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Q8VHX6

- FLNC_MOUSE

UniProt

Q8VHX6 - FLNC_MOUSE

Protein

Filamin-C

Gene

Flnc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (12 Dec 2006)
      Previous versions | rss
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    Functioni

    Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers.1 Publication

    GO - Molecular functioni

    1. actin binding Source: MGI

    GO - Biological processi

    1. actin filament-based process Source: MGI
    2. muscle fiber development Source: UniProtKB

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Filamin-C
    Short name:
    FLN-C
    Alternative name(s):
    ABP-280-like protein
    ABP-L
    Actin-binding-like protein
    Filamin-2
    Gamma-filamin
    Gene namesi
    Name:Flnc
    Synonyms:Abpl, Fln2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:95557. Flnc.

    Subcellular locationi

    Cytoplasm By similarity. Membrane By similarity; Peripheral membrane protein By similarity. Cytoplasmcytoskeleton By similarity. CytoplasmmyofibrilsarcomereZ line By similarity
    Note: A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z lines, while a minor fraction localizes with subsarcolemme By similarity. Targeting to developing and mature Z lines is mediated by the intradomain insert By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: MGI
    2. sarcolemma Source: Ensembl
    3. sarcoplasm Source: Ensembl
    4. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 27262726Filamin-CPRO_0000087302Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1162 – 11621PhosphoserineBy similarity
    Modified residuei2234 – 22341Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated by FBXL22, leading to proteasomal degradation.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8VHX6.
    PaxDbiQ8VHX6.
    PRIDEiQ8VHX6.

    PTM databases

    PhosphoSiteiQ8VHX6.

    Expressioni

    Developmental stagei

    During myogenesis, isoform 1 is expressed the first day, then is replaced by isoform 2.1 Publication

    Gene expression databases

    ArrayExpressiQ8VHX6.
    BgeeiQ8VHX6.
    CleanExiMM_FLNC.
    GenevestigatoriQ8VHX6.

    Interactioni

    Subunit structurei

    Homodimer; the filamin repeat 24 and the second hinge domain are important for dimer formation By similarity. Interacts with FLNB, INPPL1, ITGB1A, KCND2, MYOT, MYOZ1 and MYOZ3. Interacts with sarcoglycans SGCD and SGCG. Interacts (via filament repeats 17-18, 20-21 and 24) with USP25 (isoform USP25m only). Interacts with FBLIM1 By similarity. Interacts with XIRP1; this interaction is mediated by filamin 20 repeat By similarity. Interacts with KY. Interacts with IGFN1. Interacts with MICALL2. Interacts with ANK3 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi213053. 5 interactions.
    IntActiQ8VHX6. 8 interactions.
    MINTiMINT-1520143.
    STRINGi10090.ENSMUSP00000064163.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VHX6.
    SMRiQ8VHX6. Positions 23-2726.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 260260Actin-bindingAdd
    BLAST
    Domaini37 – 143107CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini160 – 260101CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati271 – 36999Filamin 1Add
    BLAST
    Repeati371 – 46999Filamin 2Add
    BLAST
    Repeati470 – 56697Filamin 3Add
    BLAST
    Repeati567 – 65993Filamin 4Add
    BLAST
    Repeati663 – 75997Filamin 5Add
    BLAST
    Repeati760 – 862103Filamin 6Add
    BLAST
    Repeati863 – 96199Filamin 7Add
    BLAST
    Repeati962 – 105796Filamin 8Add
    BLAST
    Repeati1058 – 115093Filamin 9Add
    BLAST
    Repeati1151 – 124595Filamin 10Add
    BLAST
    Repeati1246 – 1345100Filamin 11Add
    BLAST
    Repeati1346 – 143893Filamin 12Add
    BLAST
    Repeati1439 – 153496Filamin 13Add
    BLAST
    Repeati1535 – 163197Filamin 14Add
    BLAST
    Repeati1636 – 1735100Filamin 15Add
    BLAST
    Repeati1760 – 185596Filamin 16Add
    BLAST
    Repeati1856 – 194792Filamin 17Add
    BLAST
    Repeati1948 – 203487Filamin 18Add
    BLAST
    Repeati2037 – 212993Filamin 19Add
    BLAST
    Repeati2212 – 230796Filamin 20; mediates interaction with XIRP1PROSITE-ProRule annotationAdd
    BLAST
    Repeati2310 – 240293Filamin 21Add
    BLAST
    Repeati2404 – 249794Filamin 22Add
    BLAST
    Repeati2501 – 259393Filamin 23Add
    BLAST
    Repeati2631 – 272595Filamin 24Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1736 – 175924Hinge 1Add
    BLAST
    Regioni2163 – 224482Intradomain insert; mediate targeting to Z linesBy similarityAdd
    BLAST
    Regioni2404 – 2725322Interaction with INPPL1By similarityAdd
    BLAST
    Regioni2594 – 2726133Self-association site, tailBy similarityAdd
    BLAST
    Regioni2594 – 263037Hinge 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the filamin family.Curated
    Contains 1 actin-binding domain.Curated
    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 24 filamin repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5069.
    GeneTreeiENSGT00660000095431.
    HOGENOMiHOG000044235.
    HOVERGENiHBG004163.
    KOiK04437.
    PhylomeDBiQ8VHX6.

    Family and domain databases

    Gene3Di1.10.418.10. 2 hits.
    2.60.40.10. 24 hits.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR003961. Fibronectin_type3.
    IPR017868. Filamin/ABP280_repeat-like.
    IPR001298. Filamin/ABP280_rpt.
    IPR028559. FLN.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view]
    PANTHERiPTHR11915:SF173. PTHR11915:SF173. 1 hit.
    PfamiPF00307. CH. 2 hits.
    PF00630. Filamin. 23 hits.
    [Graphical view]
    SMARTiSM00033. CH. 2 hits.
    SM00060. FN3. 2 hits.
    SM00557. IG_FLMN. 24 hits.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    SSF81296. SSF81296. 24 hits.
    PROSITEiPS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS50194. FILAMIN_REPEAT. 24 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8VHX6-1) [UniParc]FASTAAdd to Basket

    Also known as: H1

    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

    MMNNSNYSDA SGLGLVDEAD EMPSTEKDLA EDAPWKKIQQ NTFTRWCNEH     50
    LKCVGKRLTD LQRDLSDGLR LIALLEVLSQ KRMYRKFHPR PNFRQMKLEN 100
    VSVALEFLER EHIKLVSIDS KAIVDGNLKL ILGLIWTLIL HYSISMPMWE 150
    DEDDEDARKQ TPKQRLLGWI QNKVPQLPIT NFNRDWQDGK ALGALVDNCA 200
    PGLCPDWEAW DPNQPVQNAR EAMQQADDWL GVPQVIAPEE IVDPNVDEHS 250
    VMTYLSQFPK AKLKPGAPVR SKQLNPKKAI AYGPGIEPQG NTVLQPAHFT 300
    VQTVDAGVGE VLVYIEDPEG HTEEAKVVPN NDKDRTYAVS YVPKVAGLHK 350
    VTVLFAGQNI ERSPFEVNVG MALGDANKVS ARGPGLEPVG NVANKPTYFD 400
    IYTAGAGTGD VAVVIVDPQG RRDTVEVALE DKGDNTFRCT YRPVMEGPHT 450
    VHVAFAGAPI TRSPFPVHVA EACNPNACRA SGRGLQPKGV RVKEVADFKV 500
    FTKGAGSGEL KVTVKGPKGT EEPVKVREAG DGVFECEYYP VVPGKYVVTI 550
    TWGGYAIPRS PFEVQVSPEA GAQKVRAWGP GLETGQVGKS ADFVVEAIGT 600
    EVGTLGFSIE GPSQAKIECD DKGDGSCDVR YWPTEPGEYA VHVICDDEDI 650
    RDSPFIAHIQ PAPPDCFPDK VKAFGPGLEP TGCIVDRPAE FTIDARAAGK 700
    GDLKLYAQDA DGCPIDIKVI PNGDGTFRCS YVPTKPIKHT IIVSWGGVNV 750
    PKSPFRVNVG EGSHPERVKV YGPGVEKTGL KANEPTYFTV DCSEAGQGDV 800
    SIGIKCAPGV VGPVEADIDF DIIKNDNDTF TVKYTPPGAG HYTIMVLFAN 850
    QEIPASPFHI KVDPSHDASK VKAEGPGLSR TGVEVGKPTH FTVLTKGAGK 900
    AKLDVHFAGA AKGEAVRDFE IIDNHDYSYT VKYTAVQQGN MAVTVTYGGD 950
    PVPKSPFVVN VAPPLDLSKV KVQGLNSKVA VGQEQAFSVN TRGAGGQGQL 1000
    DVRMTSPSRR PIPCKLEPGG GAEAQAVRYM PPEEGPYKVD ITYDGHPVPG 1050
    SPFAVEGVLP PDPSKVCAYG PGLKGGLVGT PAPFSIDTKG AGTGGLGLTV 1100
