LDB3_MOUSE - dbPTM
LDB3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LDB3_MOUSE
UniProt AC Q9JKS4
Protein Name LIM domain-binding protein 3
Gene Name Ldb3 {ECO:0000312|MGI:MGI:1344412}
Organism Mus musculus (Mouse).
Sequence Length 723
Subcellular Localization Cytoplasm, perinuclear region . Cell projection, pseudopodium . Cytoplasm, cytoskeleton . Cytoplasm, myofibril, sarcomere, Z line . Localized to the cytoplasm around nuclei and pseudopodia of undifferentiated cells and detected throughout the myotube
Protein Description May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton..
Protein Sequence MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPIQSPLPVIPHQKDPALDTNGSLATPSPSPEARASPGALEFGDTFSSSFSQTSVCSPLMEASGPVLPLGSPVAKASSEGAQGSVSPKVLPGPSQPRQYNNPIGLYSAETLREMAQMYQMSLRGKASGAGLLGGSLPVKDLAVDSASPVYQAVIKTQSKPEDEADEWARRSSNLQSRSFRILAQMTGTEYMQDPDEEALRRSSTPIEHAPVCTSQATSPLLPASAQSPAAASPIAASPTLATAAATHAAAASAAGPAASPVENPRPQASAYSPAAAASPAPSAHTSYSEGPAAPAPKPRVVTTASIRPSVYQPVPASSYSPSPGANYSPTPYTPSPAPAYTPSPAPTYTPSPAPTYSPSPAPAYTPSPAPNYTPTPSAAYSGGPSESASRPPWVTDDSFSQKFAPGKSTTTVSKQTLPRGAPAYNPTGPQVTPLARGTFQRAERFPASSRTPLCGHCNNVIRGPFLVAMGRSWHPEEFNCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPICAKCNTKIMGEVMHALRQTWHTTCFVCAACKKPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDKPLCKKHAHAINV
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
21UbiquitinationGFRLQGGKDFNMPLT
CEEECCCCCCCCCEE		67.0022790023
21 (in isoform 4)Ubiquitination-67.0022790023
28PhosphorylationKDFNMPLTISRITPG
CCCCCCEEEEEECCC		15.84-
30PhosphorylationFNMPLTISRITPGSK
CCCCEEEEEECCCCH		16.6427742792
41PhosphorylationPGSKAAQSQLSQGDL
CCCHHHHHHCCCCCE		28.50-
44PhosphorylationKAAQSQLSQGDLVVA
HHHHHHCCCCCEEEE		25.2019060867
71PhosphorylationEAQNKIKSASYNLSL
HHHHHHHHCEEEEEE		26.39-
73PhosphorylationQNKIKSASYNLSLTL
HHHHHHCEEEEEEEE		22.9628464351
74PhosphorylationNKIKSASYNLSLTLQ
HHHHHCEEEEEEEEC		21.6028576409
79PhosphorylationASYNLSLTLQKSKRP
CEEEEEEEECCCCCC		24.6228576409
83PhosphorylationLSLTLQKSKRPIPIS
EEEEECCCCCCCCCC		22.4227742792
84UbiquitinationSLTLQKSKRPIPIST
EEEECCCCCCCCCCC		70.0422790023
84 (in isoform 4)Ubiquitination-70.0422790023
90O-linked_GlycosylationSKRPIPISTTAPPIQ
CCCCCCCCCCCCCCC		17.8530016717
90PhosphorylationSKRPIPISTTAPPIQ
CCCCCCCCCCCCCCC		17.8527742792
91O-linked_GlycosylationKRPIPISTTAPPIQS
CCCCCCCCCCCCCCC		27.9130016717
91PhosphorylationKRPIPISTTAPPIQS
CCCCCCCCCCCCCCC		27.9127742792
92PhosphorylationRPIPISTTAPPIQSP
CCCCCCCCCCCCCCC		30.3127742792
98PhosphorylationTTAPPIQSPLPVIPH
CCCCCCCCCCCCCCC		29.1726824392
112 (in isoform 2)Phosphorylation-39.9925521595
112 (in isoform 4)Phosphorylation-39.9925521595
112 (in isoform 6)Phosphorylation-39.9925521595
113PhosphorylationQKDPALDTNGSLATP
CCCCCCCCCCCCCCC		42.1827742792
116PhosphorylationPALDTNGSLATPSPS
