MYH9

Functionⁱ

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 MYH10.1 Publication

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	174 – 181	ATPSequence analysis		8

GO - Molecular functionⁱ

actin binding
Source: MGI
Inferred from direct assayⁱ
- "Two-headed binding of the unphosphorylated nonmuscle heavy meromyosin.ADP complex to actin."
  Kovacs M., Toth J., Nyitray L., Sellers J.R.
  Biochemistry 43:4219-4226(2004) [PubMed] [Europe PMC] [Abstract]
actin-dependent ATPase activity
Source: MGI
Inferred from direct assayⁱ
- "Two-headed binding of the unphosphorylated nonmuscle heavy meromyosin.ADP complex to actin."
  Kovacs M., Toth J., Nyitray L., Sellers J.R.
  Biochemistry 43:4219-4226(2004) [PubMed] [Europe PMC] [Abstract]
- "Disease-associated mutations and alternative splicing alter the enzymatic and motile activity of nonmuscle myosins II-B and II-C."
  Kim K.Y., Kovacs M., Kawamoto S., Sellers J.R., Adelstein R.S.
  J. Biol. Chem. 280:22769-22775(2005) [PubMed] [Europe PMC] [Abstract]
actin filament binding
Source: UniProtKB
Inferred from direct assayⁱ
- "Mutations in human nonmuscle myosin IIA found in patients with May-Hegglin anomaly and Fechtner syndrome result in impaired enzymatic function."
  Hu A., Wang F., Sellers J.R.
  J. Biol. Chem. 277:46512-46517(2002) [PubMed] [Europe PMC] [Abstract]
- "Menin, a tumor suppressor, associates with nonmuscle myosin II-A heavy chain."
  Obungu V.H., Lee Burns A., Agarwal S.K., Chandrasekharapa S.C., Adelstein R.S., Marx S.J.
  Oncogene 22:6347-6358(2003) [PubMed] [Europe PMC] [Abstract]
ADP binding
Source: MGI
Inferred from direct assayⁱ
- "Two-headed binding of the unphosphorylated nonmuscle heavy meromyosin.ADP complex to actin."
  Kovacs M., Toth J., Nyitray L., Sellers J.R.
  Biochemistry 43:4219-4226(2004) [PubMed] [Europe PMC] [Abstract]
ATPase activity
Source: UniProtKB
Inferred from direct assayⁱ
- "Mutations in human nonmuscle myosin IIA found in patients with May-Hegglin anomaly and Fechtner syndrome result in impaired enzymatic function."
  Hu A., Wang F., Sellers J.R.
  J. Biol. Chem. 277:46512-46517(2002) [PubMed] [Europe PMC] [Abstract]
- "Characterization of three full-length human nonmuscle myosin II paralogs."
  Billington N., Wang A., Mao J., Adelstein R.S., Sellers J.R.
  J. Biol. Chem. 288:33398-33410(2013) [PubMed] [Europe PMC] [Abstract]
ATP binding
Source: MGI
Inferred from direct assayⁱ
- "Two-headed binding of the unphosphorylated nonmuscle heavy meromyosin.ADP complex to actin."
  Kovacs M., Toth J., Nyitray L., Sellers J.R.
  Biochemistry 43:4219-4226(2004) [PubMed] [Europe PMC] [Abstract]
- "Disease-associated mutations and alternative splicing alter the enzymatic and motile activity of nonmuscle myosins II-B and II-C."
  Kim K.Y., Kovacs M., Kawamoto S., Sellers J.R., Adelstein R.S.
  J. Biol. Chem. 280:22769-22775(2005) [PubMed] [Europe PMC] [Abstract]
cadherin binding
Source: BHF-UCL
Inferred from high throughput direct assayⁱ
- "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
  Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
  Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
calmodulin binding Source: UniProtKB-KW
integrin binding
Source: UniProtKB
Inferred from direct assayⁱ
- "Protein complexes involving alpha v beta 3 integrins, nonmuscle myosin heavy chain-A, and focal adhesion kinase from in thrombospondin-treated smooth muscle cells."
  Sajid M., Hu Z., Lele M., Stouffer G.A.
  J. Investig. Med. 48:190-197(2000) [PubMed] [Europe PMC] [Abstract]
microfilament motor activity
Source: UniProtKB
Inferred from direct assayⁱ
- "Mutations in human nonmuscle myosin IIA found in patients with May-Hegglin anomaly and Fechtner syndrome result in impaired enzymatic function."
  Hu A., Wang F., Sellers J.R.
  J. Biol. Chem. 277:46512-46517(2002) [PubMed] [Europe PMC] [Abstract]
motor activity
Source: UniProtKB
Non-traceable author statementⁱ
- "Cutting edge: association of the motor protein nonmuscle myosin heavy chain-IIA with the C terminus of the chemokine receptor CXCR4 in T lymphocytes."
  Rey M., Vicente-Manzanares M., Viedma F., Yanez-Mo M., Urzainqui A., Barreiro O., Vazquez J., Sanchez-Madrid F.
  J. Immunol. 169:5410-5414(2002) [PubMed] [Europe PMC] [Abstract]
protein domain specific binding
Source: UniProtKB
Inferred from physical interactionⁱ
- "Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions."
  Arora P.D., Wang Y., Bresnick A., Dawson J., Janmey P.A., McCulloch C.A.
  Mol. Biol. Cell 24:734-747(2013) [PubMed] [Europe PMC] [Abstract]
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- "Mutations in human nonmuscle myosin IIA found in patients with May-Hegglin anomaly and Fechtner syndrome result in impaired enzymatic function."
  Hu A., Wang F., Sellers J.R.
  J. Biol. Chem. 277:46512-46517(2002) [PubMed] [Europe PMC] [Abstract]
protein membrane anchor
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- "The angiogenic function of nucleolin is mediated by vascular endothelial growth factor and nonmuscle myosin."
  Huang Y., Shi H., Zhou H., Song X., Yuan S., Luo Y.
  Blood 107:3564-3571(2006) [PubMed] [Europe PMC] [Abstract]
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- "The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts."
  Baltz A.G., Munschauer M., Schwanhausser B., Vasile A., Murakawa Y., Schueler M., Youngs N., Penfold-Brown D., Drew K., Milek M., Wyler E., Bonneau R., Selbach M., Dieterich C., Landthaler M.
  Mol. Cell 46:674-690(2012) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Actin-binding, Calmodulin-binding, Motor protein, Myosin
Biological process	Cell adhesion, Cell shape
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation R-HSA-3928663 EPHA-mediated growth cone collapse R-HSA-416572 Sema4D induced cell migration and growth-cone collapse R-HSA-5625740 RHO GTPases activate PKNs R-HSA-5625900 RHO GTPases activate CIT R-HSA-5627117 RHO GTPases Activate ROCKs R-HSA-5627123 RHO GTPases activate PAKs
SIGNORⁱ	P35579

