MYO3_YEAST - dbPTM
MYO3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO3_YEAST
UniProt AC P36006
Protein Name Myosin-3
Gene Name MYO3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1272
Subcellular Localization Cytoplasm, cytoskeleton, actin patch . Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth.
Protein Description One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2..
Protein Sequence MAVIKKGARRKDVKEPKKRSAKIKKATFDANKKKEVGISDLTLLSKISDESINENLKKRFKNGIIYTYIGHVLISVNPFRDLGIYTNAVLESYKGKNRLEVPPHVFAIAESMYYNLKSYNENQCVIISGESGAGKTEAAKRIMQYIAAASNSHSESIGKIKDMVLATNPLLESFGCAKTLRNNNSSRHGKYLEIKFNSQFEPCAGNITNYLLEKQRVVGQIKNERNFHIFYQFTKGASDTYKQMFGVQMPEQYIYTAAAGCTTADTIDDVKDYEGTLEAMRTIGLVQEEQDQIFRMLAAILWIGNISFIENEEGNAQVGDTSVTDFVAYLLQVDASLLVKCLVERIMQTSHGMKRGSVYHVPLNPVQATAVRDALAKAIYNNLFDWIVDRVNVSLQAFPGADKSIGILDIYGFEIFEHNSFEQICINYVNEKLQQIFIQLTLKAEQETYEREKIKWTPIKYFDNKVVCDLIEAKNPPGILAAMNDSIATAHADSNAADQAFAQRLNLFNSNPYFELRANKFVIKHYAGDVTYDINGITDKNKDQLQKDLIELIGTTTNTFLSTIFPDDVDKDSKRRPPTAGDKIIKSANELVETLSKAEPSYIRTIKPNQTKSPNDYDDHQVLHQVKYLGLQENVRIRRAGFAYRQTFEKFVERFYLLSPDCSYAGDYTWDGDTLEAVKLILRDAMIPEKEFQLGVTSVFIKTPESLFALEDMRDKYWYNMAARIQRAWRRFLQRRIDAAIKIQRTIREKKGGNKYVKLRDYGTKLLAGKKERRSMSLLGYRAFMGDYLSCNESKTKGSYIRRQVGIKDKVVFSIKGECLHSKFGRSAQRLKKVFILTKKTFYIIGQTREQNAMKYTQDYKIDVGKIKQVSLTNLQDDWMGVILVNSTQSDPLINTPFKTELMTRLKKLNEKIMIKVGPTIEYHKQPNKLHTVRSKISDSAPKYGDIYKSSTIYVRRGHPANSKSNKKPKNPGGLSGKPIKSKKSKHKSTHKHTHSHRSHRDAAKKQPLPSQKPVNPLSLAATAAQAAYNPKPDKTVPIKSSAIPAAKVSSKHSSKPSSKEKVAVKKASSSHKSSSAKQNQVSMPPSKGVEKNKEPLKETTATATANIPIPPPPPPMGQPKDPKFEAAYDFPGSGSSSELPLKKGDIVFISRDEPSGWSLAKLLDGSKEGWVPTAYMTPYKDTRNTVPVAATGAVNDVTNQKSSQIDNTISSAQEGVQFGSATVGPTSDNQSNPVGTFSDGLASALAARANKMRAESADDDDNDDGDDDDDW
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
135UbiquitinationSGESGAGKTEAAKRI
ECCCCCCHHHHHHHH		42.5323749301
145PhosphorylationAAKRIMQYIAAASNS
HHHHHHHHHHHHCCC		3.8327214570
156PhosphorylationASNSHSESIGKIKDM
HCCCCCCCHHHHHHH		39.3927214570
159UbiquitinationSHSESIGKIKDMVLA
CCCCCHHHHHHHHHH		44.9317644757
161UbiquitinationSESIGKIKDMVLATN
CCCHHHHHHHHHHCC		43.1717644757
178UbiquitinationLESFGCAKTLRNNNS
HHHHCCCHHHCCCCC		52.7717644757
235UbiquitinationHIFYQFTKGASDTYK
EEEEEECCCCCHHHH		54.4917644757
253PhosphorylationGVQMPEQYIYTAAAG
CCCCCHHHEEHHCCC		8.3430377154
255PhosphorylationQMPEQYIYTAAAGCT
CCCHHHEEHHCCCCC		5.8430377154
256PhosphorylationMPEQYIYTAAAGCTT
CCHHHEEHHCCCCCC		10.5630377154
262PhosphorylationYTAAAGCTTADTIDD
EHHCCCCCCCCCCHH		24.8930377154
336PhosphorylationYLLQVDASLLVKCLV
HHHHCCHHHHHHHHH		20.1319795423
354AcetylationMQTSHGMKRGSVYHV
HHHCCCCCCCEEEEC		59.1925381059
357PhosphorylationSHGMKRGSVYHVPLN
CCCCCCCEEEECCCC		24.4422369663
359PhosphorylationGMKRGSVYHVPLNPV
CCCCCEEEECCCCHH		9.9722369663
369PhosphorylationPLNPVQATAVRDALA
CCCHHHHHHHHHHHH		14.4822890988
