Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myosin-9

Gene

MYH9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi174 – 181ATPSequence analysis8

GO - Molecular functioni

  • actin binding Source: MGI
  • actin-dependent ATPase activity Source: MGI
  • actin filament binding Source: UniProtKB
  • ADP binding Source: MGI
  • ATPase activity Source: UniProtKB
  • ATP binding Source: MGI
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • microfilament motor activity Source: UniProtKB
  • motor activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein anchor Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • actin filament-based movement Source: UniProtKB
  • actomyosin structure organization Source: UniProtKB
  • angiogenesis Source: UniProtKB
  • blood vessel endothelial cell migration Source: UniProtKB
  • cytokinesis Source: UniProtKB
  • establishment of meiotic spindle localization Source: Ensembl
  • establishment of T cell polarity Source: Ensembl
  • integrin-mediated signaling pathway Source: UniProtKB
  • in utero embryonic development Source: Ensembl
  • leukocyte migration Source: UniProtKB
  • meiotic spindle organization Source: Ensembl
  • membrane protein ectodomain proteolysis Source: UniProtKB
  • monocyte differentiation Source: UniProtKB
  • myoblast fusion Source: Ensembl
  • negative regulation of actin filament severing Source: UniProtKB
  • phagocytosis, engulfment Source: UniProtKB
  • platelet aggregation Source: UniProtKB
  • platelet formation Source: UniProtKB
  • positive regulation of protein processing in phagocytic vesicle Source: UniProtKB
  • protein transport Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • uropod organization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Cell adhesion, Cell shape

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100345-MONOMER.
ReactomeiR-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.
SIGNORiP35579.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:7579. MYH9.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Cytoplasmcell cortex By similarity

  • Note: Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells.1 Publication

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • actomyosin Source: UniProtKB
  • actomyosin contractile ring Source: UniProtKB
  • brush border Source: Ensembl
  • cell-cell adherens junction Source: BHF-UCL
  • cell leading edge Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • focal adhesion Source: Ensembl
  • immunological synapse Source: Ensembl
  • membrane Source: UniProtKB
  • myosin II complex Source: UniProtKB
  • myosin II filament Source: UniProtKB
  • neuromuscular junction Source: Ensembl
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • protein complex Source: UniProtKB
  • ruffle Source: UniProtKB
  • spindle Source: Ensembl
  • stress fiber Source: UniProtKB
  • uropod Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