Reactomeⁱ

R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-416572 Sema4D induced cell migration and growth-cone collapse
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5625900 RHO GTPases activate CIT
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5627123 RHO GTPases activate PAKs

SIGNORⁱ

P35579

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Myosin-9 Alternative name(s): Cellular myosin heavy chain, type A Myosin heavy chain 9 Myosin heavy chain, non-muscle IIa Non-muscle myosin heavy chain A Short name: NMMHC-A Non-muscle myosin heavy chain IIa Short name: NMMHC II-a Short name: NMMHC-IIA
Gene namesⁱ	Name:MYH9
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 22

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:7579 MYH9
MIMⁱ	160775 gene
neXtProtⁱ	NX_P35579

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Macrothrombocytopenia and granulocyte inclusions with or without nephritis or sensorineural hearing loss (MATINS)11 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant disorder characterized by thrombocytopenia, giant platelets and Dohle body-like inclusions in peripheral blood leukocytes with variable ultrastructural appearance. Some affected individuals lack leukocyte inclusion bodies on classic staining of peripheral blood smears. Alport syndrome-like features of nephritis, hearing loss, and eye abnormalities are present in some patients.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_010791	93	N → K in MATINS. 1 PublicationCorresponds to variant dbSNP:rs121913655EnsemblClinVar.	1
Natural variantⁱVAR_018308	95	A → T in MATINS. 1 Publication	1
Natural variantⁱVAR_018309	96	S → L in MATINS. 2 PublicationsCorresponds to variant dbSNP:rs121913657EnsemblClinVar.	1
Natural variantⁱVAR_018310	373	K → N in MATINS. 1 Publication	1
Natural variantⁱVAR_010792	702	R → C in MATINS. 3 PublicationsCorresponds to variant dbSNP:rs80338826EnsemblClinVar.	1
Natural variantⁱVAR_018311	702	R → H in MATINS. 3 PublicationsCorresponds to variant dbSNP:rs80338827EnsemblClinVar.	1
Natural variantⁱVAR_044226	910	K → Q in MATINS. 1 PublicationCorresponds to variant dbSNP:rs554332083Ensembl.	1
Natural variantⁱVAR_044228	1066 – 1072	Missing in MATINS. 1 Publication	7
Natural variantⁱVAR_018312	1114	S → P in MATINS. 1 PublicationCorresponds to variant dbSNP:rs200901330EnsemblClinVar.	1
Natural variantⁱVAR_010794	1155	T → I in MATINS. 2 PublicationsCorresponds to variant dbSNP:rs121913656EnsemblClinVar.	1
Natural variantⁱVAR_010795	1165	R → C in MATINS. 3 PublicationsCorresponds to variant dbSNP:rs80338829EnsemblClinVar.	1
Natural variantⁱVAR_018313	1165	R → L in MATINS. 3 PublicationsCorresponds to variant dbSNP:rs80338830EnsemblClinVar.	1
Natural variantⁱVAR_018314	1205 – 1207	Missing in MATINS. 2 Publications	3
Natural variantⁱVAR_018315	1400	R → W in MATINS; unknown pathological significance; might contribute to pathogenicity when associated with L-96. 1 PublicationCorresponds to variant dbSNP:rs76368635EnsemblClinVar.	1
Natural variantⁱVAR_010796	1424	D → H in MATINS. 5 PublicationsCorresponds to variant dbSNP:rs80338831EnsemblClinVar.	1
Natural variantⁱVAR_018316	1424	D → N in MATINS; results in reduced protein levels. 7 PublicationsCorresponds to variant dbSNP:rs80338831EnsemblClinVar.	1
Natural variantⁱVAR_018317	1424	D → Y in MATINS. 2 PublicationsCorresponds to variant dbSNP:rs80338831EnsemblClinVar.	1
Natural variantⁱVAR_030385	1816	I → V in MATINS. 1 PublicationCorresponds to variant dbSNP:rs762773112Ensembl.	1
Natural variantⁱVAR_010797	1841	E → K in MATINS. 6 PublicationsCorresponds to variant dbSNP:rs80338834EnsemblClinVar.	1

Deafness, autosomal dominant, 17 (DFNA17)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of deafness characterized by progressive high frequency hearing impairment and cochleosaccular degeneration.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_010793	705	R → H in DFNA17. 1 PublicationCorresponds to variant dbSNP:rs80338828EnsemblClinVar.		1

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.

Genetic variations in MYH9 are associated with non-diabetic end stage renal disease (ESRD).

Keywords - Diseaseⁱ

Alport syndrome, Cataract, Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4627
GeneReviewsⁱ	MYH9
MalaCards human disease database More...MalaCardsⁱ	MYH9
MIMⁱ	155100 phenotype 603622 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000100345
Orphanetⁱ	90635 Autosomal dominant non-syndromic sensorineural deafness type DFNA 182050 MYH9-related disease 477742 Nodular fasciitis
PharmGKBⁱ	PA31377

Chemistry databases

ChEMBLⁱ	CHEMBL2189151

ChEMBLⁱ

CHEMBL2189151

Polymorphism and mutation databases

BioMutaⁱ	MYH9
DMDMⁱ	6166599

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000123416	2 – 1960	Myosin-9Add BLAST		1959

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanine1 Publication	1
Modified residueⁱ	8	N6-acetyllysineCombined sources	1
Modified residueⁱ	11	PhosphotyrosineCombined sources	1
Modified residueⁱ	102	N6-acetyllysineCombined sources	1
Modified residueⁱ	299	N6-acetyllysineCombined sources	1
Modified residueⁱ	435	N6-acetyllysineBy similarity	1
Modified residueⁱ	613	N6-acetyllysineBy similarity	1
Modified residueⁱ	628	PhosphoserineCombined sources	1
Modified residueⁱ	754	PhosphotyrosineCombined sources	1
Modified residueⁱ	850	N6-succinyllysineBy similarity	1
Modified residueⁱ	860	N6-acetyllysineBy similarity	1
Modified residueⁱ	975	N6-acetyllysineBy similarity	1
Modified residueⁱ	1024	N6-acetyllysineCombined sources	1
Modified residueⁱ	1114	PhosphoserineBy similarity	1
Modified residueⁱ	1234	N6-acetyllysineBy similarity	1
Modified residueⁱ	1249	N6-acetyllysineBy similarity	1
Modified residueⁱ	1357	N6-acetyllysineCombined sources	1
Modified residueⁱ	1392	N6-acetyllysineCombined sources	1
Modified residueⁱ	1404	N6-acetyllysineCombined sources	1
Modified residueⁱ	1410	N6-acetyllysineCombined sources	1
Modified residueⁱ	1459	N6-acetyllysineCombined sources	1
Modified residueⁱ	1638	N6-acetyllysineCombined sources	1
Modified residueⁱ	1669	N6-succinyllysineBy similarity	1
Modified residueⁱ	1714	PhosphoserineCombined sources	1
Modified residueⁱ	1793	N6-acetyllysineBy similarity	1
Modified residueⁱ	1802	N6-acetyllysineBy similarity	1
Modified residueⁱ	1845	N6-acetyllysineBy similarity	1
Modified residueⁱ	1923	Omega-N-methylarginineBy similarity	1
Modified residueⁱ	1943	PhosphoserineCombined sources	1

Post-translational modificationⁱ

ISGylated.1 Publication

Ubiquitination.1 Publication

Keywords - PTMⁱ

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P35579
jPOSTⁱ	P35579
PaxDbⁱ	P35579
PeptideAtlas More...PeptideAtlasⁱ	P35579
PRIDEⁱ	P35579
ProteomicsDBⁱ	55093 55094 [P35579-2]
TopDownProteomicsⁱ	P35579-1 [P35579-1]

PTM databases

CarbonylDBⁱ	P35579
iPTMnetⁱ	P35579
PhosphoSitePlusⁱ	P35579
SwissPalmⁱ	P35579

Miscellaneous databases

PMAP-CutDBⁱ	P35579

PMAP-CutDBⁱ

P35579

Expressionⁱ

Tissue specificityⁱ

In the kidney, expressed in the glomeruli. Also expressed in leukocytes.2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000100345 Expressed in 219 organ(s), highest expression level in metanephric glomerulus
ExpressionAtlasⁱ	P35579 baseline and differential
Genevisibleⁱ	P35579 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB015386 HPA001644 HPA064783

HPAⁱ

CAB015386
HPA001644
HPA064783

Interactionⁱ

Subunit structureⁱ

Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with RASIP1 (By similarity). Interacts with DDR1 (By similarity). Interacts with SLC6A4 (By similarity). Interacts with PDLIM2 (By similarity). Interacts with SVIL (PubMed:12917436, PubMed:17925381). Interacts with HTRA3 (PubMed:22229724). Interacts with Myo7a (By similarity). Interacts with C9orf135 (PubMed:28345668). Interacts with LIMCH1; independently of the integration of MYH9 into the myosin complex (PubMed:28228547). Interacts with RAB3A (PubMed:27325790).By similarity6 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
CXCR4	P61073	5	EBI-350338,EBI-489411
GRB2	P62993	3	EBI-350338,EBI-401755
MEN1	O00255	3	EBI-350338,EBI-592789
MEN1	O00255-2	4	EBI-350338,EBI-9869387
NCL	P19338	3	EBI-350338,EBI-346967
S100A4	P26447	11	EBI-350338,EBI-717058
SVIL	O46385	2	EBI-350338,EBI-6995105	From Bos taurus.

