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P35579 (MYH9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MYH9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1960 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10. Ref.29

Subunit structure

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. Ref.12 Ref.17 Ref.33

Subcellular location

Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Note: Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells. Ref.29

Tissue specificity

In the kidney, expressed in the glomeruli. Also expressed in leukocytes. Ref.7 Ref.41

Domain

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.

Post-translational modification

ISGylated. Ref.13

Involvement in disease

May-Hegglin anomaly (MHA) [MIM:155100]: A disorder characterized by thrombocytopenia, giant platelets and Dohle body-like inclusions in peripheral blood leukocytes. appearing as highly parallel paracrystalline bodies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.25 Ref.36 Ref.37 Ref.38 Ref.39 Ref.43 Ref.44 Ref.48

Sebastian syndrome (SBS) [MIM:605249]: Autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are smaller and less organized than in May-Hegglin anomaly.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.25 Ref.43 Ref.48

Fechtner syndrome (FTNS) [MIM:153640]: Autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are small and poorly organized. Additionally, FTNS is distinguished by Alport-like clinical features of sensorineural deafness, cataracts and nephritis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.25 Ref.41 Ref.43 Ref.44 Ref.48

Alport syndrome, with macrothrombocytopenia (APSM) [MIM:153650]: An autosomal dominant disorder characterized by the association of ocular lesions, sensorineural hearing loss and nephritis (Alport syndrome) with platelet defects.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.25 Ref.48

Epstein syndrome (EPS) [MIM:153650]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy, sensorineural hearing loss and nephritis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.25 Ref.40 Ref.43 Ref.44 Ref.46 Ref.48

Deafness, autosomal dominant, 17 (DFNA17) [MIM:603622]: A form of deafness characterized by progressive high frequency hearing impairment and cochleosaccular degeneration.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.25 Ref.35 Ref.48

Macrothrombocytopenia and progressive sensorineural deafness (MPSD) [MIM:600208]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy and progressive sensorineural hearing loss without renal dysfunction.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.25 Ref.45 Ref.48

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. Ref.20 Ref.21 Ref.25 Ref.48

Genetic variations in MYH9 are associated with non-diabetic end stage renal disease (ESRD). Ref.20 Ref.21 Ref.25 Ref.48

Sequence similarities

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

Contains 1 IQ domain.

Contains 1 myosin motor domain.

Sequence caution

The sequence CAD89954.1 differs from that shown. Reason: Frameshift at position 1890.

Ontologies

Keywords
   Biological processCell adhesion
Cell shape
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAlport syndrome
Cataract
Deafness
Disease mutation
Non-syndromic deafness
   DomainCoiled coil
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 24072716. Source: UniProt

actin cytoskeleton reorganization

Inferred from mutant phenotype PubMed 15869600. Source: UniProtKB

actin filament-based movement

Inferred from direct assay PubMed 12237319. Source: UniProtKB

actomyosin structure organization

Inferred from direct assay PubMed 24072716. Source: UniProt

angiogenesis

Inferred from direct assay PubMed 16403913. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

blood vessel endothelial cell migration

Inferred from mutant phenotype PubMed 16403913. Source: UniProtKB

cytokinesis

Inferred from mutant phenotype PubMed 15774463. Source: UniProtKB

establishment of T cell polarity

Inferred from electronic annotation. Source: Ensembl

establishment of meiotic spindle localization

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

integrin-mediated signaling pathway

Non-traceable author statement PubMed 10822899. Source: UniProtKB

leukocyte migration

Non-traceable author statement PubMed 12421915. Source: UniProtKB

meiotic spindle organization

Inferred from electronic annotation. Source: Ensembl

membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 16186248. Source: UniProtKB

monocyte differentiation

Inferred from expression pattern Ref.7. Source: UniProtKB

myoblast fusion

Inferred from electronic annotation. Source: Ensembl

platelet formation

Inferred from mutant phenotype PubMed 12237319. Source: UniProtKB

protein transport

Inferred from mutant phenotype PubMed 16403913. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype PubMed 11029059. Source: UniProtKB

single organismal cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

uropod organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactin cytoskeleton