CCCCCCCCCCCCCCC		19.5327742792
118 (in isoform 2)Phosphorylation-21.1128464351
118 (in isoform 4)Phosphorylation-21.1128464351
118 (in isoform 6)Phosphorylation-21.1128464351
119PhosphorylationDTNGSLATPSPSPEA
CCCCCCCCCCCCHHH		29.5924899341
121PhosphorylationNGSLATPSPSPEARA
CCCCCCCCCCHHHHC		33.3926824392
123PhosphorylationSLATPSPSPEARASP
CCCCCCCCHHHHCCC		39.4426824392
128 (in isoform 4)Ubiquitination-27.42-
130 (in isoform 2)Phosphorylation-30.9628542873
130 (in isoform 4)Phosphorylation-30.9628542873
130 (in isoform 6)Phosphorylation-30.9628542873
133 (in isoform 2)Phosphorylation-7.5028464351
133 (in isoform 4)Phosphorylation-7.5028464351
133 (in isoform 6)Phosphorylation-7.5028464351
136 (in isoform 4)Ubiquitination-24.55-
141 (in isoform 4)Ubiquitination-31.07-
156 (in isoform 2)Phosphorylation-30.26-
156 (in isoform 4)Phosphorylation-30.26-
156 (in isoform 6)Phosphorylation-30.26-
170PhosphorylationGSPVAKASSEGAQGS
CCCCCCCCCCCCCCC		28.3727742792
171PhosphorylationSPVAKASSEGAQGSV
CCCCCCCCCCCCCCC		44.9326824392
177PhosphorylationSSEGAQGSVSPKVLP
CCCCCCCCCCCCCCC		13.8227742792
179PhosphorylationEGAQGSVSPKVLPGP
CCCCCCCCCCCCCCC		22.2425521595
181UbiquitinationAQGSVSPKVLPGPSQ
CCCCCCCCCCCCCCC		49.2322790023
181 (in isoform 3)Ubiquitination-49.2322790023
187PhosphorylationPKVLPGPSQPRQYNN
CCCCCCCCCCCCCCC		59.75-
199 (in isoform 2)Phosphorylation-10.7128464351
199 (in isoform 4)Phosphorylation-10.7128464351
199 (in isoform 6)Phosphorylation-10.7128464351
201 (in isoform 2)Phosphorylation-10.5528464351
201 (in isoform 4)Phosphorylation-10.5528464351
201 (in isoform 6)Phosphorylation-10.5528464351
209 (in isoform 4)Ubiquitination-29.79-
213 (in isoform 4)Ubiquitination-1.94-
214PhosphorylationMAQMYQMSLRGKASG
HHHHHHHHHCCCCCC		10.2119060867
216MethylationQMYQMSLRGKASGAG
HHHHHHHCCCCCCCC		36.9424129315
218UbiquitinationYQMSLRGKASGAGLL
HHHHHCCCCCCCCCC		32.7122790023
218 (in isoform 3)Ubiquitination-32.7122790023
220PhosphorylationMSLRGKASGAGLLGG
HHHCCCCCCCCCCCC		32.4427742792
238PhosphorylationVKDLAVDSASPVYQA
HHHHEECCCCHHHHH		24.8527742792
240PhosphorylationDLAVDSASPVYQAVI
HHEECCCCHHHHHHH		20.8927180971
243PhosphorylationVDSASPVYQAVIKTQ
ECCCCHHHHHHHHCC		8.3027742792
248UbiquitinationPVYQAVIKTQSKPED
HHHHHHHHCCCCCHH		33.6322790023
248 (in isoform 4)Ubiquitination-33.6322790023
249PhosphorylationVYQAVIKTQSKPEDE
HHHHHHHCCCCCHHH		27.2727742792
251PhosphorylationQAVIKTQSKPEDEAD
HHHHHCCCCCHHHHH		56.2427742792
252AcetylationAVIKTQSKPEDEADE
HHHHCCCCCHHHHHH		42.4821728379
252UbiquitinationAVIKTQSKPEDEADE
HHHHCCCCCHHHHHH		42.4822790023
252 (in isoform 4)Ubiquitination-42.4822790023
262 (in isoform 6)Phosphorylation-39.8427742792
264PhosphorylationADEWARRSSNLQSRS
HHHHHHHHHHHHHHH		20.3028542873
264 (in isoform 4)Phosphorylation-20.3028542873
