InnateDB: Systems Biology of the Innate Immune Response

Homo sapiens Protein: MYH9

Summary

InnateDB Protein

IDBP-5779.6

Last Modified

2014-10-13 [Report errors or provide feedback]

Gene Symbol

MYH9

Protein Name

myosin, heavy chain 9, non-muscle

Synonyms

BDPLT6; DFNA17; EPSTS; FTNS; MHA; NMHC-II-A; NMMHC-IIA; NMMHCA;

Species

Homo sapiens

Ensembl Protein

ENSP00000216181

InnateDB Gene

IDBG-5777 (MYH9)

Protein Structure

UniProt Annotation

Function

Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10. {ECO:0000269PubMed:20052411}.

Subcellular Localization

Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Note=Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells. {ECO:0000269PubMed:20052411}.

Disease Associations

May-Hegglin anomaly (MHA) [MIM:155100]: A disorder characterized by thrombocytopenia, giant platelets and Dohle body- like inclusions in peripheral blood leukocytes. appearing as highly parallel paracrystalline bodies. {ECO:0000269PubMed:10973260, ECO:0000269PubMed:12533692, ECO:0000269PubMed:12792306}. Note=The disease is caused by mutations affecting the gene represented in this entry.Sebastian syndrome (SBS) [MIM:605249]: Autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are smaller and less organized than in May-Hegglin anomaly. {ECO:0000269PubMed:12533692}. Note=The disease is caused by mutations affecting the gene represented in this entry.Fechtner syndrome (FTNS) [MIM:153640]: Autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are small and poorly organized. Additionally, FTNS is distinguished by Alport-like clinical features of sensorineural deafness, cataracts and nephritis. {ECO:0000269PubMed:10973259, ECO:0000269PubMed:11776386, ECO:0000269PubMed:12533692, ECO:0000269PubMed:12792306}. Note=The disease is caused by mutations affecting the gene represented in this entry.Alport syndrome, with macrothrombocytopenia (APSM) [MIM:153650]: An autosomal dominant disorder characterized by the association of ocular lesions, sensorineural hearing loss and nephritis (Alport syndrome) with platelet defects. {ECO:0000269PubMed:11590545}. Note=The disease is caused by mutations affecting the gene represented in this entry.Epstein syndrome (EPS) [MIM:153650]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy, sensorineural hearing loss and nephritis. {ECO:0000269PubMed:11752022, ECO:0000269PubMed:11935325, ECO:0000269PubMed:12533692, ECO:0000269PubMed:12792306, ECO:0000269PubMed:16969870}. Note=The disease is caused by mutations affecting the gene represented in this entry.Deafness, autosomal dominant, 17 (DFNA17) [MIM:603622]: A form of deafness characterized by progressive high frequency hearing impairment and cochleosaccular degeneration. {ECO:0000269PubMed:11023810}. Note=The disease is caused by mutations affecting the gene represented in this entry.Macrothrombocytopenia and progressive sensorineural deafness (MPSD) [MIM:600208]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy and progressive sensorineural hearing loss without renal dysfunction. {ECO:0000269PubMed:12621333}. Note=The disease is caused by mutations affecting the gene represented in this entry.Note=Subjects with mutations in the motor domain of MYH9 present with severe thrombocytopenia and develop nephritis and deafness before the age of 40 years, while those with mutations in the tail domain have a much lower risk of noncongenital complications and significantly higher platelet counts. The clinical course of patients with mutations in the four most frequently affected residues of MYH9 (responsible for 70% of MYH9- related cases) were evaluated. Mutations at residue 1933 do not induce kidney damage or cataracts and cause deafness only in the elderly, those in position 702 result in severe thrombocytopenia and produce nephritis and deafness at a juvenile age, while alterations at residue 1424 or 1841 result in intermediate clinical pictures.Note=Genetic variations in MYH9 are associated with non- diabetic end stage renal disease (ESRD).

Tissue Specificity

In the kidney, expressed in the glomeruli. Also expressed in leukocytes. {ECO:0000269PubMed:11752022, ECO:0000269PubMed:1912569}.

