MYO3_SCHPO - dbPTM
MYO3_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO3_SCHPO
UniProt AC O14157
Protein Name Myosin type-2 heavy chain 2
Gene Name myo3
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 2104
Subcellular Localization
Protein Description Stabilizes the F-actin cables forming the F-actin ring that surrounds the nucleus during interphase. May work in conjunction with myo2..
Protein Sequence MSYLSKNGSNDNNNIIKKLVDAEKHCNAVKDASFDERTWIWIPDSKESFVKAWIVEDLGEKYRVKLERDGSERIVDGFDAEKVNPPKFDMVDDMAALTCLNEPSVVNNLTQRYEKDLIYTYSGLFLVAVNPYCHLPIYGDDVVRKYQSKQFKETKPHIFGTADAAYRSLLERRINQSILVTGESGAGKTETTKKVIQYLTSVTDASTSDSQQLEKKILETNPVLEAFGNAQTVRNNNSSRFGKFIRIEFSNNGSIVGANLDWYLLEKSRVIHPSSNERNYHVFYQLLRGADGSLLESLFLDRYVDHYSYLKNGLKHINGVDDGKEFQKLCFGLRTLGFDNNEIHSLFLIIASILHIGNIEVASDRSGQARFPSLTQIDQLCHLLEIPVDGFVNAALHPKSKAGREWIVTARTREQVVHTLQSLAKGLYERNFAHLVKRLNQTMYYSQSEHDGFIGVLDIAGFEIFTFNSFEQLCINFTNEKLQQFFNHYMFVLEQEEYTQERIEWDFIDYGNDLQPTIDAIEKSEPIGIFSCLDEDCVMPMATDATFTEKLHLLFKGKSDIYRPKKFSSEGFVLKHYAGDVEYDTKDWLEKNKDPLNACLAALMFKSTNSHVSSLFDDYSSNASGRDNIEKKGIFRTVSQRHRRQLSSLMHQLEATQPHFVRCIIPNNLKQPHNLDKSLVLHQLRCNGVLEGIRIAQTGFPNKLFYTEFRARYGILSQSLKRGYVEAKKATITIINELKLPSTVYRLGETKVFFKASVLGSLEDRRNALLRVIFNSFSARIRGFLTRRRLYRFNHRQDAAILLQHNLRQLKLLKPHPWWNLFLHLKPLLGTTQTDEYLRRKDALINNLQNQLESTKEVANELTITKERVLQLTNDLQEEQALAHEKDILVERANSRVEVVHERLSSLENQVTIADEKYEFLYAEKQSIEEDLANKQTEISYLSDLSSTLEKKLSSIKKDEQTISSKYKELEKDYLNIMADYQHSSQHLSNLEKAINEKNLNIRELNEKLMRLDDELLLKQRSYDTKVQELREENASLKDQCRTYESQLASLVSKYSETESELNKKEAELVIFQKEITEYRDQLHKAFQNPEKTHNINDVKSGPLNSDENIYSTSSTTLSILKDVQELKSLHTKEANQLSERIKEISEMLEQSIATEEKLRRKNSELCDIIEALKYQIQDQETEIISLNADNLDLKDTNGVLEKNASDFIDFQGIKSRYEHKISDLLNQLQKERCKVGLLKQKTENRSVTQHTLDGNSPHPSFEEKHSGDPLKRIDGNNDDRKIDNKLLKTISKSLDALQLTVEEELSNLYSLSKDLSFTDISGHIPNSIRKLEKGLSTLSELKERLNASNSDRPSPDIFKDTQAIMNSRKLLSNPNSDAQSGLISSLQKKLYNPESNMEFTGLKPLSPSKISNLPSSQPGSPSKRSGKMEALIRNFDQNSSIPDPFIVNQRNSVLQTEFEKINLKLKEATKSGILDNKDLSKFSELIQSLLKENEELKNLTTSNLGSDDKMLDFAPLLEDVPNNTRNQIKGFVEKAISSKRAIAKLYSASEEKLFSTEKALREITKERDRLLHGLQGPSVPTSPLKAPTASQLIIPNFDGSITNYSGEEETEWLQEEVNIMKIKELTSTVNKYREQLAMVQSLNEHAESSLSKAERSKNYLTGRLQEVEELARGFQTTNADLQNELADAVVKQKEYEVLYVEKSNDYNTLLLQKEKLMKQIDEFHVIRVQDLEEREKKDQLLFQRYQKELNGFKVQLEEEREKNLRIRQDNRHMHAEIGDIRTKFDELVLEKTNLLKENSILQADLQSLSRVNNSSSTAQQNAQSQLLSLTAQLQEVREANQTLRKDQDTLLRENRNLERKLHEVSEQLNKKFDSSARPFDEIEMEKEVLTLKSNLAQKDDLLSSLVERIKQIEMFALKTQKDSNNHREENLQLHRQLGVLQKEKKDLELKLFDLDLKTYPISTSKDVRMLQKQISDLEASFAASDIERIKGIDECRNRDRTIRQLEAQISKFDDDKKRIQSSVSRLEERNAQLRNQLEDVQASETQWKFALRRTEHALQEERERVKSLETDFDKYRSLLEGQRVKRSESRLSMRSNRSPSVLR
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
927PhosphorylationFLYAEKQSIEEDLAN
HHHHHHCCHHHHHHC		42.9329996109
1257PhosphorylationQHTLDGNSPHPSFEE
CCCCCCCCCCCCCCC		30.0725720772
1349PhosphorylationLKERLNASNSDRPSP
HHHHHCCCCCCCCCC		35.4721712547
1351PhosphorylationERLNASNSDRPSPDI
HHHCCCCCCCCCCCH		32.2821712547
1355PhosphorylationASNSDRPSPDIFKDT
CCCCCCCCCCHHHHH		35.7821712547