Inferred from direct assay PubMed 15869600. Source: UniProtKB

actomyosin

Inferred from direct assay PubMed 24072716. Source: UniProt

actomyosin contractile ring

Inferred from direct assay PubMed 11029059. Source: UniProtKB

cell leading edge

Inferred from direct assay PubMed 12421915. Source: UniProtKB

cell-cell adherens junction

Inferred from electronic annotation. Source: Ensembl

cleavage furrow

Inferred from direct assay PubMed 14508515PubMed 7699007. Source: UniProtKB

cortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 7699007. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 14508515. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

immunological synapse

Inferred from electronic annotation. Source: Ensembl

myosin II complex

Inferred from direct assay PubMed 24072716. Source: UniProt

myosin II filament

Inferred from direct assay PubMed 24072716. Source: UniProt

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 14508515. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 16186248PubMed 16403913. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 12421915. Source: UniProtKB

ruffle

Inferred from direct assay PubMed 16403913. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: Ensembl

stress fiber

Inferred from direct assay PubMed 14508515PubMed 14706930PubMed 16403913PubMed 7699007. Source: UniProtKB

uropod

Inferred from direct assay PubMed 15064761. Source: MGI

   Molecular_functionADP binding

Inferred from direct assay PubMed 15065866. Source: MGI

ATP binding

Inferred from direct assay PubMed 15065866PubMed 15845534. Source: MGI

ATPase activity

Inferred from direct assay PubMed 12237319. Source: UniProtKB

actin binding

Inferred from direct assay PubMed 15065866. Source: MGI

actin filament binding

Inferred from direct assay PubMed 12237319PubMed 14508515. Source: UniProtKB

actin-dependent ATPase activity

Inferred from direct assay PubMed 15065866PubMed 15845534. Source: MGI

microfilament motor activity

Inferred from direct assay PubMed 12237319. Source: UniProtKB

motor activity

Non-traceable author statement PubMed 12421915. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein anchor

Inferred from mutant phenotype PubMed 16403913. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10822899PubMed 12421915PubMed 14508515PubMed 14640694PubMed 15479433PubMed 16186248PubMed 16403913Ref.33. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 12237319. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35579-1)

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.
Isoform 2 (identifier: P35579-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 19601959Myosin-9
PRO_0000123416

Regions

Domain81 – 776696Myosin motor
Domain779 – 80830IQ
Nucleotide binding174 – 1818ATP Potential
Region654 – 67623Actin-binding
Coiled coil837 – 19261090 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.28
Modified residue81N6-acetyllysine Ref.28
Modified residue111Phosphotyrosine Ref.27
Modified residue1021N6-acetyllysine Ref.28
Modified residue2991N6-acetyllysine Ref.28
Modified residue6131N6-acetyllysine By similarity
Modified residue7541Phosphotyrosine By similarity
Modified residue8501N6-succinyllysine By similarity
Modified residue8601N6-acetyllysine By similarity
Modified residue9751N6-acetyllysine By similarity
Modified residue10241N6-acetyllysine Ref.28
Modified residue12491N6-acetyllysine By similarity
Modified residue13571N6-acetyllysine Ref.28
Modified residue13921N6-acetyllysine Ref.28
Modified residue14041N6-acetyllysine Ref.28
Modified residue14101N6-acetyllysine Ref.28
Modified residue14591N6-acetyllysine Ref.28
Modified residue16381N6-acetyllysine Ref.28
Modified residue16691N6-succinyllysine By similarity
Modified residue17141Phosphoserine Ref.30
Modified residue17931N6-acetyllysine By similarity
Modified residue18021N6-acetyllysine By similarity
Modified residue18451N6-acetyllysine By similarity
Modified residue19431Phosphoserine Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.23 Ref.26 Ref.27 Ref.30 Ref.32

