P53671 (LIMK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
LIM domain kinase 2
Short name=LIMK-2
EC=2.7.11.1

Gene names

Name:

LIMK2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. Ref.10 Ref.11
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Binds ROCK1 and LKAP. Interacts with PARD3. Interacts with NISCH By similarity. Ref.9 Ref.10 Ref.11 Ref.13
Subcellular location	Isoform LIMK2a: Cytoplasm. Nucleus. Note: Isoform LIMK2a is distributed in the cytoplasm and the nucleus. Ref.2 Isoform LIMK2b: Cytoplasm. Nucleus. Note: Isoform LIMK2b occurs mainly in the cytoplasm and is scarcely translocated to the nucleus. Ref.2
Tissue specificity	Highest expression in the placenta; moderate level in liver, lung, kidney, and pancreas. LIMK2a is found to be more abundant then LIMK2b in liver, colon, stomach, and spleen, while in brain, kidney, and placenta LIMK2b is the dominant form. In adult lung, both LIMK2a and LIMK2b is nearly equally observed. Ref.2
Post-translational modification	Phosphorylated on serine and/or threonine residues by ROCK1. Ref.11 Ref.12
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.
Sequence caution	The sequence AAB54055.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	LIM domain Repeat
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	cis-Golgi network Inferred from electronic annotation. Source: Compara cytoplasm Traceable author statement Ref.1Ref.2. Source: UniProtKB nucleus Traceable author statement Ref.2. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Traceable author statement Ref.1. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-1384350,EBI-352572

Alternative products

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

Isoform LIMK2a (identifier: P53671-1)

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 LIMK2b (identifier: P53671-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MSALAGEDVWRCPGCGDHIAPSQIWYRTVNETWHGSC → MGSYLSVPAYFTSRDL

Isoform 3 (identifier: P53671-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MSALAGEDVWRCPGCGDHIAPSQIWYRTVNETWHGSC → MGSYLSVPAYFTSRDL
     592-638: PAFSKLEDSF...QYGLTRDSPP → APPGAAGEGP...MQKLSTPQKK

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 638

638

LIM domain kinase 2

PRO_0000075809

Regions

Domain

12 – 63

52

LIM zinc-binding 1

Domain

72 – 124

53

LIM zinc-binding 2

Domain

152 – 239

88

PDZ

Domain

331 – 608

278

Protein kinase

Nucleotide binding

337 – 345

9

ATP By similarity

Sites

Active site

451

1

By similarity

Binding site

360

1

ATP By similarity

Amino acid modifications

Modified residue

210

1

Phosphothreonine Ref.14

Modified residue

293

1

Phosphoserine Ref.14 Ref.15

Modified residue

298

1

Phosphoserine Ref.15

Modified residue

505

1

Phosphothreonine; by ROCK1 and CDC42BP Ref.11 Ref.12

Natural variations

Alternative sequence

1 – 37

37

MSALA…WHGSC → MGSYLSVPAYFTSRDL in isoform LIMK2b and isoform 3.

VSP_012287

Alternative sequence

592 – 638

47

PAFSK…RDSPP → APPGAAGEGPGCADDEGPVR RQGKVTIKYDPKELRKHLNL EEWILEQLTRLYDCQEEEIS ELEIDVDELLDMESDDAWAS RVKELLVDCYKPTEAFISGL LDKIRAMQKLSTPQKK in isoform 3.

VSP_043332

Natural variant

35

1

G → S. Ref.18
Corresponds to variant rs5997917 [ dbSNP | Ensembl ].

VAR_034069

Natural variant

45

1

D → N. Ref.18
Corresponds to variant rs35923988 [ dbSNP | Ensembl ].

VAR_042249

Natural variant

213

1

R → C. Ref.18
Corresponds to variant rs34930775 [ dbSNP | Ensembl ].

VAR_042250

Natural variant

296

1

P → R. Ref.18
Corresponds to variant rs34875793 [ dbSNP | Ensembl ].

VAR_042251

Natural variant

381

1

R → H.
Corresponds to variant rs2229874 [ dbSNP | Ensembl ].

VAR_050149

Natural variant

418

1

R → C. Ref.18
Corresponds to variant rs35422808 [ dbSNP | Ensembl ].

VAR_042252

Experimental info

Mutagenesis

505

1

T → E: Increases kinase activity. Ref.11

Mutagenesis

505

1

T → V: Abolishes cofilin phosphorylation and enhancement of stress fiber formation. Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

638

Helix Strand Turn

Details...

