MYO7A_HUMAN - dbPTM
MYO7A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO7A_HUMAN
UniProt AC Q13402
Protein Name Unconventional myosin-VIIa
Gene Name MYO7A
Organism Homo sapiens (Human).
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 (PubMed:8842737). In retinal pigment epithelial cells colocal
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. In the inner ear, plays an important role in differentiation, morphogenesis and organization of cochlear hair cell bundles. Involved in hair-cell vesicle trafficking of aminoglycosides, which are known to induce ototoxicity (By similarity). 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..
Protein Sequence MVILQQGDHVWMDLRLGQEFDVPIGAVVKLCDSGQVQVVDDEDNEHWISPQNATHIKPMHPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERDKAITDRVILLQKVIRGFKDRSNFLKLKNAATLIQRHWRGHNCRKNYGLMRLGFLRLQALHRSRKLHQQYRLARQRIIQFQARCRAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQRLRAEYLWRLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERARHEPVNHSDMVDKMFGFLGTSGGLPGQEGQAPSGFEDLERGRREMVEEDLDAALPLPDEDEEDLSEYKFAKFAATYFQGTTTHSYTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPKYHTAMSDGSEKIPVMTKIYETLGKKTYKRELQALQGEGEAQLPEGQKKSSVRHKLVHLTLKKKSKLTEEVTKRLHDGESTVQGNSMLEDRPTSNLEKLHFIIGNGILRPALRDEIYCQISKQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIHGGPPGYAPYCEERLRRTFVNGTRTQPPSWLELQATKSKKPIMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQERNAPWRLFFRKEVFTPWHSPSEDNVATNLIYQQVVRGVKFGEYRCEKEDDLAELASQQYFVDYGSEMILERLLNLVPTYIPDREITPLKTLEKWAQLAIAAHKKGIYAQRRTDAQKVKEDVVSYARFKWPLLFSRFYEAYKFSGPSLPKNDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSRECRVWLSLGCSDLGCAAPHSGWAGLTPAGPCSPCWSCRGAKTTAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLRKRSKYVVALQDNPNPAGEESGFLSFAKGDLIILDHDTGEQVMNSGWANGINERTKQRGDFPTDSVYVMPTVTMPPREIVALVTMTPDQRQDVVRLLQLRTAEPEVRAKPYTLEEFSYDYFRPPPKHTLSRVMVSKARGKDRLWSHTREPLKQALLKKLLGSEELSQEACLAFIAVLKYMGDYPSKRTRSVNELTDQIFEGPLKAEPLKDEAYVQILKQLTDNHIRYSEERGWELLWLCTGLFPPSNILLPHVQRFLQSRKHCPLAIDCLQRLQKALRNGSRKYPPHLVEVEAIQHKTTQIFHKVYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKVLSVPENDFFFDFVRHLTDWIKKARPIKDGIVPSLTYQVFFMKKLWTTTVPGKDPMADSIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPKLLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPKTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKMDDLLTSYISQMLTAMSKQRGSRSGK
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
122PhosphorylationSPEHIRQYTNKKIGE
CHHHHHHHCCCCCCC		11.4825072903
123PhosphorylationPEHIRQYTNKKIGEM
HHHHHHHCCCCCCCC		32.0225072903
165PhosphorylationGESGAGKTESTKLIL
CCCCCCCCHHHHHHH		33.96-
210PhosphorylationKTIRNDNSSRFGKYI
EEECCCCCCCCCEEE		26.2529514088
211PhosphorylationTIRNDNSSRFGKYID
EECCCCCCCCCEEEE		37.5729514088
235PhosphorylationEGAKIEQYLLEKSRV
CCHHHHHHHHHHHHH		10.64-
239UbiquitinationIEQYLLEKSRVCRQA
HHHHHHHHHHHHHHH		43.46-
252PhosphorylationQALDERNYHVFYCML
HHHHHCCCHHHHHHH		12.9425002506
256PhosphorylationERNYHVFYCMLEGMS
HCCCHHHHHHHCCCC		3.9425002506
263PhosphorylationYCMLEGMSEDQKKKL
HHHHCCCCHHHHHHC		49.2121082442
349PhosphorylationDACEVLFSPSLATAA
CHHHHHCCHHHHHHH		14.9322210691
357PhosphorylationPSLATAASLLEVNPP
HHHHHHHHHHCCCCH		30.9022210691
368PhosphorylationVNPPDLMSCLTSRTL
CCCHHHHHHHHCCCE		17.1722210691
607UbiquitinationGAETRKRSPTLSSQF
CCCHHCCCCCHHHHH		25.8522505724
