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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 1818ATPSequence analysis

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

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931N → K in MHA. 1 Publication
Corresponds to variant rs121913655 [ dbSNP | Ensembl ].
VAR_010791
Natural varianti95 – 951A → T in MHA. 1 Publication
VAR_018308
Natural varianti373 – 3731K → N in MHA and SBS. 1 Publication
VAR_018310
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338826 [ dbSNP | Ensembl ].
VAR_010792
Natural varianti1066 – 10727Missing in MHA and SBS. 1 Publication
VAR_044228
Natural varianti1155 – 11551T → I in MHA and FTNS. 2 Publications
Corresponds to variant rs121913656 [ dbSNP | Ensembl ].
VAR_010794
Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338830 [ dbSNP | Ensembl ].
VAR_018313
Natural varianti1424 – 14241D → H in FTNS and MHA. 5 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_010796
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_018316
Natural varianti1424 – 14241D → Y in MHA. 2 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_018317
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
Corresponds to variant rs80338834 [ dbSNP | Ensembl ].
VAR_010797
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti373 – 3731K → N in MHA and SBS. 1 Publication
VAR_018310
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338826 [ dbSNP | Ensembl ].
VAR_010792
Natural varianti1066 – 10727Missing in MHA and SBS. 1 Publication
VAR_044228
Natural varianti1165 – 11651R → C in FTNS and SBS. 3 Publications
Corresponds to variant rs80338829 [ dbSNP | Ensembl ].
VAR_010795
Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338830 [ dbSNP | Ensembl ].
VAR_018313
Natural varianti1205 – 12073Missing in SBS. 2 Publications
VAR_018314
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_018316
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
Corresponds to variant rs80338834 [ dbSNP | Ensembl ].
VAR_010797
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338826 [ dbSNP | Ensembl ].
VAR_010792
Natural varianti910 – 9101K → Q in FTNS. 1 Publication
Corresponds to variant rs554332083 [ dbSNP | Ensembl ].
VAR_044226
Natural varianti1155 – 11551T → I in MHA and FTNS. 2 Publications
Corresponds to variant rs121913656 [ dbSNP | Ensembl ].
VAR_010794
Natural varianti1165 – 11651R → C in FTNS and SBS. 3 Publications
Corresponds to variant rs80338829 [ dbSNP | Ensembl ].
VAR_010795
Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338830 [ dbSNP | Ensembl ].
VAR_018313
Natural varianti1424 – 14241D → H in FTNS and MHA. 5 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_010796
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_018316
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
Corresponds to variant rs80338834 [ dbSNP | Ensembl ].
VAR_010797
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338826 [ dbSNP | Ensembl ].
VAR_010792
Natural varianti702 – 7021R → H in APSM and EPS. 3 Publications
Corresponds to variant rs80338827 [ dbSNP | Ensembl ].
VAR_018311
Natural varianti1114 – 11141S → P in APSM. 1 Publication
Corresponds to variant rs200901330 [ dbSNP | Ensembl ].
VAR_018312
Epstein syndrome (EPS)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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961S → L in EPS. 2 Publications
Corresponds to variant rs121913657 [ dbSNP | Ensembl ].
VAR_018309
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338826 [ dbSNP | Ensembl ].
VAR_010792
Natural varianti702 – 7021R → H in APSM and EPS. 3 Publications
Corresponds to variant rs80338827 [ dbSNP | Ensembl ].
VAR_018311
Natural varianti1400 – 14001R → W in a EPS patient; might contribute to pathogenicity; when associated with L-96. 1 Publication
Corresponds to variant rs76368635 [ dbSNP | Ensembl ].
VAR_018315
Natural varianti1816 – 18161I → V in EPS. 1 Publication
Corresponds to variant rs762773112 [ dbSNP | Ensembl ].
VAR_030385
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
Corresponds to variant rs80338834 [ dbSNP | Ensembl ].
VAR_010797
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti705 – 7051R → H in DFNA17. 1 Publication
Corresponds to variant rs80338828 [ dbSNP | Ensembl ].
VAR_010793
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_018316

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

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

Chemistry

ChEMBLiCHEMBL2189151.

Polymorphism and mutation databases

BioMutaiMYH9.
DMDMi6166599.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 19601959Myosin-9PRO_0000123416Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei8 – 81N6-acetyllysineCombined sources
Modified residuei11 – 111PhosphotyrosineCombined sources
Modified residuei102 – 1021N6-acetyllysineCombined sources
Modified residuei299 – 2991N6-acetyllysineCombined sources
Modified residuei613 – 6131N6-acetyllysineBy similarity
Modified residuei628 – 6281PhosphoserineCombined sources
Modified residuei754 – 7541PhosphotyrosineCombined sources
Modified residuei850 – 8501N6-succinyllysineBy similarity
Modified residuei860 – 8601N6-acetyllysineBy similarity
Modified residuei975 – 9751N6-acetyllysineBy similarity
Modified residuei1024 – 10241N6-acetyllysineCombined sources
Modified residuei1114 – 11141PhosphoserineBy similarity
Modified residuei1249 – 12491N6-acetyllysineBy similarity
Modified residuei1357 – 13571N6-acetyllysineCombined sources
Modified residuei1392 – 13921N6-acetyllysineCombined sources
Modified residuei1404 – 14041N6-acetyllysineCombined sources
Modified residuei1410 – 14101N6-acetyllysineCombined sources
Modified residuei1459 – 14591N6-acetyllysineCombined sources
Modified residuei1638 – 16381N6-acetyllysineCombined sources
Modified residuei1669 – 16691N6-succinyllysineBy similarity
Modified residuei1714 – 17141PhosphoserineCombined sources
Modified residuei1793 – 17931N6-acetyllysineBy similarity
Modified residuei1802 – 18021N6-acetyllysineBy similarity
Modified residuei1845 – 18451N6-acetyllysineBy similarity
Modified residuei1943 – 19431PhosphoserineCombined sources

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.
PhosphoSiteiP35579.
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 interactions.
DIPiDIP-33103N.
IntActiP35579. 268 interactions.
MINTiMINT-7901706.
STRINGi9606.ENSP00000216181.

