MYO7A_MOUSE - dbPTM
MYO7A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO7A_MOUSE
UniProt AC P97479
Protein Name Unconventional myosin-VIIa
Gene Name Myo7a
Organism Mus musculus (Mouse).
Sequence Length 2215
Subcellular Localization Cytoplasm . Cytoplasm, cell cortex . Cytoplasm, cytoskeleton . In the photoreceptor cells, mainly localized in the inner and base of outer segments as well as in the synaptic ending region (By similarity).In retinal pigment epithelial cells colocaliz
Protein Description Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. In the retina, plays an important role in the renewal of the outer photoreceptor disks. Plays an important role in the distribution and migration of retinal pigment epithelial (RPE) melanosomes and phagosomes, and in the regulation of opsin transport in retinal photoreceptors. Mediates intracellular transport of RPE65 in the retina pigment epithelium. In the inner ear, plays an important role in differentiation, morphogenesis and organization of cochlear hair cell bundles. Motor protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing. Involved in hair-cell vesicle trafficking of aminoglycosides, which are known to induce ototoxicity..
Protein Sequence MVILQKGDYVWMDLKSGQEFDVPIGAVVKLCDSGQIQVVDDEDNEHWISPQNATHIKPMHPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERDKAITDRVILLQKVIRGFKDRSNFLRLKSAATLIQRHWRGHHCRKNYELIRLGFLRLQALHRSRKLHKQYRLARQRIIEFQARCRAYLVRKAFRHRLWAVITVQAYARGMIARRLHRRLRVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKARHEPINHSDMVDKMFGFLGTSGSLPGQEGQAPSGFEDLERGRREMVEEDVDAALPLPDEDEEDLSEYKFAKFAATYFQGTTTHSYTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPKYHTAMSDGSEKIPVMTKIYETLGKKTYKRELQALQGEGETQLPEGQKKTSVRHKLVHLTLKKKSKLTEEVTKRLNDGESTVQGNSMLEDRPTSNLEKLHFIIGNGILRPALRDEIYCQISKQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIHGGPPGYAPYCEERLRRTFVNGTRTQPPSWLELQATKSKKPIMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQERNAPWRLFFRKEVFTPWHNPSEDNVATNLIYQQVVRGVKFGEYRCEKEDDLAELASQQYFVDYGSEMILERLLSLVPTYIPDREITPLKNLEKWAQLAIAAHKKGIYAQRRTDSQKVKEDVVNYARFKWPLLFSRFYEAYKFSGPPLPKSDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSRECRVLLSLGCSDLGCATCQSGRAGLTPAGPCSPCWSCRGTKMMAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLRKRSKYVVALQDNPNPAGEESGFLSFAKGDLIILDHDTGEQVMNSGWANGINERTKQRGDFPTDCVYVMPTVTLPPREIVALVTMTPDQRQDVVRLLQLRTAEPEVRAKPYTLEEFSYDYFRPPPKHTLSRVMVSKARGKDRLWSHTREPLKQALLKKILGSEELSQEACMAFVAVLKYMGDYPSKRMRSVNELTDQIFEWALKAEPLKDEAYVQILKQLTDNHIRYSEERGWELLWLCTGLFPPSNILLPHVQRFLQSRKHCPLAIDCLQRLQKALRNGSRKYPPHLVEVEAIQHKTTQIFHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISVPENDFFFDFVRHLTDWIKKARPIKDGIVPSLTYQVFFMKKLWTTTVPGKDPMADSIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPKLLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPRTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKMDDLLTSYISQMLTAMSKQRNSRSGR
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
211PhosphorylationTIRNDNSSRFGKYID
EECCCCCCCCCEEEE		37.5726824392
216PhosphorylationNSSRFGKYIDIHFNK
CCCCCCEEEEEEECC		12.2828576409
311PhosphorylationAMKVLMFTDTENWEI
HHHHHHCCCCCCHHH		28.2228576409
572PhosphorylationFLEKNRDTLHGDIIQ
HHHHCCCCCCHHHHH		19.8821183079
583PhosphorylationDIIQLVHSSRNKFIK
HHHHHHHHCCHHHHH		24.4221183079
666MethylationSGMMETIRIRHAGYP
CCCHHEEEEEECCCC		27.5818961507
666DimethylationSGMMETIRIRHAGYP
CCCHHEEEEEECCCC		27.58-
668DimethylationMMETIRIRHAGYPIR
CHHEEEEEECCCCEE		12.07-
668MethylationMMETIRIRHAGYPIR
CHHEEEEEECCCCEE		12.0718961515
768UbiquitinationRSNFLRLKSAATLIQ
CHHHHHHHHHHHHHH		31.4522790023
952PhosphorylationKMFGFLGTSGSLPGQ
HHHHHCCCCCCCCCC		31.8725293948
953PhosphorylationMFGFLGTSGSLPGQE
HHHHCCCCCCCCCCC		25.2925293948
955PhosphorylationGFLGTSGSLPGQEGQ
HHCCCCCCCCCCCCC		31.0325293948
965PhosphorylationGQEGQAPSGFEDLER
CCCCCCCCCCCHHHH		60.1619131326
1075PhosphorylationIPVMTKIYETLGKKT
CCHHHHHHHHHCHHH		12.3825367039
1105PhosphorylationLPEGQKKTSVRHKLV
CCCCCCCHHHHHHHH		39.2224719451
1115PhosphorylationRHKLVHLTLKKKSKL
HHHHHHHHHHCCCCC		22.9626824392
1135PhosphorylationKRLNDGESTVQGNSM
HHHCCCCCCCCCCCC		39.1330635358
1136PhosphorylationRLNDGESTVQGNSML
HHCCCCCCCCCCCCC		16.7330635358
1263PhosphorylationKPIMLPVTFMDGTTK
CCEEEEEEECCCCCC		15.99-
1563PhosphorylationPCWSCRGTKMMAPSF
CCCCCCCCCCCCCCE		9.0921183079
1569PhosphorylationGTKMMAPSFTLATIK
CCCCCCCCEEEEEEC		22.7121183079
1571PhosphorylationKMMAPSFTLATIKGD
CCCCCCEEEEEECCC		21.5915654330
1664PhosphorylationKQRGDFPTDCVYVMP
HHCCCCCCCCEEEEE		41.8622345495
1668PhosphorylationDFPTDCVYVMPTVTL
CCCCCCEEEEECCCC		9.4322345495
1672PhosphorylationDCVYVMPTVTLPPRE
CCEEEEECCCCCHHH		14.1822345495
1674PhosphorylationVYVMPTVTLPPREIV
EEEEECCCCCHHHEE		35.7022345495
1685PhosphorylationREIVALVTMTPDQRQ
HHEEEEEECCHHHHH		19.0422345495
1687PhosphorylationIVALVTMTPDQRQDV
EEEEEECCHHHHHHH		17.8522345495
1939PhosphorylationASRLLLKSSEGFSLF
HHHHHHHCCCCCEEE		33.3230482847
2136PhosphorylationLLIAINKYGVSLIDP
EEEEHHHHCCCCCCC		20.4721183079
2139PhosphorylationAINKYGVSLIDPRTK
EHHHHCCCCCCCCCC		18.4221183079
2145PhosphorylationVSLIDPRTKDILTTH
CCCCCCCCCCEECCC		38.1621183079
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 MYO7A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO7A_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 MYO7A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PKHB1_MOUSEPlekhb1physical
15976448
PCD15_MOUSEPcdh15physical
16481439
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO7A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-965, AND MASSSPECTROMETRY.

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