    EGPCEAKIEC QDNGDGSCAV SYLPTEPGEY TINILFAEAH IPGSPFKATI 1150
    QPVFDPSKVR ASGPGLERGK AGEAATFTVD CSEAGEAELT IEILSDAGVK 1200
    AEVLIQNNAD GTYHITYSPA FPGTYTITIK YGGHPIPKFP TRVHVQPAVD 1250
    TSGIKVSGPG VEPHGVLREV TTEFTVDARS LTATGGNHVT ARVLNPSGAK 1300
    TDTYVTDNGD GTYRVQYTAY EEGVHLVEVL YDEVAVPKSP FRVGVTEGCD 1350
    PTRVRAFGPG LEGGLVNKAN RFTVETRGAG TGGLGLAIEG PSEAKMSCKD 1400
    NKDGSCTVEY IPFTPGDYDV NITFGGQPIP GSPFRVPVKD VVDPGKVKCS 1450
    GPGLGTGVRA RVPQTFTVDC SQAGRAPLQV AVLGPTGVAE PVEVRDNGDG 1500
    THTVHYTPAT DGPYTVAVKY ADQEVPRSPF KIKVLPSHDA SKVRASGPGL 1550
    NASGIPASLP VEFTIDARDA GQGLLTVQIL DPEGKPKKAN IRDNGDGTYT 1600
    VSYLPDMSGR YTITIKYGGD EIPYSPFRIH ALPTGDASKC LVTVSIGGHG 1650
    LGACLGPRIQ IGEETVITVD AKAAGKGKVT CTVSTPDGAE LDVDVVENHD 1700
    GTFDIYYTAP EPGKYVITIR FGGEHIPNSP FHVLACDPLP HVEEPAEMLQ 1750
    MRQPYAPLRP GTCPTHWATE EPVVPVEPLE SMLRPFNLVI PFTVQKGELT 1800
    GEVRMPSGKT ARPNITDNKD GTITVRYAPT EKGLHQMGIK YDGNHIPGSP 1850
    LQFYVDAINS RHVSAYGPGL SHGMVNKPAT FTIVTKDAGE GGLSLAVEGP 1900
    SKAEITCKDN KDGTCTVSYL PTAPGDYSII VRFDDKHIPG SPFTAKITGD 1950
    DSMRTSQLNV GTSTDVSLKI TEGDLSQLTA SIRAPSGNEE PCLLKRLPNR 2000
    HIGISFTPKE VGEHVVSVRK SGKHVTNSPF KILVGPSEIG DASKVRVWGK 2050
    GLSEGQTFQV AEFIVDTRNA GYGGLGLSIE GPSKVDINCE DMEDGTCKVT 2100
    YCPTEPGTYI INIKFADKHV PGSPFTVKVT GEGRMKESIT RRRQAPSIAT 2150
    IGSTCDLNLK IPGNWFQMVS AQERLTRTFT RSSHTYTRTE RTEISKTRGG 2200
    ETKREVRVEE STQVGGDPFP AVFGDFLGRE RLGSFGSITR QQEGEASSQD 2250
    MTAQVTSPSG KTEAAEIVEG EDSAYSVRFV PQEMGPHTVT VKYRGQHVPG 2300
    SPFQFTVGPL GEGGAHKVRA GGTGLERGVA GVPAEFSIWT REAGAGGLSI 2350
    AVEGPSKAEI AFEDRKDGSC GVSYVVQEPG DYEVSIKFND EHIPDSPFVV 2400
    PVASLSDDAR RLTVTSLQET GLKVNQPASF AVQLNGARGV IDARVHTPSG 2450
    AVEECYVSEL DSDKHTIRFI PHENGVHSID VKFNGAHIPG SPFKIRVGEQ 2500
    SQAGDPGLVS AYGPGLEGGT TGVSSEFIVN TQNAGSGALS VTIDGPSKVQ 2550
    LDCRECPEGH VVTYTPMAPG NYLIAIKYGG PQHIVGSPFK AKVTGPRLSG 2600
    GHSLHETSTV LVETVTKSSS SRGASYSSIP KFSSDASKVV TRGPGLSQAF 2650
    VGQKNSFTVD CSKAGTNMMM VGVHGPKTPC EEVYVKHMGN RVYNVTYTVK 2700
    EKGDYILIVK WGDESVPGSP FKVNVP 2726
    Length:2,726
    Mass (Da):291,119
    Last modified:December 12, 2006 - v3
    Checksum:iBFBE03CBFFEE3863
    GO
    Isoform 2 (identifier: Q8VHX6-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta-H1

