LIMK1_DROME - dbPTM
LIMK1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIMK1_DROME
UniProt AC Q8IR79
Protein Name LIM domain kinase 1
Gene Name LIMK1
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1257
Subcellular Localization Cytoplasm. Cleavage furrow. Midbody. Localizes to the cleavage furrow and the midbody at cytokinesis.
Protein Description Protein kinase which regulates actin filament dynamics. Phosphorylates and inactivates the actin binding/depolymerizing factor tsr/cofilin, thereby stabilizing the actin cytoskeleton. Modulation of actin cytoskeleton dynamics may be essential for imaginal disk morphogenesis and axon guidance..
Protein Sequence MHHQQRLRANGGRGGTGLGAGSGPVSGGHSPLCAHCRGQLLPHPEEPIVMALGQQWHCDCFRCSVCEGHLHNWYFEREGLLYCREDYYGRFGDACQQCMAVITGPVMVAGEHKFHPECFCCTACGSFIGEGESYALVERSKLYCGQCYGKRSCQPADAKARITTAGKPMHSIRLVEIPKDATPGLRVDGVALDDGCPTVRITDLFCNFFLWLTSMAEQCCGAPYRIDVNLTNLHIGDRILEVNGTPVSDSSVEQIDKLIRSNEKMLQLTVEHDPVQVCRSCSQADIQRAMSASTLILPLSTSASSVEVGRERLYKTPGEQGTKARKLRQATNASTTIPPAAGATAMTQLKEKERCSSLSKLLDEQHQAQQHSAHPQLYDLSRTQSCRVVQKPQRIFRATDLVIGEKLGEGFFGKVFKVTHRQSGEVMVLKELHRADEEAQRNFIKEVAVLRLLDHRHVLKFIGVLYKDKKLHMVTEYVAGGCLKELIHDPAQVLPWPQRVRLARDIACGMSYLHSMNIIHRDLNSMNCLVREDRSVIVADFGLARSVDAPRLPSGNMTPGGYGSGANSDAPMSPSGTLRRSKSRQRRQRYTVVGNPYWMAPEMMKGLKYDEKVDVFSFGIMLCEIIGRVEADPDFMPRNSDFSLNQQEFREKFCAQCPEPFVKVAFVCCDLNPDMRPCFETLHVWLQRLADDLAADRVPPERLLHEIETFQEWYASSEDALSPTSQRSLNNLDELVKSAVDSEISPVEKEKENMVIKPQDIPKSPHLGKDFSPSGERLRDSMRARRRQRFLGAQEERRNLTPDTESKERALKKALKKCRPFGERGYLVDLRAGAELQLEDVRDLNTYSDVDSSCDTSLNYHDVNNLPAAQEDENTVKPGKEELLEESTNKPSNQESQHHRLAIDDMRTRLNQCRSKFEHLEEASRRNFNQSQHSMKNFFKTPPVALKMFQRLEHEAAALNGGNNCPPPPPRTQRINQTPIFGRKNPPVAIVGQKLQHAESLEDLASSGVAKQLATPAPKRSKATATTKGGQSSNPPLFLPPSLNISVALNSNGNVTTTTNTNSSCPPSASDWLPKKHKLTLPLPSAQQQRTSSNHRLPMCNNKGKTLKPLPSRTGSQGIPASNCVSPTRSSRPGSPTKHLAQRHTAATAQRLTNAAATHQQQHQQQSSKTTRLNILSPEKVHRLGARLTDQKQKMREEAAATASSVGGAGCAAGTAAGSLNGHRTIGSSGTPNSAVGERRRRAAPSPPVRTHFNTRC
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
282PhosphorylationVQVCRSCSQADIQRA
HHHHHCCCHHHHHHH		29.6521082442
728PhosphorylationLSPTSQRSLNNLDEL
CCCCCHHHHCCHHHH		28.0119429919
745PhosphorylationSAVDSEISPVEKEKE
HHHCCCCCCCHHHHH		20.8827794539
764PhosphorylationKPQDIPKSPHLGKDF
CCCCCCCCCCCCCCC		16.5221082442
801PhosphorylationQEERRNLTPDTESKE
HHHHHCCCCCHHHHH		23.7519429919
804PhosphorylationRRNLTPDTESKERAL
HHCCCCCHHHHHHHH		43.2819429919
806PhosphorylationNLTPDTESKERALKK
CCCCCHHHHHHHHHH		41.7419429919
978PhosphorylationRTQRINQTPIFGRKN
CCCCCCCCCCCCCCC		17.5425749252
1000PhosphorylationQKLQHAESLEDLASS
CCHHCHHHHHHHHHC		37.5321082442
1080PhosphorylationLPKKHKLTLPLPSAQ
CCCCCEEEECCCHHH		31.0022817900
1126PhosphorylationIPASNCVSPTRSSRP
CCHHHCCCCCCCCCC		23.8225749252
1135PhosphorylationTRSSRPGSPTKHLAQ
CCCCCCCCCCHHHHH		31.8919429919
1145PhosphorylationKHLAQRHTAATAQRL
HHHHHHHHHHHHHHH		21.8521082442
1177PhosphorylationTTRLNILSPEKVHRL
CCCCCCCCHHHHHHH		27.5019429919
1228PhosphorylationNGHRTIGSSGTPNSA
CCCCCCCCCCCCCCH		23.0322817900
1246PhosphorylationRRRRAAPSPPVRTHF
HHHHCCCCCCCCCCC		36.7925749252
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

Oops, there are no upstream regulatory protein records of LIMK1_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIMK1_DROME !!
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 LIMK1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP7D_DROMEHsc70-4physical
14605208
RL4_DROMERpL4physical
14605208
RING1_DROMEScephysical
14605208
PRD_DROMEprdphysical
14605208
TLD_DROMEtldphysical
14605208
IF4A_DROMEeIF-4aphysical
14605208
COF1_MOUSECfl1physical
11832213
RG190_DROMERhoGAPp190genetic
14972681
RG190_DROMERhoGAPp190genetic
15572110
CDC42_DROMECdc42genetic
15572110
SICK_DROMEsickgenetic
25411210
DIA_DROMEdiagenetic
14972681
DIA_DROMEdiagenetic
15572110
PKN_DROMEPkngenetic
14972681
RHO1_DROMERho1genetic
15572110
RHO1_DROMERho1genetic
14972681
CADF_DROMEtsrgenetic
15572110
CADF_DROMEtsrgenetic
16529736
SRF_DROMEbsgenetic
14972681
RAC1_DROMERac1genetic
15572110
RAC1_DROMERac1genetic
25411210
STUB_DROMESbgenetic
14972681
SSH_DROMEsshgenetic
25411210
SSH_DROMEsshgenetic
15572110
SIF2_DROMEsifgenetic
15572110
SIF1_DROMEsifgenetic
15572110
BRC1_DROMEbrgenetic
14972681
BRC4_DROMEbrgenetic
14972681
ORB2_DROMEorb2physical
24523662
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIMK1_DROME

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory