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P53671

- LIMK2_HUMAN

UniProt

P53671 - LIMK2_HUMAN

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Protein

LIM domain kinase 2

Gene

LIMK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei360 – 3601ATPPROSITE-ProRule annotation
Active sitei451 – 4511By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi337 – 3459ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. phosphorylation Source: UniProtKB
  2. spermatogenesis Source: Ensembl
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

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_19277. Sema4D induced cell migration and growth-cone collapse.

Names & Taxonomyi

Protein namesi
Recommended name:
LIM domain kinase 2 (EC:2.7.11.1)
Short name:
LIMK-2
Gene namesi
Name:LIMK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:6614. LIMK2.

Subcellular locationi

Isoform LIMK2a : Cytoplasm. Nucleus
Note: Isoform LIMK2a is distributed in the cytoplasm and the nucleus.
Isoform LIMK2b : Cytoplasm. Nucleus
Note: Isoform LIMK2b occurs mainly in the cytoplasm and is scarcely translocated to the nucleus.

GO - Cellular componenti

  1. cis-Golgi network Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi505 – 5051T → E: Increases kinase activity. 1 Publication
Mutagenesisi505 – 5051T → V: Abolishes cofilin phosphorylation and enhancement of stress fiber formation. 1 Publication

Organism-specific databases

PharmGKBiPA30387.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 638638LIM domain kinase 2PRO_0000075809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101Phosphothreonine1 Publication
Modified residuei293 – 2931Phosphoserine2 Publications
Modified residuei298 – 2981Phosphoserine1 Publication
Modified residuei505 – 5051Phosphothreonine; by ROCK1 and CDC42BP2 Publications

Post-translational modificationi

Phosphorylated on serine and/or threonine residues by ROCK1.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53671.
PaxDbiP53671.
PRIDEiP53671.

PTM databases

PhosphoSiteiP53671.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP53671.
CleanExiHS_LIMK2.
ExpressionAtlasiP53671. baseline and differential.
GenevestigatoriP53671.

Organism-specific databases

HPAiCAB019313.
HPA008183.
HPA053882.

Interactioni

Subunit structurei

Binds ROCK1 and LKAP. Interacts with PARD3. Interacts with NISCH By similarity.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-1384350,EBI-352572

Protein-protein interaction databases

BioGridi110173. 11 interactions.
IntActiP53671. 5 interactions.
MINTiMINT-1190610.
STRINGi9606.ENSP00000339916.

Structurei

Secondary structure

1
638
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni73 – 753Combined sources
Turni99 – 1013Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi119 – 1213Combined sources
Helixi122 – 1298Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X6ANMR-A62-129[»]
ProteinModelPortaliP53671.
SMRiP53671. Positions 12-132, 139-246, 276-623.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53671.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 6352LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini72 – 12453LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini152 – 23988PDZPROSITE-ProRule annotationAdd
BLAST
Domaini331 – 608278Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

eggNOGiCOG0515.
GeneTreeiENSGT00530000063025.
HOGENOMiHOG000013121.
HOVERGENiHBG052328.
InParanoidiP53671.
KOiK05744.
OMAiDARLSPH.
PhylomeDBiP53671.
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]
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform LIMK2a (identifier: P53671-1) [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
MSALAGEDVW RCPGCGDHIA PSQIWYRTVN ETWHGSCFRC SECQDSLTNW
60 70 80 90 100
YYEKDGKLYC PKDYWGKFGE FCHGCSLLMT GPFMVAGEFK YHPECFACMS
110 120 130 140 150
CKVIIEDGDA YALVQHATLY CGKCHNEVVL APMFERLSTE SVQEQLPYSV
160 170 180 190 200
TLISMPATTE GRRGFSVSVE SACSNYATTV QVKEVNRMHI SPNNRNAIHP
210 220 230 240 250
GDRILEINGT PVRTLRVEEV EDAISQTSQT LQLLIEHDPV SQRLDQLRLE
260 270 280 290 300
ARLAPHMQNA GHPHALSTLD TKENLEGTLR RRSLRRSNSI SKSPGPSSPK
310 320 330 340 350
EPLLFSRDIS RSESLRCSSS YSQQIFRPCD LIHGEVLGKG FFGQAIKVTH
360 370 380 390 400
KATGKVMVMK ELIRCDEETQ KTFLTEVKVM RSLDHPNVLK FIGVLYKDKK
410 420 430 440 450
LNLLTEYIEG GTLKDFLRSM DPFPWQQKVR FAKGIASGMA YLHSMCIIHR
460 470 480 490 500
DLNSHNCLIK LDKTVVVADF GLSRLIVEER KRAPMEKATT KKRTLRKNDR
510 520 530 540 550
KKRYTVVGNP YWMAPEMLNG KSYDETVDIF SFGIVLCEII GQVYADPDCL
560 570 580 590 600
PRTLDFGLNV KLFWEKFVPT DCPPAFFPLA AICCRLEPES RPAFSKLEDS
610 620 630
FEALSLYLGE LGIPLPAELE ELDHTVSMQY GLTRDSPP
Length:638
Mass (Da):72,232
Last modified:October 1, 1996 - v1
Checksum:iFB51813D99AFAC18
GO
Isoform LIMK2b (identifier: P53671-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:617
Mass (Da):69,904
Checksum:i07449F035F01562C
GO
Isoform 3 (identifier: P53671-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:686
Mass (Da):77,886
Checksum:i5BEF0CE326A851B5
GO

