LIMK2_HUMAN - dbPTM
LIMK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIMK2_HUMAN
UniProt AC P53671
Protein Name LIM domain kinase 2
Gene Name LIMK2
Organism Homo sapiens (Human).
Sequence Length 638
Subcellular Localization Isoform LIMK2a: Cytoplasm. Nucleus. Isoform LIMK2a is distributed in the cytoplasm and the nucleus.
Isoform LIMK2b: Cytoplasm. Nucleus. Isoform LIMK2b occurs mainly in the cytoplasm and is scarcely translocated to the nucleus.
Protein Description Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro..
Protein Sequence MSALAGEDVWRCPGCGDHIAPSQIWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYWGKFGEFCHGCSLLMTGPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQEQLPYSVTLISMPATTEGRRGFSVSVESACSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAISQTSQTLQLLIEHDPVSQRLDQLRLEARLAPHMQNAGHPHALSTLDTKENLEGTLRRRSLRRSNSISKSPGPSSPKEPLLFSRDISRSESLRCSSSYSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALSLYLGELGIPLPAELEELDHTVSMQYGLTRDSPP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3 (in isoform 2)Phosphorylation-10.5123663014
3 (in isoform 3)Phosphorylation-10.5123663014
4 (in isoform 3)Phosphorylation-5.0223663014
4 (in isoform 2)Phosphorylation-5.0223663014
6 (in isoform 3)Phosphorylation-32.2723663014
6 (in isoform 2)Phosphorylation-32.2723663014
10 (in isoform 2)Phosphorylation-14.4223663014
10 (in isoform 3)Phosphorylation-14.4223663014
12 (in isoform 3)Phosphorylation-1.6723663014
12 (in isoform 2)Phosphorylation-1.6723663014
13 (in isoform 3)Phosphorylation-32.3223663014
13 (in isoform 2)Phosphorylation-32.3223663014
57UbiquitinationWYYEKDGKLYCPKDY
EEEEECCEEECCHHH		46.55-
59PhosphorylationYEKDGKLYCPKDYWG
EEECCEEECCHHHHH		15.3623612710
62UbiquitinationDGKLYCPKDYWGKFG
CCEEECCHHHHHCHH		60.95-
149PhosphorylationVQEQLPYSVTLISMP
HHHHCCCEEEEEECC		13.49-
151PhosphorylationEQLPYSVTLISMPAT
HHCCCEEEEEECCCC		16.66-
166PhosphorylationTEGRRGFSVSVESAC
CCCCCCEEEEHHHHH		19.12-
168PhosphorylationGRRGFSVSVESACSN
CCCCEEEEHHHHHCC		20.97-
179PhosphorylationACSNYATTVQVKEVN
HHCCCCEEEEEEEEC		10.77-
191PhosphorylationEVNRMHISPNNRNAI
EECCCCCCCCCCCCC		13.5917192257
210PhosphorylationRILEINGTPVRTLRV
CEEEECCEECEEEEH		17.7017192257
246PhosphorylationPVSQRLDQLRLEARL
HHHHHHHHHHHHHHH		32.8327251275
251 (in isoform 3)Ubiquitination-19.17-
257PhosphorylationEARLAPHMQNAGHPH
HHHHHHHHHHCCCCC		2.9827251275
266PhosphorylationNAGHPHALSTLDTKE
HCCCCCCCCCCCCHH		3.5024719451
267PhosphorylationAGHPHALSTLDTKEN
CCCCCCCCCCCCHHC		27.9227251275
268PhosphorylationGHPHALSTLDTKENL
CCCCCCCCCCCHHCH		29.5124719451
270PhosphorylationPHALSTLDTKENLEG
CCCCCCCCCHHCHHH		56.6824719451
271 (in isoform 3)Ubiquitination-43.29-
271PhosphorylationHALSTLDTKENLEGT
CCCCCCCCHHCHHHH		43.2920068231
272PhosphorylationALSTLDTKENLEGTL
CCCCCCCHHCHHHHH		44.2524719451
272UbiquitinationALSTLDTKENLEGTL
CCCCCCCHHCHHHHH		44.25-
276PhosphorylationLDTKENLEGTLRRRS
CCCHHCHHHHHHHHH		62.8124719451
278PhosphorylationTKENLEGTLRRRSLR
CHHCHHHHHHHHHHH		14.0227050516
279 (in isoform 3)Ubiquitination-6.20-
283PhosphorylationEGTLRRRSLRRSNSI
HHHHHHHHHHHCCCC		25.1515923181
287PhosphorylationRRRSLRRSNSISKSP
HHHHHHHCCCCCCCC		28.6123927012
289PhosphorylationRSLRRSNSISKSPGP
HHHHHCCCCCCCCCC		29.5023401153
291PhosphorylationLRRSNSISKSPGPSS
HHHCCCCCCCCCCCC		27.2323927012
292UbiquitinationRRSNSISKSPGPSSP
HHCCCCCCCCCCCCC		60.03-
293PhosphorylationRSNSISKSPGPSSPK
HCCCCCCCCCCCCCC		28.4423401153
297PhosphorylationISKSPGPSSPKEPLL
CCCCCCCCCCCCCCE		66.2523401153
298PhosphorylationSKSPGPSSPKEPLLF
CCCCCCCCCCCCCEE		43.0323927012
299PhosphorylationKSPGPSSPKEPLLFS
CCCCCCCCCCCCEEC		49.7427251275
300UbiquitinationSPGPSSPKEPLLFSR
CCCCCCCCCCCEECC		74.12-
306PhosphorylationPKEPLLFSRDISRSE
CCCCCEECCCCCCCC		29.0723403867
310PhosphorylationLLFSRDISRSESLRC
CEECCCCCCCCCCCC		33.7627251275
318PhosphorylationRSESLRCSSSYSQQI
CCCCCCCCCCCHHHH		18.8427251275
319PhosphorylationSESLRCSSSYSQQIF
CCCCCCCCCCHHHHC		36.6027251275
320PhosphorylationESLRCSSSYSQQIFR
CCCCCCCCCHHHHCC		16.7127251275