1396PhosphorylationKKLYNPESNMEFTGL
HHHHCCCCCCCCCCC		42.6129996109
1401PhosphorylationPESNMEFTGLKPLSP
CCCCCCCCCCCCCCH		28.4421712547
1407PhosphorylationFTGLKPLSPSKISNL
CCCCCCCCHHHHCCC		35.3424763107
1409PhosphorylationGLKPLSPSKISNLPS
CCCCCCHHHHCCCCC		38.9729996109
1412PhosphorylationPLSPSKISNLPSSQP
CCCHHHHCCCCCCCC		35.7329996109
1416PhosphorylationSKISNLPSSQPGSPS
HHHCCCCCCCCCCCC		44.7825720772
1417PhosphorylationKISNLPSSQPGSPSK
HHCCCCCCCCCCCCC		38.1525720772
1421PhosphorylationLPSSQPGSPSKRSGK
CCCCCCCCCCCCCCC		32.4628889911
1423PhosphorylationSSQPGSPSKRSGKME
CCCCCCCCCCCCCHH		42.2625720772
1579PhosphorylationLHGLQGPSVPTSPLK
HHHCCCCCCCCCCCC		47.7724763107
1582PhosphorylationLQGPSVPTSPLKAPT
CCCCCCCCCCCCCCC		40.6024763107
1583PhosphorylationQGPSVPTSPLKAPTA
CCCCCCCCCCCCCCC		23.3621712547
2096PhosphorylationESRLSMRSNRSPSVL
HHHHHCCCCCCCCCC		28.1429996109
2099PhosphorylationLSMRSNRSPSVLR--
HHCCCCCCCCCCC--		26.2725720772
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 MYO3_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO3_SCHPO !!
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 MYO3_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACT_SCHPOact1genetic
9459302
TPM_SCHPOcdc8genetic
9459302
CDC11_SCHPOcdc11genetic
9398685
CDC14_SCHPOcdc14genetic
9398685
CDC16_SCHPOcdc16genetic
9398685
CHS2_SCHPOchs2physical
16772338
MLR4_SCHPOcdc4physical
10769212
MLR1_SCHPOrlc1physical
11069761
MYO1_SCHPOmyo1physical
19805578
RNG2_SCHPOrng2physical
19805578
MYO3_SCHPOmyp2physical
19805578
MYO2_SCHPOmyo2physical
19805578
MYO52_SCHPOmyo52physical
19805578
MCP7_SCHPOmcp7physical
19805578
CHS2_SCHPOchs2genetic
16772338
MYO2_SCHPOmyo2genetic
20110347
EME1_SCHPOeme1genetic
18818364
YB3C_SCHPOcay1genetic
18818364
CAF1_SCHPOcaf1genetic
18818364
YFE6_SCHPOgmh5genetic
18818364
RSV2_SCHPOrsv2genetic
18818364
VPS71_SCHPOvps71genetic
18818364
GEF2_SCHPOgef2genetic
22298427
MYO2_SCHPOmyo2genetic
10637292
YEYA_SCHPOcsc4genetic
22681890
YNVD_SCHPOfar10genetic
22681890
YGD1_SCHPOfar8genetic
22681890
YAC5_SCHPOcph1genetic
22681890
BST1_SCHPObst1genetic
22681890
GYP1_SCHPOgyp1genetic
22681890
ZRG17_SCHPOzrg17genetic
22681890
TRX2_SCHPOtrx2genetic
22681890
POM1_SCHPOpom1genetic
22681890
SEC63_SCHPOsec63genetic
22681890
YDHE_SCHPOSPAC6G9.14genetic
22681890
YE98_SCHPOerp2genetic
22681890
YCS3_SCHPOSPCC613.03genetic
22681890
YOR2_SCHPOrng9genetic
22681890
YGVA_SCHPOdef1genetic
22681890
SEC14_SCHPOspo20genetic
22681890
CIS4_SCHPOcis4genetic
22681890
MID1_SCHPOmid1genetic
22681890
PRZ1_SCHPOprz1genetic
22681890
ATC1_SCHPOpmr1genetic
22681890
KIN1_SCHPOkin1genetic
23294323
CDC15_SCHPOcdc15genetic
25159149
MLR1_SCHPOrlc1physical
26771498
TPM_SCHPOcdc8genetic
26092938
RICTR_SCHPOste20physical
27206859
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO3_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1421, AND MASSSPECTROMETRY.

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