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	110712, 352 interactors
CORUMⁱ	P35579
Database of interacting proteins More...DIPⁱ	DIP-33103N
IntActⁱ	P35579, 302 interactors
Molecular INTeraction database More...MINTⁱ	P35579
STRINGⁱ	9606.ENSP00000216181

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	1895 – 1897	Combined sources	3
Helixⁱ	1899 – 1903	Combined sources	5
Helixⁱ	1904 – 1921	Combined sources	18
Beta strandⁱ	1922 – 1925	Combined sources	4

Show more details

3D structure databases

SMRⁱ	P35579
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	27 – 77	Myosin N-terminal SH3-likePROSITE-ProRule annotationAdd BLAST	51
Domainⁱ	81 – 776	Myosin motorPROSITE-ProRule annotationAdd BLAST	696
Domainⁱ	779 – 808	IQPROSITE-ProRule annotationAdd BLAST	30

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	2 – 838	Mediates interaction with LIMCH11 PublicationAdd BLAST		837
Regionⁱ	654 – 676	Actin-bindingAdd BLAST		23

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	837 – 1926	Sequence analysisAdd BLAST		1090

Domainⁱ

The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.

Sequence similaritiesⁱ

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.Curated

Keywords - Domainⁱ

Coiled coil

Phylogenomic databases

eggNOGⁱ	KOG0161 Eukaryota COG5022 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155632
HOGENOMⁱ	HOG000173958
InParanoidⁱ	P35579
KEGG Orthology (KO) More...KOⁱ	K10352
OMAⁱ	CKQVRRA
Database of Orthologous Groups More...OrthoDBⁱ	47111at2759
PhylomeDBⁱ	P35579
TreeFamⁱ	TF333601

Family and domain databases

Gene3Dⁱ	2.30.30.360, 1 hit 3.40.850.10, 1 hit 4.10.270.10, 1 hit
InterProⁱ	View protein in InterPro IPR000048 IQ_motif_EF-hand-BS IPR036961 Kinesin_motor_dom_sf IPR001609 Myosin_head_motor_dom IPR027401 Myosin_IQ_contain_sf IPR004009 Myosin_N IPR008989 Myosin_S1_N IPR002928 Myosin_tail IPR027417 P-loop_NTPase IPR036305 RGS_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00063 Myosin_head, 1 hit PF02736 Myosin_N, 1 hit PF01576 Myosin_tail_1, 1 hit
PRINTSⁱ	PR00193 MYOSINHEAVY
SMARTⁱ	View protein in SMART SM00015 IQ, 1 hit SM00242 MYSc, 1 hit
SUPFAMⁱ	SSF48097 SSF48097, 1 hit SSF52540 SSF52540, 1 hit
PROSITEⁱ	View protein in PROSITE PS50096 IQ, 1 hit PS51456 MYOSIN_MOTOR, 1 hit PS51844 SH3_LIKE, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P35579-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSDKSG FEPASLKEEV 
        60         70         80         90        100
GEEAIVELVE NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN 
       110        120        130        140        150
LKERYYSGLI YTYSGLFCVV INPYKNLPIY SEEIVEMYKG KKRHEMPPHI 
       160        170        180        190        200
YAITDTAYRS MMQDREDQSI LCTGESGAGK TENTKKVIQY LAYVASSHKS 
       210        220        230        240        250
KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR INFDVNGYIV 
       260        270        280        290        300
GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY 
       310        320        330        340        350
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEEEQMGLL RVISGVLQLG 
       360        370        380        390        400
NIVFKKERNT DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY 
       410        420        430        440        450
VQKAQTKEQA DFAIEALAKA TYERMFRWLV LRINKALDKT KRQGASFIGI 
       460        470        480        490        500
LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF NHTMFILEQE EYQREGIEWN 
       510        520        530        540        550
FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK SFVEKVMQEQ 
       560        570        580        590        600
GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL 
       610        620        630        640        650
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY 
       660        670        680        690        700
KEQLAKLMAT LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG 
       710        720        730        740        750
IRICRQGFPN RVVFQEFRQR YEILTPNSIP KGFMDGKQAC VLMIKALELD 
       760        770        780        790        800
SNLYRIGQSK VFFRAGVLAH LEEERDLKIT DVIIGFQACC RGYLARKAFA 
       810        820        830        840        850
KRQQQLTAMK VLQRNCAAYL KLRNWQWWRL FTKVKPLLQV SRQEEEMMAK 
       860        870        880        890        900
EEELVKVREK QLAAENRLTE METLQSQLMA EKLQLQEQLQ AETELCAEAE 
       910        920        930        940        950
ELRARLTAKK QELEEICHDL EARVEEEEER CQHLQAEKKK MQQNIQELEE 
       960        970        980        990       1000
QLEEEESARQ KLQLEKVTTE AKLKKLEEEQ IILEDQNCKL AKEKKLLEDR 
      1010       1020       1030       1040       1050
IAEFTTNLTE EEEKSKSLAK LKNKHEAMIT DLEERLRREE KQRQELEKTR 
      1060       1070       1080       1090       1100
RKLEGDSTDL SDQIAELQAQ IAELKMQLAK KEEELQAALA RVEEEAAQKN 
      1110       1120       1130       1140       1150
MALKKIRELE SQISELQEDL ESERASRNKA EKQKRDLGEE LEALKTELED 
      1160       1170       1180       1190       1200
TLDSTAAQQE LRSKREQEVN ILKKTLEEEA KTHEAQIQEM RQKHSQAVEE 
      1210       1220       1230       1240       1250
LAEQLEQTKR VKANLEKAKQ TLENERGELA NEVKVLLQGK GDSEHKRKKV 
      1260       1270       1280       1290       1300
EAQLQELQVK FNEGERVRTE LADKVTKLQV ELDNVTGLLS QSDSKSSKLT 
      1310       1320       1330       1340       1350
KDFSALESQL QDTQELLQEE NRQKLSLSTK LKQVEDEKNS FREQLEEEEE 
      1360       1370       1380       1390       1400
AKHNLEKQIA TLHAQVADMK KKMEDSVGCL ETAEEVKRKL QKDLEGLSQR 
      1410       1420       1430       1440       1450
HEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSACNLE KKQKKFDQLL 
      1460       1470       1480       1490       1500
AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK 
      1510       1520       1530       1540       1550
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA 
      1560       1570       1580       1590       1600
TEDAKLRLEV NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED 
      1610       1620       1630       1640       1650
ERKQRSMAVA ARKKLEMDLK DLEAHIDSAN KNRDEAIKQL RKLQAQMKDC 
      1660       1670       1680       1690       1700
MRELDDTRAS REEILAQAKE NEKKLKSMEA EMIQLQEELA AAERAKRQAQ 
      1710       1720       1730       1740       1750
QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE EQGNTELIND 
      1760       1770       1780       1790       1800
RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KVKLQEMEGT 
      1810       1820       1830       1840       1850
VKSKYKASIT ALEAKIAQLE EQLDNETKER QAACKQVRRT EKKLKDVLLQ 
      1860       1870       1880       1890       1900
VDDERRNAEQ YKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL 
      1910       1920       1930       1940       1950
EDATETADAM NREVSSLKNK LRRGDLPFVV PRRMARKGAG DGSDEEVDGK 
      1960
ADGAEAKPAE

