| UniProt ID | MYH10_MOUSE | |
|---|---|---|
| UniProt AC | Q61879 | |
| Protein Name | Myosin-10 | |
| Gene Name | Myh10 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 1976 | |
| Subcellular Localization | Cell projection, lamellipodium. Colocalizes with MCC at the leading edge of migrating cells.. | |
| Protein Description | Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9 (By similarity). Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.. | |
| Protein Sequence | MAQRTGLEDPERYLFVDRAVIYNPATQADWTAKKLVWIPSERHGFEAASIKEERGDEVMVELAENGKKAMVNKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRGGPISFSSSRSGRRQLHIEGASLELSDDDTESKTSDVNDTQPPQSE | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MAQRTGLEDPER ---CCCCCCCCCHHH | 33.76 | 29514104 | |
| 13 | Phosphorylation | GLEDPERYLFVDRAV CCCCHHHEEEEEEEE | 11.66 | 29514104 | |
| 18 | Methylation | ERYLFVDRAVIYNPA HHEEEEEEEEEECCC | 26.00 | 24129315 | |
| 22 | Phosphorylation | FVDRAVIYNPATQAD EEEEEEEECCCCCCC | 14.43 | 18563927 | |
| 83 | Ubiquitination | IQKMNPPKFSKVEDM HHHCCCCCCCCHHHH | 64.62 | - | |
| 85 | Phosphorylation | KMNPPKFSKVEDMAE HCCCCCCCCHHHHHH | 41.75 | 29550500 | |
| 95 | Glutathionylation | EDMAELTCLNEASVL HHHHHHHHCCHHHHH | 6.33 | 24333276 | |
| 185 | Phosphorylation | GESGAGKTENTKKVI CCCCCCCCCCHHHHH | 33.28 | 17203969 | |
| 188 | Phosphorylation | GAGKTENTKKVIQYL CCCCCCCHHHHHHHH | 26.47 | 17203969 | |
| 190 | Ubiquitination | GKTENTKKVIQYLAH CCCCCHHHHHHHHHH | 42.40 | - | |
| 194 | Phosphorylation | NTKKVIQYLAHVASS CHHHHHHHHHHHHHH | 8.50 | - | |
| 200 | Phosphorylation | QYLAHVASSHKGRKD HHHHHHHHHCCCCCC | 31.70 | 26824392 | |
| 201 | Phosphorylation | YLAHVASSHKGRKDH HHHHHHHHCCCCCCC | 21.34 | 26824392 | |
| 232 | Ubiquitination | LESFGNAKTVKNDNS HHHHCCCCCCCCCCC | 58.83 | - | |
| 240 | Phosphorylation | TVKNDNSSRFGKFIR CCCCCCCCCCCEEEE | 37.57 | 26824392 | |
| 244 | Acetylation | DNSSRFGKFIRINFD CCCCCCCEEEEEEEE | 34.60 | 133157 | |
| 352 | Phosphorylation | SMLKVVSSVLQFGNI HHHHHHHHHHHHCCC | 18.42 | 22802335 | |
| 360 | Phosphorylation | VLQFGNISFKKERNT HHHHCCCEEECCCCC | 34.71 | 22802335 | |
| 371 | Phosphorylation | ERNTDQASMPENTVA CCCCCCCCCCHHHHH | 29.27 | 26824392 | |
| 407 | Phosphorylation | RIKVGRDYVQKAQTK CCCCCHHHHHHHCCH | 11.92 | 25195567 | |
| 410 | Malonylation | VGRDYVQKAQTKEQA CCHHHHHHHCCHHHH | 32.20 | 26320211 | |
| 410 | Ubiquitination | VGRDYVQKAQTKEQA CCHHHHHHHCCHHHH | 32.20 | - | |
| 442 | Acetylation | WLVHRINKALDRTKR HHHHHHHHHHHHHHH | 48.21 | - | |