    The sequence of this isoform differs from the canonical sequence as follows:
         1735-1767: Missing.

    Show »
    Length:2,693
    Mass (Da):287,365
    Checksum:i3CB7C227D50195F4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1406 – 14061C → R in AAI51098. (PubMed:15489334)Curated
    Sequence conflicti2606 – 26061E → Q in AAF97411. (PubMed:10679933)Curated
    Sequence conflicti2609 – 26091T → S in AAF97411. (PubMed:10679933)Curated
    Sequence conflicti2617 – 26171K → H in AAF97411. (PubMed:10679933)Curated
    Sequence conflicti2631 – 26311K → N in AAF97411. (PubMed:10679933)Curated
    Sequence conflicti2663 – 26653KAG → QAR in AAF97411. (PubMed:10679933)Curated
    Sequence conflicti2669 – 26691M → I in AAF97411. (PubMed:10679933)Curated
    Sequence conflicti2695 – 26951V → F in AAF97411. (PubMed:10679933)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1735 – 176733Missing in isoform 2. 2 PublicationsVSP_007580Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC044807 Genomic DNA. No translation available.
    BC052186 mRNA. Translation: AAH52186.1.
    BC060276 mRNA. Translation: AAH60276.1.
    BC151097 mRNA. Translation: AAI51098.1.
    BC158128 mRNA. Translation: AAI58129.1.
    AF353670 mRNA. Translation: AAL68446.1.
    AF119148 mRNA. Translation: AAF97411.1.
    CCDSiCCDS39452.1. [Q8VHX6-1]
    RefSeqiNP_001074654.1. NM_001081185.1. [Q8VHX6-1]
    XP_006505227.1. XM_006505164.1. [Q8VHX6-2]
    UniGeneiMm.39046.

    Genome annotation databases

    EnsembliENSMUST00000090474; ENSMUSP00000087960; ENSMUSG00000068699. [Q8VHX6-1]
    GeneIDi68794.
    KEGGimmu:68794.
    UCSCiuc009bdn.1. mouse. [Q8VHX6-1]
    uc009bdo.2. mouse. [Q8VHX6-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC044807 Genomic DNA. No translation available.
    BC052186 mRNA. Translation: AAH52186.1 .
    BC060276 mRNA. Translation: AAH60276.1 .
    BC151097 mRNA. Translation: AAI51098.1 .
    BC158128 mRNA. Translation: AAI58129.1 .
    AF353670 mRNA. Translation: AAL68446.1 .
    AF119148 mRNA. Translation: AAF97411.1 .
    CCDSi CCDS39452.1. [Q8VHX6-1 ]
    RefSeqi NP_001074654.1. NM_001081185.1. [Q8VHX6-1 ]
    XP_006505227.1. XM_006505164.1. [Q8VHX6-2 ]
    UniGenei Mm.39046.

