Search Results
Overview
| Uniprot ID | P35579 |
|---|---|
| Protein Name | Myosin-9 |
| Gene Name | MYH9 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1014 | NLTEEEEKSKSLAKL |
| 1016 | TEEEEKSKSLAKLKN |
| 1024 | SLAKLKNKHEAMITD |
| 1081 | LKMQLAKKEEELQAA |
| 1099 | VEEEAAQKNMALKKI |
| 1173 | EQEVNILKKTLEEEA |
| 1174 | QEVNILKKTLEEEAK |
| 1193 | QIQEMRQKHSQAVEE |
| 1209 | AEQLEQTKRVKANLE |
| 1212 | LEQTKRVKANLEKAK |
| 1219 | KANLEKAKQTLENER |
| 1234 | GELANEVKVLLQGKG |
| 1240 | VKVLLQGKGDSEHKR |
| 1249 | DSEHKRKKVEAQLQE |
| 1274 | VRTELADKVTKLQVE |
| 1324 | LQEENRQKLSLSTKL |
| 1332 | LSLSTKLKQVEDEKN |
| 1338 | LKQVEDEKNSFREQL |
| 1352 | LEEEEEAKHNLEKQI |
| 1357 | EAKHNLEKQIATLHA |
| 1370 | HAQVADMKKKMEDSV |
| 1371 | AQVADMKKKMEDSVG |
| 1372 | QVADMKKKMEDSVGC |
| 1392 | EVKRKLQKDLEGLSQ |
| 1404 | LSQRHEEKVAAYDKL |
| 1410 | EKVAAYDKLEKTKTR |
| 1441 | QSACNLEKKQKKFDQ |
| 1445 | NLEKKQKKFDQLLAE |
| 1454 | DQLLAEEKTISAKYA |
| 1459 | EEKTISAKYAEERDR |
| 1477 | EAREKETKALSLARA |
| 1492 | LEEAMEQKAELERLN |
| 1518 | SSKDDVGKSVHELEK |
| 1525 | KSVHELEKSKRALEQ |
| 1603 | AELEDERKQRSMAVA |
| 1614 | MAVAARKKLEMDLKD |
| 1638 | KNRDEAIKQLRKLQA |
| 1642 | EAIKQLRKLQAQMKD |
| 1669 | EEILAQAKENEKKLK |
| 1724 | GALALEEKRRLEARI |
| 1775 | LERSHAQKNENARQQ |
| 1793 | QNKELKVKLQEMEGT |
| 1802 | QEMEGTVKSKYKASI |
| 1806 | GTVKSKYKASITALE |
| 1828 | EQLDNETKERQAACK |
| 1835 | KERQAACKQVRRTEK |
| 1845 | RRTEKKLKDVLLQVD |
| 1862 | RRNAEQYKDQADKAS |
| 1918 | NREVSSLKNKLRRGD |
| 1920 | EVSSLKNKLRRGDLP |
| 199 | AYVASSHKSKKDQGE |
| 201 | VASSHKSKKDQGELE |
| 202 | ASSHKSKKDQGELER |
| 228 | FGNAKTVKNDNSSRF |
| 29 | AQADWAAKKLVWVPS |
| 299 | LLLEPYNKYRFLSNG |
| 30 | QADWAAKKLVWVPSD |
| 403 | VGRDYVQKAQTKEQA |
| 435 | WLVLRINKALDKTKR |
| 540 | WFPKATDKSFVEKVM |
| 555 | QEQGTHPKFQKPKQL |
| 560 | HPKFQKPKQLKDKAD |
| 565 | KPKQLKDKADFCIIH |
| 613 | KFVSELWKDVDRIIG |
| 651 | RTVGQLYKEQLAKLM |
| 678 | CIIPNHEKKAGKLDP |
| 74 | VNKDDIQKMNPPKFS |
| 760 | LYRIGQSKVFFRAGV |
| 79 | IQKMNPPKFSKVEDM |
| 8 | MAQQAADKYLYVDKN |
| 821 | RNCAAYLKLRNWQWW |
| 835 | WRLFTKVKPLLQVSR |
| 856 | AKEEELVKVREKQLA |
| 860 | ELVKVREKQLAAENR |
| 910 | RARLTAKKQELEEIC |
| 961 | EEESARQKLQLEKVT |
| 966 | RQKLQLEKVTTEAKL |
| 972 | EKVTTEAKLKKLEEE |
| 974 | VTTEAKLKKLEEEQI |
| 975 | TTEAKLKKLEEEQII |
Function
Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Promotes cell motility in conjunction with S100A4 (PubMed:16707441). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (PubMed:20052411)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0015629 | actin cytoskeleton |
| Cellular Component | GO:0042641 | actomyosin |
| Cellular Component | GO:0005826 | actomyosin contractile ring |
| Cellular Component | GO:0005912 | adherens junction |
| Cellular Component | GO:0005903 | brush border |
| Cellular Component | GO:0031252 | cell leading edge |
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0032154 | cleavage furrow |
| Cellular Component | GO:0060473 | cortical granule |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0009898 | cytoplasmic side of plasma membrane |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0001772 | immunological synapse |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0032982 | myosin filament |
| Cellular Component | GO:0016460 | myosin II complex |
| Cellular Component | GO:0097513 | myosin II filament |
| Cellular Component | GO:0031594 | neuromuscular junction |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0001726 | ruffle |
| Cellular Component | GO:0005819 | spindle |
| Cellular Component | GO:0001725 | stress fiber |
| Cellular Component | GO:0001931 | uropod |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0043531 | ADP binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0005516 | calmodulin binding |
| Molecular Function | GO:0003774 | cytoskeletal motor activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0005178 | integrin binding |
| Molecular Function | GO:0000146 | microfilament motor activity |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0043495 | protein-membrane adaptor activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0001618 | virus receptor activity |
| Biological Process | GO:0030036 | actin cytoskeleton organization |
| Biological Process | GO:0030048 | actin filament-based movement |
| Biological Process | GO:0031032 | actomyosin structure organization |
| Biological Process | GO:0001525 | angiogenesis |
| Biological Process | GO:0043534 | blood vessel endothelial cell migration |
| Biological Process | GO:0060471 | cortical granule exocytosis |
| Biological Process | GO:0032506 | cytokinetic process |
| Biological Process | GO:0007229 | integrin-mediated signaling pathway |
| Biological Process | GO:0050900 | leukocyte migration |
| Biological Process | GO:0032418 | lysosome localization |
| Biological Process | GO:0006509 | membrane protein ectodomain proteolysis |
| Biological Process | GO:0030224 | monocyte differentiation |
| Biological Process | GO:1903919 | negative regulation of actin filament severing |
| Biological Process | GO:0006911 | phagocytosis, engulfment |
| Biological Process | GO:0001778 | plasma membrane repair |
| Biological Process | GO:0070527 | platelet aggregation |
| Biological Process | GO:0030220 | platelet formation |
| Biological Process | GO:1903923 | positive regulation of protein processing in phagocytic vesicle |
| Biological Process | GO:0015031 | protein transport |
| Biological Process | GO:0045055 | regulated exocytosis |
| Biological Process | GO:0008360 | regulation of cell shape |
| Biological Process | GO:1905684 | regulation of plasma membrane repair |
| Biological Process | GO:0046718 | symbiont entry into host cell |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[6] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[7] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[8] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.
[9] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.