Turn

73 – 75

3

Turn

99 – 101

3

Beta strand

111 – 113

3

Beta strand

115 – 117

3

Beta strand

119 – 121

3

Helix

122 – 129

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform LIMK2a [UniParc]. Last modified October 1, 1996. Version 1. Checksum: FB51813D99AFAC18	FASTA	638	72,232
	10 20 30 40 50 60 MSALAGEDVW RCPGCGDHIA PSQIWYRTVN ETWHGSCFRC SECQDSLTNW YYEKDGKLYC 70 80 90 100 110 120 PKDYWGKFGE FCHGCSLLMT GPFMVAGEFK YHPECFACMS CKVIIEDGDA YALVQHATLY 130 140 150 160 170 180 CGKCHNEVVL APMFERLSTE SVQEQLPYSV TLISMPATTE GRRGFSVSVE SACSNYATTV 190 200 210 220 230 240 QVKEVNRMHI SPNNRNAIHP GDRILEINGT PVRTLRVEEV EDAISQTSQT LQLLIEHDPV 250 260 270 280 290 300 SQRLDQLRLE ARLAPHMQNA GHPHALSTLD TKENLEGTLR RRSLRRSNSI SKSPGPSSPK 310 320 330 340 350 360 EPLLFSRDIS RSESLRCSSS YSQQIFRPCD LIHGEVLGKG FFGQAIKVTH KATGKVMVMK 370 380 390 400 410 420 ELIRCDEETQ KTFLTEVKVM RSLDHPNVLK FIGVLYKDKK LNLLTEYIEG GTLKDFLRSM 430 440 450 460 470 480 DPFPWQQKVR FAKGIASGMA YLHSMCIIHR DLNSHNCLIK LDKTVVVADF GLSRLIVEER 490 500 510 520 530 540 KRAPMEKATT KKRTLRKNDR KKRYTVVGNP YWMAPEMLNG KSYDETVDIF SFGIVLCEII 550 560 570 580 590 600 GQVYADPDCL PRTLDFGLNV KLFWEKFVPT DCPPAFFPLA AICCRLEPES RPAFSKLEDS 610 620 630 FEALSLYLGE LGIPLPAELE ELDHTVSMQY GLTRDSPP
	Isoform LIMK2b [UniParc]. Checksum: 07449F035F01562C	FASTA	617	69,904
	10 20 30 40 50 60 MGSYLSVPAY FTSRDLFRCS ECQDSLTNWY YEKDGKLYCP KDYWGKFGEF CHGCSLLMTG 70 80 90 100 110 120 PFMVAGEFKY HPECFACMSC KVIIEDGDAY ALVQHATLYC GKCHNEVVLA PMFERLSTES 130 140 150 160 170 180 VQEQLPYSVT LISMPATTEG RRGFSVSVES ACSNYATTVQ VKEVNRMHIS PNNRNAIHPG 190 200 210 220 230 240 DRILEINGTP VRTLRVEEVE DAISQTSQTL QLLIEHDPVS QRLDQLRLEA RLAPHMQNAG 250 260 270 280 290 300 HPHALSTLDT KENLEGTLRR RSLRRSNSIS KSPGPSSPKE PLLFSRDISR SESLRCSSSY 310 320 330 340 350 360 SQQIFRPCDL IHGEVLGKGF FGQAIKVTHK ATGKVMVMKE LIRCDEETQK TFLTEVKVMR 370 380 390 400 410 420 SLDHPNVLKF IGVLYKDKKL NLLTEYIEGG TLKDFLRSMD PFPWQQKVRF AKGIASGMAY 430 440 450 460 470 480 LHSMCIIHRD LNSHNCLIKL DKTVVVADFG LSRLIVEERK RAPMEKATTK KRTLRKNDRK 490 500 510 520 530 540 KRYTVVGNPY WMAPEMLNGK SYDETVDIFS FGIVLCEIIG QVYADPDCLP RTLDFGLNVK 550 560 570 580 590 600 LFWEKFVPTD CPPAFFPLAA ICCRLEPESR PAFSKLEDSF EALSLYLGEL GIPLPAELEE 610 LDHTVSMQYG LTRDSPP
	Isoform 3 [UniParc]. Checksum: 5BEF0CE326A851B5	FASTA	686	77,886
	10 20 30 40 50 60 MGSYLSVPAY FTSRDLFRCS ECQDSLTNWY YEKDGKLYCP KDYWGKFGEF CHGCSLLMTG 70 80 90 100 110 120 PFMVAGEFKY HPECFACMSC KVIIEDGDAY ALVQHATLYC GKCHNEVVLA PMFERLSTES 130 140 150 160 170 180 VQEQLPYSVT LISMPATTEG RRGFSVSVES ACSNYATTVQ VKEVNRMHIS PNNRNAIHPG 190 200 210 220 230 240 DRILEINGTP VRTLRVEEVE DAISQTSQTL QLLIEHDPVS QRLDQLRLEA RLAPHMQNAG 250 260 270 280 290 300 HPHALSTLDT KENLEGTLRR RSLRRSNSIS KSPGPSSPKE PLLFSRDISR SESLRCSSSY 310 320 330 340 350 360 SQQIFRPCDL IHGEVLGKGF FGQAIKVTHK ATGKVMVMKE LIRCDEETQK TFLTEVKVMR 370 380 390 400 410 420 SLDHPNVLKF IGVLYKDKKL NLLTEYIEGG TLKDFLRSMD PFPWQQKVRF AKGIASGMAY 430 440 450 460 470 480 LHSMCIIHRD LNSHNCLIKL DKTVVVADFG LSRLIVEERK RAPMEKATTK KRTLRKNDRK 490 500 510 520 530 540 KRYTVVGNPY WMAPEMLNGK SYDETVDIFS FGIVLCEIIG QVYADPDCLP RTLDFGLNVK 550 560 570 580 590 600 LFWEKFVPTD CPPAFFPLAA ICCRLEPESR APPGAAGEGP GCADDEGPVR RQGKVTIKYD 610 620 630 640 650 660 PKELRKHLNL EEWILEQLTR LYDCQEEEIS ELEIDVDELL DMESDDAWAS RVKELLVDCY 670 680 KPTEAFISGL LDKIRAMQKL STPQKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs." Okano I., Hiraoka J., Otera H., Nunoue K., Ohashi K., Iwashita S., Hirai M., Mizuno K. J. Biol. Chem. 270:31321-31330(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LIMK2A). Tissue: Hepatoma.
[2]	"Subcellular localization and protein interaction of the human LIMK2 gene expressing alternative transcripts with tissue-specific regulation." Osada H., Hasada K., Inazawa J., Uchida K., Ueda R., Takahashi T., Takahashi T. Biochem. Biophys. Res. Commun. 229:582-589(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LIMK2A AND LIMK2B), SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Lung.
[3]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LIMK2B). Tissue: Uterus.
[4]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LIMK2A).
[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 LIMK2A). Tissue: Placenta.
[6]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Ovary.
[9]	"Molecular cloning and characterization of novel large protein, limkain b1, which associates with the LIM-kinase 2." Miyamoto K., Nakamura T., Shirakawa K., Matsumoto K. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: INTERACTION WITH LKAP.
[10]	"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.
[11]	"Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase." Sumi T., Matsumoto K., Nakamura T. J. Biol. Chem. 276:670-676(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-505, MUTAGENESIS OF THR-505, FUNCTION, INTERACTION WITH ROCK1.
[12]	"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 AT THR-505 BY CDC42BP.
[13]	"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARD3. Tissue: Embryonic kidney.
[14]	"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 THR-210 AND SER-293, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-298, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"Solution structures of the second LIM domain of human LIM-kinase 2 (LIMK2)." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 62-129.
[18]	"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] SER-35; ASN-45; CYS-213; ARG-296 AND CYS-418.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D45906 mRNA. Translation: BAA08312.1.
D85527 mRNA. Translation: BAA12827.1.
AL117466 mRNA. Translation: CAB55941.1.
CR456513 mRNA. Translation: CAG30399.1.
AK291640 mRNA. Translation: BAF84329.1.
AC002073 Genomic DNA. Translation: AAB54055.1. Sequence problems.
AC002073 Genomic DNA. Translation: AAB54056.1.
CH471095 Genomic DNA. Translation: EAW59954.1.
CH471095 Genomic DNA. Translation: EAW59956.1.
CH471095 Genomic DNA. Translation: EAW59958.1.
BC013051 mRNA. Translation: AAH13051.1.