Length:1,960

Mass (Da):226,532

Last modified:January 23, 2007 - v4

Checksum:ⁱ588F84BB8C106E6F

GO

Isoform 2 (identifier: P35579-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-136: Missing.
980-1421: Missing.

« Hide

        10         20         30         40         50
MYKGKKRHEM PPHIYAITDT AYRSMMQDRE DQSILCTGES GAGKTENTKK 
        60         70         80         90        100
VIQYLAYVAS SHKSKKDQGE LERQLLQANP ILEAFGNAKT VKNDNSSRFG 
       110        120        130        140        150
KFIRINFDVN GYIVGANIET YLLEKSRAIR QAKEERTFHI FYYLLSGAGE 
       160        170        180        190        200
HLKTDLLLEP YNKYRFLSNG HVTIPGQQDK DMFQETMEAM RIMGIPEEEQ 
       210        220        230        240        250
MGLLRVISGV LQLGNIVFKK ERNTDQASMP DNTAAQKVSH LLGINVTDFT 
       260        270        280        290        300
RGILTPRIKV GRDYVQKAQT KEQADFAIEA LAKATYERMF RWLVLRINKA 
       310        320        330        340        350
LDKTKRQGAS FIGILDIAGF EIFDLNSFEQ LCINYTNEKL QQLFNHTMFI 
       360        370        380        390        400
LEQEEYQREG IEWNFIDFGL DLQPCIDLIE KPAGPPGILA LLDEECWFPK 
       410        420        430        440        450
ATDKSFVEKV MQEQGTHPKF QKPKQLKDKA DFCIIHYAGK VDYKADEWLM 
       460        470        480        490        500
KNMDPLNDNI ATLLHQSSDK FVSELWKDVD RIIGLDQVAG MSETALPGAF 
       510        520        530        540        550
KTRKGMFRTV GQLYKEQLAK LMATLRNTNP NFVRCIIPNH EKKAGKLDPH 
       560        570        580        590        600
LVLDQLRCNG VLEGIRICRQ GFPNRVVFQE FRQRYEILTP NSIPKGFMDG 
       610        620        630        640        650
KQACVLMIKA LELDSNLYRI GQSKVFFRAG VLAHLEEERD LKITDVIIGF 
       660        670        680        690        700
QACCRGYLAR KAFAKRQQQL TAMKVLQRNC AAYLKLRNWQ WWRLFTKVKP 
       710        720        730        740        750
LLQVSRQEEE MMAKEEELVK VREKQLAAEN RLTEMETLQS QLMAEKLQLQ 
       760        770        780        790        800
EQLQAETELC AEAEELRARL TAKKQELEEI CHDLEARVEE EEERCQHLQA 
       810        820        830        840        850
EKKKMQQNIQ ELEEQLEEEE SARQKLQLEK VTTEAKLKKL EEELDDLLVD 
       860        870        880        890        900
LDHQRQSACN LEKKQKKFDQ LLAEEKTISA KYAEERDRAE AEAREKETKA 
       910        920        930        940        950
LSLARALEEA MEQKAELERL NKQFRTEMED LMSSKDDVGK SVHELEKSKR 
       960        970        980        990       1000
ALEQQVEEMK TQLEELEDEL QATEDAKLRL EVNLQAMKAQ FERDLQGRDE 
      1010       1020       1030       1040       1050
QSEEKKKQLV RQVREMEAEL EDERKQRSMA VAARKKLEMD LKDLEAHIDS 
      1060       1070       1080       1090       1100
ANKNRDEAIK QLRKLQAQMK DCMRELDDTR ASREEILAQA KENEKKLKSM 
      1110       1120       1130       1140       1150
EAEMIQLQEE LAAAERAKRQ AQQERDELAD EIANSSGKGA LALEEKRRLE 
      1160       1170       1180       1190       1200
ARIAQLEEEL EEEQGNTELI NDRLKKANLQ IDQINTDLNL ERSHAQKNEN 
      1210       1220       1230       1240       1250
ARQQLERQNK ELKVKLQEME GTVKSKYKAS ITALEAKIAQ LEEQLDNETK 
      1260       1270       1280       1290       1300
ERQAACKQVR RTEKKLKDVL LQVDDERRNA EQYKDQADKA STRLKQLKRQ 
      1310       1320       1330       1340       1350
LEEAEEEAQR ANASRRKLQR ELEDATETAD AMNREVSSLK NKLRRGDLPF 
      1360       1370       1380 
VVPRRMARKG AGDGSDEEVD GKADGAEAKP AE