Natural variations

Alternative sequence1 – 136136Missing in isoform 2.
VSP_035409
Alternative sequence980 – 1421442Missing in isoform 2.
VSP_035410
Natural variant931N → K in MHA. Ref.36
VAR_010791
Natural variant951A → T in MHA. Ref.39
VAR_018308
Natural variant961S → L in EPS. Ref.41 Ref.46
VAR_018309
Natural variant3731K → N in MHA and SBS. Ref.38
VAR_018310
Natural variant7021R → C in APSM, EPS, FTNS, MHA and SBS. Ref.36 Ref.38 Ref.44
VAR_010792
Natural variant7021R → H in APSM and EPS. Ref.38 Ref.40 Ref.44
VAR_018311
Natural variant7051R → H in DFNA17. Ref.35
VAR_010793
Natural variant8101K → N in a breast cancer sample; somatic mutation. Ref.47
VAR_036006
Natural variant9101K → Q in FTNS. Ref.44
VAR_044226
Natural variant9671V → E.
Corresponds to variant rs16996652 [ dbSNP | Ensembl ].
VAR_044227
Natural variant1066 – 10727Missing in MHA and SBS.
VAR_044228
Natural variant11141S → P in APSM. Ref.38
VAR_018312
Natural variant11551T → I in MHA and FTNS. Ref.37 Ref.44
VAR_010794
Natural variant11651R → C in FTNS and SBS. Ref.36 Ref.39 Ref.43
VAR_010795
Natural variant11651R → L in FTNS, MHA and SBS. Ref.39 Ref.41 Ref.43
VAR_018313
Natural variant1205 – 12073Missing in SBS.
VAR_018314
Natural variant14001R → W in a EPS patient; might contribute to pathogenicity; when associated with L-96. Ref.41
Corresponds to variant rs76368635 [ dbSNP | Ensembl ].
VAR_018315
Natural variant14241D → H in FTNS and MHA. Ref.36 Ref.38 Ref.39 Ref.43 Ref.44
VAR_010796
Natural variant14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. Ref.38 Ref.39 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45
VAR_018316
Natural variant14241D → Y in MHA. Ref.39 Ref.43
VAR_018317
Natural variant16261I → V. Ref.39
Corresponds to variant rs2269529 [ dbSNP | Ensembl ].
VAR_018318
Natural variant18161I → V in EPS. Ref.43
VAR_030385
Natural variant18411E → K in FTNS, SBS, MHA and EPS. Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.43
VAR_010797

Experimental info

Sequence conflict53 – 553EAI → RGH Ref.9
Sequence conflict6601T → S Ref.9
Sequence conflict8691T → M in AAA36349. Ref.11
Sequence conflict9311C → Y in AAA36349. Ref.11
Sequence conflict10001R → I in BAF84298. Ref.8
Sequence conflict1240 – 12412KG → GR in AAA36349. Ref.11
Sequence conflict13501E → EE Ref.11
Sequence conflict14621E → G in CAD89954. Ref.1
Sequence conflict15461D → G in CAD89954. Ref.1
Sequence conflict17641T → A in AAA36349. Ref.11
Sequence conflict17711S → G in AAA36349. Ref.11

Secondary structure

......... 1960
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 588F84BB8C106E6F

FASTA1,960226,532
        10         20         30         40         50         60 
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSDKSG FEPASLKEEV GEEAIVELVE 

        70         80         90        100        110        120 
NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKERYYSGLI YTYSGLFCVV 

       130        140        150        160        170        180 
INPYKNLPIY SEEIVEMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK 

       190        200        210        220        230        240 
TENTKKVIQY LAYVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR 

       250        260        270        280        290        300 
INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY 

       310        320        330        340        350        360 
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEEEQMGLL RVISGVLQLG NIVFKKERNT 

       370        380        390        400        410        420 
DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA 

       430        440        450        460        470        480 
TYERMFRWLV LRINKALDKT KRQGASFIGI LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF 

       490        500        510        520        530        540 
NHTMFILEQE EYQREGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK 

       550        560        570        580        590        600 
SFVEKVMQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL 

       610        620        630        640        650        660 
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT 

       670        680        690        700        710        720 
LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR 

       730        740        750        760        770        780 
YEILTPNSIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRAGVLAH LEEERDLKIT 

       790        800        810        820        830        840 
DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL KLRNWQWWRL FTKVKPLLQV 

       850        860        870        880        890        900 
SRQEEEMMAK EEELVKVREK QLAAENRLTE METLQSQLMA EKLQLQEQLQ AETELCAEAE 

       910        920        930        940        950        960 
ELRARLTAKK QELEEICHDL EARVEEEEER CQHLQAEKKK MQQNIQELEE QLEEEESARQ 

       970        980        990       1000       1010       1020 
KLQLEKVTTE AKLKKLEEEQ IILEDQNCKL AKEKKLLEDR IAEFTTNLTE EEEKSKSLAK 

      1030       1040       1050       1060       1070       1080 
LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSTDL SDQIAELQAQ IAELKMQLAK 

