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Q9Z239

- PLM_MOUSE

UniProt

Q9Z239 - PLM_MOUSE

Protein

Phospholemman

Gene

Fxyd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    May have a functional role in muscle contraction. Induces a hyperpolarization-activated chloride current when exogenously expressed By similarity.By similarity

    GO - Molecular functioni

    1. chloride channel activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular calcium ion homeostasis Source: Ensembl
    2. muscle contraction Source: Ensembl

    Keywords - Molecular functioni

    Chloride channel, Ion channel

    Keywords - Biological processi

    Ion transport, Transport

    Keywords - Ligandi

    Chloride

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospholemman
    Alternative name(s):
    FXYD domain-containing ion transport regulator 1
    Gene namesi
    Name:Fxyd1
    Synonyms:Plm
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1889273. Fxyd1.

    Subcellular locationi

    GO - Cellular componenti

    1. chloride channel complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Chaini21 – 9272PhospholemmanPRO_0000010360Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi60 – 601S-palmitoyl cysteineBy similarity
    Lipidationi62 – 621S-palmitoyl cysteineBy similarity
    Modified residuei79 – 791Phosphothreonine1 Publication
    Modified residuei83 – 831Phosphoserine; alternate1 Publication
    Modified residuei83 – 831Phosphoserine; by PKA and PKC; alternateBy similarity
    Modified residuei88 – 881Phosphoserine; by PKABy similarity

    Post-translational modificationi

    Major plasma membrane substrate for cAMP-dependent protein kinase (PK-A) and protein kinase C (PK-C) in several different tissues. Phosphorylated in response to insulin and adrenergic stimulation. May be phosphorylated by DMPK By similarity.By similarity
    Palmitoylation increases half-life and stability, it is enhanced upon phosphorylation at Ser-88 by PKA.By similarity

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiQ9Z239.
    PRIDEiQ9Z239.

    PTM databases

    PhosphoSiteiQ9Z239.

    Expressioni

    Gene expression databases

    BgeeiQ9Z239.
    CleanExiMM_FXYD1.
    GenevestigatoriQ9Z239.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000048460.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z239.
    SMRiQ9Z239. Positions 21-92.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 3515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini57 – 9236CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei36 – 5621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FXYD family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG42110.
    GeneTreeiENSGT00530000063932.
    HOGENOMiHOG000234467.
    HOVERGENiHBG008212.
    InParanoidiQ9Z239.
    KOiK13360.
    OMAiQEPDPFT.
    OrthoDBiEOG7WHHDM.
    PhylomeDBiQ9Z239.
    TreeFamiTF333443.

    Family and domain databases

    InterProiIPR000272. Ion-transport_regulator_FXYD.
    [Graphical view]
    PfamiPF02038. ATP1G1_PLM_MAT8. 1 hit.
    [Graphical view]
    ProDomiPD005989. PD005989. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    PROSITEiPS01310. FXYD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9Z239-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASPGHILAL CVCLLSMASA EAPQEPDPFT YDYHTLRIGG LTIAGILFIL   50
    GILIILSKRC RCKFNQQQRT GEPDEEEGTF RSSIRRLSSR RR 92
    Length:92
    Mass (Da):10,323
    Last modified:May 1, 1999 - v1
    Checksum:i0BDB1DC83417F3AD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091390 Genomic DNA. Translation: AAD11781.1.
    AF089734 mRNA. Translation: AAD41683.1.
    AK002585 mRNA. Translation: BAB22208.1.
    BC024671 mRNA. Translation: AAH24671.1.
    CCDSiCCDS21123.1.
    RefSeqiNP_062376.2. NM_019503.4.
    NP_443717.1. NM_052991.4.
    NP_443718.1. NM_052992.3.
    NP_919302.1. NM_194321.2.
    XP_006540283.1. XM_006540220.1.
    UniGeneiMm.1491.

    Genome annotation databases

    EnsembliENSMUST00000039909; ENSMUSP00000048460; ENSMUSG00000036570.
    ENSMUST00000071697; ENSMUSP00000071617; ENSMUSG00000036570.
    ENSMUST00000108110; ENSMUSP00000103745; ENSMUSG00000036570.
    GeneIDi56188.
    KEGGimmu:56188.
    UCSCiuc009ghu.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091390 Genomic DNA. Translation: AAD11781.1 .
    AF089734 mRNA. Translation: AAD41683.1 .
    AK002585 mRNA. Translation: BAB22208.1 .
    BC024671 mRNA. Translation: AAH24671.1 .
    CCDSi CCDS21123.1.
    RefSeqi NP_062376.2. NM_019503.4.
    NP_443717.1. NM_052991.4.
    NP_443718.1. NM_052992.3.
    NP_919302.1. NM_194321.2.
    XP_006540283.1. XM_006540220.1.
    UniGenei Mm.1491.

    3D structure databases

    ProteinModelPortali Q9Z239.
    SMRi Q9Z239. Positions 21-92.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000048460.

    PTM databases

    PhosphoSitei Q9Z239.

    Proteomic databases

    PaxDbi Q9Z239.
    PRIDEi Q9Z239.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000039909 ; ENSMUSP00000048460 ; ENSMUSG00000036570 .
    ENSMUST00000071697 ; ENSMUSP00000071617 ; ENSMUSG00000036570 .
    ENSMUST00000108110 ; ENSMUSP00000103745 ; ENSMUSG00000036570 .
    GeneIDi 56188.
    KEGGi mmu:56188.
    UCSCi uc009ghu.2. mouse.

    Organism-specific databases

    CTDi 5348.
    MGIi MGI:1889273. Fxyd1.

    Phylogenomic databases

    eggNOGi NOG42110.
    GeneTreei ENSGT00530000063932.
    HOGENOMi HOG000234467.
    HOVERGENi HBG008212.
    InParanoidi Q9Z239.
    KOi K13360.
    OMAi QEPDPFT.
    OrthoDBi EOG7WHHDM.
    PhylomeDBi Q9Z239.
    TreeFami TF333443.

    Miscellaneous databases

    ChiTaRSi FXYD1. mouse.
    NextBioi 311978.
    PROi Q9Z239.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Z239.
    CleanExi MM_FXYD1.
    Genevestigatori Q9Z239.

    Family and domain databases

    InterProi IPR000272. Ion-transport_regulator_FXYD.
    [Graphical view ]
    Pfami PF02038. ATP1G1_PLM_MAT8. 1 hit.
    [Graphical view ]
    ProDomi PD005989. PD005989. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    PROSITEi PS01310. FXYD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
    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: Kidney.
    3. "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: FVB/N.
      Tissue: Colon.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiPLM_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z239
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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