| UniProt ID | MYO5_YEAST | |
|---|---|---|
| UniProt AC | Q04439 | |
| Protein Name | Myosin-5 | |
| Gene Name | MYO5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1219 | |
| 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 | MAILKRGARKKVHQEPAKRSANIKKATFDSSKKKEVGVSDLTLLSKISDEAINENLKKRFLNATIYTYIGHVLISVNPFRDLGIYTDAVMNEYKGKNRLEVPPHVFAIAESMYYNMKSYNENQCVIISGESGAGKTEAAKRIMQYIAAASSTHTESIGKIKDMVLATNPLLESFGCAKTLRNNNSSRHGKYLEIKFNNQFEPCAGNITNYLLEKQRVVSQIKNERNFHIFYQFTKGASDAYRQTFGVQKPEQYVYTAAAGCISAETIDDLQDYQETLKAMRVIGLGQEEQDQIFRMLAAILWIGNVSFIENEEGNAQVRDTSVTDFVAYLLQIDSQLLIKSLVERIMETNHGMKRGSVYHVPLNIVQADAVRDALAKAIYNNLFDWIVSRVNKSLQAFPGAEKSIGILDIYGFEIFEHNSFEQICINYVNEKLQQIFIQLTLKSEQETYEREKIQWTPIKYFDNKVVCDLIEARRPPGIFAAMNDSVATAHADSNAADQAFAQRLNLFTTNPHFDLRSNKFVIKHYAGDVTYDIDGITDKNKDQLQKDLVELIGTTTNTFLATIFPDTVDRESKRRPPTAGDKIIKSANDLVETLSKAQPSYIRTIKPNETKSPNDYDDRQVLHQIKYLGLQENVRIRRAGFAYRQVFEKFVERFYLLSPHCSYAGDYTWQGDTLDAVKYILQDSSIPQQEYQLGVTSVFIKTPETLFALEHMRDRYWHNMAARIQRAWRRFLQRRIDAATKIQRTIRERKEGNKYEKLRDYGTKVLGGRKERRSMSLLGYRAFMGDYLSCNESKSKGAYIKRQVSIKEKVIFSIHGEALHTKFGRSAQRLKKTFLLTPTTLYIVGQTLVQNAMTYTQDYKIDVRNIQAVSLTNLQDDWVAIKLASSGQPDPLINTYFKTELITHLKRLNDKIQIKIGSAIEYQKKPGKLHSVKCQINESAPKYGDIYKSSTISVRRGNPPNSQVHKKPRKKSSISSGYHASSSQATRRPVSIAAAQHVPTAPASRHSKKPAPPPPGMQNKAATRRSVPNPASTLTASQSNARPSPPTAATRATPAATPAAAAMGSGRQANIPPPPPPPPPSSKPKEPMFEAAYDFPGSGSPSELPLKKGDVIYITREEPSGWSLGKLLDGSKEGWVPTAYMKPHSGNNNIPTPPQNRDVPKPVLNSVQHDNTSANVIPAAAQASLGDGLANALAARANKMRLESDDEEANEDEEEDDW | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 39 | Phosphorylation | KKKEVGVSDLTLLSK CCCCCCCCHHHHHHH | 22.45 | 21551504 | |
| 42 | Phosphorylation | EVGVSDLTLLSKISD CCCCCHHHHHHHCCH | 30.55 | 21551504 | |
| 48 | Phosphorylation | LTLLSKISDEAINEN HHHHHHCCHHHHHHH | 32.89 | 28889911 | |
| 135 | Ubiquitination | SGESGAGKTEAAKRI ECCCCCCHHHHHHHH | 42.53 | 23749301 | |
| 159 | Ubiquitination | THTESIGKIKDMVLA CCCCCCHHHHHHHHH | 44.93 | 17644757 | |
| 161 | Ubiquitination | TESIGKIKDMVLATN CCCCHHHHHHHHHCC | 43.17 | 17644757 | |
| 178 | Ubiquitination | LESFGCAKTLRNNNS HHHHCCCHHHCCCCC | 52.77 | 17644757 | |
| 235 | Ubiquitination | HIFYQFTKGASDAYR EEEEEECCCCCHHHH | 54.49 | 17644757 | |
| 341 | Phosphorylation | DSQLLIKSLVERIME CHHHHHHHHHHHHHH | 30.56 | 27017623 | |
| 349 | Phosphorylation | LVERIMETNHGMKRG HHHHHHHHCCCCCCC | 18.35 | 28889911 | |
| 354 | Acetylation | METNHGMKRGSVYHV HHHCCCCCCCCEEEC | 59.19 | 25381059 | |
| 357 | Phosphorylation | NHGMKRGSVYHVPLN CCCCCCCCEEECCCC | 24.44 | 25521595 | |
| 359 | Phosphorylation | GMKRGSVYHVPLNIV CCCCCCEEECCCCHH | 9.97 | 22369663 | |