      1090       1100       1110       1120       1130       1140 
KEEELQAALA RVEEEAAQKN MALKKIRELE SQISELQEDL ESERASRNKA EKQKRDLGEE 

      1150       1160       1170       1180       1190       1200 
LEALKTELED TLDSTAAQQE LRSKREQEVN ILKKTLEEEA KTHEAQIQEM RQKHSQAVEE 

      1210       1220       1230       1240       1250       1260 
LAEQLEQTKR VKANLEKAKQ TLENERGELA NEVKVLLQGK GDSEHKRKKV EAQLQELQVK 

      1270       1280       1290       1300       1310       1320 
FNEGERVRTE LADKVTKLQV ELDNVTGLLS QSDSKSSKLT KDFSALESQL QDTQELLQEE 

      1330       1340       1350       1360       1370       1380 
NRQKLSLSTK LKQVEDEKNS FREQLEEEEE AKHNLEKQIA TLHAQVADMK KKMEDSVGCL 

      1390       1400       1410       1420       1430       1440 
ETAEEVKRKL QKDLEGLSQR HEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSACNLE 

      1450       1460       1470       1480       1490       1500 
KKQKKFDQLL AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK 

      1510       1520       1530       1540       1550       1560 
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA TEDAKLRLEV 

      1570       1580       1590       1600       1610       1620 
NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED ERKQRSMAVA ARKKLEMDLK 

      1630       1640       1650       1660       1670       1680 
DLEAHIDSAN KNRDEAIKQL RKLQAQMKDC MRELDDTRAS REEILAQAKE NEKKLKSMEA 

      1690       1700       1710       1720       1730       1740 
EMIQLQEELA AAERAKRQAQ QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE 

      1750       1760       1770       1780       1790       1800 
EQGNTELIND RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KVKLQEMEGT 

      1810       1820       1830       1840       1850       1860 
VKSKYKASIT ALEAKIAQLE EQLDNETKER QAACKQVRRT EKKLKDVLLQ VDDERRNAEQ 

      1870       1880       1890       1900       1910       1920 
YKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL EDATETADAM NREVSSLKNK 

      1930       1940       1950       1960 
LRRGDLPFVV PRRMARKGAG DGSDEEVDGK ADGAEAKPAE 

« Hide

Isoform 2 [UniParc].

Checksum: 02727B4F964F5839
Show »