May-Hegglin anomaly (MHA)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by thrombocytopenia, giant platelets and Dohle body-like inclusions in peripheral blood leukocytes. appearing as highly parallel paracrystalline bodies.
See also OMIM:155100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01079193N → K in MHA. 1 PublicationCorresponds to variant rs121913655dbSNPEnsembl.1
Natural variantiVAR_01830895A → T in MHA. 1 Publication1
Natural variantiVAR_018310373K → N in MHA and SBS. 1 Publication1
Natural variantiVAR_010792702R → C in APSM, EPSTNS, FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338826dbSNPEnsembl.1
Natural variantiVAR_0442281066 – 1072Missing in MHA and SBS. 1 Publication7
Natural variantiVAR_0107941155T → I in MHA and FTNS. 2 PublicationsCorresponds to variant rs121913656dbSNPEnsembl.1
Natural variantiVAR_0183131165R → L in FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338830dbSNPEnsembl.1
Natural variantiVAR_0107961424D → H in FTNS and MHA. 5 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.1
Natural variantiVAR_0183161424D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.1
Natural variantiVAR_0183171424D → Y in MHA. 2 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.1
Natural variantiVAR_0107971841E → K in FTNS, SBS, MHA and EPSTNS. 6 PublicationsCorresponds to variant rs80338834dbSNPEnsembl.1
Sebastian syndrome (SBS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are smaller and less organized than in May-Hegglin anomaly.
See also OMIM:605249
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018310373K → N in MHA and SBS. 1 Publication1
Natural variantiVAR_010792702R → C in APSM, EPSTNS, FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338826dbSNPEnsembl.1
Natural variantiVAR_0442281066 – 1072Missing in MHA and SBS. 1 Publication7
Natural variantiVAR_0107951165R → C in FTNS and SBS. 3 PublicationsCorresponds to variant rs80338829dbSNPEnsembl.1
Natural variantiVAR_0183131165R → L in FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338830dbSNPEnsembl.1
Natural variantiVAR_0183141205 – 1207Missing in SBS. 2 Publications3
Natural variantiVAR_0183161424D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.1
Natural variantiVAR_0107971841E → K in FTNS, SBS, MHA and EPSTNS. 6 PublicationsCorresponds to variant rs80338834dbSNPEnsembl.1
Fechtner syndrome (FTNS)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal 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.
See also OMIM:153640
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010792702R → C in APSM, EPSTNS, FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338826dbSNPEnsembl.1
Natural variantiVAR_044226910K → Q in FTNS. 1 PublicationCorresponds to variant rs554332083dbSNPEnsembl.1
Natural variantiVAR_0107941155T → I in MHA and FTNS. 2 PublicationsCorresponds to variant rs121913656dbSNPEnsembl.1
Natural variantiVAR_0107951165R → C in FTNS and SBS. 3 PublicationsCorresponds to variant rs80338829dbSNPEnsembl.1
Natural variantiVAR_0183131165R → L in FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338830dbSNPEnsembl.1
Natural variantiVAR_0107961424D → H in FTNS and MHA. 5 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.1
Natural variantiVAR_0183161424D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.1
Natural variantiVAR_0107971841E → K in FTNS, SBS, MHA and EPSTNS. 6 PublicationsCorresponds to variant rs80338834dbSNPEnsembl.1
Alport syndrome, with macrothrombocytopenia (APSM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by the association of ocular lesions, sensorineural hearing loss and nephritis (Alport syndrome) with platelet defects.
See also OMIM:153650
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010792702R → C in APSM, EPSTNS, FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338826dbSNPEnsembl.1
Natural variantiVAR_018311702R → H in APSM and EPSTNS. 3 PublicationsCorresponds to variant rs80338827dbSNPEnsembl.1
Natural variantiVAR_0183121114S → P in APSM. 1 PublicationCorresponds to variant rs200901330dbSNPEnsembl.1
Epstein syndrome (EPSTNS)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by the association of macrothrombocytopathy, sensorineural hearing loss and nephritis.
See also OMIM:153650
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01830996S → L in EPSTNS. 2 PublicationsCorresponds to variant rs121913657dbSNPEnsembl.1
Natural variantiVAR_010792702R → C in APSM, EPSTNS, FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338826dbSNPEnsembl.1
Natural variantiVAR_018311702R → H in APSM and EPSTNS. 3 PublicationsCorresponds to variant rs80338827dbSNPEnsembl.1
Natural variantiVAR_0183151400R → W in a EPSTNS patient; might contribute to pathogenicity; when associated with L-96. 1 PublicationCorresponds to variant rs76368635dbSNPEnsembl.1
Natural variantiVAR_0303851816I → V in EPSTNS. 1 PublicationCorresponds to variant rs762773112dbSNPEnsembl.1
Natural variantiVAR_0107971841E → K in FTNS, SBS, MHA and EPSTNS. 6 PublicationsCorresponds to variant rs80338834dbSNPEnsembl.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.
See also OMIM:603622
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010793705R → H in DFNA17. 1 PublicationCorresponds to variant rs80338828dbSNPEnsembl.1
Macrothrombocytopenia and progressive sensorineural deafness (MPSD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by the association of macrothrombocytopathy and progressive sensorineural hearing loss without renal dysfunction.
See also OMIM:600208
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0183161424D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.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

DisGeNETi4627.
MalaCardsiMYH9.
MIMi153640. phenotype.
153650. phenotype.
155100. phenotype.
600208. phenotype.
603622. phenotype.
605249. phenotype.
OpenTargetsiENSG00000100345.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
182050. MYH9-related disease.
PharmGKBiPA31377.

Chemistry databases

ChEMBLiCHEMBL2189151.

Polymorphism and mutation databases

BioMutaiMYH9.
DMDMi6166599.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001234162 – 1960Myosin-9Add BLAST1959

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei8N6-acetyllysineCombined sources1
Modified residuei11PhosphotyrosineCombined sources1
Modified residuei102N6-acetyllysineCombined sources1
Modified residuei299N6-acetyllysineCombined sources1
Modified residuei613N6-acetyllysineBy similarity1
Modified residuei628PhosphoserineCombined sources1
Modified residuei754PhosphotyrosineCombined sources1
Modified residuei850N6-succinyllysineBy similarity1
Modified residuei860N6-acetyllysineBy similarity1
Modified residuei975N6-acetyllysineBy similarity1
Modified residuei1024N6-acetyllysineCombined sources1
Modified residuei1114PhosphoserineBy similarity1
Modified residuei1249N6-acetyllysineBy similarity1
Modified residuei1357N6-acetyllysineCombined sources1
Modified residuei1392N6-acetyllysineCombined sources1
Modified residuei1404N6-acetyllysineCombined sources1
Modified residuei1410N6-acetyllysineCombined sources1
Modified residuei1459N6-acetyllysineCombined sources1
Modified residuei1638N6-acetyllysineCombined sources1
Modified residuei1669N6-succinyllysineBy similarity1
Modified residuei1714PhosphoserineCombined sources1
Modified residuei1793N6-acetyllysineBy similarity1
Modified residuei1802N6-acetyllysineBy similarity1
Modified residuei1845N6-acetyllysineBy similarity1
Modified residuei1943PhosphoserineCombined sources1

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP35579.
PaxDbiP35579.
PeptideAtlasiP35579.
PRIDEiP35579.
TopDownProteomicsiP35579-1. [P35579-1]

PTM databases

iPTMnetiP35579.
PhosphoSitePlusiP35579.
SwissPalmiP35579.