| 377 | Ubiquitination | AVRDALAKAIYNNLF HHHHHHHHHHHHHHH | 35.85 | 17644757 | |
| 393 | Acetylation | WIVSRVNKSLQAFPG HHHHHHHHHHHHCCC | 50.08 | 24489116 | |
| 457 | Phosphorylation | EREKIQWTPIKYFDN HHHHCCCCCCEECCC | 9.96 | 21440633 | |
| 460 | Acetylation | KIQWTPIKYFDNKVV HCCCCCCEECCCCCH | 40.86 | 24489116 | |
| 542 | Acetylation | DGITDKNKDQLQKDL CCCCCCCHHHHHHHH | 53.22 | 24489116 | |
| 579 | Phosphorylation | ESKRRPPTAGDKIIK CHHCCCCCCHHHHHH | 46.05 | 27214570 | |
| 586 | Acetylation | TAGDKIIKSANDLVE CCHHHHHHCHHHHHH | 47.17 | 24489116 | |
| 587 | Phosphorylation | AGDKIIKSANDLVET CHHHHHHCHHHHHHH | 23.15 | 23749301 | |
| 650 | Acetylation | AYRQVFEKFVERFYL HHHHHHHHHHHHHHH | 43.15 | 24489116 | |
| 775 | Phosphorylation | GGRKERRSMSLLGYR CCCCCCCCCHHHCHH | 20.95 | 22369663 | |
| 777 | Phosphorylation | RKERRSMSLLGYRAF CCCCCCCHHHCHHHH | 22.99 | 22369663 | |
| 781 | Phosphorylation | RSMSLLGYRAFMGDY CCCHHHCHHHHHCCC | 9.95 | 22890988 | |
| 788 | Phosphorylation | YRAFMGDYLSCNESK HHHHHCCCCCCCCCC | 8.52 | 19823750 | |
| 790 | Phosphorylation | AFMGDYLSCNESKSK HHHCCCCCCCCCCCC | 14.52 | 19823750 | |
| 794 | Phosphorylation | DYLSCNESKSKGAYI CCCCCCCCCCCCCEE | 28.39 | 19823750 | |
| 806 | Phosphorylation | AYIKRQVSIKEKVIF CEEEECCCCCEEEEE | 21.43 | 23749301 | |
| 907 | Acetylation | TELITHLKRLNDKIQ HHHHHHHHHCCCCEE | 47.43 | 22865919 | |
| 932 | Phosphorylation | KKPGKLHSVKCQINE CCCCCCEEEEEEECC | 33.44 | 28889911 | |
| 940 | Phosphorylation | VKCQINESAPKYGDI EEEEECCCCCCCCCE | 45.44 | 28889911 | |
| 949 | Acetylation | PKYGDIYKSSTISVR CCCCCEEECCEEEEC | 37.96 | 24489116 | |
| 973 | Phosphorylation | HKKPRKKSSISSGYH CCCCCCCCCCCCCCC | 35.62 | 22369663 | |
| 974 | Phosphorylation | KKPRKKSSISSGYHA CCCCCCCCCCCCCCC | 35.06 | 22369663 | |
| 976 | Phosphorylation | PRKKSSISSGYHASS CCCCCCCCCCCCCCC | 21.47 | 22369663 | |
| 977 | Phosphorylation | RKKSSISSGYHASSS CCCCCCCCCCCCCCC | 41.52 | 22369663 | |
| 979 | Phosphorylation | KSSISSGYHASSSQA CCCCCCCCCCCCCCC | 9.00 | 22369663 | |
| 982 | Phosphorylation | ISSGYHASSSQATRR CCCCCCCCCCCCCCC | 19.74 | 22369663 | |
| 983 | Phosphorylation | SSGYHASSSQATRRP CCCCCCCCCCCCCCC | 27.53 | 22369663 | |
| 984 | Phosphorylation | SGYHASSSQATRRPV CCCCCCCCCCCCCCC | 22.72 | 22369663 | |
| 987 | Phosphorylation | HASSSQATRRPVSIA CCCCCCCCCCCCCHH | 21.41 | 22369663 | |
| 992 | Phosphorylation | QATRRPVSIAAAQHV CCCCCCCCHHHHHCC | 14.81 | 17330950 | |
| 1027 | Phosphorylation | NKAATRRSVPNPAST CHHHCCCCCCCCHHH | 38.34 | 29136822 | |
