation. Ref.4
	Mutagenesis	503 – 505	3	RKK → GAA: Abolishes kinase activity. Ref.4
	Mutagenesis	508	1	T → A: Abolishes activation by ROCK1. Ref.4 Ref.7
	Mutagenesis	508	1	T → EE: Enhances kinase activity. Ref.4 Ref.7
	Mutagenesis	508	1	T → V or E: Reduces kinase activity. Ref.4 Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 3. Checksum: 9838BEFBE7006447	FASTA	647	72,585
	10 20 30 40 50 60 MRLTLLCCTW REERMGEEGS ELPVCASCGQ RIYDGQYLQA LNADWHADCF RCCDCSASLS 70 80 90 100 110 120 HQYYEKDGQL FCKKDYWARY GESCHGCSEQ ITKGLVMVAG ELKYHPECFI CLTCGTFIGD 130 140 150 160 170 180 GDTYTLVEHS KLYCGHCYYQ TVVTPVIEQI LPDSPGSHLP HTVTLVSIPA SSHGKRGLSV 190 200 210 220 230 240 SIDPPHGPPG CGTEHSHTVR VQGVDPGCMS PDVKNSIHVG DRILEINGTP IRNVPLDEID 250 260 270 280 290 300 LLIQETSRLL QLTLEHDPHD TLGHGLGPET SPLSSPAYTP SGEAGSSARQ KPVLRSCSID 310 320 330 340 350 360 RSPGAGSLGS PASQRKDLGR SESLRVVCRP HRIFRPSDLI HGEVLGKGCF GQAIKVTHRE 370 380 390 400 410 420 TGEVMVMKEL IRFDEETQRT FLKEVKVMRC LEHPNVLKFI GVLYKDKRLN FITEYIKGGT 430 440 450 460 470 480 LRGIIKSMDS QYPWSQRVSF AKDIASGMAY LHSMNIIHRD LNSHNCLVRE NKNVVVADFG 490 500 510 520 530 540 LARLMVDEKT QPEGLRSLKK PDRKKRYTVV GNPYWMAPEM INGRSYDEKV DVFSFGIVLC 550 560 570 580 590 600 EIIGRVNADP DYLPRTMDFG LNVRGFLDRY CPPNCPPSFF PITVRCCDLD PEKRPSFVKL 610 620 630 640 EHWLETLRMH LAGHLPLGPQ LEQLDRGFWE TYRRGESGLP AHPEVPD
	Isoform 2. Checksum: EAF0A3B93916D9FA	FASTA	633	70,793
	10 20 30 40 50 60 MGEEGSELPV CASCGQRIYD GQYLQALNAD WHADCFRCCD CSASLSHQYY EKDGQLFCKK 70 80 90 100 110 120 DYWARYGESC HGCSEQITKG LVMVAGELKY HPECFICLTC GTFIGDGDTY TLVEHSKLYC 130 140 150 160 170 180 GHCYYQTVVT PVIEQILPDS PGSHLPHTVT LVSIPASSHG KRGLSVSIDP PHGPPGCGTE 190 200 210 220 230 240 HSHTVRVQGV DPGCMSPDVK NSIHVGDRIL EINGTPIRNV PLDEIDLLIQ ETSRLLQLTL 250 260 270 280 290 300 EHDPHDTLGH GLGPETSPLS SPAYTPSGEA GSSARQKPVL RSCSIDRSPG AGSLGSPASQ 310 320 330 340 350 360 RKDLGRSESL RVVCRPHRIF RPSDLIHGEV LGKGCFGQAI KVTHRETGEV MVMKELIRFD 370 380 390 400 410 420 EETQRTFLKE VKVMRCLEHP NVLKFIGVLY KDKRLNFITE YIKGGTLRGI IKSMDSQYPW 430 440 450 460 470 480 SQRVSFAKDI ASGMAYLHSM NIIHRDLNSH NCLVRENKNV VVADFGLARL MVDEKTQPEG 490 500 510 520 530 540 LRSLKKPDRK KRYTVVGNPY WMAPEMINGR SYDEKVDVFS FGIVLCEIIG RVNADPDYLP 550 560 570 580 590 600 RTMDFGLNVR GFLDRYCPPN CPPSFFPITV RCCDLDPEKR PSFVKLEHWL ETLRMHLAGH 610 620 630 LPLGPQLEQL DRGFWETYRR GESGLPAHPE VPD
	Isoform 3. Checksum: 65FEF49849CCA142	FASTA	305	33,373
	10 20 30 40 50 60 MRLTLLCCTW REERMGEEGS ELPVCASCGQ RIYDGQYLQA LNADWHADCF RCCDCSASLS 70 80 90 100 110 120 HQYYEKDGQL FCKKDYWARY GESCHGCSEQ ITKGLVMVAG ELKYHPECFI CLTCGTFIGD 130 140 150 160 170 180 GDTYTLVEHS KLYCGHCYYQ TVVTPVIEQI LPDSPGSHLP HTVTLVSIPA SSHGKRGLSV 190 200 210 220 230 240 SIDPPHGPPG CGTEHSHTVR VQGVDPGCMS PDVKNSIHVG DRILEINGTP IRNVPLDEID 250 260 270 280 290 300 LLIQETSRLL QLTLEHDPHD TLGHGLGPET SPLSSPAYTP SGEAGSSARQ KPVFARTWVA LSPSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8183554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"LIM-kinase1 hemizygosity implicated in impaired visuospatial constructive cognition." Frangiskakis J.M., Ewart A.K., Morris C.A., Mervis C.B., Bertrand J., Robinson B.F., Klein B.P., Ensing G.J., Everett L.A., Green E.D., Proeschel C., Gutowski N.J., Noble M., Atkinson D.L., Odelberg S.J., Keating M.T. Cell 86:59-69(1996) [PubMed: 8689688] [Abstract] 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: 8812460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-580.
[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: 10196227] [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]	"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: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 10436159] [Abstract] Cited for: FUNCTION, INTERACTION WITH ROCK1.