Sequence cautioni

The sequence AAB54055.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351G → S.1 Publication
Corresponds to variant rs5997917 [ dbSNP | Ensembl ].
VAR_034069
Natural varianti45 – 451D → N.1 Publication
Corresponds to variant rs35923988 [ dbSNP | Ensembl ].
VAR_042249
Natural varianti213 – 2131R → C.1 Publication
Corresponds to variant rs34930775 [ dbSNP | Ensembl ].
VAR_042250
Natural varianti296 – 2961P → R.1 Publication
Corresponds to variant rs34875793 [ dbSNP | Ensembl ].
VAR_042251
Natural varianti381 – 3811R → H.
Corresponds to variant rs2229874 [ dbSNP | Ensembl ].
VAR_050149
Natural varianti418 – 4181R → C.1 Publication
Corresponds to variant rs35422808 [ dbSNP | Ensembl ].
VAR_042252

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3737MSALA…WHGSC → MGSYLSVPAYFTSRDL in isoform LIMK2b and isoform 3. 3 PublicationsVSP_012287Add
BLAST
Alternative sequencei592 – 63847PAFSK…RDSPP → APPGAAGEGPGCADDEGPVR RQGKVTIKYDPKELRKHLNL EEWILEQLTRLYDCQEEEIS ELEIDVDELLDMESDDAWAS RVKELLVDCYKPTEAFISGL LDKIRAMQKLSTPQKK in isoform 3. 1 PublicationVSP_043332Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13891.1. [P53671-1]
CCDS13892.1. [P53671-2]
CCDS33637.1. [P53671-3]
PIRiA59196.
RefSeqiNP_001026971.1. NM_001031801.1. [P53671-3]
NP_005560.1. NM_005569.3. [P53671-1]
NP_057952.1. NM_016733.2. [P53671-2]
UniGeneiHs.474596.

Genome annotation databases

EnsembliENST00000331728; ENSP00000332687; ENSG00000182541. [P53671-1]
ENST00000333611; ENSP00000330470; ENSG00000182541. [P53671-2]
ENST00000340552; ENSP00000339916; ENSG00000182541. [P53671-3]
GeneIDi3985.
KEGGihsa:3985.
UCSCiuc003akh.3. human. [P53671-1]
uc003akj.3. human. [P53671-3]
uc003akk.3. human. [P53671-2]

Polymorphism databases

DMDMi1708824.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13891.1. [P53671-1 ]
CCDS13892.1. [P53671-2 ]
CCDS33637.1. [P53671-3 ]
PIRi A59196.
RefSeqi NP_001026971.1. NM_001031801.1. [P53671-3 ]
NP_005560.1. NM_005569.3. [P53671-1 ]
NP_057952.1. NM_016733.2. [P53671-2 ]
UniGenei Hs.474596.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X6A NMR - A 62-129 [» ]
ProteinModelPortali P53671.
SMRi P53671. Positions 12-132, 139-246, 276-623.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110173. 11 interactions.
IntActi P53671. 5 interactions.
MINTi MINT-1190610.
STRINGi 9606.ENSP00000339916.

Chemistry

BindingDBi P53671.
ChEMBLi CHEMBL5932.
GuidetoPHARMACOLOGYi 2055.

PTM databases

PhosphoSitei P53671.

Polymorphism databases

DMDMi 1708824.

Proteomic databases

MaxQBi P53671.
PaxDbi P53671.
PRIDEi P53671.

Protocols and materials databases

DNASUi 3985.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331728 ; ENSP00000332687 ; ENSG00000182541 . [P53671-1 ]
ENST00000333611 ; ENSP00000330470 ; ENSG00000182541 . [P53671-2 ]
ENST00000340552 ; ENSP00000339916 ; ENSG00000182541 . [P53671-3 ]
GeneIDi 3985.
KEGGi hsa:3985.
UCSCi uc003akh.3. human. [P53671-1 ]
uc003akj.3. human. [P53671-3 ]
uc003akk.3. human. [P53671-2 ]

Organism-specific databases

CTDi 3985.
GeneCardsi GC22P031608.
HGNCi HGNC:6614. LIMK2.
HPAi CAB019313.
HPA008183.
HPA053882.
MIMi 601988. gene.
neXtProti NX_P53671.
PharmGKBi PA30387.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063025.
HOGENOMi HOG000013121.
HOVERGENi HBG052328.
InParanoidi P53671.
KOi K05744.
OMAi DARLSPH.
PhylomeDBi P53671.
TreeFami TF318014.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_19277. Sema4D induced cell migration and growth-cone collapse.

Miscellaneous databases

ChiTaRSi LIMK2. human.
EvolutionaryTracei P53671.
GeneWikii LIMK2.
GenomeRNAii 3985.
NextBioi 15630.
PROi P53671.
SOURCEi Search...

Gene expression databases

Bgeei P53671.
CleanExi HS_LIMK2.
ExpressionAtlasi P53671. baseline and differential.
Genevestigatori P53671.

Family and domain databases

Gene3Di 2.10.110.10. 2 hits.
2.30.42.10. 1 hit.
InterProi IPR011009. 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 ]
Pfami PF00412. LIM. 2 hits.
PF00595. PDZ. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
SMARTi SM00132. LIM. 2 hits.
SM00228. PDZ. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LIMK2B).
    Tissue: Uterus.
  4. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. 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.
    , 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.

Entry informationi

Entry nameiLIMK2_HUMAN
AccessioniPrimary (citable) accession number: P53671
Secondary accession number(s): A8K6H5
, Q7KZ80, Q7L3H5, Q96E10, Q99464, Q9UFU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 155 of the entry and version 1 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 22
    Human chromosome 22: 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

External Data

Dasty 3