FASTA1,382159,864

References

« Hide 'large scale' references
[1]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]"Vector-capping: a simple method for preparing a high-quality full-length cDNA library."
Kato S., Ohtoko K., Ohtake H., Kimura T.
DNA Res. 12:53-62(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Spinal cord.
[4]"Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free recombination: Preparation of full-lemgth cDNA clones encoding motor proteins."
Yamakawa H., Kikuno R.F., Nagase T., Ohara O.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Cellular myosin heavy chain in human leukocytes: isolation of 5' cDNA clones, characterization of the protein, chromosomal localization, and upregulation during myeloid differentiation."
Toothaker L.E., Gonzalez D.A., Tung N., Lemons R.S., le Beau M.M., Arnaout M.A., Clayton L.K., Tenen D.G.
Blood 78:1826-1833(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1337, TISSUE SPECIFICITY.
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1009.
Tissue: Placenta.
[9]"Human nonmuscle myosin heavy chains are encoded by two genes located on different chromosomes."
Simons M., Wang M., McBride O.W., Kawamoto S., Yamakawa K., Gdula D., Adelstein R.S., Weir L.
Circ. Res. 69:530-539(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-715.
[10]Bienvenut W.V., Claeys R.
Submitted (AUG-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-47; 67-74; 126-139; 187-199; 203-225; 241-261; 290-299; 328-355; 359-387; 408-419; 476-494; 546-555; 581-613; 618-637; 645-651; 657-670; 683-693; 712-718; 721-731; 746-755; 765-775; 802-810; 824-829; 834-842; 861-867; 924-930; 995-1014; 1042-1048; 1052-1075; 1081-1099; 1136-1162; 1166-1191; 1261-1266; 1278-1295; 1302-1322; 1393-1400; 1405-1413; 1418-1433; 1484-1492; 1504-1513; 1519-1525; 1529-1555; 1558-1566; 1606-1612; 1614-1638; 1642-1648; 1662-1669; 1704-1724; 1794-1802; 1807-1828; 1857-1867; 1899-1912; 1923-1932 AND 1951-1960, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[11]"Human nonmuscle myosin heavy chain mRNA: generation of diversity through alternative polyadenylylation."
Saez C.G., Myers J.C., Shows T.B., Leinwand L.A.
Proc. Natl. Acad. Sci. U.S.A. 87:1164-1168(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 714-1960.
[12]"F-actin and myosin II binding domains in supervillin."
Chen Y., Takizawa N., Crowley J.L., Oh S.W., Gatto C.L., Kambara T., Sato O., Li X.-D., Ikebe M., Luna E.J.
J. Biol. Chem. 278:46094-46106(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SVIL.
[13]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[17]"Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery."
Takizawa N., Ikebe R., Ikebe M., Luna E.J.
J. Cell Sci. 120:3792-3803(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SVIL.
[18]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[19]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[20]"MYH9 is a major-effect risk gene for focal segmental glomerulosclerosis."
Kopp J.B., Smith M.W., Nelson G.W., Johnson R.C., Freedman B.I., Bowden D.W., Oleksyk T., McKenzie L.M., Kajiyama H., Ahuja T.S., Berns J.S., Briggs W., Cho M.E., Dart R.A., Kimmel P.L., Korbet S.M., Michel D.M., Mokrzycki M.H. expand/collapse author list , Schelling J.R., Simon E., Trachtman H., Vlahov D., Winkler C.A.
Nat. Genet. 40:1175-1184(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
[21]"MYH9 is associated with nondiabetic end-stage renal disease in African Americans."
Kao W.H., Klag M.J., Meoni L.A., Reich D., Berthier-Schaad Y., Li M., Coresh J., Patterson N., Tandon A., Powe N.R., Fink N.E., Sadler J.H., Weir M.R., Abboud H.E., Adler S.G., Divers J., Iyengar S.K., Freedman B.I. expand/collapse author list , Kimmel P.L., Knowler W.C., Kohn O.F., Kramp K., Leehey D.J., Nicholas S.B., Pahl M.V., Schelling J.R., Sedor J.R., Thornley-Brown D., Winkler C.A., Smith M.W., Parekh R.S.
Nat. Genet. 40:1185-1192(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[24]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Polymorphisms in the non-muscle myosin heavy chain 9 gene (MYH9) are strongly associated with end-stage renal disease historically attributed to hypertension in African Americans."
Freedman B.I., Hicks P.J., Bostrom M.A., Cunningham M.E., Liu Y., Divers J., Kopp J.B., Winkler C.A., Nelson G.W., Langefeld C.D., Bowden D.W.
Kidney Int. 75:736-745(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
[26]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11 AND SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[28]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-102; LYS-299; LYS-1024; LYS-1357; LYS-1392; LYS-1404; LYS-1410; LYS-1459 AND LYS-1638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading."
Betapudi V.
PLoS ONE 5:E8560-E8560(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[30]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714 AND SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"Application of the wheat-germ cell-free translation system to produce high temperature requirement A3 (HtrA3) proteases."
Singh H., Makino S., Endo Y., Li Y., Stephens A.N., Nie G.
BioTechniques 52:23-28(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTRA3.
[34]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"Human nonsyndromic hereditary deafness DFNA17 is due to a mutation in nonmuscle myosin MYH9."
Lalwani A.K., Goldstein J.A., Kelley M.J., Luxford W., Castelein C.M., Mhatre A.N.
Am. J. Hum. Genet. 67:1121-1128(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNA17 HIS-705.
[36]"Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and Sebastian syndromes."
Seri M., Cusano M., Gangarossa S., Caridi G., Bordo D., Lo Nigro C., Ghiggeri G.M., Ravazzolo R., Savino M., Del Vecchio M., d'Apolito M., Iolascon A., Zelante L.L., Savoia A., Balduini C.L., Noris P., Magrini U., Belletti S. expand/collapse author list , Heath K.E., Babcock M., Glucksman M.J., Aliprandis E., Bizzaro N., Desnick R.J., Martignetti J.A.
