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P35579

- MYH9_HUMAN

UniProt

P35579 - MYH9_HUMAN

Protein

Myosin-9

Gene

MYH9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    1. actin binding Source: MGI
    2. actin-dependent ATPase activity Source: MGI
    3. actin filament binding Source: UniProtKB
    4. ADP binding Source: MGI
    5. ATPase activity Source: UniProtKB
    6. ATP binding Source: MGI
    7. microfilament motor activity Source: UniProtKB
    8. motor activity Source: UniProtKB
    9. poly(A) RNA binding Source: UniProtKB
    10. protein anchor Source: UniProtKB
    11. protein binding Source: UniProtKB
    12. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. actin filament-based movement Source: UniProtKB
    3. actomyosin structure organization Source: UniProt
    4. angiogenesis Source: UniProtKB
    5. ATP catabolic process Source: UniProt
    6. axon guidance Source: Reactome
    7. blood vessel endothelial cell migration Source: UniProtKB
    8. cytokinesis Source: UniProtKB
    9. establishment of meiotic spindle localization Source: Ensembl
    10. establishment of T cell polarity Source: Ensembl
    11. integrin-mediated signaling pathway Source: UniProtKB
    12. in utero embryonic development Source: Ensembl
    13. leukocyte migration Source: UniProtKB
    14. meiotic spindle organization Source: Ensembl
    15. membrane protein ectodomain proteolysis Source: UniProtKB
    16. monocyte differentiation Source: UniProtKB
    17. myoblast fusion Source: Ensembl
    18. platelet formation Source: UniProtKB
    19. protein transport Source: UniProtKB
    20. regulation of cell shape Source: UniProtKB
    21. single organismal cell-cell adhesion Source: Ensembl
    22. termination of G-protein coupled receptor signaling pathway Source: InterPro
    23. uropod organization Source: Ensembl

    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

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.

    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
    ProteomesiUP000005640: 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

    1. actin cytoskeleton Source: UniProtKB
    2. actomyosin Source: UniProt
    3. actomyosin contractile ring Source: UniProtKB
    4. cell-cell adherens junction Source: Ensembl
    5. cell leading edge Source: UniProtKB
    6. cleavage furrow Source: UniProtKB
    7. cortical cytoskeleton Source: Ensembl
    8. cytoplasm Source: UniProtKB
    9. cytosol Source: UniProtKB
    10. extracellular vesicular exosome Source: UniProtKB
    11. immunological synapse Source: Ensembl
    12. membrane Source: UniProtKB
    13. myosin II complex Source: UniProt
    14. myosin II filament Source: UniProt
    15. neuromuscular junction Source: Ensembl
    16. nucleus Source: UniProtKB
    17. plasma membrane Source: UniProtKB
    18. protein complex Source: UniProtKB
    19. ruffle Source: UniProtKB
    20. spindle Source: Ensembl
    21. stress fiber Source: UniProtKB
    22. uropod Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti93 – 931N → K in MHA. 1 Publication
    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
    VAR_010792
    Natural varianti1066 – 10727Missing in MHA and SBS.
    VAR_044228
    Natural varianti1155 – 11551T → I in MHA and FTNS. 2 Publications
    VAR_010794
    Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
    VAR_018313
    Natural varianti1424 – 14241D → H in FTNS and MHA. 5 Publications
    VAR_010796
    Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
    VAR_018316
    Natural varianti1424 – 14241D → Y in MHA. 2 Publications
    VAR_018317
    Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
    VAR_010797
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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
    VAR_010792
    Natural varianti1066 – 10727Missing in MHA and SBS.
    VAR_044228
    Natural varianti1165 – 11651R → C in FTNS and SBS. 3 Publications
    VAR_010795
    Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
    VAR_018313
    Natural varianti1205 – 12073Missing in SBS.
    VAR_018314
    Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
    VAR_018316
    Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
    VAR_010797
    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
    VAR_010792
    Natural varianti910 – 9101K → Q in FTNS. 1 Publication
    VAR_044226
    Natural varianti1155 – 11551T → I in MHA and FTNS. 2 Publications
    VAR_010794
    Natural varianti1165 – 11651R → C in FTNS and SBS. 3 Publications
    VAR_010795
    Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
    VAR_018313
    Natural varianti1424 – 14241D → H in FTNS and MHA. 5 Publications
    VAR_010796
    Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
    VAR_018316
    Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
    VAR_010797
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
    VAR_010792
    Natural varianti702 – 7021R → H in APSM and EPS. 3 Publications
    VAR_018311
    Natural varianti1114 – 11141S → P in APSM. 1 Publication
    VAR_018312
    Epstein syndrome (EPS) [MIM:153650]: An autosomal dominant disorder characterized by the association of macrothrombocytopathy, sensorineural hearing loss and nephritis.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961S → L in EPS. 2 Publications
    VAR_018309
    Natural varianti702 – 7021R → C in APSM, EPS, FTNS, MHA and SBS. 3 Publications
    VAR_010792
    Natural varianti702 – 7021R → H in APSM and EPS. 3 Publications
    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
    VAR_030385
    Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
    VAR_010797
    Deafness, autosomal dominant, 17 (DFNA17) [MIM:603622]: A form of deafness characterized by progressive high frequency hearing impairment and cochleosaccular degeneration.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti705 – 7051R → H in DFNA17. 1 Publication
    VAR_010793
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
    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

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 19601959Myosin-9PRO_0000123416Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei8 – 81N6-acetyllysine1 Publication
    Modified residuei11 – 111Phosphotyrosine1 Publication
    Modified residuei102 – 1021N6-acetyllysine1 Publication
    Modified residuei299 – 2991N6-acetyllysine1 Publication
    Modified residuei613 – 6131N6-acetyllysineBy similarity
    Modified residuei754 – 7541PhosphotyrosineBy similarity
    Modified residuei850 – 8501N6-succinyllysineBy similarity
    Modified residuei860 – 8601N6-acetyllysineBy similarity
    Modified residuei975 – 9751N6-acetyllysineBy similarity
    Modified residuei1024 – 10241N6-acetyllysine1 Publication
    Modified residuei1249 – 12491N6-acetyllysineBy similarity
    Modified residuei1357 – 13571N6-acetyllysine1 Publication
    Modified residuei1392 – 13921N6-acetyllysine1 Publication
    Modified residuei1404 – 14041N6-acetyllysine1 Publication
    Modified residuei1410 – 14101N6-acetyllysine1 Publication
    Modified residuei1459 – 14591N6-acetyllysine1 Publication
    Modified residuei1638 – 16381N6-acetyllysine1 Publication
    Modified residuei1669 – 16691N6-succinyllysineBy similarity
    Modified residuei1714 – 17141Phosphoserine1 Publication
    Modified residuei1793 – 17931N6-acetyllysineBy similarity
    Modified residuei1802 – 18021N6-acetyllysineBy similarity
    Modified residuei1845 – 18451N6-acetyllysineBy similarity
    Modified residuei1943 – 19431Phosphoserine10 Publications

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP35579.
    PaxDbiP35579.
    PeptideAtlasiP35579.
    PRIDEiP35579.

    PTM databases

    PhosphoSiteiP35579.

    Miscellaneous databases

    PMAP-CutDBP35579.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP35579.
    BgeeiP35579.
    CleanExiHS_MYH9.
    GenevestigatoriP35579.

    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
    MEN1O002557EBI-350338,EBI-592789
    NCLP193383EBI-350338,EBI-346967
    SVILO463852EBI-350338,EBI-6995105From a different organism.

    Protein-protein interaction databases

    BioGridi110712. 94 interactions.
    DIPiDIP-33103N.
    IntActiP35579. 49 interactions.
    MINTiMINT-7901706.
    STRINGi9606.ENSP00000216181.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 7-897, 1894-1935.
    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

    eggNOGiCOG5022.
    HOGENOMiHOG000173958.
    HOVERGENiHBG004704.
    InParanoidiP35579.
    KOiK10352.
    OMAiKRENDSI.
    OrthoDBiEOG71CFK3.
    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. Regulat_G_prot_signal_superfam.
    [Graphical view]
    PfamiPF00612. IQ. 1 hit.
    PF00063. 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. Align

    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

    MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSDKSG FEPASLKEEV     50
    GEEAIVELVE NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN 100
    LKERYYSGLI YTYSGLFCVV INPYKNLPIY SEEIVEMYKG KKRHEMPPHI 150
    YAITDTAYRS MMQDREDQSI LCTGESGAGK TENTKKVIQY LAYVASSHKS 200
    KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR INFDVNGYIV 250
    GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY 300
    RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEEEQMGLL RVISGVLQLG 350
    NIVFKKERNT DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY 400
    VQKAQTKEQA DFAIEALAKA TYERMFRWLV LRINKALDKT KRQGASFIGI 450
    LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF NHTMFILEQE EYQREGIEWN 500
    FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK SFVEKVMQEQ 550
    GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL 600
    HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY 650
    KEQLAKLMAT LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG 700
    IRICRQGFPN RVVFQEFRQR YEILTPNSIP KGFMDGKQAC VLMIKALELD 750
    SNLYRIGQSK VFFRAGVLAH LEEERDLKIT DVIIGFQACC RGYLARKAFA 800
    KRQQQLTAMK VLQRNCAAYL KLRNWQWWRL FTKVKPLLQV SRQEEEMMAK 850
    EEELVKVREK QLAAENRLTE METLQSQLMA EKLQLQEQLQ AETELCAEAE 900
    ELRARLTAKK QELEEICHDL EARVEEEEER CQHLQAEKKK MQQNIQELEE 950
    QLEEEESARQ KLQLEKVTTE AKLKKLEEEQ IILEDQNCKL AKEKKLLEDR 1000
    IAEFTTNLTE EEEKSKSLAK LKNKHEAMIT DLEERLRREE KQRQELEKTR 1050
    RKLEGDSTDL SDQIAELQAQ IAELKMQLAK KEEELQAALA RVEEEAAQKN 1100
    MALKKIRELE SQISELQEDL ESERASRNKA EKQKRDLGEE LEALKTELED 1150
    TLDSTAAQQE LRSKREQEVN ILKKTLEEEA KTHEAQIQEM RQKHSQAVEE 1200
    LAEQLEQTKR VKANLEKAKQ TLENERGELA NEVKVLLQGK GDSEHKRKKV 1250
    EAQLQELQVK FNEGERVRTE LADKVTKLQV ELDNVTGLLS QSDSKSSKLT 1300
    KDFSALESQL QDTQELLQEE NRQKLSLSTK LKQVEDEKNS FREQLEEEEE 1350
    AKHNLEKQIA TLHAQVADMK KKMEDSVGCL ETAEEVKRKL QKDLEGLSQR 1400
    HEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSACNLE KKQKKFDQLL 1450
    AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK 1500
    QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA 1550
    TEDAKLRLEV NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED 1600
    ERKQRSMAVA ARKKLEMDLK DLEAHIDSAN KNRDEAIKQL RKLQAQMKDC 1650
    MRELDDTRAS REEILAQAKE NEKKLKSMEA EMIQLQEELA AAERAKRQAQ 1700
    QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE EQGNTELIND 1750
    RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KVKLQEMEGT 1800
    VKSKYKASIT ALEAKIAQLE EQLDNETKER QAACKQVRRT EKKLKDVLLQ 1850
    VDDERRNAEQ YKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL 1900
    EDATETADAM NREVSSLKNK LRRGDLPFVV PRRMARKGAG DGSDEEVDGK 1950
    ADGAEAKPAE 1960
    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 CAD89954.1 differs from that shown. Reason: Frameshift at position 1890.

    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
    VAR_010791
    Natural varianti95 – 951A → T in MHA. 1 Publication
    VAR_018308
    Natural varianti96 – 961S → L in EPS. 2 Publications
    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
    VAR_010792
    Natural varianti702 – 7021R → H in APSM and EPS. 3 Publications
    VAR_018311
    Natural varianti705 – 7051R → H in DFNA17. 1 Publication
    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
    VAR_044226
    Natural varianti967 – 9671V → E.
    Corresponds to variant rs16996652 [ dbSNP | Ensembl ].
    VAR_044227
    Natural varianti1066 – 10727Missing in MHA and SBS.
    VAR_044228
    Natural varianti1114 – 11141S → P in APSM. 1 Publication
    VAR_018312
    Natural varianti1155 – 11551T → I in MHA and FTNS. 2 Publications
    VAR_010794
    Natural varianti1165 – 11651R → C in FTNS and SBS. 3 Publications
    VAR_010795
    Natural varianti1165 – 11651R → L in FTNS, MHA and SBS. 3 Publications
    VAR_018313
    Natural varianti1205 – 12073Missing in SBS.
    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
    VAR_010796
    Natural varianti1424 – 14241D → N in FTNS, MHA, SBS and MPSD; results in reduced protein levels. 6 Publications
    VAR_018316
    Natural varianti1424 – 14241D → Y in MHA. 2 Publications
    VAR_018317
    Natural varianti1626 – 16261I → V.1 Publication
    Corresponds to variant rs2269529 [ dbSNP | Ensembl ].
    VAR_018318
    Natural varianti1816 – 18161I → V in EPS. 1 Publication
    VAR_030385
    Natural varianti1841 – 18411E → K in FTNS, SBS, MHA and EPS. 6 Publications
    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:
    EMBL
    GenBank
    DDBJ
    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_002473.4. [P35579-1]
    UniGeneiHs.474751.

    Genome annotation databases

    EnsembliENST00000216181; ENSP00000216181; ENSG00000100345. [P35579-1]
    GeneIDi4627.
    KEGGihsa:4627.
    UCSCiuc003apg.3. human. [P35579-1]

    Polymorphism databases

    DMDMi6166599.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13927.1. [P35579-1 ]
    PIRi A61231.
    RefSeqi NP_002464.1. NM_002473.4. [P35579-1 ]
    UniGenei Hs.474751.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LNK NMR - C 1897-1935 [» ]
    3ZWH X-ray 1.94 Q 1893-1937 [» ]
    4CFQ X-ray 1.37 Q/R 1893-1937 [» ]
    4CFR X-ray 1.40 Q 1893-1937 [» ]
    4ETO X-ray 1.54 P 1908-1923 [» ]
    ProteinModelPortali P35579.
    SMRi P35579. Positions 7-897, 1894-1935.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110712. 94 interactions.
    DIPi DIP-33103N.
    IntActi P35579. 49 interactions.
    MINTi MINT-7901706.
    STRINGi 9606.ENSP00000216181.

    Chemistry

    ChEMBLi CHEMBL2189151.

    PTM databases

    PhosphoSitei P35579.

    Polymorphism databases

    DMDMi 6166599.

    Proteomic databases

    MaxQBi P35579.
    PaxDbi P35579.
    PeptideAtlasi P35579.
    PRIDEi P35579.

    Protocols and materials databases

    DNASUi 4627.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216181 ; ENSP00000216181 ; ENSG00000100345 . [P35579-1 ]
    GeneIDi 4627.
    KEGGi hsa:4627.
    UCSCi uc003apg.3. human. [P35579-1 ]

    Organism-specific databases

    CTDi 4627.
    GeneCardsi GC22M036677.
    GeneReviewsi MYH9.
    HGNCi HGNC:7579. MYH9.
    HPAi CAB015386.
    HPA001644.
    MIMi 153640. phenotype.
    153650. phenotype.
    155100. phenotype.
    160775. gene.
    600208. phenotype.
    603622. phenotype.
    605249. phenotype.
    neXtProti NX_P35579.
    Orphaneti 90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
    182050. MYH9-related disease.
    PharmGKBi PA31377.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5022.
    HOGENOMi HOG000173958.
    HOVERGENi HBG004704.
    InParanoidi P35579.
    KOi K10352.
    OMAi KRENDSI.
    OrthoDBi EOG71CFK3.
    PhylomeDBi P35579.
    TreeFami TF333601.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.

    Miscellaneous databases

    ChiTaRSi MYH9. human.
    GeneWikii MYH9.
    GenomeRNAii 4627.
    NextBioi 17810.
    PMAP-CutDB P35579.
    PROi P35579.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35579.
    Bgeei P35579.
    CleanExi HS_MYH9.
    Genevestigatori P35579.

    Family and domain databases

    Gene3Di 4.10.270.10. 1 hit.
    InterProi IPR000048. 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 ]
    Pfami PF00612. IQ. 1 hit.
    PF00063. Myosin_head. 1 hit.
    PF02736. Myosin_N. 1 hit.
    PF01576. Myosin_tail_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    SMARTi SM00015. IQ. 1 hit.
    SM00242. MYSc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48097. SSF48097. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50096. IQ. 1 hit.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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. 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.
      , 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. 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.
      , 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
      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. Cited for: INTERACTION WITH SVIL.
    13. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    20. Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
    21. Cited for: ASSOCIATION WITH END STAGE RENAL DISEASE.
    22. 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. 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. 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. 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. 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. 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.
      , 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-810.
    48. Cited for: POSITION OF MUTATIONS IN MYH9-RELATED DISEASE.

    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: October 1, 2014
    This is version 175 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

    External Data

    Dasty 3