Comments

Interactions

Number of Interactions

This gene and/or its encoded proteins are associated with 135 experimentally validated interaction(s) in this database.
They are also associated with 10 interaction(s) predicted by orthology.

Experimentally validated
Total	135 [view]
Protein-Protein	133 [view]
Protein-DNA	2 [view]
Protein-RNA	0
DNA-DNA	0
RNA-RNA	0
DNA-RNA	0

Predicted by orthology
Total	10 [view]

Gene Ontology

Molecular Function

Accession	GO Term
GO:0000146	microfilament motor activity
GO:0000166	nucleotide binding
GO:0003700	sequence-specific DNA binding transcription factor activity
GO:0003774	motor activity
GO:0003779	actin binding
GO:0004871	signal transducer activity
GO:0005515	protein binding
GO:0005516	calmodulin binding
GO:0005524	ATP binding
GO:0016887	ATPase activity
GO:0030898	actin-dependent ATPase activity
GO:0042803	protein homodimerization activity
GO:0043495	protein anchor
GO:0043531	ADP binding
GO:0044822	poly(A) RNA binding
GO:0051015	actin filament binding

Biological Process

GO:0000212	meiotic spindle organization
GO:0000904	cell morphogenesis involved in differentiation
GO:0000910	cytokinesis
GO:0001525	angiogenesis
GO:0001701	in utero embryonic development
GO:0001768	establishment of T cell polarity
GO:0006200	ATP catabolic process
GO:0006355	regulation of transcription, DNA-templated
GO:0006509	membrane protein ectodomain proteolysis
GO:0006928	cellular component movement
GO:0007155	cell adhesion
GO:0007165	signal transduction
GO:0007229	integrin-mediated signaling pathway
GO:0007411	axon guidance
GO:0007520	myoblast fusion
GO:0008152	metabolic process
GO:0008360	regulation of cell shape
GO:0015031	protein transport
GO:0016337	single organismal cell-cell adhesion
GO:0030048	actin filament-based movement
GO:0030220	platelet formation
GO:0030224	monocyte differentiation
GO:0031032	actomyosin structure organization
GO:0031532	actin cytoskeleton reorganization
GO:0032796	uropod organization
GO:0038032	termination of G-protein coupled receptor signaling pathway
GO:0043534	blood vessel endothelial cell migration
GO:0045087	innate immune response (InnateDB)
GO:0050900	leukocyte migration
GO:0051295	establishment of meiotic spindle localization

Cellular Component

GO:0001725	stress fiber
GO:0001726	ruffle
GO:0001772	immunological synapse
GO:0001931	uropod
GO:0005634	nucleus
GO:0005737	cytoplasm
GO:0005819	spindle
GO:0005826	actomyosin contractile ring
GO:0005829	cytosol
GO:0005886	plasma membrane
GO:0005913	cell-cell adherens junction
GO:0005938	cell cortex
GO:0008180	COP9 signalosome
GO:0008305	integrin complex
GO:0015629	actin cytoskeleton
GO:0016020	membrane
GO:0016459	myosin complex
GO:0016460	myosin II complex
GO:0030863	cortical cytoskeleton
GO:0031252	cell leading edge
GO:0031594	neuromuscular junction
GO:0032154	cleavage furrow
GO:0042641	actomyosin
GO:0043234	protein complex
GO:0070062	extracellular vesicular exosome
GO:0097513	myosin II filament

Protein Structure and Domains

PDB ID

InterPro

IPR000048 IQ motif, EF-hand binding site
IPR001609 Myosin head, motor domain
IPR002928 Myosin tail
IPR004009 Myosin, N-terminal, SH3-like
IPR008989 Myosin S1 fragment, N-terminal
IPR009053 Prefoldin
IPR010978 tRNA-binding arm
IPR015988 STAT transcription factor, coiled coil
IPR016137 Regulator of G protein signalling superfamily
IPR027417 P-loop containing nucleoside triphosphate hydrolase

PFAM

PF00612
PF00063
PF01576
PF02736

PRINTS

PR00193

PIRSF

SMART

SM00015
SM00242
SM00315

TIGRFAMs

Post-translational Modifications

Modification

Cross-References

SwissProt