265PhosphorylationDEWARRSSNLQSRSF
HHHHHHHHHHHHHHH		39.4828542873
266 (in isoform 6)Phosphorylation-43.2627742792
270 (in isoform 4)Phosphorylation-27.1827742792
277 (in isoform 4)O-linked_Glycosylation-26.9030016717
277 (in isoform 4)Phosphorylation-26.9027742792
279PhosphorylationFRILAQMTGTEYMQD
HHHHHHHHCCCCCCC		28.9519060867
280 (in isoform 4)O-linked_Glycosylation-15.9430016717
280 (in isoform 6)Phosphorylation-15.9428542873
287 (in isoform 6)Ubiquitination-33.74-
288 (in isoform 6)Phosphorylation-74.7327742792
291 (in isoform 4)Methylation-12.3424129315
296PhosphorylationEEALRRSSTPIEHAP
HHHHHHCCCCCCCCC		36.07-
301 (in isoform 5)Phosphorylation-35.7327742792
303 (in isoform 3)Phosphorylation-24.5128542873
305 (in isoform 5)Phosphorylation-2.7027742792
309 (in isoform 3)Phosphorylation-15.1527742792
316 (in isoform 3)Phosphorylation-19.9127742792
319 (in isoform 5)Phosphorylation-47.6728542873
326 (in isoform 5)Ubiquitination-18.60-
327 (in isoform 5)Phosphorylation-4.6627742792
330 (in isoform 3)Methylation-14.9224129315
406 (in isoform 4)Ubiquitination-19.17-
483MethylationGPSESASRPPWVTDD
CCCCCCCCCCCCCCC		40.8058858345
501PhosphorylationQKFAPGKSTTTVSKQ
CCCCCCCCCCEECCC		36.5828464351
507UbiquitinationKSTTTVSKQTLPRGA
CCCCEECCCCCCCCC		42.8622790023
507 (in isoform 4)Ubiquitination-42.8622790023
512MethylationVSKQTLPRGAPAYNP
ECCCCCCCCCCCCCC		57.9524129315
517PhosphorylationLPRGAPAYNPTGPQV
CCCCCCCCCCCCCCC		22.1825177544
525PhosphorylationNPTGPQVTPLARGTF
CCCCCCCCCCCCCCC		13.8225177544
529DimethylationPQVTPLARGTFQRAE
CCCCCCCCCCCHHHH		52.98-
529MethylationPQVTPLARGTFQRAE
CCCCCCCCCCCHHHH		52.9824129315
531PhosphorylationVTPLARGTFQRAERF
CCCCCCCCCHHHHCC		15.8425177544
534MethylationLARGTFQRAERFPAS
CCCCCCHHHHCCCCC		33.9416188487
612UbiquitinationICAKCNTKIMGEVMH
HHHHCCCHHHHHHHH		19.39-
653S-nitrosocysteineMEDGEPYCEKDYINL
CCCCCCCCCHHHEEE		8.40-
653S-nitrosylationMEDGEPYCEKDYINL
CCCCCCCCCHHHEEE		8.4021278135
657PhosphorylationEPYCEKDYINLFSTK
CCCCCHHHEEEECCC		11.6322210690
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
265SPhosphorylationKinasePKACAP05132
PSP
296SPhosphorylationKinasePKACAP05132
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LDB3_MOUSE !!
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 LDB3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTN2_MOUSEActn2physical
10391924
KPCA_MOUSEPrkcaphysical
10391924
KPCB_MOUSEPrkcbphysical
10391924
KPCG_MOUSEPrkcgphysical
10391924
KPCE_MOUSEPrkcephysical
10391924
KPCD_MOUSEPrkcdphysical
10391924
KPCZ_MOUSEPrkczphysical
10391924
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LDB3_MOUSE

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Related Literatures of Post-Translational Modification

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