| 442 | Malonylation | WLVHRINKALDRTKR HHHHHHHHHHHHHHH | 48.21 | 26320211 | |
| 447 | Phosphorylation | INKALDRTKRQGASF HHHHHHHHHHCCCCE | 30.19 | 18779572 | |
| 559 | Phosphorylation | KLVQEQGSHSKFQKP HHHHHCCCCCCCCCC | 25.04 | 26824392 | |
| 561 | Phosphorylation | VQEQGSHSKFQKPRQ HHHCCCCCCCCCCCC | 36.54 | 28066266 | |
| 576 | Glutathionylation | LKDKADFCIIHYAGK CCCCCCEEEEECCCC | 2.69 | 24333276 | |
| 587 | Ubiquitination | YAGKVDYKADEWLMK CCCCCCCCCCHHHHH | 44.92 | - | |
| 587 | Acetylation | YAGKVDYKADEWLMK CCCCCCCCCCHHHHH | 44.92 | 66700227 | |
| 641 | Phosphorylation | MTETAFGSAYKTKKG CCHHHCCCCHHCCCC | 23.21 | 26824392 | |
| 689 | Ubiquitination | NHEKRAGKLDPHLVL CCHHHCCCCCHHHHH | 49.05 | - | |
| 728 | Phosphorylation | FQEFRQRYEILTPNA HHHHHHHHCCCCCCC | 10.05 | 22817900 | |
| 732 | Phosphorylation | RQRYEILTPNAIPKG HHHHCCCCCCCCCCC | 21.84 | - | |
| 761 | Phosphorylation | LELDPNLYRIGQSKI HCCCCCCEEECCCCH | 13.56 | 29514104 | |
| 857 | Ubiquitination | QEEELQAKDEELLKV CHHHHHHCCHHHHHH | 53.35 | - | |
| 929 | Phosphorylation | EILHDLESRVEEEEE HHHHHHHHHHHHHHH | 49.26 | 26824392 | |
| 1011 | Glutathionylation | MEDRIAECSSQLAEE HHHHHHHHHHHHHHH | 3.33 | 24333276 | |
| 1013 | Phosphorylation | DRIAECSSQLAEEEE HHHHHHHHHHHHHHH | 40.65 | 26824392 | |
| 1037 | Phosphorylation | NKQEVMISDLEERLK CCHHHHHHHHHHHHH | 20.32 | 20495213 | |
| 1129 | Phosphorylation | ELQEDFESEKASRNK HHHHHHHHHHHHHHH | 44.37 | 26824392 | |
| 1145 | Phosphorylation | EKQKRDLSEELEALK HHHHHHHHHHHHHHH | 33.06 | 26239621 | |
| 1153 | Phosphorylation | EELEALKTELEDTLD HHHHHHHHHHHHHHC | 46.80 | 26239621 | |
| 1158 | Phosphorylation | LKTELEDTLDTTAAQ HHHHHHHHHCHHHHH | 19.70 | 26239621 | |
| 1203 | Phosphorylation | DMRQRHATALEELSE HHHHHHHHHHHHHHH | 26.17 | 26824392 | |
| 1241 | Acetylation | KELACEVKVLQQVKA HHHHHHHHHHHHHHC | 18.22 | 23806337 | |
| 1293 | Phosphorylation | QNELDNVSTLLEEAE HHHHHHHHHHHHHHH | 21.42 | 26824392 | |
| 1294 | Phosphorylation | NELDNVSTLLEEAEK HHHHHHHHHHHHHHH | 30.95 | 26824392 | |
| 1301 | Acetylation | TLLEEAEKKGIKFAK HHHHHHHHHCCCHHH | 64.45 | 23806337 | |
| 1335 | Phosphorylation | TRQKLNLSSRIRQLE HHHHCCHHHHHHHHH | 19.25 | 29514104 | |
| 1371 | Phosphorylation | KQVLALQSQLADTKK HHHHHHHHHHHHHHH | 28.19 | 28059163 | |
| 1377 | Acetylation | QSQLADTKKKVDDDL HHHHHHHHHHHCCCC | 51.66 | 19850995 | |
| 1405 | Phosphorylation | LKDVEALSQRLEEKV HHHHHHHHHHHHHHH | 21.94 | 26824392 | |
| 1415 | Phosphorylation | LEEKVLAYDKLEKTK HHHHHHHHHHHHHHH | 14.95 | 17242355 | |