Show »

Length:1,382

Mass (Da):159,864

Checksum:ⁱ02727B4F964F5839

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

Q5BKV1	Q5BKV1_HUMAN	MYH9 protein MYH9 protein (Myosin-9)	MYH9	218	Annotation score:
B1AH99	B1AH99_HUMAN	Myosin-9 Myosin-9	MYH9	103	Annotation score:

Sequence cautionⁱ

The sequence CAD89954 differs from that shown. Reason: Frameshift at position 1890.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	53 – 55	EAI → RGH (PubMed:1860190).Curated	3
Sequence conflictⁱ	660	T → S (PubMed:1860190).Curated	1
Sequence conflictⁱ	869	T → M in AAA36349 (PubMed:1967836).Curated	1
Sequence conflictⁱ	931	C → Y in AAA36349 (PubMed:1967836).Curated	1
Sequence conflictⁱ	1000	R → I in BAF84298 (PubMed:14702039).Curated	1
Sequence conflictⁱ	1240 – 1241	KG → GR in AAA36349 (PubMed:1967836).Curated	2
Sequence conflictⁱ	1350	E → EE (PubMed:1967836).Curated	1
Sequence conflictⁱ	1462	E → G in CAD89954 (PubMed:15461802).Curated	1
Sequence conflictⁱ	1546	D → G in CAD89954 (PubMed:15461802).Curated	1
Sequence conflictⁱ	1764	T → A in AAA36349 (PubMed:1967836).Curated	1
Sequence conflictⁱ	1771	S → G in AAA36349 (PubMed:1967836).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_010791	93	N → K in MATINS. 1 PublicationCorresponds to variant dbSNP:rs121913655EnsemblClinVar.	1
Natural variantⁱVAR_018308	95	A → T in MATINS. 1 Publication	1
Natural variantⁱVAR_018309	96	S → L in MATINS. 2 PublicationsCorresponds to variant dbSNP:rs121913657EnsemblClinVar.	1
Natural variantⁱVAR_018310	373	K → N in MATINS. 1 Publication	1
Natural variantⁱVAR_010792	702	R → C in MATINS. 3 PublicationsCorresponds to variant dbSNP:rs80338826EnsemblClinVar.	1
Natural variantⁱVAR_018311	702	R → H in MATINS. 3 PublicationsCorresponds to variant dbSNP:rs80338827EnsemblClinVar.	1
Natural variantⁱVAR_010793	705	R → H in DFNA17. 1 PublicationCorresponds to variant dbSNP:rs80338828EnsemblClinVar.	1
Natural variantⁱVAR_036006	810	K → N in a breast cancer sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_044226	910	K → Q in MATINS. 1 PublicationCorresponds to variant dbSNP:rs554332083Ensembl.	1
Natural variantⁱVAR_044227	967	V → E. Corresponds to variant dbSNP:rs16996652EnsemblClinVar.	1
Natural variantⁱVAR_044228	1066 – 1072	Missing in MATINS. 1 Publication	7
Natural variantⁱVAR_018312	1114	S → P in MATINS. 1 PublicationCorresponds to variant dbSNP:rs200901330EnsemblClinVar.	1
Natural variantⁱVAR_010794	1155	T → I in MATINS. 2 PublicationsCorresponds to variant dbSNP:rs121913656EnsemblClinVar.	1
Natural variantⁱVAR_010795	1165	R → C in MATINS. 3 PublicationsCorresponds to variant dbSNP:rs80338829EnsemblClinVar.	1
Natural variantⁱVAR_018313	1165	R → L in MATINS. 3 PublicationsCorresponds to variant dbSNP:rs80338830EnsemblClinVar.	1
Natural variantⁱVAR_018314	1205 – 1207	Missing in MATINS. 2 Publications	3
Natural variantⁱVAR_018315	1400	R → W in MATINS; unknown pathological significance; might contribute to pathogenicity when associated with L-96. 1 PublicationCorresponds to variant dbSNP:rs76368635EnsemblClinVar.	1
Natural variantⁱVAR_010796	1424	D → H in MATINS. 5 PublicationsCorresponds to variant dbSNP:rs80338831EnsemblClinVar.	1
Natural variantⁱVAR_018316	1424	D → N in MATINS; results in reduced protein levels. 7 PublicationsCorresponds to variant dbSNP:rs80338831EnsemblClinVar.	1
Natural variantⁱVAR_018317	1424	D → Y in MATINS. 2 PublicationsCorresponds to variant dbSNP:rs80338831EnsemblClinVar.	1
Natural variantⁱVAR_018318	1626	I → V1 PublicationCorresponds to variant dbSNP:rs2269529EnsemblClinVar.	1
Natural variantⁱVAR_030385	1816	I → V in MATINS. 1 PublicationCorresponds to variant dbSNP:rs762773112Ensembl.	1
Natural variantⁱVAR_010797	1841	E → K in MATINS. 6 PublicationsCorresponds to variant dbSNP:rs80338834EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_035409	1 – 136	Missing in isoform 2. 1 PublicationAdd BLAST		136
Alternative sequenceⁱVSP_035410	980 – 1421	Missing in isoform 2. 1 PublicationAdd BLAST		442