Miscellaneous databases

PMAP-CutDBP35579.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000100345.
CleanExiHS_MYH9.
ExpressionAtlasiP35579. baseline and differential.
GenevisibleiP35579. HS.

Organism-specific databases

HPAiCAB015386.
HPA001644.

Interactioni

Subunit structurei

Interacts with PDLIM2 (By similarity). Interacts with SLC6A4 (By similarity). 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. Interacts with DDR1 (By similarity). Interacts with SVIL and HTRA3.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CXCR4P610735EBI-350338,EBI-489411
GRB2P629933EBI-350338,EBI-401755
MEN1O002553EBI-350338,EBI-592789
MEN1O00255-24EBI-350338,EBI-9869387
NCLP193383EBI-350338,EBI-346967
SVILO463852EBI-350338,EBI-6995105From a different organism.

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • protein anchor Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi110712. 308 interactors.
DIPiDIP-33103N.
IntActiP35579. 270 interactors.
MINTiMINT-7901706.
STRINGi9606.ENSP00000216181.

Structurei

Secondary structure

11960
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1895 – 1897Combined sources3
Helixi1899 – 1903Combined sources5
Helixi1904 – 1921Combined sources18
Beta strandi1922 – 1925Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LNKNMR-C1897-1935[»]
3ZWHX-ray1.94Q1893-1937[»]
4CFQX-ray1.37Q/R1893-1937[»]
4CFRX-ray1.40Q1893-1937[»]
4ETOX-ray1.54P1908-1923[»]
ProteinModelPortaliP35579.
SMRiP35579.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini81 – 776Myosin motorAdd BLAST696
Domaini779 – 808IQPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni654 – 676Actin-bindingAdd BLAST23

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili837 – 1926Sequence analysisAdd BLAST1090

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

Contains 1 IQ domain.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiP35579.
KOiK10352.
OMAiFEDECAN.
OrthoDBiEOG091G009J.
PhylomeDBiP35579.
TreeFamiTF333601.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
IPR016137. RGS.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

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. AlignAdd to basket

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

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

Show »
Length:1,382
Mass (Da):159,864
Checksum:i02727B4F964F5839
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53 – 55EAI → RGH (PubMed:1860190).Curated3
Sequence conflicti660T → S (PubMed:1860190).Curated1
Sequence conflicti869T → M in AAA36349 (PubMed:1967836).Curated1
Sequence conflicti931C → Y in AAA36349 (PubMed:1967836).Curated1
Sequence conflicti1000R → I in BAF84298 (PubMed:14702039).Curated1
Sequence conflicti1240 – 1241KG → GR in AAA36349 (PubMed:1967836).Curated2
Sequence conflicti1350E → EE (PubMed:1967836).Curated1
Sequence conflicti1462E → G in CAD89954 (PubMed:15461802).Curated1
Sequence conflicti1546D → G in CAD89954 (PubMed:15461802).Curated1
Sequence conflicti1764T → A in AAA36349 (PubMed:1967836).Curated1
Sequence conflicti1771S → G in AAA36349 (PubMed:1967836).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01079193N → K in MHA. 1 PublicationCorresponds to variant rs121913655dbSNPEnsembl.1
Natural variantiVAR_01830895A → T in MHA. 1 Publication1
Natural variantiVAR_01830996S → L in EPSTNS. 2 PublicationsCorresponds to variant rs121913657dbSNPEnsembl.1
Natural variantiVAR_018310373K → N in MHA and SBS. 1 Publication1
Natural variantiVAR_010792702R → C in APSM, EPSTNS, FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338826dbSNPEnsembl.1
Natural variantiVAR_018311702R → H in APSM and EPSTNS. 3 PublicationsCorresponds to variant rs80338827dbSNPEnsembl.1
Natural variantiVAR_010793705R → H in DFNA17. 1 PublicationCorresponds to variant rs80338828dbSNPEnsembl.1
Natural variantiVAR_036006810K → N in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_044226910K → Q in FTNS. 1 PublicationCorresponds to variant rs554332083dbSNPEnsembl.1
Natural variantiVAR_044227967V → E.Corresponds to variant rs16996652dbSNPEnsembl.1
Natural variantiVAR_0442281066 – 1072Missing in MHA and SBS. 1 Publication7
Natural variantiVAR_0183121114S → P in APSM. 1 PublicationCorresponds to variant rs200901330dbSNPEnsembl.1
Natural variantiVAR_0107941155T → I in MHA and FTNS. 2 PublicationsCorresponds to variant rs121913656dbSNPEnsembl.1
Natural variantiVAR_0107951165R → C in FTNS and SBS. 3 PublicationsCorresponds to variant rs80338829dbSNPEnsembl.1
Natural variantiVAR_0183131165R → L in FTNS, MHA and SBS. 3 PublicationsCorresponds to variant rs80338830dbSNPEnsembl.1
Natural variantiVAR_0183141205 – 1207Missing in SBS. 2 Publications3
Natural variantiVAR_0183151400R → W in a EPSTNS patient; might contribute to pathogenicity; when associated with L-96. 1 PublicationCorresponds to variant rs76368635dbSNPEnsembl.1
Natural variantiVAR_0107961424D → H in FTNS and MHA. 5 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.1
Natural variantiVAR_0183161424D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.1
Natural variantiVAR_0183171424D → Y in MHA. 2 PublicationsCorresponds to variant rs80338831dbSNPEnsembl.1
Natural variantiVAR_0183181626I → V.1 PublicationCorresponds to variant rs2269529dbSNPEnsembl.1
Natural variantiVAR_0303851816I → V in EPSTNS. 1 PublicationCorresponds to variant rs762773112dbSNPEnsembl.1
Natural variantiVAR_0107971841E → K in FTNS, SBS, MHA and EPSTNS. 6 PublicationsCorresponds to variant rs80338834dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0354091 – 136Missing in isoform 2. 1 PublicationAdd BLAST136
Alternative sequenceiVSP_035410980 – 1421Missing in isoform 2. 1 PublicationAdd BLAST442