Nat. Genet. 26:103-105(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHA/FTNS/SBS LYS-93; CYS-702; CYS-1165; HIS-1424 AND LYS-1841.
[37]"Mutation of MYH9, encoding non-muscle myosin heavy chain A, in May-Hegglin anomaly."
Kelley M.J., Jawien W., Ortel T.L., Korczak J.F.
Nat. Genet. 26:106-108(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHA ILE-1155 AND LYS-1841.
[38]"Nonmuscle myosin heavy chain IIA mutations define a spectrum of autosomal dominant macrothrombocytopenias: May-Hegglin anomaly and Fechtner, Sebastian, Epstein, and Alport-like syndromes."
Heath K.E., Campos-Barros A., Toren A., Rozenfeld-Granot G., Carlsson L.E., Savige J., Denison J.C., Gregory M.C., White J.G., Barker D.F., Greinacher A., Epstein C.J., Glucksman M.J., Martignetti J.A.
Am. J. Hum. Genet. 69:1033-1045(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHA/SBS/FTNS/EPS/APSM ASN-373; CYS-702; HIS-702; PRO-1114; ASN-1424; HIS-1424 AND LYS-1841.
[39]"Identification of six novel MYH9 mutations and genotype-phenotype relationships in autosomal dominant macrothrombocytopenia with leukocyte inclusions."
Kunishima S., Matsushita T., Kojima T., Amemiya N., Choi Y.M., Hosaka N., Inoue M., Jung Y., Mamiya S., Matsumoto K., Miyajima Y., Zhang G., Ruan C., Saito K., Song K.S., Yoon H.-J., Kamiya T., Saito H.
J. Hum. Genet. 46:722-729(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHA/FTNS/SBS THR-95; CYS-1165; LEU-1165; 1205-LEU--GLN-1207 DEL; HIS-1424; ASN-1424; TYR-1424 AND LYS-1841, VARIANT VAL-1626.
[40]"Epstein syndrome: another renal disorder with mutations in the nonmuscle myosin heavy chain 9 gene."
Seri M., Savino M., Bordo D., Cusano R., Rocca B., Meloni I., Di Bari F., Koivisto P.A., Bolognesi M., Ghiggeri G.M., Landolfi R., Balduini C.L., Zelante L., Ravazzolo R., Renieri A., Savoia A.
Hum. Genet. 110:182-186(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPS HIS-702.
[41]"Expression of the nonmuscle myosin heavy chain IIA in the human kidney and screening for MYH9 mutations in Epstein and Fechtner syndromes."
Arrondel C., Vodovar N., Knebelmann B., Gruenfeld J.-P., Gubler M.-C., Antignac C., Heidet L.
J. Am. Soc. Nephrol. 13:65-74(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FTNS/EPS LEU-96; LEU-1165; ASN-1424 AND LYS-1841, VARIANT TRP-1400, TISSUE SPECIFICITY.
[42]"Asp1424Asn MYH9 mutation results in an unstable protein responsible for the phenotypes in May-Hegglin anomaly/Fechtner syndrome."
Deutsch S., Rideau A., Bochaton-Piallat M.-L., Merla G., Geinoz A., Gabbiani G., Schwede T., Matthes T., Antonarakis S.E., Beris P.
Blood 102:529-534(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT ASN-1424.
[43]"Immunofluorescence analysis of neutrophil nonmuscle myosin heavy chain-A in MYH9 disorders: association of subcellular localization with MYH9 mutations."
Kunishima S., Matsushita T., Kojima T., Sako M., Kimura F., Jo E.-K., Inoue C., Kamiya T., Saito H.
Lab. Invest. 83:115-122(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FTNS/SBS CYS-1165, VARIANTS SBS LEU-1165 AND 1205-LEU--GLN-1207 DEL, VARIANTS MHA HIS-1424; ASN-1424; TYR-1424 AND LYS-1841, VARIANT EPS VAL-1816, VARIANT FTNS/MHA LYS-1841.
[44]"MYH9-related disease: may-Hegglin anomaly, Sebastian syndrome, Fechtner syndrome, and Epstein syndrome are not distinct entities but represent a variable expression of a single illness."
Seri M., Pecci A., Di Bari F., Cusano R., Savino M., Panza E., Nigro A., Noris P., Gangarossa S., Rocca B., Gresele P., Bizzaro N., Malatesta P., Koivisto P.A., Longo I., Musso R., Pecoraro C., Iolascon A. expand/collapse author list , Magrini U., Rodriguez Soriano J., Renieri A., Ghiggeri G.M., Ravazzolo R., Balduini C.L., Savoia A.
Medicine (Baltimore) 82:203-215(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPS HIS-702, VARIANTS FTNS GLN-910; ILE-1155 AND HIS-1424, VARIANTS MHA/SBS 1066-GLU--ALA-1072 DEL AND ASN-1424, VARIANT EPS/FTNS/MHA/SBS CYS-702.
[45]"Macrothrombocytopenia and progressive deafness is due to a mutation in MYH9."
Mhatre A.N., Kim Y., Brodie H.A., Lalwani A.K.
Otol. Neurotol. 24:205-209(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPSD ASN-1424.
[46]"Bladder exstrophy and Epstein type congenital macrothrombocytopenia: evidence for a common cause?"
Utsch B., DiFeo A., Kujat A., Karle S., Schuster V., Lenk H., Jacobs U., Mueller M., Doetsch J., Rascher W., Reutter H., Martignetti J.A., Ludwig M., Troebs R.-B.
Am. J. Med. Genet. A 140:2251-2253(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPS LEU-96.
[47]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-810.
[48]"Position of nonmuscle myosin heavy chain IIA (NMMHC-IIA) mutations predicts the natural history of MYH9-related disease."
Pecci A., Panza E., Pujol-Moix N., Klersy C., Di Bari F., Bozzi V., Gresele P., Lethagen S., Fabris F., Dufour C., Granata A., Doubek M., Pecoraro C., Koivisto P.A., Heller P.G., Iolascon A., Alvisi P., Schwabe D. expand/collapse author list , De Candia E., Rocca B., Russo U., Ramenghi U., Noris P., Seri M., Balduini C.L., Savoia A.
Hum. Mutat. 29:409-417(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: POSITION OF MUTATIONS IN MYH9-RELATED DISEASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13927.1. [P35579-1]
PIRA61231.
RefSeqNP_002464.1. NM_002473.4. [P35579-1]
UniGeneHs.474751.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LNKNMR-C1897-1935[»]
3ZWHX-ray1.94Q1893-1937[»]
4CFQX-ray1.37Q/R1893-1937[»]
4CFRX-ray1.40Q1893-1937[»]
4ETOX-ray1.54P1908-1923[»]
ProteinModelPortalP35579.
SMRP35579. Positions 7-897, 1894-1935.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110712. 105 interactions.
DIPDIP-33103N.
IntActP35579. 49 interactions.
MINTMINT-7901706.
STRING9606.ENSP00000216181.