[7]	"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: 10652353] [Abstract] Cited for: PHOSPHORYLATION AT THR-508, MUTAGENESIS OF THR-508, INTERACTION WITH ROCK1.
[8]	"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: 11832213] [Abstract] Cited for: FUNCTION.
[9]	"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: 12807904] [Abstract] Cited for: FUNCTION.
[10]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed: 14759258] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[11]	"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: 15660133] [Abstract] Cited for: FUNCTION, INTERACTION WITH SSH1, PHOSPHORYLATION AT THR-508, DEPHOSPHORYLATION.
[12]	"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: 16230460] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"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: 18028908] [Abstract] Cited for: INTERACTION WITH TPPP.
[14]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-310, MASS SPECTROMETRY.
[15]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; THR-229; SER-298; SER-310 AND SER-337, MASS SPECTROMETRY.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-307 AND SER-310, MASS SPECTROMETRY.
[17]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-310, MASS SPECTROMETRY.
[18]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; THR-229; THR-261; THR-270; SER-296; SER-298; SER-302; SER-307; SER-310 AND SER-313, MASS SPECTROMETRY.
[19]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-190; ASN-247 AND GLN-422.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. AC005056 Genomic DNA. No translation available. AC005057 Genomic DNA. Translation: AAS07438.1.
IPI	IPI00216433. IPI00216434. IPI00291702.
PIR	JP0078.
RefSeq	NP_002305.1.
UniGene	Hs.647035
3D structure databases
SMR	P53667. Positions 20-140, 154-277, 335-607, 339-640.
ModBase	Search...
Protein-protein interaction databases
IntAct	P53667. 5 interactions.
STRING	P53667.
PTM databases
PhosphoSite	P53667.
Proteomic databases
PRIDE	P53667.
Genome annotation databases
Ensembl	ENST00000336180; ENSP00000336740; ENSG00000106683; Homo sapiens. [Genome view]
GeneID	3984.
KEGG	hsa:3984.
UCSC	uc003uaa.1. human.
Organism-specific databases
CTD	3984.
GeneCards	GC07P073136.
H-InvDB	HIX0006762.
HGNC	HGNC:6613. LIMK1.
MIM	194050. phenotype. 601329. gene.
Orphanet	904. Williams syndrome.
PharmGKB	PA30386.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16629.
HOVERGEN	P53667.
InParanoid	P53667.
PhylomeDB	P53667.
Enzyme and pathway databases
BRENDA	2.7.11.1. 247.
Pathway_Interaction_DB	caspase_pathway. Caspase cascade in apoptosis.
Reactome	REACT_18266. Axon guidance.
Gene expression databases
ArrayExpress	P53667.
Bgee	P53667.
CleanEx	HS_LIMK1.
Genevestigator	P53667.
GermOnline	ENSG00000106683. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR001478. PDZ/DHR/GLGF. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001781. Znf_LIM. [Graphical view]
Gene3D	G3DSA:2.10.110.10. Znf_LIM. 1 hit.
Pfam	PF00412. LIM. 2 hits. PF00595. PDZ. 1 hit. [Graphical view]
SMART	SM00132. LIM. 2 hits. SM00228. PDZ. 1 hit. [Graphical view]
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. PS00108. PROTEIN_KINASE_ST. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	15626.
SOURCE	Search...

Entry information

Entry name

LIMK1_HUMAN

Accession

Primary (citable) accession number: P53667
Secondary accession number(s): O15283 , Q15820, Q15821, Q75MU3, Q9Y5Q1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 7, 2006
Last modified:	February 9, 2010
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.