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Q9CQ19

- MYL9_MOUSE

UniProt

Q9CQ19 - MYL9_MOUSE

Protein

Myosin regulatory light polypeptide 9

Gene

Myl9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi42 – 5312Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    Keywords - Molecular functioni

    Motor protein, Muscle protein, Myosin

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin regulatory light polypeptide 9
    Alternative name(s):
    Myosin regulatory light chain 2, smooth muscle isoform
    Myosin regulatory light chain 9
    Gene namesi
    Name:Myl9
    Synonyms:Myrl2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2138915. Myl9.

    Subcellular locationi

    GO - Cellular componenti

    1. myosin II complex Source: MGI
    2. stress fiber Source: MGI
    3. Z disc Source: MGI

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 172171Myosin regulatory light polypeptide 9PRO_0000198736Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei19 – 191Phosphothreonine; by MLCK, CIT and ROCK2
    Modified residuei20 – 201Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1, ROCK2, DAPK1; DAPK2 and ZIPK/DAPK31 Publication

    Post-translational modificationi

    Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9CQ19.
    PaxDbiQ9CQ19.
    PRIDEiQ9CQ19.

    PTM databases

    PhosphoSiteiQ9CQ19.

    Expressioni

    Gene expression databases

    BgeeiQ9CQ19.
    CleanExiMM_MYL9.
    GenevestigatoriQ9CQ19.

    Interactioni

    Subunit structurei

    Myosin is a hexamer of 2 heavy chains and 4 light chains.By similarity

    Protein-protein interaction databases

    BioGridi221155. 1 interaction.
    IntActiQ9CQ19. 3 interactions.
    MINTiMINT-4102187.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CQ19.
    SMRiQ9CQ19. Positions 26-168.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 6436EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini98 – 13336EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini134 – 16936EF-hand 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 3 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5126.
    GeneTreeiENSGT00730000110490.
    HOGENOMiHOG000233018.
    HOVERGENiHBG012180.
    InParanoidiQ9CQ19.
    KOiK12755.
    OMAiITPSKTM.
    OrthoDBiEOG7992RX.
    PhylomeDBiQ9CQ19.
    TreeFamiTF314218.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF00036. EF-hand_1. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 2 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9CQ19-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID    50
    KEDLHDMLAS LGKNPTDEYL EGMMNEAPGP INFTMFLTMF GEKLNGTDPE 100
    DVIRNAFACF DEEASGFIHE DHLRELLTTM GDRFTDEEVD EMYREAPIDK 150
    KGNFNYVEFT RILKHGAKDK DD 172
    Length:172
    Mass (Da):19,854
    Last modified:January 23, 2007 - v3
    Checksum:iD588C708BF5A2D56
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321D → V in BAE35452. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK007972 mRNA. Translation: BAB25381.1.
    AK020258 mRNA. Translation: BAB32043.1.
    AK159880 mRNA. Translation: BAE35452.1.
    BC049974 mRNA. Translation: AAH49974.2.
    BC055439 mRNA. Translation: AAH55439.1.
    CCDSiCCDS50779.1.
    RefSeqiNP_742116.1. NM_172118.1.
    XP_006500516.1. XM_006500453.1.
    UniGeneiMm.271770.

    Genome annotation databases

    EnsembliENSMUST00000088552; ENSMUSP00000085913; ENSMUSG00000067818.
    GeneIDi98932.
    KEGGimmu:98932.
    UCSCiuc008nnw.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK007972 mRNA. Translation: BAB25381.1 .
    AK020258 mRNA. Translation: BAB32043.1 .
    AK159880 mRNA. Translation: BAE35452.1 .
    BC049974 mRNA. Translation: AAH49974.2 .
    BC055439 mRNA. Translation: AAH55439.1 .
    CCDSi CCDS50779.1.
    RefSeqi NP_742116.1. NM_172118.1.
    XP_006500516.1. XM_006500453.1.
    UniGenei Mm.271770.

    3D structure databases

    ProteinModelPortali Q9CQ19.
    SMRi Q9CQ19. Positions 26-168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 221155. 1 interaction.
    IntActi Q9CQ19. 3 interactions.
    MINTi MINT-4102187.

    PTM databases

    PhosphoSitei Q9CQ19.

    Proteomic databases

    MaxQBi Q9CQ19.
    PaxDbi Q9CQ19.
    PRIDEi Q9CQ19.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000088552 ; ENSMUSP00000085913 ; ENSMUSG00000067818 .
    GeneIDi 98932.
    KEGGi mmu:98932.
    UCSCi uc008nnw.2. mouse.

    Organism-specific databases

    CTDi 10398.
    MGIi MGI:2138915. Myl9.

    Phylogenomic databases

    eggNOGi COG5126.
    GeneTreei ENSGT00730000110490.
    HOGENOMi HOG000233018.
    HOVERGENi HBG012180.
    InParanoidi Q9CQ19.
    KOi K12755.
    OMAi ITPSKTM.
    OrthoDBi EOG7992RX.
    PhylomeDBi Q9CQ19.
    TreeFami TF314218.

    Miscellaneous databases

    NextBioi 353711.
    PROi Q9CQ19.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CQ19.
    CleanExi MM_MYL9.
    Genevestigatori Q9CQ19.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF00036. EF-hand_1. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 2 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Colon, Osteoclast and Pancreas.
    2. "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].
      Strain: Czech II and FVB/N.
      Tissue: Mammary gland and Salivary gland.
    3. "Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication."
      Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K.
      Mol. Cell. Biol. 26:9016-9034(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-20.

    Entry informationi

    Entry nameiMYL9_MOUSE
    AccessioniPrimary (citable) accession number: Q9CQ19
    Secondary accession number(s): Q3TW15, Q80X77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This chain binds calcium.By similarity

    Keywords - Technical termi

    Complete proteome, 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