MYO1D_HUMAN - dbPTM
MYO1D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO1D_HUMAN
UniProt AC O94832
Protein Name Unconventional myosin-Id
Gene Name MYO1D
Organism Homo sapiens (Human).
Sequence Length 1006
Subcellular Localization
Protein Description Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity)..
Protein Sequence MAEQESLEFGKADFVLMDTVSMPEFMANLRLRFEKGRIYTFIGEVVVSVNPYKLLNIYGRDTIEQYKGRELYERPPHLFAIADAAYKAMKRRSKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIVQQPGERSFHSFYQLLQGGSEQMLRSLHLQKSLSSYNYIHVGAQLKSSINDAAEFRVVADAMKVIGFKPEEIQTVYKILAAILHLGNLKFVVDGDTPLIENGKVVSIIAELLSTKTDMVEKALLYRTVATGRDIIDKQHTEQEASYGRDAFAKAIYERLFCWIVTRINDIIEVKNYDTTIHGKNTVIGVLDIYGFEIFDNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIIAILDDACMNVGKVTDEMFLEALNSKLGKHAHFSSRKLCASDKILEFDRDFRIRHYAGDVVYSVIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERCGFQDDVAYGKTKIFIRTPRTLFTLEELRAQMLIRIVLFLQKVWRGTLARMRYKRTKAALTIIRYYRRYKVKSYIHEVARRFHGVKTMRDYGKHVKWPSPPKVLRRFEEALQTIFNRWRASQLIKSIPASDLPQVRAKVAAVEMLKGQRADLGLQRAWEGNYLASKPDTPQTSGTFVPVANELKRKDKYMNVLFSCHVRKVNRFSKVEDRAIFVTDRHLYKMDPTKQYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNKDLIVCLFSKQPTHESRIGELVGVLVNHFKSEKRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPQPDFTKNRSGFILSVPGN
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------MAEQESLEF
------CCCHHHHHC		38.18-
39PhosphorylationRFEKGRIYTFIGEVV
EECCCCEEEEEEEEE		8.34-
52PhosphorylationVVVSVNPYKLLNIYG
EEEEECHHHHEEEEC		14.74-
58PhosphorylationPYKLLNIYGRDTIEQ
HHHHEEEECCCHHHH		12.6823898821
67UbiquitinationRDTIEQYKGRELYER
CCHHHHHCCCCHHHC		51.70-
72PhosphorylationQYKGRELYERPPHLF
HHCCCCHHHCCCHHH		12.73-
93PhosphorylationYKAMKRRSKDTCIVI
HHHHHHCCCCEEEEE		38.6323312004
96PhosphorylationMKRRSKDTCIVISGE
HHHCCCCEEEEEECC		14.1023312004
108UbiquitinationSGESGAGKTEASKYI
ECCCCCCHHHHHHHH		42.53-
114PhosphorylationGKTEASKYIMQYIAA
CHHHHHHHHHHHHHH		10.1022817900
126PhosphorylationIAAITNPSQRAEVER
HHHHCCHHHHHHHHH		34.0824719451
153PhosphorylationEAFGNAKTNRNDNSS
HCCCCCCCCCCCCCC		36.6824719451
159PhosphorylationKTNRNDNSSRFGKYM
CCCCCCCCCCCEEEE		26.2529514088
160PhosphorylationTNRNDNSSRFGKYMD
CCCCCCCCCCEEEEE		37.5729514088
164UbiquitinationDNSSRFGKYMDINFD
CCCCCCEEEEEEEEE		34.39-
188UbiquitinationINNYLLEKSRVIVQQ
HHHHHHHHCCEEEEC		43.46-
200PhosphorylationVQQPGERSFHSFYQL
EECCCCCCHHHHHHH		24.0218669648
203PhosphorylationPGERSFHSFYQLLQG
CCCCCHHHHHHHHHC		24.5218669648
205PhosphorylationERSFHSFYQLLQGGS
CCCHHHHHHHHHCCC		10.98-
212PhosphorylationYQLLQGGSEQMLRSL
HHHHHCCCHHHHHHH		31.3218669648
224PhosphorylationRSLHLQKSLSSYNYI
HHHHHHHHHHCCCEE		22.1122210691
226PhosphorylationLHLQKSLSSYNYIHV
HHHHHHHHCCCEEEE		37.5622210691
239PhosphorylationHVGAQLKSSINDAAE
EECCCHHHCCCCHHH		45.07-
298PhosphorylationIENGKVVSIIAELLS
EECCEEHHHHHHHHC		15.9721406692
305PhosphorylationSIIAELLSTKTDMVE
HHHHHHHCCCCHHHH		40.2524719451
306PhosphorylationIIAELLSTKTDMVEK
HHHHHHCCCCHHHHH		37.6221406692
308PhosphorylationAELLSTKTDMVEKAL
HHHHCCCCHHHHHHH		29.43-
317PhosphorylationMVEKALLYRTVATGR
HHHHHHHHHHHHCCC		12.70-
329 (in isoform 1)Ubiquitination-33.3021906983
329MalonylationTGRDIIDKQHTEQEA
CCCCCCCHHHHHHHH		33.3026320211
329UbiquitinationTGRDIIDKQHTEQEA
CCCCCCCHHHHHHHH		33.30-
368PhosphorylationDIIEVKNYDTTIHGK
HHEEECCCCCEECCC		14.67-
370PhosphorylationIEVKNYDTTIHGKNT
EEECCCCCEECCCCC		19.7928857561
371PhosphorylationEVKNYDTTIHGKNTV
EECCCCCEECCCCCE		14.2128857561
402PhosphorylationFEQFCINYCNEKLQQ
HHHHHHHHHHHHHHH		4.0918452278
423PhosphorylationLKQEQEEYQREGIPW