646UbiquitinationNEFKKPMLFDRHLCV
CCCCCCCCCCHHHHH		5.6822505724
682UbiquitinationRYSFVEFVERYRVLL
EEEHHHHHHHHHHHC		2.31-
693UbiquitinationRVLLPGVKPAYKQGD
HHHCCCCCCHHHCCC		29.8222505724
723UbiquitinationHDDWQIGKTKIFLKD
CCCCCCCCEEEEECC		48.5522505724
772PhosphorylationLKLKNAATLIQRHWR
HHHHHHHHHHHHHHC		23.2228857561
945AcetylationNHSDMVDKMFGFLGT
CHHHHHHHHHHHHCC		25.397927317
1007PhosphorylationKFAKFAATYFQGTTT
HHHHHHHHHCCCCCC		22.8024043423
1008PhosphorylationFAKFAATYFQGTTTH
HHHHHHHHCCCCCCC		6.8124043423
1012PhosphorylationAATYFQGTTTHSYTR
HHHHCCCCCCCCCCC		20.1024043423
1013PhosphorylationATYFQGTTTHSYTRR
HHHCCCCCCCCCCCC		29.3624043423
1014PhosphorylationTYFQGTTTHSYTRRP
HHCCCCCCCCCCCCC		14.5224043423
1016PhosphorylationFQGTTTHSYTRRPLK
CCCCCCCCCCCCCCC		26.5524043423
1017PhosphorylationQGTTTHSYTRRPLKQ
CCCCCCCCCCCCCCC		9.1722468782
1018PhosphorylationGTTTHSYTRRPLKQP
CCCCCCCCCCCCCCC		24.1822468782
1075PhosphorylationIPVMTKIYETLGKKT
CCHHHHHHHHHCHHH		12.3829341593
1115PhosphorylationRHKLVHLTLKKKSKL
HHHHHHHHHHCCCCC		22.9624719451
1256UbiquitinationLQATKSKKPIMLPVT
EEECCCCCCEEEEEE		47.03-
1278PhosphorylationTLLTDSATTAKELCN
EECCCCHHHHHHHHH		31.10-
1480PhosphorylationFYEAYKFSGPSLPKN
HHHHHHCCCCCCCCC		45.7227251275
1483PhosphorylationAYKFSGPSLPKNDVI
HHHCCCCCCCCCCEE		61.9127251275
1569PhosphorylationGAKTTAPSFTLATIK
CCCCCCCCEEEEEEC		28.53-
1571PhosphorylationKTTAPSFTLATIKGD
CCCCCCEEEEEECCC		21.59-
1668PhosphorylationDFPTDSVYVMPTVTM
CCCCCCEEEEECCCC		9.43-
1685PhosphorylationREIVALVTMTPDQRQ
HHEEEEEECCHHHHH		19.0425404012
1687PhosphorylationIVALVTMTPDQRQDV
EEEEEECCHHHHHHH		17.8522817900
1780PhosphorylationAFIAVLKYMGDYPSK
HHHHHHHHHCCCCCC		11.36-
1784PhosphorylationVLKYMGDYPSKRTRS
HHHHHCCCCCCCCCC		12.04-
1786PhosphorylationKYMGDYPSKRTRSVN
HHHCCCCCCCCCCHH		28.65-
1789PhosphorylationGDYPSKRTRSVNELT
CCCCCCCCCCHHHHH		30.91-
1885PhosphorylationLRNGSRKYPPHLVEV
HHCCCCCCCCCEEEE		22.3820049867
1999PhosphorylationFFMKKLWTTTVPGKD
EEEHHHHCCCCCCCC		24.0326074081
2000PhosphorylationFMKKLWTTTVPGKDP
EEHHHHCCCCCCCCC		17.7626074081
2001PhosphorylationMKKLWTTTVPGKDPM
EHHHHCCCCCCCCCC		19.8226074081
2016PhosphorylationADSIFHYYQELPKYL
HHHHHHHHHHHHHHH		6.22-
2051PhosphorylationVKFEEDKSYFPSIPK
EECCCCHHHCCCHHH		44.3123663014
2052PhosphorylationKFEEDKSYFPSIPKL
ECCCCHHHCCCHHHH		25.8323663014
2055PhosphorylationEDKSYFPSIPKLLRE
CCHHHCCCHHHHHHH		41.4423663014
2097AcetylationGKSKEEAKLAFLKLI
CCCHHHHHHHHHHHH		43.568082843
2106AcetylationAFLKLIFKWPTFGSA
HHHHHHHHCCCCCCC		45.328082853
2145PhosphorylationVSLIDPKTKDILTTH
CCCCCCCCCCEECCC		39.06-
2199PhosphorylationDLLTSYISQMLTAMS
HHHHHHHHHHHHHHH		10.9922964224
2203PhosphorylationSYISQMLTAMSKQRG
HHHHHHHHHHHHHHC		18.2522964224
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO7A_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 MYO7A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAP0_HUMANPRKAR1Aphysical
10889203
VEZA_HUMANVEZTphysical
11080149
CTNA1_HUMANCTNNA1physical
11080149
CTNB1_HUMANCTNNB1physical
11080149
CADH1_HUMANCDH1physical
11080149
KEAP1_HUMANKEAP1physical
11921171
MTAP2_HUMANMAP2physical
11171103
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO7A_HUMAN

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Related Literatures of Post-Translational Modification

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