MYO5A_MOUSE - dbPTM
MYO5A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO5A_MOUSE
UniProt AC Q99104
Protein Name Unconventional myosin-Va
Gene Name Myo5a
Organism Mus musculus (Mouse).
Sequence Length 1853
Subcellular Localization
Protein Description Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation..
Protein Sequence MAASELYTKFARVWIPDPEEVWKSAELLKDYKPGDKVLLLHLEEGKDLEYRLDPKTGELPHLRNPDILVGENDLTALSYLHEPAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTRVPVKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKRYLCMQRAAITVQRYVRGYQARCYAKFLRRTKAATTIQKYWRMYVVRRRYKIRRAATIVIQSYLRGYLTRNRYRKILREYKAVIIQKRVRGWLARTHYKRTMKAIVYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMLNVPKPGHKRTDSTHSSNESEYTFSSEFAETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIPRKEKDFQGMLEYKREDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFIARV
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
2Acetylation------MAASELYTK
------CCHHHHHHH		30.88-
174UbiquitinationAGKTVSAKYAMRYFA
CCCCHHHHHHHHHHH		26.49-
210UbiquitinationMESIGNAKTTRNDNS
HHHHCCCCCCCCCCC		55.20-
218PhosphorylationTTRNDNSSRFGKYIE
CCCCCCCCCCEEEEE		37.5726824392
223PhosphorylationNSSRFGKYIEIGFDK
CCCCCEEEEEEECCC		12.2630387612
600PhosphorylationQDDEKAISPTSATSS
CCCCCCCCCCCCCCC		27.3025521595
602PhosphorylationDEKAISPTSATSSGR
CCCCCCCCCCCCCCC		24.9725521595
603PhosphorylationEKAISPTSATSSGRT
CCCCCCCCCCCCCCC		32.6925159016
605PhosphorylationAISPTSATSSGRTPL
CCCCCCCCCCCCCCC		24.1625159016
606PhosphorylationISPTSATSSGRTPLT
CCCCCCCCCCCCCCC		30.4325159016
607PhosphorylationSPTSATSSGRTPLTR
CCCCCCCCCCCCCCC		28.1225521595
689PhosphorylationRACGVLETIRISAAG
HHCCCCCEEEHHCCC		16.0521454597
902AcetylationCFRRMMAKRELKKLK
HHHHHHHHHHHHHCC		28.637681483
909AcetylationKRELKKLKIEARSVE
HHHHHHCCCCHHHHH		47.5930987007
919AcetylationARSVERYKKLHIGME
HHHHHHHHHHHHHHH		55.8930987013
941AcetylationRKVDEQNKDYKCLME
HHHHHCCHHHHHHHH		63.237631123
979UbiquitinationQLSEEEAKVATGRVL
HCCHHHHHHHHHHHH		35.36-
1032PhosphorylationSNLKEENTLLKQEKE
HHHHHHCHHHHHHHH		36.43-
1113PhosphorylationPKPGHKRTDSTHSSN
CCCCCCCCCCCCCCC		38.8219060867
1115PhosphorylationPGHKRTDSTHSSNES
CCCCCCCCCCCCCCC		27.6619060867
1116PhosphorylationGHKRTDSTHSSNESE
CCCCCCCCCCCCCCC		28.6919060867
1118PhosphorylationKRTDSTHSSNESEYT
CCCCCCCCCCCCCEE		34.6419060867
1119PhosphorylationRTDSTHSSNESEYTF
CCCCCCCCCCCCEEE		36.6929899451
1122PhosphorylationSTHSSNESEYTFSSE
CCCCCCCCCEEECCC		39.9019060867
1124PhosphorylationHSSNESEYTFSSEFA
CCCCCCCEEECCCCC		23.5119060867
1125PhosphorylationSSNESEYTFSSEFAE
CCCCCCEEECCCCCC		17.0019060867
1127PhosphorylationNESEYTFSSEFAETE
CCCCEEECCCCCCCC		22.5925777480
1128PhosphorylationESEYTFSSEFAETED
CCCEEECCCCCCCCC		32.3225777480
1133PhosphorylationFSSEFAETEDIAPRT
ECCCCCCCCCCCCCC		35.2125777480
1153PhosphorylationKKVPLDMSLFLKLQK
HCCCCCHHHHHHHHH		18.6829899451
1207UbiquitinationELEYESLKRQELESE
HHHHHHHHHHHHHHH		62.40-
1232UbiquitinationLRKALSEKSAPEVTA
HHHHHHHCCCCCCCC		48.84-
1263AcetylationSEELDVRKEEVLILR
CHHCCCCHHHHHHHH		59.062415589
1277UbiquitinationRSQLVSQKEAIQPKD
HHHHHCCHHCCCCCC		41.42-
1288PhosphorylationQPKDDKNTMTDSTIL
CCCCCCCCCCCCEEH		27.4729899451
1450PhosphorylationVGQMENISPGQIIDE
CCCCCCCCCCCCCCC		34.2625521595
1509PhosphorylationLIPGLPAYILFMCVR
CCCCCCHHHHHHHHH		9.0225619855
1648PhosphorylationPTGLRKRTSSIADEG
CCCCCHHCCCCCCCC		29.8425521595
1649PhosphorylationTGLRKRTSSIADEGT
CCCCHHCCCCCCCCC		24.6325521595
1650PhosphorylationGLRKRTSSIADEGTY
CCCHHCCCCCCCCCC		22.6025521595
1656PhosphorylationSSIADEGTYTLDSIL
CCCCCCCCCCHHHHH		15.9825159016
1657PhosphorylationSIADEGTYTLDSILR
CCCCCCCCCHHHHHH		19.0325159016
1658PhosphorylationIADEGTYTLDSILRQ
CCCCCCCCHHHHHHH		24.7525159016
1661PhosphorylationEGTYTLDSILRQLNS
CCCCCHHHHHHHHHC		27.0025159016
1668PhosphorylationSILRQLNSFHSVMCQ
HHHHHHHCHHHHHHH		32.6922802335
1671PhosphorylationRQLNSFHSVMCQHGM
HHHHCHHHHHHHCCC		14.9922802335
1758PhosphorylationLLQVKKKTDDDAEAI
HHHHHCCCCCCHHHH		54.24-
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
1650SPhosphorylationKinaseAKT2P31751
PSP
1650SPhosphorylationKinaseAKT2Q60823
PSP
1650SPhosphorylationKinaseCAMK2AP11798
PSP
1650SPhosphorylationKinaseCAMK2-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO5A_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 MYO5A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFL_MOUSENeflphysical
12403814
GFAP_MOUSEGfapphysical
12403814
DCP1_ARATHDCP1physical
24525673
DCP1_YEASTDCP1physical
24525673
DCP1A_HUMANDCP1Aphysical
24525673
DCP1B_HUMANDCP1Bphysical
24525673
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO5A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, AND MASSSPECTROMETRY.

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