MYSN_DROME - dbPTM
MYSN_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYSN_DROME
UniProt AC Q99323
Protein Name Myosin heavy chain, non-muscle
Gene Name zip
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2057
Subcellular Localization Cell projection, cilium . Expression in neurons and scolopale cells is increased at the apical tips of cilia.
Protein Description Nonmuscle myosin appears to be responsible for cellularization. Required for morphogenesis and cytokinesis. [PubMed: 24786584 Necessary for auditory transduction: plays a role in Johnston's organ organization by acting in scolopidial apical attachment]
Protein Sequence MKSAWLALKSKSALHPKSEYPVSNIHYPKAANYRQTRNYLEIAAKMSEEVDRNDPELKYLSVERNQFNPIRPRRPSGHRSVLVWVPHENQGFVAASIKREHGDEVEVELAETGKRVMILRDDIQKMNPPKFDKVEDMAELTCLNEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLINFSVNTNKYIKVKIMAQNQNQTIEVVNGLKMVEVNSNCQEGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFRAGVLAHLEEERDFKISDLIVNFQAFCRGFLARRNYQKRLQQLNAIRIIQRNCAAYLKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATITELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEADGKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRRTGGIGLSSSRLTGTPSSKRAGGGGGSDDSSVQDESLDGEDSAN
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
2 (in isoform 4)Phosphorylation-61.2527794539
2 (in isoform 2)Phosphorylation-61.2527794539
58AcetylationDRNDPELKYLSVERN
HCCCCCHHEEEEECC
42.3519608861
61PhosphorylationDPELKYLSVERNQFN
CCCHHEEEEECCCCC
20.8825749252
125AcetylationILRDDIQKMNPPKFD
EECHHHHHHCCCCCC
40.7619608861
336AcetylationDNSSRFGKFIRINFD
CCCCCCEEEEEEEEC
34.6019608861
742AcetylationRTVSHLYKEQLAKLM
HHHHHHHHHHHHHHH
45.4019608861
1229PhosphorylationEKVRRDLSEELEALK
HHHHHHHHHHHHHHH
33.0619429919
1286PhosphorylationADMRHKHSQELNSIN
HHHHHHHHHHHHHHH
30.1019429919
1291PhosphorylationKHSQELNSINDQLEN
HHHHHHHHHHHHHHH
35.0819429919
1326PhosphorylationDLATELRSVNSSRQE
HHHHHHHHHCCHHHH
37.9725749252
1680AcetylationEKRRGLVKQLRDLET
HHHHHHHHHHHHHHH
48.97-
2007PhosphorylationAMNREINSLKTKLRR
HHHHHHHHHHHHHHH
36.5825749252
2015PhosphorylationLKTKLRRTGGIGLSS
HHHHHHHCCCCCCCC
33.0719429919
2021PhosphorylationRTGGIGLSSSRLTGT
HCCCCCCCCCCCCCC
22.5122817900
2022PhosphorylationTGGIGLSSSRLTGTP
CCCCCCCCCCCCCCC
25.2327331610
2026PhosphorylationGLSSSRLTGTPSSKR
CCCCCCCCCCCCCCC
37.5925749252
2028PhosphorylationSSSRLTGTPSSKRAG
CCCCCCCCCCCCCCC
18.1129892262
2030PhosphorylationSRLTGTPSSKRAGGG
CCCCCCCCCCCCCCC
48.6121082442
2031PhosphorylationRLTGTPSSKRAGGGG
CCCCCCCCCCCCCCC
27.6221082442
2049PhosphorylationDSSVQDESLDGEDSA
CCCCCCCCCCCCCCC
39.8022817900
2055PhosphorylationESLDGEDSAN-----
CCCCCCCCCC-----
25.9619060867

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
2021SPhosphorylationKinasePKC-FAMILY-GPS
2021SPhosphorylationKinasePKC_GROUP-PhosphoELM
2022SPhosphorylationKinasePKC-FAMILY-GPS
2022SPhosphorylationKinasePKC_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYSN_DROME !!

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 MYSN_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRYA_DROMESry-alphaphysical
14605208
EFHD2_DROMESwip-1physical
22036573
DNAT_DROMEDatphysical
22036573
CP2B_DROMECapaphysical
22036573
EOGT_DROMEEogtphysical
22036573
PROF_DROMEchicgenetic
20553709
MYO7A_DROMEckgenetic
20599890
FRIZ_DROMEfzgenetic
20599890
APKC_DROMEaPKCgenetic
20392741
MLC2_DROMEMlc-cphysical
16917818
SQH_DROMEsqhphysical
16917818
L2GL_DROMEl(2)glphysical
15694314
MYSN_DROMEzipphysical
17901043
MYSN_DROMEzipphysical
17989074

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYSN_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2021 AND SER-2022, ANDMASS SPECTROMETRY.

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