| UniProt ID | MYO2_YEAST | |
|---|---|---|
| UniProt AC | P19524 | |
| Protein Name | Myosin-2 | |
| Gene Name | MYO2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1574 | |
| Subcellular Localization | Bud neck . Bud tip . Concentrates to sites of polarized growth, namely to the bud tip during S and G2 phases of the cell cycle and to the bud neck during cytokinesis. | |
| Protein Description | Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Essential for the delivery of secretory vesicles to sites of active growth during bud emergence and cytokinesis. Required for segregation and inheritance of peroxisomes, late Golgi compartments, mitochondria and the vacuole to the daughter cell during cell division. Also required for correct alignment of the spindle during mitosis.. | |
| Protein Sequence | MSFEVGTRCWYPHKELGWIGAEVIKNEFNDGKYHLELQLEDDEIVSVDTKDLNNDKDQSLPLLRNPPILEATEDLTSLSYLNEPAVLHAIKQRYSQLNIYTYSGIVLIATNPFDRVDQLYTQDMIQAYAGKRRGELEPHLFAIAEEAYRLMKNDKQNQTIVVSGESGAGKTVSAKYIMRYFASVEEENSATVQHQVEMSETEQKILATNPIMEAFGNAKTTRNDNSSRFGKYLEILFDKDTSIIGARIRTYLLERSRLVYQPPIERNYHIFYQLMAGLPAQTKEELHLTDASDYFYMNQGGDTKINGIDDAKEYKITVDALTLVGITKETQHQIFKILAALLHIGNIEIKKTRNDASLSADEPNLKLACELLGIDAYNFAKWVTKKQIITRSEKIVSNLNYSQALVAKDSVAKFIYSALFDWLVENINTVLCNPAVNDQISSFIGVLDIYGFEHFEKNSFEQFCINYANEKLQQEFNQHVFKLEQEEYVKEEIEWSFIEFNDNQPCIDLIENKLGILSLLDEESRLPAGSDESWTQKLYQTLDKSPTNKVFSKPRFGQTKFIVSHYALDVAYDVEGFIEKNRDTVSDGHLEVLKASTNETLINILEGLEKAAKKLEEAKKLELEQAGSKKPGPIRTVNRKPTLGSMFKQSLIELMNTINSTNVHYIRCIKPNADKEAWQFDNLMVLSQLRACGVLETIRISCAGFPSRWTFEEFVLRYYILIPHEQWDLIFKKKETTEEDIISVVKMILDATVKDKSKYQIGNTKIFFKAGMLAYLEKLRSNKMHNSIVMIQKKIRAKYYRKQYLQISQAIKYLQNNIKGFIIRQRVNDEMKVNCATLLQAAYRGHSIRANVFSVLRTITNLQKKIRKELKQRQLKQEHEYNAAVTIQSKVRTFEPRSRFLRTKKDTVVVQSLIRRRAAQRKLKQLKADAKSVNHLKEVSYKLENKVIELTQNLASKVKENKEMTERIKELQVQVEESAKLQETLENMKKEHLIDIDNQKSKDMELQKTIENNLQSTEQTLKDAQLELEDMVKQHDELKEESKKQLEELEQTKKTLVEYQTLNGDLQNEVKSLKEEIARLQTAMSLGTVTTSVLPQTPLKDVMGGGASNFNNMMLENSDLSPNDLNLKSRSTPSSGNNHIDSLSVDRENGVNATQINEELYRLLEDTEILNQEITEGLLKGFEVPDAGVAIQLSKRDVVYPARILIIVLSEMWRFGLTKQSESFLAQVLTTIQKVVTQLKGNDLIPSGVFWLANVRELYSFVVFALNSILTEETFKNGMTDEEYKEYVSLVTELKDDFEALSYNIYNIWLKKLQKQLQKKAINAVVISESLPGFSAGETSGFLNKIFANTEEYTMDDILTFFNSIYWCMKSFHIENEVFHAVVTTLLNYVDAICFNELIMKRNFLSWKRGLQLNYNVTRLEEWCKTHGLTDGTECLQHLIQTAKLLQVRKYTIEDIDILRGICYSLTPAQLQKLISQYQVADYESPIPQEILRYVADIVKKEAALSSSGNDSKGHEHSSSIFITPETGPFTDPFSLIKTRKFDQVEAYIPAWLSLPSTKRIVDLVAQQVVQDGH | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSFEVGTRC ------CCCCCCCCC | 41.22 | 22814378 | |
