Myosin-9 (MYH9)
The protein contains 1960 amino acids for an estimated molecular weight of 226532 Da.
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). (updated: June 2, 2021)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
Biological Process
Actin cytoskeleton reorganization
Actin filament-based movement
Actomyosin structure organization
Angiogenesis
Axon guidance
Blood vessel endothelial cell migration
Cortical granule exocytosis
Cytokinesis
Cytokinetic process
Ephrin receptor signaling pathway
Establishment of meiotic spindle localization
Establishment of T cell polarity
In utero embryonic development
Integrin-mediated signaling pathway
Leukocyte migration
Lysosome localization
Meiotic spindle organization
Membrane protein ectodomain proteolysis
Microtubule-based movement
Monocyte differentiation
Myoblast fusion
Negative regulation of actin filament severing
Negative regulation of inflammatory response to antigenic stimulus
Phagocytosis, engulfment
Plasma membrane repair
Platelet aggregation
Platelet formation
Positive regulation of protein processing in phagocytic vesicle
Protein transport
Regulated exocytosis
Regulation of cell shape
Regulation of plasma membrane repair
Termination of G-protein coupled receptor signaling pathway
Uropod organization
Cellular Component
Actin cytoskeleton
Actomyosin
Actomyosin contractile ring
Adherens junction
Brush border
Cell leading edge
Cell-cell adherens junction
Cleavage furrow
Cortical cytoskeleton
Cortical granule
Cytoplasm
Cytoplasmic side of plasma membrane
Cytosol
Extracellular exosome
Extracellular matrix
Focal adhesion
Immunological synapse
Membrane
Myosin II complex
Myosin II filament
Neuromuscular junction
Nucleus
Obsolete cell
Plasma membrane
Protein complex
Protein-containing complex
Ruffle
Spindle
Stress fiber
Uropod
Molecular Function
Actin binding
Actin filament binding
Actin-dependent ATPase activity
ADP binding
ATP binding
ATPase
Cadherin binding
Calmodulin binding
Identical protein binding
Integrin binding
Microfilament motor activity
Microtubule binding
Microtubule motor activity
Motor activity
Poly(A) RNA binding
Protein domain specific binding
Protein homodimerization activity
Protein-membrane adaptor activity
RNA binding
The reference OMIM entry for this protein is 153640
Fechtner syndrome; ftns
Macrothrombocytopenia, nephritis, deafness, and leukocyte inclusions
Alport syndrome with macrothrombocytopenia, formerly; apsm, formerly
A number sign (#) is used with entry because Fechtner syndrome is caused by heterozygous mutation in the gene encoding nonmuscle myosin heavy chain-9 (MYH9; 160775) on chromosome 22q11.
DESCRIPTION
Fechtner syndrome is an autosomal dominant disorder characterized by the triad of thrombocytopenia, giant platelets, and Dohle body-like inclusions in peripheral blood leukocytes, with the additional features of nephritis, hearing loss, and eye abnormalities, mostly cataracts (Peterson et al., 1985). There are several other disorders caused by mutation in the MYH9 gene that share overlapping features with Fechtner syndrome. May-Hegglin anomaly (155100) is characterized by the triad of thrombocytopenia, giant platelets, and Dohle body-like inclusions in peripheral blood leukocytes. Epstein syndrome (153650) has the platelet defect, deafness, and nephritis, but does not have cataract and lacks leukocyte inclusion bodies on classic staining of peripheral blood smears. The findings of nephritis, hearing loss, and occasional cataracts in Fechtner and Epstein syndromes are reminiscent of Alport syndrome (see 301050). Sebastian syndrome (605249) is similar to May-Hegglin anomaly, but has a different ultrastructural appearance of the leukocyte inclusions. Seri et al. (2003) suggested that these 4 disorders, May-Hegglin, Sebastian, Epstein, and Fechtner syndromes, are not distinct entities, but rather represent a single disorder with a continuous clinical spectrum, for which they proposed the term 'MYH9-related disease.' However, other disorders, e.g., macrothrombocytopenia and progressive sensorineural deafness (600208) and a form of nonsyndromic deafness (DFNA17; 603622), are also caused by mutation in the MYH9 gene.CLINICAL FEATURES
Peterson et al. (1985) reported a family in which 8 members of 4 generations showed nephritis, deafness, congenital cataracts, macrothrombocytopenia, and leukocyte inclusions in various combinations. The authors referred to the disorder as the 'Fechtner syndrome,' presumably from the surname of the family. The family differed from others reported, such as families with Epstein syndrome, in that their hematologic abnormalities included not only macrothrombocytopenia but also small, pale blue cytoplasmic inclusions in the neutrophils and eosinophils. Light microscopic appearance of the inclusions resembled that of toxic Dohle bodies and inclusions of May-Hegglin anomaly, but their ultrastructural appearance was unique. Deafness was high-tone sensorineural. Renal disease ranged from microscopic hematuria to end-stage renal failure necessitating dialysis and kidney transplantation. All affected adults had cataracts. Gershoni-Baruch et al. (1988) reported a second family with Fechtner syndrome; 16 members were affected. The authors noted that since the hematologic abnormalities are a consistent feature of the syndrome and seem to be present at birth, they would presumably permit prenatal diagnosis by detection of the changes in fetal blood samples. Heynen et al. (1988) described the Fechtner syndrome in a female patient who had developed multiple ecchymoses from the time she started walking at the age of 1 year, due to severe thrombocytopenia. Hearing problems developing at the age of 8 years progressed to almost complete deafness. The blood smear showed giant platelets the size of granulocytes. The patient had moderate proteinuria, but there were no abnormalities in the urinary sediment or in renal fu ... More on the omim web site
July 1, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
April 10, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 20, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 153640 was added.