IPI

IPI00022872.
IPI00025698.
IPI00100853.

PIR

A59196.

RefSeq

NP_001026971.1. NM_001031801.1.
NP_005560.1. NM_005569.3.
NP_057952.1. NM_016733.2.

UniGene

Hs.474596.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X6A	NMR	-	A	62-129	[»]

ProteinModelPortal

P53671.

ModBase

Search...

Protein-protein interaction databases

IntAct

P53671. 2 interactions.

MINT

MINT-1190610.

STRING

9606.ENSP00000339916.

PTM databases

PhosphoSite

P53671.

Polymorphism databases

DMDM

1708824.

Proteomic databases

PaxDb

P53671.

PRIDE

P53671.

Protocols and materials databases

DNASU

3985.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000331728; ENSP00000332687; ENSG00000182541.
ENST00000333611; ENSP00000330470; ENSG00000182541.
ENST00000340552; ENSP00000339916; ENSG00000182541.

GeneID

3985.

KEGG

hsa:3985.

UCSC

uc003akh.3. human.
uc003akj.3. human.
uc003akk.3. human.

Organism-specific databases

CTD

3985.

GeneCards

GC22P031608.

HGNC

HGNC:6614. LIMK2.

HPA

CAB019313.
HPA008183.

MIM

601988. gene.

neXtProt

NX_P53671.

PharmGKB

PA30387.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000013121.

HOVERGEN

HBG052328.

KO

K05744.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

P53671.

Bgee

P53671.

CleanEx

HS_LIMK2.

Genevestigator

P53671.

GermOnline

ENSG00000182541. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 2 hits.

InterPro

IPR011009. Kinase-like_dom.
IPR001478. PDZ.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 2 hits.
PF00595. PDZ. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

SMART

SM00132. LIM. 2 hits.
SM00228. PDZ. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50156. PDZ. 1 hit.

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

BindingDB

P53671.

ChEMBL

CHEMBL5932.

ChiTaRS

LIMK2. human.

EvolutionaryTrace

P53671.

GenomeRNAi

3985.

NextBio

15630.

SOURCE

Search...

Entry information

Entry name

LIMK2_HUMAN

Accession

Primary (citable) accession number: P53671
Secondary accession number(s): A8K6H5 , Q7KZ80, Q7L3H5, Q96E10, Q99464, Q9UFU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 141 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.