Structurei

Secondary structure

1
1960
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1895 – 18973Combined sources
Helixi1899 – 19035Combined sources
Helixi1904 – 192118Combined sources
Beta strandi1922 – 19254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 7-956, 1902-1930.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 776696Myosin motorAdd
BLAST
Domaini779 – 80830IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni654 – 67623Actin-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili837 – 19261090Sequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 553EAI → RGH (PubMed:1860190).Curated
Sequence conflicti660 – 6601T → S (PubMed:1860190).Curated
Sequence conflicti869 – 8691T → M in AAA36349 (PubMed:1967836).Curated
Sequence conflicti931 – 9311C → Y in AAA36349 (PubMed:1967836).Curated
Sequence conflicti1000 – 10001R → I in BAF84298 (PubMed:14702039).Curated
Sequence conflicti1240 – 12412KG → GR in AAA36349 (PubMed:1967836).Curated
Sequence conflicti1350 – 13501E → EE (PubMed:1967836).Curated
Sequence conflicti1462 – 14621E → G in CAD89954 (PubMed:15461802).Curated
Sequence conflicti1546 – 15461D → G in CAD89954 (PubMed:15461802).Curated
Sequence conflicti1764 – 17641T → A in AAA36349 (PubMed:1967836).Curated
Sequence conflicti1771 – 17711S → G in AAA36349 (PubMed:1967836).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931N → K in MHA. 1 Publication
Corresponds to variant rs121913655 [ dbSNP | Ensembl ].
VAR_010791
Natural varianti95 – 951A → T in MHA. 1 Publication
VAR_018308
Natural varianti96 – 961S → L in EPS. 2 Publications
Corresponds to variant rs121913657 [ dbSNP | Ensembl ].
VAR_018309
Natural varianti373 – 3731K → N in MHA and SBS. 1 Publication
VAR_018310
Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338826 [ dbSNP | Ensembl ].
VAR_010792
Natural varianti702 – 7021R → H in APSM and EPS. 3 Publications
Corresponds to variant rs80338827 [ dbSNP | Ensembl ].
VAR_018311
Natural varianti705 – 7051R → H in DFNA17. 1 Publication
Corresponds to variant rs80338828 [ dbSNP | Ensembl ].
VAR_010793
Natural varianti810 – 8101K → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_036006
Natural varianti910 – 9101K → Q in FTNS. 1 Publication
Corresponds to variant rs554332083 [ dbSNP | Ensembl ].
VAR_044226
Natural varianti967 – 9671V → E.
Corresponds to variant rs16996652 [ dbSNP | Ensembl ].
VAR_044227
Natural varianti1066 – 10727Missing in MHA and SBS. 1 Publication
VAR_044228
Natural varianti1114 – 11141S → P in APSM. 1 Publication
Corresponds to variant rs200901330 [ dbSNP | Ensembl ].
VAR_018312
Natural varianti1155 – 11551T → I in MHA and FTNS. 2 Publications
Corresponds to variant rs121913656 [ dbSNP | Ensembl ].
VAR_010794
Natural varianti1165 – 11651R → C in FTNS and SBS. 3 Publications
Corresponds to variant rs80338829 [ dbSNP | Ensembl ].
VAR_010795
Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
Corresponds to variant rs80338830 [ dbSNP | Ensembl ].
VAR_018313
Natural varianti1205 – 12073Missing in SBS. 2 Publications
VAR_018314
Natural varianti1400 – 14001R → W in a EPS patient; might contribute to pathogenicity; when associated with L-96. 1 Publication
Corresponds to variant rs76368635 [ dbSNP | Ensembl ].
VAR_018315
Natural varianti1424 – 14241D → H in FTNS and MHA. 5 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_010796
Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 7 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_018316
Natural varianti1424 – 14241D → Y in MHA. 2 Publications
Corresponds to variant rs80338831 [ dbSNP | Ensembl ].
VAR_018317
Natural varianti1626 – 16261I → V.1 Publication
Corresponds to variant rs2269529 [ dbSNP | Ensembl ].
VAR_018318
Natural varianti1816 – 18161I → V in EPS. 1 Publication
Corresponds to variant rs762773112 [ dbSNP | Ensembl ].
VAR_030385
Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
Corresponds to variant rs80338834 [ dbSNP | Ensembl ].
VAR_010797

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 136136Missing in isoform 2. 1 PublicationVSP_035409Add
BLAST
Alternative sequencei980 – 1421442Missing in isoform 2. 1 PublicationVSP_035410Add
BLAST

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]
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]
UniGeneiHs.474751.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 7-956, 1902-1930.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110712. 308 interactions.
DIPiDIP-33103N.
IntActiP35579. 268 interactions.
MINTiMINT-7901706.
STRINGi9606.ENSP00000216181.

Chemistry

ChEMBLiCHEMBL2189151.

PTM databases

iPTMnetiP35579.
PhosphoSiteiP35579.
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.
GeneCardsiMYH9.
GeneReviewsiMYH9.
HGNCiHGNC:7579. MYH9.
HPAiCAB015386.
HPA001644.
MalaCardsiMYH9.
MIMi153640. phenotype.
153650. phenotype.
155100. phenotype.
160775. gene.
600208. phenotype.
603622. phenotype.
605249. phenotype.
neXtProtiNX_P35579.
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

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: September 7, 2016
This is version 197 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.