| 1033 | Phosphorylation | RSVPNPASTLTASQS CCCCCCHHHCCCCHH | 25.80 | 28889911 | |
| 1034 | Phosphorylation | SVPNPASTLTASQSN CCCCCHHHCCCCHHC | 30.18 | 23749301 | |
| 1036 | Phosphorylation | PNPASTLTASQSNAR CCCHHHCCCCHHCCC | 25.09 | 22369663 | |
| 1038 | Phosphorylation | PASTLTASQSNARPS CHHHCCCCHHCCCCC | 28.98 | 23749301 | |
| 1040 | Phosphorylation | STLTASQSNARPSPP HHCCCCHHCCCCCCC | 29.93 | 22369663 | |
| 1045 | Phosphorylation | SQSNARPSPPTAATR CHHCCCCCCCCCCCC | 37.65 | 23749301 | |
| 1048 | Phosphorylation | NARPSPPTAATRATP CCCCCCCCCCCCCCC | 32.10 | 29734811 | |
| 1051 | Phosphorylation | PSPPTAATRATPAAT CCCCCCCCCCCCCCC | 20.55 | 22369663 | |
| 1058 | Phosphorylation | TRATPAATPAAAAMG CCCCCCCCHHHHHCC | 18.63 | 27017623 | |
| 1066 | Phosphorylation | PAAAAMGSGRQANIP HHHHHCCCCCCCCCC | 20.09 | 30377154 | |
| 1101 | Phosphorylation | YDFPGSGSPSELPLK CCCCCCCCCCCCCCC | 27.27 | 27017623 | |
| 1103 | Phosphorylation | FPGSGSPSELPLKKG CCCCCCCCCCCCCCC | 54.16 | 21440633 | |
| 1127 | Acetylation | PSGWSLGKLLDGSKE CCCCCHHHHCCCCCC | 51.69 | 24489116 | |
| 1146 | Phosphorylation | TAYMKPHSGNNNIPT CEECCCCCCCCCCCC | 52.31 | 21551504 | |
| 1153 | Phosphorylation | SGNNNIPTPPQNRDV CCCCCCCCCCCCCCC | 43.75 | 19795423 | |
| 1174 | Phosphorylation | SVQHDNTSANVIPAA CCCCCCCCCCCHHHH | 24.89 | 21551504 | |
| 1205 | Phosphorylation | ANKMRLESDDEEANE HHHHCCCCCHHHHCC | 55.76 | 25521595 |
| 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 MYO5_YEAST !! | ||||||
* 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 MYO5_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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 AND TYR-359, ANDMASS SPECTROMETRY. | |
| "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 MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(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; TYR-359; SER-992AND SER-1205, AND MASS SPECTROMETRY. | |
| "TEDS site phosphorylation of the yeast myosins I is required forligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p."; Grosshans B.L., Groetsch H., Mukhopadhyay D., Fernandez I.M.,Pfannstiel J., Idrissi F.-Z., Lechner J., Riezman H., Geli M.I.; J. Biol. Chem. 281:11104-11114(2006). Cited for: FUNCTION, PHOSPHORYLATION AT SER-357 AND SER-777, MASS SPECTROMETRY,MUTAGENESIS OF SER-357, SUBCELLULAR LOCATION, AND INTERACTION WITHPKH1; PKH2; YPK1 AND YPK2. | |
| "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-357 AND SER-777, ANDMASS SPECTROMETRY. | |
| "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. | |