| 56 | Acetylation | TKDLNNDKDQSLPLL CHHCCCCCCCCCCHH | 60.84 | 24489116 | |
| 120 | Phosphorylation | FDRVDQLYTQDMIQA CCCHHHHCHHHHHHH | 9.20 | 28132839 | |
| 128 | Phosphorylation | TQDMIQAYAGKRRGE HHHHHHHHCCCCCCC | 10.26 | 28132839 | |
| 155 | Ubiquitination | YRLMKNDKQNQTIVV HHHHHCCCCCCEEEE | 61.62 | 23749301 | |
| 159 | Phosphorylation | KNDKQNQTIVVSGES HCCCCCCEEEEECCC | 24.24 | 22369663 | |
| 163 | Phosphorylation | QNQTIVVSGESGAGK CCCEEEEECCCCCCC | 26.42 | 22369663 | |
| 166 | Phosphorylation | TIVVSGESGAGKTVS EEEEECCCCCCCCCC | 37.15 | 22369663 | |
| 170 | Ubiquitination | SGESGAGKTVSAKYI ECCCCCCCCCCHHHH | 45.26 | 23749301 | |
| 219 | Ubiquitination | MEAFGNAKTTRNDNS HHHHCCCCCCCCCCC | 55.20 | 24961812 | |
| 231 | Ubiquitination | DNSSRFGKYLEILFD CCCCCHHHHHHHHCC | 43.90 | 17644757 | |
| 239 | Ubiquitination | YLEILFDKDTSIIGA HHHHHCCCCCCHHHH | 56.42 | 17644757 | |
| 312 | Succinylation | INGIDDAKEYKITVD ECCCCCCCCEEEEEE | 69.44 | 23954790 | |
| 366 | Ubiquitination | SADEPNLKLACELLG CCCCCCHHHHHHHHC | 40.45 | 17644757 | |
| 513 | Ubiquitination | CIDLIENKLGILSLL CHHHHHHHHCHHHHC | 34.99 | 22106047 | |
| 518 | Phosphorylation | ENKLGILSLLDEESR HHHHCHHHHCCCCCC | 25.60 | 21440633 | |
| 545 | Phosphorylation | LYQTLDKSPTNKVFS HHHHHCCCCCCCCCC | 36.30 | 17330950 | |
| 547 | Phosphorylation | QTLDKSPTNKVFSKP HHHCCCCCCCCCCCC | 55.55 | 30377154 | |
| 564 | Phosphorylation | GQTKFIVSHYALDVA CCCEEEEEEHHHHHH | 13.13 | 30377154 | |
| 566 | Phosphorylation | TKFIVSHYALDVAYD CEEEEEEHHHHHHHC | 11.01 | 30377154 | |
| 572 | Phosphorylation | HYALDVAYDVEGFIE EHHHHHHHCCHHHHH | 21.99 | 30377154 | |
| 660 | Phosphorylation | ELMNTINSTNVHYIR HHHHHHCCCCCEEEE | 19.94 | 24909858 | |
| 719 | Phosphorylation | EEFVLRYYILIPHEQ HHHHHHHHEECCHHH | 5.26 | 23749301 | |
| 732 | Ubiquitination | EQWDLIFKKKETTEE HHHHEEEECCCCCHH | 56.81 | 23749301 | |
| 754 | Acetylation | MILDATVKDKSKYQI HHHHCCCCCHHHCCC | 55.90 | 24489116 | |
| 765 | Acetylation | KYQIGNTKIFFKAGM HCCCCCEEEHHHHHH | 41.33 | 24489116 | |
| 778 | Acetylation | GMLAYLEKLRSNKMH HHHHHHHHHHCCCCC | 46.75 | 24489116 | |
| 907 | Phosphorylation | FLRTKKDTVVVQSLI HCCCCCCHHHHHHHH | 24.87 | 21126336 | |
| 932 | Phosphorylation | QLKADAKSVNHLKEV HHHCCCHHCCHHHHH | 29.85 | 27017623 | |
| 1052 | Phosphorylation | QLEELEQTKKTLVEY HHHHHHHHHHHHHHH | 25.73 | 27017623 | |
| 1072 | Phosphorylation | DLQNEVKSLKEEIAR HHHHHHHHHHHHHHH | 50.26 | 23749301 | |
| 1097 | Phosphorylation | TTSVLPQTPLKDVMG CCCCCCCCCCCCCCC | 28.75 | 20377248 | |