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CR456526 mRNA Translation: CAG30412.1 AB191263 mRNA Translation: BAD52439.1 AL832639 mRNA Translation: CAD89954.1 Frameshift. AB290175 mRNA Translation: BAG06729.1 Z82215 Genomic DNA No translation available. CH471095 Genomic DNA Translation: EAW60096.1 M81105 mRNA Translation: AAA59888.1 AK291609 mRNA Translation: BAF84298.1 M69180 mRNA Translation: AAA61765.1 M31013 mRNA Translation: AAA36349.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13927.1 [P35579-1]
PIRⁱ	A61231
NCBI Reference Sequences More...RefSeqⁱ	NP_002464.1, NM_002473.5 [P35579-1] XP_011528499.1, XM_011530197.2 [P35579-1] XP_016884292.1, XM_017028803.1 [P35579-1] XP_016884293.1, XM_017028804.1 [P35579-1] XP_016884294.1, XM_017028805.1 [P35579-1] XP_016884295.1, XM_017028806.1 [P35579-1]

Genome annotation databases

Ensemblⁱ	ENST00000216181; ENSP00000216181; ENSG00000100345 [P35579-1]
GeneIDⁱ	4627
KEGGⁱ	hsa:4627
UCSC genome browser More...UCSCⁱ	uc003apg.4 human [P35579-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P35579	Myosin, heavy polypeptide 9, non-muscle, isoform CRA_a		HUMAN		1960	UniRef100_P35579
MYH9 isoform 1		PANTR		1960
Myosin heavy chain 9		GORGO		1849
UPI0008F4661A		GORGO		1824

Protein	Similar proteins		Species	Score	Length	Source
P35579	Myosin-9		RAT		1961	UniRef90_P35579
Myosin-9		CANLF		1960
Myosin-9		MOUSE		1960
Myosin-9		CHICK		1959
Myosin, heavy polypeptide 9, non-muscle, isoform CRA_a		HUMAN		1960
+265

Protein	Similar proteins		Species	Score	Length	Source
P35579	Myosin-9		RAT		1961	UniRef50_P35579
Myosin-9		MOUSE		1960
Myosin-9		CANLF		1960
Myosin-9		CHICK		1959
Myosin, heavy polypeptide 9, non-muscle, isoform CRA_a		HUMAN		1960
+384
P35579-2	Myosin-11 (Fragments)		RAT		1327	UniRef50_P35579-2
Uncharacterized protein		Macrostomum lignano		1212
Myosin 2 heavy chain	)	SCHMA		974
LOC398083 protein (Fragment)		XENLA		1250
Uncharacterized protein		ONCMY		1240
+23

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CR456526 mRNA Translation: CAG30412.1 AB191263 mRNA Translation: BAD52439.1 AL832639 mRNA Translation: CAD89954.1 Frameshift. AB290175 mRNA Translation: BAG06729.1 Z82215 Genomic DNA No translation available. CH471095 Genomic DNA Translation: EAW60096.1 M81105 mRNA Translation: AAA59888.1 AK291609 mRNA Translation: BAF84298.1 M69180 mRNA Translation: AAA61765.1 M31013 mRNA Translation: AAA36349.1
CCDSⁱ	CCDS13927.1 [P35579-1]
PIRⁱ	A61231
RefSeqⁱ	NP_002464.1, NM_002473.5 [P35579-1] XP_011528499.1, XM_011530197.2 [P35579-1] XP_016884292.1, XM_017028803.1 [P35579-1] XP_016884293.1, XM_017028804.1 [P35579-1] XP_016884294.1, XM_017028805.1 [P35579-1] XP_016884295.1, XM_017028806.1 [P35579-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2LNK	NMR	-	C	1897-1935	[»]
	3ZWH	X-ray	1.94	Q	1893-1937	[»]
	4CFQ	X-ray	1.37	Q/R	1893-1937	[»]
	4CFR	X-ray	1.40	Q	1893-1937	[»]
	4ETO	X-ray	1.54	P	1908-1923	[»]
SMRⁱ	P35579
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110712, 352 interactors
CORUMⁱ	P35579
DIPⁱ	DIP-33103N
IntActⁱ	P35579, 302 interactors
MINTⁱ	P35579
STRINGⁱ	9606.ENSP00000216181