    3D structure databases

    ProteinModelPortali Q8VHX6.
    SMRi Q8VHX6. Positions 23-2726.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213053. 5 interactions.
    IntActi Q8VHX6. 8 interactions.
    MINTi MINT-1520143.
    STRINGi 10090.ENSMUSP00000064163.

    PTM databases

    PhosphoSitei Q8VHX6.

    Proteomic databases

    MaxQBi Q8VHX6.
    PaxDbi Q8VHX6.
    PRIDEi Q8VHX6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090474 ; ENSMUSP00000087960 ; ENSMUSG00000068699 . [Q8VHX6-1 ]
    GeneIDi 68794.
    KEGGi mmu:68794.
    UCSCi uc009bdn.1. mouse. [Q8VHX6-1 ]
    uc009bdo.2. mouse. [Q8VHX6-2 ]

    Organism-specific databases

    CTDi 2318.
    MGIi MGI:95557. Flnc.

    Phylogenomic databases

    eggNOGi COG5069.
    GeneTreei ENSGT00660000095431.
    HOGENOMi HOG000044235.
    HOVERGENi HBG004163.
    KOi K04437.
    PhylomeDBi Q8VHX6.

    Miscellaneous databases

    NextBioi 327935.
    PROi Q8VHX6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VHX6.
    Bgeei Q8VHX6.
    CleanExi MM_FLNC.
    Genevestigatori Q8VHX6.

    Family and domain databases

    Gene3Di 1.10.418.10. 2 hits.
    2.60.40.10. 24 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR003961. Fibronectin_type3.
    IPR017868. Filamin/ABP280_repeat-like.
    IPR001298. Filamin/ABP280_rpt.
    IPR028559. FLN.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view ]
    PANTHERi PTHR11915:SF173. PTHR11915:SF173. 1 hit.
    Pfami PF00307. CH. 2 hits.
    PF00630. Filamin. 23 hits.
    [Graphical view ]
    SMARTi SM00033. CH. 2 hits.
    SM00060. FN3. 2 hits.
    SM00557. IG_FLMN. 24 hits.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    SSF81296. SSF81296. 24 hits.
    PROSITEi PS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS50194. FILAMIN_REPEAT. 24 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6.
      Tissue: Brain and Embryo.
    3. "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits."
      van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A.
      J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1687-1800 (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE.
      Strain: C3H.
    4. "Filamin isogene expression during mouse myogenesis."
      Chiang W., Greaser M.L., Lyons G.E.
      Dev. Dyn. 217:99-108(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2535-2726.
      Strain: C3H.
      Tissue: Myotube.
    5. "Filamin C interacts with the muscular dystrophy KY protein and is abnormally distributed in mouse KY deficient muscle fibres."
      Beatham J., Romero R., Townsend S.K.M., Hacker T., van der Ven P.F.M., Blanco G.
      Hum. Mol. Genet. 13:2863-2874(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KY.
    6. "Loss of FilaminC (FLNc) results in severe defects in myogenesis and myotube structure."
      Dalkilic I., Schienda J., Thompson T.G., Kunkel L.M.
      Mol. Cell. Biol. 26:6522-6534(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "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 SER-2234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    8. "Identification of a Z-band associated protein complex involving KY, FLNC and IGFN1."
      Baker J., Riley G., Romero M.R., Haynes A.R., Hilton H., Simon M., Hancock J., Tateossian H., Ripoll V.M., Blanco G.
      Exp. Cell Res. 316:1856-1870(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGFN1.
    9. "Junctional Rab13-binding protein (JRAB) regulates cell spreading via filamins."
      Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T., Imoto I., Matsushita N., Sasaki T.
      Genes Cells 18:810-822(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MICALL2.

    Entry informationi

    Entry nameiFLNC_MOUSE
    AccessioniPrimary (citable) accession number: Q8VHX6
    Secondary accession number(s): B2RY80
    , B9EKT2, Q6PAI6, Q9JJ38
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2003
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 115 of the entry and version 3 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