MYO1F_HUMAN - dbPTM
MYO1F_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO1F_HUMAN
UniProt AC O00160
Protein Name Unconventional myosin-If
Gene Name MYO1F
Organism Homo sapiens (Human).
Sequence Length 1098
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 MGSKERFHWQSHNVKQSGVDDMVLLPQITEDAIAANLRKRFMDDYIFTYIGSVLISVNPFKQMPYFTDREIDLYQGAAQYENPPHIYALTDNMYRNMLIDCENQCVIISGESGAGKTVAAKYIMGYISKVSGGGEKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSRGGEPDGGKISNFLLEKSRVVMQNENERNFHIYYQLLEGASQEQRQNLGLMTPDYYYYLNQSDTYQVDGTDDRSDFGETLSAMQVIGIPPSIQQLVLQLVAGILHLGNISFCEDGNYARVESVDLLAFPAYLLGIDSGRLQEKLTSRKMDSRWGGRSESINVTLNVEQAAYTRDALAKGLYARLFDFLVEAINRAMQKPQEEYSIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIQYFNNKVVCDLIENKLSPPGIMSVLDDVCATMHATGGGADQTLLQKLQAAVGTHEHFNSWSAGFVIHHYAGKVSYDVSGFCERNRDVLFSDLIELMQTSEQAFLRMLFPEKLDGDKKGRPSTAGSKIKKQANDLVATLMRCTPHYIRCIKPNETKRPRDWEENRVKHQVEYLGLKENIRVRRAGFAYRRQFAKFLQRYAILTPETWPRWRGDERQGVQHLLRAVNMEPDQYQMGSTKVFVKNPESLFLLEEVRERKFDGFARTIQKAWRRHVAVRKYEEMREEASNILLNKKERRRNSINRNFVGDYLGLEERPELRQFLGKRERVDFADSVTKYDRRFKPIKRDLILTPKCVYVIGREKVKKGPEKGQVCEVLKKKVDIQALRGVSLSTRQDDFFILQEDAADSFLESVFKTEFVSLLCKRFEEATRRPLPLTFSDTLQFRVKKEGWGGGGTRSVTFSRGFGDLAVLKVGGRTLTVSVGDGLPKSSKPTRKGMAKGKPRRSSQAPTRAAPAPPRGMDRNGVPPSARGGPLPLEIMSGGGTHRPPRGPPSTSLGASRRPRARPPSEHNTEFLNVPDQGMAGMQRKRSVGQRPVPGVGRPKPQPRTHGPRCRALYQYVGQDVDELSFNVNEVIEILMEDPSGWWKGRLHGQEGLFPGNYVEKI
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
45PhosphorylationRKRFMDDYIFTYIGS
HHHHCCHHHHHHCCC		8.1530174305
49PhosphorylationMDDYIFTYIGSVLIS
CCHHHHHHCCCEEEE		7.7930174305
65PhosphorylationNPFKQMPYFTDREID
CCCCCCCCCCCCCEE		17.4830174305
67PhosphorylationFKQMPYFTDREIDLY
CCCCCCCCCCCEEEC		28.4430174305
109PhosphorylationENQCVIISGESGAGK
CCCEEEEECCCCCCH		25.94-
116UbiquitinationSGESGAGKTVAAKYI
ECCCCCCHHHHHHHH		39.01-
121AcetylationAGKTVAAKYIMGYIS
CCHHHHHHHHHHHHH		26.107925233
122PhosphorylationGKTVAAKYIMGYISK
CHHHHHHHHHHHHHC		7.4520068231
126PhosphorylationAAKYIMGYISKVSGG
HHHHHHHHHHCCCCC		5.6620068231
128PhosphorylationKYIMGYISKVSGGGE
HHHHHHHHCCCCCCC		20.6520068231
131PhosphorylationMGYISKVSGGGEKVQ
HHHHHCCCCCCCCCC		35.1420068231
141UbiquitinationGEKVQHVKDIILQSN
CCCCCCHHHHHHHCC		40.88-
158UbiquitinationLEAFGNAKTVRNNNS
HHHHCCCEEECCCCC		52.1021890473
170UbiquitinationNNSSRFGKYFEIQFS
CCCCCCEEEEEEEEE		44.0121890473
194UbiquitinationISNFLLEKSRVVMQN
CCHHHHHHCEEEEEC		43.4621890473
195PhosphorylationSNFLLEKSRVVMQNE
CHHHHHHCEEEEECC		22.41-
229PhosphorylationRQNLGLMTPDYYYYL
HHHCCCCCCCEEEEC		20.3224043423
232PhosphorylationLGLMTPDYYYYLNQS
CCCCCCCEEEECCCC		8.4524043423
233PhosphorylationGLMTPDYYYYLNQSD
CCCCCCEEEECCCCC		7.9424043423
234PhosphorylationLMTPDYYYYLNQSDT
CCCCCEEEECCCCCC		8.6824043423
235PhosphorylationMTPDYYYYLNQSDTY
CCCCEEEECCCCCCE		5.3124043423
239PhosphorylationYYYYLNQSDTYQVDG
EEEECCCCCCEEECC		30.7424043423
241PhosphorylationYYLNQSDTYQVDGTD
EECCCCCCEEECCCC		22.5424043423
242PhosphorylationYLNQSDTYQVDGTDD
ECCCCCCEEECCCCC		16.1324043423
247PhosphorylationDTYQVDGTDDRSDFG