Chemistry databases

ChEMBLⁱ	CHEMBL2189151

ChEMBLⁱ

CHEMBL2189151

PTM databases

CarbonylDBⁱ	P35579
iPTMnetⁱ	P35579
PhosphoSitePlusⁱ	P35579
SwissPalmⁱ	P35579

Polymorphism and mutation databases

BioMutaⁱ	MYH9
DMDMⁱ	6166599

Proteomic databases

EPDⁱ	P35579
jPOSTⁱ	P35579
PaxDbⁱ	P35579
PeptideAtlasⁱ	P35579
PRIDEⁱ	P35579
ProteomicsDBⁱ	55093 55094 [P35579-2]
TopDownProteomicsⁱ	P35579-1 [P35579-1]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	4627
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000216181; ENSP00000216181; ENSG00000100345 [P35579-1]
GeneIDⁱ	4627
KEGGⁱ	hsa:4627
UCSCⁱ	uc003apg.4 human [P35579-1]

Organism-specific databases

CTDⁱ	4627
DisGeNETⁱ	4627
GeneCardsⁱ	MYH9
GeneReviewsⁱ	MYH9
HGNCⁱ	HGNC:7579 MYH9
HPAⁱ	CAB015386 HPA001644 HPA064783
MalaCardsⁱ	MYH9
MIMⁱ	155100 phenotype 160775 gene 603622 phenotype
neXtProtⁱ	NX_P35579
OpenTargetsⁱ	ENSG00000100345
Orphanetⁱ	90635 Autosomal dominant non-syndromic sensorineural deafness type DFNA 182050 MYH9-related disease 477742 Nodular fasciitis
PharmGKBⁱ	PA31377
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0161 Eukaryota COG5022 LUCA
GeneTreeⁱ	ENSGT00940000155632
HOGENOMⁱ	HOG000173958
InParanoidⁱ	P35579
KOⁱ	K10352
OMAⁱ	CKQVRRA
OrthoDBⁱ	47111at2759
PhylomeDBⁱ	P35579
TreeFamⁱ	TF333601

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation R-HSA-3928663 EPHA-mediated growth cone collapse R-HSA-416572 Sema4D induced cell migration and growth-cone collapse R-HSA-5625740 RHO GTPases activate PKNs R-HSA-5625900 RHO GTPases activate CIT R-HSA-5627117 RHO GTPases Activate ROCKs R-HSA-5627123 RHO GTPases activate PAKs
SIGNORⁱ	P35579

Reactomeⁱ

R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-416572 Sema4D induced cell migration and growth-cone collapse
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5625900 RHO GTPases activate CIT
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5627123 RHO GTPases activate PAKs

SIGNORⁱ

P35579

Miscellaneous databases

ChiTaRSⁱ	MYH9 human
GeneWikiⁱ	MYH9
GenomeRNAiⁱ	4627
PMAP-CutDBⁱ	P35579
Protein Ontology More...PROⁱ	PR:P35579
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000100345 Expressed in 219 organ(s), highest expression level in metanephric glomerulus
ExpressionAtlasⁱ	P35579 baseline and differential
Genevisibleⁱ	P35579 HS

Family and domain databases

Gene3Dⁱ	2.30.30.360, 1 hit 3.40.850.10, 1 hit 4.10.270.10, 1 hit
InterProⁱ	View protein in InterPro IPR000048 IQ_motif_EF-hand-BS IPR036961 Kinesin_motor_dom_sf IPR001609 Myosin_head_motor_dom IPR027401 Myosin_IQ_contain_sf IPR004009 Myosin_N IPR008989 Myosin_S1_N IPR002928 Myosin_tail IPR027417 P-loop_NTPase IPR036305 RGS_sf
Pfamⁱ	View protein in Pfam PF00063 Myosin_head, 1 hit PF02736 Myosin_N, 1 hit PF01576 Myosin_tail_1, 1 hit
PRINTSⁱ	PR00193 MYOSINHEAVY
SMARTⁱ	View protein in SMART SM00015 IQ, 1 hit SM00242 MYSc, 1 hit
SUPFAMⁱ	SSF48097 SSF48097, 1 hit SSF52540 SSF52540, 1 hit
PROSITEⁱ	View protein in PROSITE PS50096 IQ, 1 hit PS51456 MYOSIN_MOTOR, 1 hit PS51844 SH3_LIKE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MYH9_HUMAN
Accessionⁱ	P35579Primary (citable) accession number: P35579 Secondary accession number(s): A8K6E4 , O60805, Q60FE2, Q86T83
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
	Last sequence update:	January 23, 2007
	Last modified:	June 5, 2019
	This is version 226 of the entry and version 4 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human chromosome 22
Human chromosome 22: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

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Supporting data

UniProtKB - P35579 (MYH9_HUMAN)

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Myosin-9

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoskeleton

Other locations

Cytoskeleton

Cytosol

Extracellular region or secreted

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Coiled coil

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