474UbiquitinationVCDLIEAKNPPGILA
EHHHHHHCCCCCHHH		58.1417644757
555PhosphorylationDLIELIGTTTNTFLS
HHHHHHCCCCCCHHH		24.3719779198
579PhosphorylationDSKRRPPTAGDKIIK
CCCCCCCCHHHHHHH		46.0527214570
587PhosphorylationAGDKIIKSANELVET
HHHHHHHHHHHHHHH		26.3930377154
612UbiquitinationTIKPNQTKSPNDYDD
EECCCCCCCCCCCCH		54.9017644757
627UbiquitinationHQVLHQVKYLGLQEN
HHHHHHHHHHCCCCC		28.3417644757
627AcetylationHQVLHQVKYLGLQEN
HHHHHHHHHHCCCCC		28.3424489116
650AcetylationAYRQTFEKFVERFYL
HHHHHHHHHHHHHHH		50.9824489116
762PhosphorylationKYVKLRDYGTKLLAG
EEEEEEHHHCHHCCC		21.9125533186
765AcetylationKLRDYGTKLLAGKKE
EEEHHHCHHCCCCCC		36.8224489116
775PhosphorylationAGKKERRSMSLLGYR
CCCCCHHCCHHHCHH		20.9522369663
777PhosphorylationKKERRSMSLLGYRAF
CCCHHCCHHHCHHHH		22.9922369663
781PhosphorylationRSMSLLGYRAFMGDY
HCCHHHCHHHHHCCC		9.9522890988
788PhosphorylationYRAFMGDYLSCNESK
HHHHHCCCCCCCCCC		8.5219823750
790PhosphorylationAFMGDYLSCNESKTK
HHHCCCCCCCCCCCC		14.5219823750
794PhosphorylationDYLSCNESKTKGSYI
CCCCCCCCCCCCCHH		31.4719823750
822PhosphorylationIKGECLHSKFGRSAQ
EECHHHHCCCCCHHH		19.4128889911
838PhosphorylationLKKVFILTKKTFYII
HHEEEEEECCEEEEE		26.1925533186
920PhosphorylationIMIKVGPTIEYHKQP
CEEEECCCCEECCCC		22.1021551504
932PhosphorylationKQPNKLHTVRSKISD
CCCCCCHHCHHHCCC		28.2228889911
935PhosphorylationNKLHTVRSKISDSAP
CCCHHCHHHCCCCCC		29.9728889911
943AcetylationKISDSAPKYGDIYKS
HCCCCCCCCCCEEEC		62.6824489116
1048AcetylationSSAIPAAKVSSKHSS
CCCCCHHHHCCCCCC		44.7622865919
1050PhosphorylationAIPAAKVSSKHSSKP
CCCHHHHCCCCCCCC		32.7221440633
1069PhosphorylationKVAVKKASSSHKSSS
HHHHHHHHCCCCCCC		41.0521440633
1070PhosphorylationVAVKKASSSHKSSSA
HHHHHHHCCCCCCCH		41.1221440633
1083PhosphorylationSAKQNQVSMPPSKGV
CHHHCCCCCCCCCCC		18.7928889911
1087PhosphorylationNQVSMPPSKGVEKNK
CCCCCCCCCCCCCCC		35.8519779198
1134PhosphorylationAAYDFPGSGSSSELP
CCCCCCCCCCCCCCC		35.4222369663
1136PhosphorylationYDFPGSGSSSELPLK
CCCCCCCCCCCCCCC		32.1822369663
1137PhosphorylationDFPGSGSSSELPLKK
CCCCCCCCCCCCCCC		31.2122369663
1138PhosphorylationFPGSGSSSELPLKKG
CCCCCCCCCCCCCCC		44.8722369663
1257PhosphorylationANKMRAESADDDDND
HHHHHHHCCCCCCCC		35.6928889911
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_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
357SPhosphorylation

9388196
357SPhosphorylation

9388196
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_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARPC4_YEASTARC19physical
10648568
ARPC1_YEASTARC40physical
10648568
SHE4_YEASTSHE4physical
12725728
BBC1_YEASTBBC1physical
11901111
BNR1_YEASTBNR1physical
11901111
UBP7_YEASTUBP7physical
11901111
VRP1_YEASTVRP1physical
11901111
VRP1_YEASTVRP1physical
9628892
BNR1_YEASTBNR1physical
11743162
BBC1_YEASTBBC1physical
11743162
BNI1_YEASTBNI1physical
11743162
MYO5_YEASTMYO5physical
