MYO1_SCHPO - dbPTM
MYO1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO1_SCHPO
UniProt AC Q9Y7Z8
Protein Name Myosin-1
Gene Name myo1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1217
Subcellular Localization Cytoplasm, cytoskeleton, actin patch . Localizes to cortical patches at the tips of growing cells and at sites of cell division.
Protein Description Type-I myosin implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Contributes to proper septation by transporting vesicles containing septal material to the division site and is involved in the formation of sterol-rich membrane domains at the cell division site. Required also for mating..
Protein Sequence MAILKRTNRAKAATAAAPNSTGKSNGIKKAVYTSTRKKTVGVDDLTLLSKITDEEINKNLELRFRNGEIYTYIGHVLISVNPFRDLGIYTMDILKSYQGKNRLETSPHVYAIAENAYYQMKSYHENQCIIISGESGAGKTEAAKRIMQYITHVSKSVGTEIERVSEIILATNPLLESFGCAKTLRNNNSSRHGKYLEMIFNSGGVPVGAKITNYLLEKNRIVNQVRNERNFHIFYQFTKSAPQKYRDTYGIQGPENYVYTSACQCLSVDGISDEKDFQGTMNAMKVIGITEPEQDEIFRMLSIILWLGNIQFQEGQDGGSVISDKSITEFLGYLIGVPVAAIERALTIRIMQTQHGARRGSVYEVPLNPTQALAVRDALSMAIYNCLFDWIVERVNKALVTSDNSVSNSIGILDIYGFEIFENNSFEQLCINYVNEKLQQIFIELTLKTEQEEYVREQIAWTPIKYFNNKVVCDLIESKRPPGLFAAMNDAIATAHADSAAADSAFAQRLNFLSSNPHFEQRQNQFIVKHYAGDVTYSITGMTDKNKDQLATDILNLIHSSNNEFMKSIFPVAEESNSRRRPPTAGDRIKTSANDLVETLMKCQPSYIRTIKPNQTKSPNDYDQQMVLHQIKYLGLQENIRIRRAGFAYRQAFDTFAQRFAVLSGKTSYAGEYTWQGDDKSACEQILKDTNIPSSEYQMGTSKVFIKNPETLFALEDMRDKFWDTMATRIQRAWRSYVRRRSEAAACIQKLWNRNKVNMELERVRNEGTKLLQGKKQRRRYSILGSRKFYGDYLSASKPNGTLWNTCGLSQNDHVIFSMRCEVLVHKLGRTSKPSPRQLVLTKKNLYLVITKIVDQKLTQQVEKKFAVSSIDSVGLTNLQDDWVAIRNKSSQNGDMFLRCFFKTEFITTLKRINRNIQVIVGPTIQYCRKPGKVQTVKTAKDETTKDYDYYKSGTIHVGTGLPPTSKSKPFPRLATGGSTAAARGPRPVVQNKPAATKPVSMPAAKSKPAPMANPVSTAQQTQNRPPAPAMQARPNTTQAAAPVTSTTTTIKQATTVSASKPAPSTVTSAASSPSNISKPSAPVANNVSKPSAVPPPPPPPPAEVEKKDLYLALYDFAGRSPNEMTIKKDEIIEIVQKEPSGWWLALKNGAEGWVPATYVTEYKGSTPQTTASSTNVAAQANNNASPAEVNNLAGSLADALRMRASAVRGSDEEEDW
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
20PhosphorylationATAAAPNSTGKSNGI
HHHCCCCCCCCCCCC		37.1627738172
39PhosphorylationYTSTRKKTVGVDDLT
EECCCCCCCCCCHHH		26.0628889911
361PhosphorylationQHGARRGSVYEVPLN
CCCCCCCCEEECCCC		21.5128889911
363PhosphorylationGARRGSVYEVPLNPT
CCCCCCEEECCCCHH		16.9528889911
742PhosphorylationRSYVRRRSEAAACIQ
HHHHHHHHHHHHHHH		29.7628889911
781PhosphorylationGKKQRRRYSILGSRK
CCHHHHCEEECCCCC		9.7625720772
782PhosphorylationKKQRRRYSILGSRKF
CHHHHCEEECCCCCC		14.9928889911
786PhosphorylationRRYSILGSRKFYGDY
HCEEECCCCCCHHHH		28.9329996109
1065PhosphorylationSASKPAPSTVTSAAS
CCCCCCCCCCCCCCC		37.3024763107
1068PhosphorylationKPAPSTVTSAASSPS
CCCCCCCCCCCCCCC		16.8527738172
1069PhosphorylationPAPSTVTSAASSPSN
CCCCCCCCCCCCCCC		19.9421712547
1072PhosphorylationSTVTSAASSPSNISK
CCCCCCCCCCCCCCC		42.3624763107
1073PhosphorylationTVTSAASSPSNISKP
CCCCCCCCCCCCCCC		27.8524763107
1081PhosphorylationPSNISKPSAPVANNV
CCCCCCCCCCCCCCC		49.2821712547
1173PhosphorylationSTPQTTASSTNVAAQ
CCCCCCCCHHCHHHH		35.2925720772
1174PhosphorylationTPQTTASSTNVAAQA
CCCCCCCHHCHHHHH		22.8725720772
1175PhosphorylationPQTTASSTNVAAQAN
CCCCCCHHCHHHHHC		31.0829996109
1211PhosphorylationRASAVRGSDEEEDW-
HHHHHCCCCCCCCC-		31.1428889911
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 MYO1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO1_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 MYO1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VRP1_SCHPOvrp1genetic
16087707
WSP1_SCHPOwsp1genetic
11076964
CDC15_SCHPOcdc15physical
12939254
WSP1_SCHPOwsp1physical
12939254
CALM_SCHPOcam1physical
11260263
CAM2_SCHPOcam2physical
15504913
ARP3_SCHPOarp3physical
16087707
ARP2_SCHPOarp2physical
16087707
MYO1_SCHPOmyo1physical
19805578
WSP1_SCHPOwsp1physical
19805578
MYO2_SCHPOmyo2physical
19805578
MYO52_SCHPOmyo52physical
19805578
MYO3_SCHPOmyp2physical
19805578
RGF1_SCHPOrgf1physical
19805578
SPP42_SCHPOspp42physical
19805578
YBOE_SCHPOcsi1physical
19805578
MCP7_SCHPOmcp7physical
19805578
RNG2_SCHPOrng2physical
19805578
ULA1_SCHPOuba5physical
19805578
WSP1_SCHPOwsp1genetic
21885283
ENG2_SCHPOeng2genetic
25040903
CAM2_SCHPOcam2physical
26092123
TEA1_SCHPOtea1genetic
27180904
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO1_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-361; TYR-363; SER-742;SER-782 AND SER-1211, AND MASS SPECTROMETRY.

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