| 1464 | Phosphorylation | LAEEKGISARYAEER HHHHHCCCHHHHHHH | 18.50 | 18779572 | |
| 1487 | Phosphorylation | EKETKALSLARALEE HHHHHHHHHHHHHHH | 25.50 | 27149854 | |
| 1520 | Acetylation | MEDLMSSKDDVGKNV HHHHHCCCCHHHHHH | 51.12 | 7713333 | |
| 1533 | Phosphorylation | NVHELEKSKRALEQQ HHHHHHHHHHHHHHH | 20.28 | 25159016 | |
| 1546 | Phosphorylation | QQVEEMRTQLEELED HHHHHHHHHHHHHHH | 35.87 | 26239621 | |
| 1645 | Acetylation | KARDEVIKQLRKLQA HHHHHHHHHHHHHHH | 48.75 | - | |
| 1684 | Phosphorylation | ESEKKLKSLEAEILQ HHHHHHHHHHHHHHH | 41.71 | 29899451 | |
| 1720 | Phosphorylation | LADEIANSASGKSAL HHHHHHHCCCCHHHH | 18.13 | 26824392 | |
| 1750 | Phosphorylation | EELEEEQSNMELLND HHHHHHHHHHHHHHH | 41.23 | 26824392 | |
| 1922 | Phosphorylation | EGLSREVSTLKNRLR HHHHHHHHHHHHHHH | 24.22 | 27149854 | |
| 1930 | Methylation | TLKNRLRRGGPISFS HHHHHHHCCCCCCCC | 60.04 | 24129315 | |
| 1935 | Phosphorylation | LRRGGPISFSSSRSG HHCCCCCCCCCCCCC | 23.39 | 26824392 | |
| 1937 | Phosphorylation | RGGPISFSSSRSGRR CCCCCCCCCCCCCCE | 22.18 | 23527152 | |
| 1938 | Phosphorylation | GGPISFSSSRSGRRQ CCCCCCCCCCCCCEE | 27.97 | 23684622 | |
| 1939 | Phosphorylation | GPISFSSSRSGRRQL CCCCCCCCCCCCEEE | 29.30 | 26824392 | |
| 1940 | Methylation | PISFSSSRSGRRQLH CCCCCCCCCCCEEEE | 45.11 | 24129315 | |
| 1941 | Phosphorylation | ISFSSSRSGRRQLHI CCCCCCCCCCEEEEE | 38.30 | 29514104 | |
| 1952 | Phosphorylation | QLHIEGASLELSDDD EEEEEEEEEECCCCC | 32.98 | 25521595 | |
| 1956 | Phosphorylation | EGASLELSDDDTESK EEEEEECCCCCCCCC | 29.62 | 27087446 | |
| 1960 | Phosphorylation | LELSDDDTESKTSDV EECCCCCCCCCCCCC | 49.50 | 24925903 | |
| 1962 | Phosphorylation | LSDDDTESKTSDVND CCCCCCCCCCCCCCC | 43.24 | 24925903 | |
| 1964 | Phosphorylation | DDDTESKTSDVNDTQ CCCCCCCCCCCCCCC | 39.16 | 25521595 | |
| 1965 | Phosphorylation | DDTESKTSDVNDTQP CCCCCCCCCCCCCCC | 43.21 | 27087446 | |
| 1970 | Phosphorylation | KTSDVNDTQPPQSE- CCCCCCCCCCCCCC- | 37.46 | 27087446 | |
| 1975 | Phosphorylation | NDTQPPQSE------ CCCCCCCCC------ | 100.00 | 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 MYH10_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MYH10_MOUSE !! | ||||||
* 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 MYH10_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, AND MASSSPECTROMETRY. | |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1952 AND SER-1956, ANDMASS SPECTROMETRY. | |
| "Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1952 AND SER-1956, ANDMASS SPECTROMETRY. | |