| 1118 | Phosphorylation | NNMMLENSDLSPNDL HHCCCCCCCCCCCCC | 30.47 | 25521595 | |
| 1121 | Phosphorylation | MLENSDLSPNDLNLK CCCCCCCCCCCCCCC | 27.01 | 25521595 | |
| 1129 | Phosphorylation | PNDLNLKSRSTPSSG CCCCCCCCCCCCCCC | 34.33 | 28889911 | |
| 1131 | Phosphorylation | DLNLKSRSTPSSGNN CCCCCCCCCCCCCCC | 52.33 | 23749301 | |
| 1132 | Phosphorylation | LNLKSRSTPSSGNNH CCCCCCCCCCCCCCC | 26.53 | 21082442 | |
| 1134 | Phosphorylation | LKSRSTPSSGNNHID CCCCCCCCCCCCCCC | 51.47 | 21082442 | |
| 1135 | Phosphorylation | KSRSTPSSGNNHIDS CCCCCCCCCCCCCCC | 46.90 | 21082442 | |
| 1142 | Phosphorylation | SGNNHIDSLSVDREN CCCCCCCCCEEECCC | 23.18 | 19779198 | |
| 1144 | Phosphorylation | NNHIDSLSVDRENGV CCCCCCCEEECCCCC | 26.39 | 28889911 | |
| 1154 | Phosphorylation | RENGVNATQINEELY CCCCCCHHHHHHHHH | 25.44 | 19779198 | |
| 1221 | Phosphorylation | RFGLTKQSESFLAQV HCCCCCCCHHHHHHH | 36.44 | 19795423 | |
| 1223 | Phosphorylation | GLTKQSESFLAQVLT CCCCCCHHHHHHHHH | 30.70 | 19795423 | |
| 1230 | Phosphorylation | SFLAQVLTTIQKVVT HHHHHHHHHHHHHHH | 24.01 | 19823750 | |
| 1231 | Phosphorylation | FLAQVLTTIQKVVTQ HHHHHHHHHHHHHHH | 19.76 | 19795423 | |
| 1330 | Phosphorylation | NAVVISESLPGFSAG CEEEEECCCCCCCCC | 32.83 | 30377154 | |
| 1335 | Phosphorylation | SESLPGFSAGETSGF ECCCCCCCCCCCCHH | 41.08 | 30377154 | |
| 1339 | Phosphorylation | PGFSAGETSGFLNKI CCCCCCCCCHHHHHH | 32.98 | 30377154 | |
| 1340 | Phosphorylation | GFSAGETSGFLNKIF CCCCCCCCHHHHHHH | 24.20 | 21551504 | |
| 1364 | Phosphorylation | DILTFFNSIYWCMKS HHHHHHHHHHHHHHH | 16.34 | 28889911 | |
| 1501 | Ubiquitination | YVADIVKKEAALSSS HHHHHHHHHHHHHCC | 41.51 | 23749301 | |
| 1506 | Phosphorylation | VKKEAALSSSGNDSK HHHHHHHHCCCCCCC | 20.10 | 30377154 | |
| 1507 | Phosphorylation | KKEAALSSSGNDSKG HHHHHHHCCCCCCCC | 43.01 | 28889911 | |
| 1508 | Phosphorylation | KEAALSSSGNDSKGH HHHHHHCCCCCCCCC | 37.93 | 25752575 | |
| 1512 | Phosphorylation | LSSSGNDSKGHEHSS HHCCCCCCCCCCCCC | 44.53 | 30377154 | |
| 1518 | Phosphorylation | DSKGHEHSSSIFITP CCCCCCCCCCEEECC | 23.85 | 19779198 | |
| 1559 | Ubiquitination | WLSLPSTKRIVDLVA HHCCCCCHHHHHHHH | 44.45 | 17644757 |
| 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 MYO2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MYO2_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 MYO2_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-545; THR-1097; SER-1121;SER-1135 AND SER-1144, AND MASS 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-545, AND MASSSPECTROMETRY. | |
