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P53671 (LIMK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LIM domain kinase 2

Short name=LIMK-2
EC=2.7.11.1
Gene names
Name:LIMK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Protein existenceEvidence 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

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSP90AB1P082382EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 638638LIM domain kinase 2
PRO_0000075809

Regions

Domain12 – 6352LIM zinc-binding 1
Domain72 – 12453LIM zinc-binding 2
Domain152 – 23988PDZ
Domain331 – 608278Protein kinase
Nucleotide binding337 – 3459ATP By similarity

Sites

Active site4511 By similarity
Binding site3601ATP By similarity

Amino acid modifications

Modified residue2101Phosphothreonine Ref.13
Modified residue2931Phosphoserine Ref.13 Ref.14
Modified residue2981Phosphoserine Ref.14
Modified residue5051Phosphothreonine; by ROCK1 and CDC42BP Ref.11 Ref.12

Natural variations

Alternative sequence1 – 3737MSALA…WHGSC → MGSYLSVPAYFTSRDL in isoform LIMK2b and isoform 3.
VSP_012287
Alternative sequence592 – 63847PAFSK…RDSPP → APPGAAGEGPGCADDEGPVR RQGKVTIKYDPKELRKHLNL EEWILEQLTRLYDCQEEEIS ELEIDVDELLDMESDDAWAS RVKELLVDCYKPTEAFISGL LDKIRAMQKLSTPQKK in isoform 3.
VSP_043332
Natural variant351G → S. Ref.17
Corresponds to variant rs5997917 [ dbSNP | Ensembl ].
VAR_034069
Natural variant451D → N. Ref.17
Corresponds to variant rs35923988 [ dbSNP | Ensembl ].
VAR_042249
Natural variant2131R → C. Ref.17
Corresponds to variant rs34930775 [ dbSNP | Ensembl ].
VAR_042250
Natural variant2961P → R. Ref.17
Corresponds to variant rs34875793 [ dbSNP | Ensembl ].
VAR_042251
Natural variant3811R → H.
Corresponds to variant rs2229874 [ dbSNP | Ensembl ].
VAR_050149
Natural variant4181R → C. Ref.17
Corresponds to variant rs35422808 [ dbSNP | Ensembl ].
VAR_042252

Experimental info

Mutagenesis5051T → E: Increases kinase activity. Ref.11
Mutagenesis5051T → V: Abolishes cofilin phosphorylation and enhancement of stress fiber formation. Ref.11

Secondary structure

............ 638
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform LIMK2a [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: FB51813D99AFAC18

FASTA63872,232
        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 

« Hide

Isoform LIMK2b [UniParc].

Checksum: 07449F035F01562C
Show »

FASTA61769,904
Isoform 3 [UniParc].

Checksum: 5BEF0CE326A851B5
Show »

FASTA68677,886

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"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.
[17]"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. expand/collapse author list , 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.
PIRA59196.
RefSeqNP_001026971.1. NM_001031801.1.
NP_005560.1. NM_005569.3.
NP_057952.1. NM_016733.2.
UniGeneHs.474596.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X6ANMR-A62-129[»]
ProteinModelPortalP53671.
SMRP53671. Positions 12-132, 139-246, 276-623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110173. 10 interactions.
IntActP53671. 4 interactions.
MINTMINT-1190610.
STRING9606.ENSP00000339916.

Chemistry

BindingDBP53671.
ChEMBLCHEMBL5932.
GuidetoPHARMACOLOGY2055.

PTM databases

PhosphoSiteP53671.

Polymorphism databases

DMDM1708824.

Proteomic databases

PaxDbP53671.
PRIDEP53671.

Protocols and materials databases

DNASU3985.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331728; ENSP00000332687; ENSG00000182541. [P53671-1]
ENST00000333611; ENSP00000330470; ENSG00000182541. [P53671-2]
ENST00000340552; ENSP00000339916; ENSG00000182541. [P53671-3]
GeneID3985.
KEGGhsa:3985.
UCSCuc003akh.3. human. [P53671-1]
uc003akj.3. human. [P53671-3]
uc003akk.3. human. [P53671-2]

Organism-specific databases

CTD3985.
GeneCardsGC22P031608.
HGNCHGNC:6614. LIMK2.
HPACAB019313.
HPA008183.
HPA053882.
MIM601988. gene.
neXtProtNX_P53671.
PharmGKBPA30387.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000013121.
HOVERGENHBG052328.
KOK05744.
OMADARLSPH.
PhylomeDBP53671.
TreeFamTF318014.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressP53671.
BgeeP53671.
CleanExHS_LIMK2.
GenevestigatorP53671.

Family and domain databases

Gene3D2.10.110.10. 2 hits.
2.30.42.10. 1 hit.
InterProIPR011009. 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]
PfamPF00412. LIM. 2 hits.
PF00595. PDZ. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTSM00132. LIM. 2 hits.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00478. 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]
ProtoNetSearch...

Other

ChiTaRSLIMK2. human.
EvolutionaryTraceP53671.
GeneWikiLIMK2.
GenomeRNAi3985.
NextBio15630.
PROP53671.
SOURCESearch...

Entry information

Entry nameLIMK2_HUMAN
AccessionPrimary (citable) accession number: P53671
Secondary accession number(s): A8K6H5 expand/collapse secondary AC list , Q7KZ80, Q7L3H5, Q96E10, Q99464, Q9UFU0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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SIMILARITY comments

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PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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