HHHHHHHHHHCCCCH		16.4722817900
435PhosphorylationIPWKHIDYFNNQIIV
CCHHHHHHCCCEEHH		13.9627259358
478UbiquitinationFLEALNSKLGKHAHF
HHHHHHHHCCCCCCC		61.25-
491S-palmitoylationHFSSRKLCASDKILE
CCCCCCCCCCCCEEE		3.7021044946
493PhosphorylationSSRKLCASDKILEFD
CCCCCCCCCCEEECC		38.1426657352
501MethylationDKILEFDRDFRIRHY
CCEEECCCCCHHHHH		50.73115484247
514PhosphorylationHYAGDVVYSVIGFID
HHCCCEEEEEEEEEC		9.32-
524UbiquitinationIGFIDKNKDTLFQDF
EEEECCCCCCHHHHH		58.80-
536PhosphorylationQDFKRLMYNSSNPVL
HHHHHHHHCCCCHHH		19.2426356563
553PhosphorylationMWPEGKLSITEVTKR
CCCCCCCCEEEECCC		30.8322985185
555PhosphorylationPEGKLSITEVTKRPL
CCCCCCEEEECCCCC		22.4928348404
559UbiquitinationLSITEVTKRPLTAAT
CCEEEECCCCCCHHH		58.1421890473
563PhosphorylationEVTKRPLTAATLFKN
EECCCCCCHHHHCCC		19.54-
571PhosphorylationAATLFKNSMIALVDN
HHHHCCCCHHHHHHH		16.5029507054
585PhosphorylationNLASKEPYYVRCIKP
HHHCCCCEEEEEECC		18.71-
586PhosphorylationLASKEPYYVRCIKPN
HHCCCCEEEEEECCC		7.6726356563
612PhosphorylationRCRHQVEYLGLLENV
HHHHHHHHHHHHHHH		13.7628152594
674PhosphorylationGFQDDVAYGKTKIFI
CCCCCCCCCCEEEEE		21.00-
683PhosphorylationKTKIFIRTPRTLFTL
CEEEEEECCCCCCCH		16.59-
686PhosphorylationIFIRTPRTLFTLEEL
EEEECCCCCCCHHHH		27.6828176443
689PhosphorylationRTPRTLFTLEELRAQ
ECCCCCCCHHHHHHH		36.0528176443
726PhosphorylationKRTKAALTIIRYYRR
HHHHHHHHHHHHHHH		15.0523312004
734PhosphorylationIIRYYRRYKVKSYIH
HHHHHHHHCHHHHHH		15.9022817900
738PhosphorylationYRRYKVKSYIHEVAR
HHHHCHHHHHHHHHH		32.1023312004
739PhosphorylationRRYKVKSYIHEVARR
HHHCHHHHHHHHHHH		10.6923312004
756PhosphorylationGVKTMRDYGKHVKWP
CCCCHHHCCCCCCCC		20.08-
767UbiquitinationVKWPSPPKVLRRFEE
CCCCCCHHHHHHHHH		58.2321890473
811MethylationVAAVEMLKGQRADLG
HHHHHHHCCCCCCCC		52.2544496109
811UbiquitinationVAAVEMLKGQRADLG
HHHHHHHCCCCCCCC		52.2521890473
830PhosphorylationWEGNYLASKPDTPQT
HCCCCCCCCCCCCCC		41.9723312004
831UbiquitinationEGNYLASKPDTPQTS
CCCCCCCCCCCCCCC		41.11-
834PhosphorylationYLASKPDTPQTSGTF
CCCCCCCCCCCCCCC		26.3124719451
837PhosphorylationSKPDTPQTSGTFVPV
CCCCCCCCCCCCCCC		30.2623312004
838PhosphorylationKPDTPQTSGTFVPVA
CCCCCCCCCCCCCCC		30.5023312004
840PhosphorylationDTPQTSGTFVPVANE
CCCCCCCCCCCCCHH		22.6423312004
886UbiquitinationVTDRHLYKMDPTKQY
EECCCCCCCCCCCCE		43.09-
898PhosphorylationKQYKVMKTIPLYNLT
CCEEEEEECEEEECC		15.1021406692
902PhosphorylationVMKTIPLYNLTGLSV
EEEECEEEECCCEEE		11.6321406692
905PhosphorylationTIPLYNLTGLSVSNG
ECEEEECCCEEEECC		32.2221406692
908PhosphorylationLYNLTGLSVSNGKDQ
EEECCCEEEECCCCE		25.5021406692
910PhosphorylationNLTGLSVSNGKDQLV
ECCCEEEECCCCEEE		36.1721406692
921PhosphorylationDQLVVFHTKDNKDLI
CEEEEEEECCCCCEE		28.73-
933PhosphorylationDLIVCLFSKQPTHES
CEEEEEEECCCCCHH		19.8924719451
955PhosphorylationVLVNHFKSEKRHLQV
HHHHHHHHCCCEEEE		47.6227251275
971PhosphorylationVTNPVQCSLHGKKCT
CCCCEEEECCCCEEE		13.3024719451
976UbiquitinationQCSLHGKKCTVSVET
EEECCCCEEEEEEEE		39.47-
997PhosphorylationPDFTKNRSGFILSVP
CCCCCCCCCEEEECC		47.6627251275
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 MYO1D_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO1D_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 MYO1D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBB_HUMANUBBphysical
26186194
TBC9B_HUMANTBC1D9Bphysical
26186194
UBB_HUMANUBBphysical
28514442
TBC9B_HUMANTBC1D9Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO1D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-203 ANDSER-212, AND MASS SPECTROMETRY.

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