Chemistry

ChEMBLCHEMBL2189151.

PTM databases

PhosphoSiteP35579.

Polymorphism databases

DMDM6166599.

Proteomic databases

MaxQBP35579.
PaxDbP35579.
PeptideAtlasP35579.
PRIDEP35579.

Protocols and materials databases

DNASU4627.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216181; ENSP00000216181; ENSG00000100345. [P35579-1]
GeneID4627.
KEGGhsa:4627.
UCSCuc003apg.3. human. [P35579-1]

Organism-specific databases

CTD4627.
GeneCardsGC22M036677.
GeneReviewsMYH9.
HGNCHGNC:7579. MYH9.
HPACAB015386.
HPA001644.
MIM153640. phenotype.
153650. phenotype.
155100. phenotype.
160775. gene.
600208. phenotype.
603622. phenotype.
605249. phenotype.
neXtProtNX_P35579.
Orphanet90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
182050. MYH9-related disease.
PharmGKBPA31377.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000173958.
HOVERGENHBG004704.
InParanoidP35579.
KOK10352.
OMAKRENDSI.
OrthoDBEOG71CFK3.
PhylomeDBP35579.
TreeFamTF333601.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP35579.
BgeeP35579.
CleanExHS_MYH9.
GenevestigatorP35579.

Family and domain databases

Gene3D4.10.270.10. 1 hit.
InterProIPR000048. 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. Regulat_G_prot_signal_superfam.
[Graphical view]
PfamPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYH9. human.
GeneWikiMYH9.
GenomeRNAi4627.
NextBio17810.
PMAP-CutDBP35579.
PROP35579.
SOURCESearch...

Entry information

Entry nameMYH9_HUMAN
AccessionPrimary (citable) accession number: P35579
Secondary accession number(s): A8K6E4 expand/collapse secondary AC list , O60805, Q60FE2, Q86T83
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 173 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM