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Q8VDD5

- MYH9_MOUSE

UniProt

Q8VDD5 - MYH9_MOUSE

Protein

Myosin-9

Gene

Myh9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 4 (02 Sep 2008)
      Previous versions | rss
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    Functioni

    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 By similarity. Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.By similarity1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi174 – 1818ATPSequence Analysis

    GO - Molecular functioni

    1. actin-dependent ATPase activity Source: Ensembl
    2. actin filament binding Source: UniProtKB
    3. ADP binding Source: Ensembl
    4. ATPase activity Source: UniProtKB
    5. ATP binding Source: UniProtKB-KW
    6. microfilament motor activity Source: UniProtKB
    7. protein anchor Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. actin filament-based movement Source: UniProtKB
    3. angiogenesis Source: UniProtKB
    4. blood vessel endothelial cell migration Source: UniProtKB
    5. cell adhesion Source: MGI
    6. cell morphogenesis involved in differentiation Source: MGI
    7. cellular component movement Source: MGI
    8. cytokinesis Source: UniProtKB
    9. establishment of meiotic spindle localization Source: MGI
    10. establishment of T cell polarity Source: MGI
    11. in utero embryonic development Source: MGI
    12. meiotic spindle organization Source: MGI
    13. membrane protein ectodomain proteolysis Source: UniProtKB
    14. monocyte differentiation Source: UniProtKB
    15. myoblast fusion Source: MGI
    16. platelet formation Source: UniProtKB
    17. protein transport Source: UniProtKB
    18. regulation of cell shape Source: UniProtKB
    19. single organismal cell-cell adhesion Source: MGI
    20. uropod organization Source: MGI

    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_199054. Translocation of GLUT4 to the plasma membrane.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:107717. Myh9.

    Subcellular locationi

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

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. actomyosin contractile ring Source: UniProtKB
    3. cell-cell adherens junction Source: MGI
    4. cell cortex Source: MGI
    5. cell leading edge Source: UniProtKB
    6. cleavage furrow Source: UniProtKB
    7. COP9 signalosome Source: Ensembl
    8. cortical cytoskeleton Source: MGI
    9. cytoplasm Source: UniProtKB
    10. cytosol Source: UniProtKB
    11. extracellular vesicular exosome Source: Ensembl
    12. integrin complex Source: Ensembl
    13. myosin complex Source: MGI
    14. myosin II complex Source: MGI
    15. nucleus Source: UniProtKB
    16. plasma membrane Source: UniProtKB
    17. protein complex Source: UniProtKB
    18. ruffle Source: UniProtKB
    19. stress fiber Source: UniProtKB
    20. uropod Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 19601959Myosin-9PRO_0000123417Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei8 – 81N6-acetyllysine1 Publication
    Modified residuei11 – 111PhosphotyrosineBy similarity
    Modified residuei102 – 1021N6-acetyllysineBy similarity
    Modified residuei299 – 2991N6-acetyllysine1 Publication
    Modified residuei613 – 6131N6-acetyllysine1 Publication
    Modified residuei754 – 7541Phosphotyrosine1 Publication
    Modified residuei850 – 8501N6-succinyllysine1 Publication
    Modified residuei860 – 8601N6-acetyllysine1 Publication
    Modified residuei975 – 9751N6-acetyllysine1 Publication
    Modified residuei1024 – 10241N6-acetyllysine1 Publication
    Modified residuei1249 – 12491N6-acetyllysine1 Publication
    Modified residuei1357 – 13571N6-acetyllysineBy similarity
    Modified residuei1392 – 13921N6-acetyllysineBy similarity
    Modified residuei1404 – 14041N6-acetyllysineBy similarity
    Modified residuei1410 – 14101N6-acetyllysineBy similarity
    Modified residuei1459 – 14591N6-acetyllysine1 Publication
    Modified residuei1638 – 16381N6-acetyllysineBy similarity
    Modified residuei1669 – 16691N6-succinyllysine1 Publication
    Modified residuei1714 – 17141PhosphoserineBy similarity
    Modified residuei1793 – 17931N6-acetyllysine1 Publication
    Modified residuei1802 – 18021N6-acetyllysine1 Publication
    Modified residuei1845 – 18451N6-acetyllysine1 Publication
    Modified residuei1939 – 19391Phosphothreonine2 Publications
    Modified residuei1943 – 19431Phosphoserine5 Publications

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8VDD5.
    PaxDbiQ8VDD5.
    PRIDEiQ8VDD5.

    PTM databases

    PhosphoSiteiQ8VDD5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8VDD5.
    BgeeiQ8VDD5.
    CleanExiMM_MYH9.
    GenevestigatoriQ8VDD5.

    Interactioni

    Subunit structurei

    Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with SVIL, HTRA3 and SLC6A4 By similarity. Interacts with PDLIM2. Interacts with RASIP1. Interacts with DDR1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Trpm7Q923J13EBI-400906,EBI-8010314

    Protein-protein interaction databases

    BioGridi201650. 14 interactions.
    DIPiDIP-29546N.
    IntActiQ8VDD5. 14 interactions.
    MINTiMINT-2524850.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VDD5.
    SMRiQ8VDD5. Positions 7-897, 1894-1934.
    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 coili841 – 19261086Sequence 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.
    GeneTreeiENSGT00650000092896.
    HOGENOMiHOG000173958.
    HOVERGENiHBG004704.
    InParanoidiQ8VDD5.
    KOiK10352.
    OMAiMANSSGK.
    OrthoDBiEOG71CFK3.
    PhylomeDBiQ8VDD5.
    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.
    [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]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS50096. IQ. 1 hit.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8VDD5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSSKNG FEPASLKEEV     50
    GEEAIVELVE NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN 100
    LKERYYSGLI YTYSGLFCVV INPYKNLPIY SEEIVEMYKG KKRHEMPPHI 150
    YAITDTAYRS MMQDREDQSI LCTGESGAGK TENTKKVIQY LAHVASSHKS 200
    KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR INFDVNGYIV 250
    GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY 300
    RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEDEQMGLL RVISGVLQLG 350
    NIAFKKERNT DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY 400
    VQKAQTKEQA DFAIEALAKA TYERMFRWLV LRINKALDKT KRQGASFIGI 450
    LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF NHTMFILEQE EYQREGIEWN 500
    FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK SFVEKVVQEQ 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 RLRNWQWWRL FTKVKPLLNS IRHEDELLAK 850
    EAELTKVREK HLAAENRLTE METMQSQLMA EKLQLQEQLQ AETELCAEAE 900
    ELRARLTAKK QELEEICHDL EARVEEEEER CQYLQAEKKK MQQNIQELEE 950
    QLEEEESARQ KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR 1000
    VAEFTTNLME EEEKSKSLAK LKNKHEAMIT DLEERLRREE KQRQELEKTR 1050
    RKLEGDSTDL SDQIAELQAQ IAELKMQLAK KEEELQAALA RVEEEAAQKN 1100
    MALKKIRELE TQISELQEDL ESERASRNKA EKQKRDLGEE LEALKTELED 1150
    TLDSTAAQQE LRSKREQEVS ILKKTLEDEA KTHEAQIQEM RQKHSQAVEE 1200
    LADQLEQTKR VKATLEKAKQ TLENERGELA NEVKALLQGK GDSEHKRKKV 1250
    EAQLQELQVK FSEGERVRTE LADKVTKLQV ELDSVTGLLS QSDSKSSKLT 1300
    KDFSALESQL QDTQELLQEE NRQKLSLSTK LKQMEDEKNS FREQLEEEEE 1350
    AKRNLEKQIA TLHAQVTDMK KKMEDGVGCL ETAEEAKRRL QKDLEGLSQR 1400
    LEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSVSNLE KKQKKFDQLL 1450
    AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK 1500
    QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA 1550
    TEDAKLRLEV NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED 1600
    ERKQRSMAMA ARKKLEMDLK DLEAHIDTAN KNREEAIKQL RKLQAQMKDC 1650
    MRELDDTRAS REEILAQAKE NEKKLKSMEA EMIQLQEELA AAERAKRQAQ 1700
    QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE EQGNTELIND 1750
    RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KAKLQEMESA 1800
    VKSKYKASIA ALEAKIAQLE EQLDNETKER QAASKQVRRT EKKLKDVLLQ 1850
    VEDERRNAEQ FKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL 1900
    EDATETADAM NREVSSLKNK LRRGDLPFVV TRRIVRKGTG DCSDEEVDGK 1950
    ADGADAKAAE 1960
    Length:1,960
    Mass (Da):226,372
    Last modified:September 2, 2008 - v4
    Checksum:iAAAC0E83A0A4F24A
    GO

    Sequence cautioni

    The sequence BAE27768.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1733 – 17331Q → L in CAC85955. (PubMed:11943476)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ312390 mRNA. Translation: CAC85955.1.
    AK147203 mRNA. Translation: BAE27761.1.
    AK147206 mRNA. Translation: BAE27763.1.
    AK147208 mRNA. Translation: BAE27765.1.
    AK147209 mRNA. Translation: BAE27766.1.
    AK147210 mRNA. Translation: BAE27767.1.
    AK147211 mRNA. Translation: BAE27768.1. Different initiation.
    AK147215 mRNA. Translation: BAE27772.1.
    AK147216 mRNA. Translation: BAE27773.1.
    AK147221 mRNA. Translation: BAE27776.1.
    AK147222 mRNA. Translation: BAE27777.1.
    AK147223 mRNA. Translation: BAE27778.1.
    AK147233 mRNA. Translation: BAE27783.1.
    AK147235 mRNA. Translation: BAE27785.1.
    AK147296 mRNA. Translation: BAE27829.1.
    AK147407 mRNA. Translation: BAE27894.1.
    AK147430 mRNA. Translation: BAE27906.1.
    AL583886 Genomic DNA. Translation: CAM23428.1.
    AK131171 mRNA. Translation: BAD21421.1.
    BC044834 mRNA. Translation: AAH44834.1.
    CCDSiCCDS27605.1.
    RefSeqiNP_071855.2. NM_022410.3.
    UniGeneiMm.29677.

    Genome annotation databases

    EnsembliENSMUST00000016771; ENSMUSP00000016771; ENSMUSG00000022443.
    GeneIDi17886.
    KEGGimmu:17886.
    UCSCiuc007woc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ312390 mRNA. Translation: CAC85955.1 .
    AK147203 mRNA. Translation: BAE27761.1 .
    AK147206 mRNA. Translation: BAE27763.1 .
    AK147208 mRNA. Translation: BAE27765.1 .
    AK147209 mRNA. Translation: BAE27766.1 .
    AK147210 mRNA. Translation: BAE27767.1 .
    AK147211 mRNA. Translation: BAE27768.1 . Different initiation.
    AK147215 mRNA. Translation: BAE27772.1 .
    AK147216 mRNA. Translation: BAE27773.1 .
    AK147221 mRNA. Translation: BAE27776.1 .
    AK147222 mRNA. Translation: BAE27777.1 .
    AK147223 mRNA. Translation: BAE27778.1 .
    AK147233 mRNA. Translation: BAE27783.1 .
    AK147235 mRNA. Translation: BAE27785.1 .
    AK147296 mRNA. Translation: BAE27829.1 .
    AK147407 mRNA. Translation: BAE27894.1 .
    AK147430 mRNA. Translation: BAE27906.1 .
    AL583886 Genomic DNA. Translation: CAM23428.1 .
    AK131171 mRNA. Translation: BAD21421.1 .
    BC044834 mRNA. Translation: AAH44834.1 .
    CCDSi CCDS27605.1.
    RefSeqi NP_071855.2. NM_022410.3.
    UniGenei Mm.29677.

    3D structure databases

    ProteinModelPortali Q8VDD5.
    SMRi Q8VDD5. Positions 7-897, 1894-1934.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201650. 14 interactions.
    DIPi DIP-29546N.
    IntActi Q8VDD5. 14 interactions.
    MINTi MINT-2524850.

    PTM databases

    PhosphoSitei Q8VDD5.

    Proteomic databases

    MaxQBi Q8VDD5.
    PaxDbi Q8VDD5.
    PRIDEi Q8VDD5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000016771 ; ENSMUSP00000016771 ; ENSMUSG00000022443 .
    GeneIDi 17886.
    KEGGi mmu:17886.
    UCSCi uc007woc.1. mouse.

    Organism-specific databases

    CTDi 4627.
    MGIi MGI:107717. Myh9.

    Phylogenomic databases

    eggNOGi COG5022.
    GeneTreei ENSGT00650000092896.
    HOGENOMi HOG000173958.
    HOVERGENi HBG004704.
    InParanoidi Q8VDD5.
    KOi K10352.
    OMAi MANSSGK.
    OrthoDBi EOG71CFK3.
    PhylomeDBi Q8VDD5.
    TreeFami TF333601.

    Enzyme and pathway databases

    Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.

    Miscellaneous databases

    ChiTaRSi MYH9. mouse.
    NextBioi 292701.
    PROi Q8VDD5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VDD5.
    Bgeei Q8VDD5.
    CleanExi MM_MYH9.
    Genevestigatori Q8VDD5.

    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.
    [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 SSF52540. SSF52540. 1 hit.
    PROSITEi PS50096. IQ. 1 hit.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the murine non-muscle myosin heavy chain IIA gene ortholog of human MYH9 responsible for May-Hegglin, Sebastian, Fechtner, and Epstein syndromes."
      D'Apolito M., Guarnieri V., Boncristiano M., Zelante L., Savoia A.
      Gene 286:215-222(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Amnion, Brain, Embryo, Embryonic liver and Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.
      Submitted (MAR-2008) to UniProtKB
      Tissue: Embryonic fibroblast.
    5. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
      DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 626-1960.
      Strain: ICR.
      Tissue: Embryonic tail.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1066-1960.
      Strain: FVB/N.
      Tissue: Mammary tumor.
    7. Cited for: ISGYLATION.
    8. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    9. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The collagen receptor DDR1 regulates cell spreading and motility by associating with myosin IIA."
      Huang Y., Arora P., McCulloch C.A., Vogel W.F.
      J. Cell Sci. 122:1637-1646(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DDR1, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    15. "Blood vessel tubulogenesis requires Rasip1 regulation of GTPase signaling."
      Xu K., Sacharidou A., Fu S., Chong D.C., Skaug B., Chen Z.J., Davis G.E., Cleaver O.
      Dev. Cell 20:526-539(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASIP1.
    16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-299; LYS-613; LYS-860; LYS-975; LYS-1024; LYS-1249; LYS-1459; LYS-1793; LYS-1802 AND LYS-1845, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-850 AND LYS-1669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiMYH9_MOUSE
    AccessioniPrimary (citable) accession number: Q8VDD5
    Secondary accession number(s): Q3UHT9
    , Q3UHU4, Q6KAN6, Q811I2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 117 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3