322PhosphorylationLRCSSSYSQQIFRPC
CCCCCCCHHHHCCCC		19.9827251275
326 (in isoform 3)Ubiquitination-6.57-
334 (in isoform 3)Ubiquitination-21.51-
339 (in isoform 3)Ubiquitination-48.67-
347UbiquitinationGFFGQAIKVTHKATG
CCCCEEEEEEECCCC		44.06-
350 (in isoform 3)Ubiquitination-22.27-
355AcetylationVTHKATGKVMVMKEL
EEECCCCCEEEEHHH		23.8511790769
355UbiquitinationVTHKATGKVMVMKEL
EEECCCCCEEEEHHH		23.85-
357 (in isoform 3)Ubiquitination-2.51-
360UbiquitinationTGKVMVMKELIRCDE
CCCEEEEHHHCCCCH		37.65-
371UbiquitinationRCDEETQKTFLTEVK
CCCHHHHHHHHHHHH		48.98-
372O-linked_GlycosylationCDEETQKTFLTEVKV
CCHHHHHHHHHHHHH		17.66OGP
378UbiquitinationKTFLTEVKVMRSLDH
HHHHHHHHHHHHCCC		24.87-
378 (in isoform 3)Ubiquitination-24.87-
407 (in isoform 3)Ubiquitination-10.07-
414UbiquitinationYIEGGTLKDFLRSMD
HCCCCCHHHHHHCCC		46.39-
428UbiquitinationDPFPWQQKVRFAKGI
CCCCHHHHHHHHHHH		21.93-
487UbiquitinationRKRAPMEKATTKKRT
HHHCCHHHCCCCCCC		44.79-
494PhosphorylationKATTKKRTLRKNDRK
HCCCCCCCCCCCCCC		39.53-
504PhosphorylationKNDRKKRYTVVGNPY
CCCCCCCEEEECCCC		16.8628122231
505PhosphorylationNDRKKRYTVVGNPYW
CCCCCCEEEECCCCC		16.8519099536
526PhosphorylationNGKSYDETVDIFSFG
CCCCCCCHHHHHHHH		22.1511018042
681Phosphorylation--------------------------------------------------
--------------------------------------------------		27251275
681 (in isoform 3)Phosphorylation--
682 (in isoform 3)Phosphorylation-28985074
682Phosphorylation---------------------------------------------------
---------------------------------------------------		24719451
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
283SPhosphorylationKinaseAURKAO14965
GPS
283SPhosphorylationKinasePRKCDQ05655
GPS
494TPhosphorylationKinaseAURKAO14965
GPS
505TPhosphorylationKinaseAURKAO14965
GPS
505TPhosphorylationKinaseCDC42BPAQ5VT25
GPS
505TPhosphorylationKinaseCDC42BPQ9Y5S2
Uniprot
505TPhosphorylationKinaseROCK1Q13464
Uniprot
505TPhosphorylationKinaseROCK2O75116
PSP
505TPhosphorylationKinaseMRCK-SUBFAMILY-GPS
505TPhosphorylationKinaseROCK-SUBFAMILY-GPS
505TPhosphorylationKinaseROCK_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIMK2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LIMK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H11_HUMANHIST1H1Aphysical
8537403
MBP_HUMANMBPphysical
8537403
HS90A_HUMANHSP90AA1physical
22939624
AT1A1_HUMANATP1A1physical
25852190
BAG2_HUMANBAG2physical
25852190
CALU_HUMANCALUphysical
25852190
CDK4_HUMANCDK4physical
25852190
DNJA1_HUMANDNAJA1physical
25852190
DNJA2_HUMANDNAJA2physical
25852190
EF2_HUMANEEF2physical
25852190
EMD_HUMANEMDphysical
25852190
FKBP5_HUMANFKBP5physical
25852190
ENPL_HUMANHSP90B1physical
25852190
HSPB1_HUMANHSPB1physical
25852190
LMNA_HUMANLMNAphysical
25852190
RCN1_HUMANRCN1physical
25852190
RCN2_HUMANRCN2physical
25852190
RUVB2_HUMANRUVBL2physical
25852190
TXTP_HUMANSLC25A1physical
25852190
CMC2_HUMANSLC25A13physical
25852190
GHC1_HUMANSLC25A22physical
25852190
TBA4A_HUMANTUBA4Aphysical
25852190
USMG5_HUMANUSMG5physical
25852190
LIMK2_HUMANLIMK2physical
9089416
LIMK1_HUMANLIMK1physical
9089416
HNRLL_HUMANHNRNPLLphysical
28514442
TTC1_HUMANTTC1physical
28514442
UBB_HUMANUBBphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIMK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287; SER-291; SER-293;SER-297 AND SER-298, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287; SER-289; SER-293AND SER-298, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; THR-210; SER-293AND SER-298, AND MASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-291 ANDSER-293, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION AT THR-505 BY CDC42BP.
"Specific activation of LIM kinase 2 via phosphorylation of threonine505 by ROCK, a Rho-dependent protein kinase.";
Sumi T., Matsumoto K., Nakamura T.;
J. Biol. Chem. 276:670-676(2001).
Cited for: PHOSPHORYLATION AT THR-505, MUTAGENESIS OF THR-505, FUNCTION, ANDINTERACTION WITH ROCK1.

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