CCEEECCCCCCCCHH		30.2024043423
299PhosphorylationGNYARVESVDLLAFP
CCCEEEEECEEEHHH		20.3422496350
355UbiquitinationYTRDALAKGLYARLF
HHHHHHHHHHHHHHH		50.7421890473
438PhosphorylationIRWTPIQYFNNKVVC
CCCCCHHHCCCEEHH		14.70-
535PhosphorylationLIELMQTSEQAFLRM
HHHHHHHCHHHHHHH		15.7219276368
558PhosphorylationDKKGRPSTAGSKIKK
CCCCCCCCCHHHHHH		37.41-
561PhosphorylationGRPSTAGSKIKKQAN
CCCCCCHHHHHHHHH		28.83-
590PhosphorylationRCIKPNETKRPRDWE
CCCCCCCCCCCCCCH		38.7129449344
602UbiquitinationDWEENRVKHQVEYLG
CCHHHHHHHHHHHCC		25.69-
607PhosphorylationRVKHQVEYLGLKENI
HHHHHHHHCCCHHCH		13.76-
611AcetylationQVEYLGLKENIRVRR
HHHHCCCHHCHHHHH		47.0925825284
611UbiquitinationQVEYLGLKENIRVRR
HHHHCCCHHCHHHHH		47.0921890473
641PhosphorylationYAILTPETWPRWRGD
HHCCCCCCCCCCCCC		41.8128450419
667PhosphorylationVNMEPDQYQMGSTKV
HCCCCHHCCCCCEEE		14.09-
671PhosphorylationPDQYQMGSTKVFVKN
CHHCCCCCEEEEECC		21.5127251275
673UbiquitinationQYQMGSTKVFVKNPE
HCCCCCEEEEECCHH		35.0621890473
734PhosphorylationKKERRRNSINRNFVG
HHHHHHHCCCHHCHH		21.3021955146
743PhosphorylationNRNFVGDYLGLEERP
CHHCHHHHCCCCCCH		9.2027174698
767PhosphorylationERVDFADSVTKYDRR
CCCCHHHHCCCCCCC		28.4026074081
769PhosphorylationVDFADSVTKYDRRFK
CCHHHHCCCCCCCCC		28.0426074081
771PhosphorylationFADSVTKYDRRFKPI
HHHHCCCCCCCCCCC		12.81-
790PhosphorylationILTPKCVYVIGREKV
ECCCCEEEEECHHHH		8.8819835603
905UbiquitinationFGDLAVLKVGGRTLT
CCCEEEEEECCEEEE		32.032189047
910PhosphorylationVLKVGGRTLTVSVGD
EEEECCEEEEEEECC		30.01-
912PhosphorylationKVGGRTLTVSVGDGL
EECCEEEEEEECCCC		15.32-
922PhosphorylationVGDGLPKSSKPTRKG
ECCCCCCCCCCCCCC		41.4723911959
923PhosphorylationGDGLPKSSKPTRKGM
CCCCCCCCCCCCCCC		49.1027080861
938PhosphorylationAKGKPRRSSQAPTRA
CCCCCCCCCCCCCCC		28.2520068231
939PhosphorylationKGKPRRSSQAPTRAA
CCCCCCCCCCCCCCC		28.6620068231
943PhosphorylationRRSSQAPTRAAPAPP
CCCCCCCCCCCCCCC		35.6420068231
973PhosphorylationPLPLEIMSGGGTHRP
CCCEEEECCCCCCCC		39.6927080861
977PhosphorylationEIMSGGGTHRPPRGP
EEECCCCCCCCCCCC		20.2727080861
986PhosphorylationRPPRGPPSTSLGASR
CCCCCCCCCCCCCCC		33.4920860994
987PhosphorylationPPRGPPSTSLGASRR
CCCCCCCCCCCCCCC		33.4723312004
988PhosphorylationPRGPPSTSLGASRRP
CCCCCCCCCCCCCCC		29.1923312004
992PhosphorylationPSTSLGASRRPRARP
CCCCCCCCCCCCCCC		27.3328857561
1001PhosphorylationRPRARPPSEHNTEFL
CCCCCCCCCCCCCCC		54.9223401153
1005PhosphorylationRPPSEHNTEFLNVPD
CCCCCCCCCCCCCCC		29.9828450419
1023PhosphorylationAGMQRKRSVGQRPVP
CHHHCCCCCCCCCCC		33.3723401153
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 MYO1F_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO1F_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 MYO1F_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OSTF1_HUMANOSTF1physical
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 MYO1F_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-734, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1023, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-734, AND MASSSPECTROMETRY.

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