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. Translation: CAB05105.1.
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.
CCDSiCCDS13927.1. [P35579-1]
PIRiA61231.
RefSeqiNP_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]
UniGeneiHs.474751.

Genome annotation databases

EnsembliENST00000216181; ENSP00000216181; ENSG00000100345. [P35579-1]
GeneIDi4627.
KEGGihsa:4627.
UCSCiuc003apg.4. human. [P35579-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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. Translation: CAB05105.1.
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.
CCDSiCCDS13927.1. [P35579-1]
PIRiA61231.
RefSeqiNP_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]
UniGeneiHs.474751.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LNKNMR-C1897-1935[»]
3ZWHX-ray1.94Q1893-1937[»]
4CFQX-ray1.37Q/R1893-1937[»]
4CFRX-ray1.40Q1893-1937[»]
4ETOX-ray1.54P1908-1923[»]
ProteinModelPortaliP35579.
SMRiP35579.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110712. 308 interactors.
DIPiDIP-33103N.
IntActiP35579. 270 interactors.
MINTiMINT-7901706.
STRINGi9606.ENSP00000216181.

Chemistry databases

ChEMBLiCHEMBL2189151.

PTM databases

iPTMnetiP35579.
PhosphoSitePlusiP35579.
SwissPalmiP35579.

Polymorphism and mutation databases

BioMutaiMYH9.
DMDMi6166599.

Proteomic databases

EPDiP35579.
PaxDbiP35579.
PeptideAtlasiP35579.
PRIDEiP35579.
TopDownProteomicsiP35579-1. [P35579-1]

Protocols and materials databases

DNASUi4627.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216181; ENSP00000216181; ENSG00000100345. [P35579-1]
GeneIDi4627.
KEGGihsa:4627.
UCSCiuc003apg.4. human. [P35579-1]

Organism-specific databases

CTDi4627.
DisGeNETi4627.
GeneCardsiMYH9.
GeneReviewsiMYH9.
HGNCiHGNC:7579. MYH9.
HPAiCAB015386.
HPA001644.
MalaCardsiMYH9.
MIMi153640. phenotype.
153650. phenotype.
155100. phenotype.
160775. gene.
600208. phenotype.
603622. phenotype.
605249. phenotype.
neXtProtiNX_P35579.
OpenTargetsiENSG00000100345.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
182050. MYH9-related disease.
PharmGKBiPA31377.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiP35579.
KOiK10352.
OMAiFEDECAN.
OrthoDBiEOG091G009J.
PhylomeDBiP35579.
TreeFamiTF333601.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100345-MONOMER.
ReactomeiR-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.
SIGNORiP35579.

Miscellaneous databases

ChiTaRSiMYH9. human.
GeneWikiiMYH9.
GenomeRNAii4627.
PMAP-CutDBP35579.
PROiP35579.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100345.
CleanExiHS_MYH9.
ExpressionAtlasiP35579. baseline and differential.
GenevisibleiP35579. HS.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
IPR016137. RGS.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYH9_HUMAN
AccessioniPrimary (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: November 30, 2016
This is version 200 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.