11743162
RV167_YEASTRVS167physical
11743162
VRP1_YEASTVRP1physical
11743162
UBP7_YEASTUBP7physical
11743162
BCK1_YEASTBCK1physical
11743162
PMG1_YEASTGPM1physical
11743162
SUMT_YEASTMET1physical
11743162
MED19_YEASTROX3physical
11743162
SRL1_YEASTSRL1physical
11743162
G3P3_YEASTTDH3physical
11743162
LAS17_YEASTLAS17physical
11743162
ARP2_YEASTARP2physical
10648569
CDC50_YEASTCDC50genetic
12589066
MYO5_YEASTMYO5genetic
9628892
MYO5_YEASTMYO5genetic
8682864
MYO5_YEASTMYO5genetic
8614799
CALM_YEASTCMD1physical
16554755
YGZ2_YEASTYGL242Cphysical
16554755
RRP43_YEASTRRP43physical
16554755
RRP4_YEASTRRP4physical
16554755
CSL4_YEASTCSL4physical
16554755
MYO5_YEASTMYO5genetic
16478726
UBP5_YEASTUBP5genetic
12589066
LAS17_YEASTLAS17genetic
12589066
BBC1_YEASTBBC1physical
19841731
BCK1_YEASTBCK1physical
19841731
END3_YEASTEND3physical
19841731
MYO5_YEASTMYO5physical
19841731
OSH2_YEASTOSH2physical
19841731
SRL1_YEASTSRL1physical
19841731
UBP7_YEASTUBP7physical
19841731
VRP1_YEASTVRP1physical
19841731
2ABA_YEASTCDC55physical
19841731
MET31_YEASTMET31physical
19841731
MTH1_YEASTMTH1physical
19841731
SAP1_YEASTSAP1physical
19841731
SERC_YEASTSER1physical
19841731
SSN8_YEASTSSN8physical
19841731
STD1_YEASTSTD1physical
19841731
MYO5_YEASTMYO5genetic
12589066
KAPC_YEASTTPK3genetic
20526336
MYO5_YEASTMYO5genetic
20526336
MYO5_YEASTMYO5genetic
21849475
CLC1_YEASTCLC1genetic
21849475
MYO3_YEASTMYO3physical
22940862
HSP72_YEASTSSA2physical
22940862
SSB1_YEASTSSB1physical
22940862
HSP71_YEASTSSA1physical
22940862
MSMO_YEASTERG25genetic
23891562
MYO5_YEASTMYO5genetic
23891562
SLX5_YEASTSLX5genetic
27708008
RS29B_YEASTRPS29Bgenetic
27708008
GCS1_YEASTGCS1genetic
27708008
SAC3_YEASTSAC3genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
RL9A_YEASTRPL9Agenetic
27708008
BGL2_YEASTBGL2genetic
27708008
ILM1_YEASTILM1genetic
27708008
YL053_YEASTYLR053Cgenetic
27708008
SIC1_YEASTSIC1genetic
27708008
PSP2_YEASTPSP2genetic
27708008
MYO5_YEASTMYO5genetic
27708008
RS10B_YEASTRPS10Bgenetic
27708008
SFL1_YEASTSFL1genetic
27708008
THP3_YEASTTHP3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO3_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; TYR-359; SER-777;THR-932; SER-935; SER-1136; SER-1137 AND SER-1138, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-777, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-777, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777, AND MASSSPECTROMETRY.
"The phosphorylation site for Ste20p-like protein kinases is essentialfor the function of myosin-I in yeast.";
Wu C., Lytvyn V., Thomas D.Y., Leberer E.;
J. Biol. Chem. 272:30623-30626(1997).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-357 BY CLA4 AND STE20, ANDMUTAGENESIS OF SER-357.

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