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Q8VHX6

- FLNC_MOUSE

UniProt

Q8VHX6 - FLNC_MOUSE

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Protein

Filamin-C

Gene

Flnc

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

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
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_243772. Cell-extracellular matrix interactions.

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. cytoplasm Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiQ8VHX6.
CleanExiMM_FLNC.
ExpressionAtlasiQ8VHX6. baseline and differential.
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.
InParanoidiQ8VHX6.
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_A/C.
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

        10         20         30         40         50
MMNNSNYSDA SGLGLVDEAD EMPSTEKDLA EDAPWKKIQQ NTFTRWCNEH
60 70 80 90 100
LKCVGKRLTD LQRDLSDGLR LIALLEVLSQ KRMYRKFHPR PNFRQMKLEN
110 120 130 140 150
VSVALEFLER EHIKLVSIDS KAIVDGNLKL ILGLIWTLIL HYSISMPMWE
160 170 180 190 200
DEDDEDARKQ TPKQRLLGWI QNKVPQLPIT NFNRDWQDGK ALGALVDNCA
210 220 230 240 250
PGLCPDWEAW DPNQPVQNAR EAMQQADDWL GVPQVIAPEE IVDPNVDEHS
260 270 280 290 300
VMTYLSQFPK AKLKPGAPVR SKQLNPKKAI AYGPGIEPQG NTVLQPAHFT
310 320 330 340 350
VQTVDAGVGE VLVYIEDPEG HTEEAKVVPN NDKDRTYAVS YVPKVAGLHK
360 370 380 390 400
VTVLFAGQNI ERSPFEVNVG MALGDANKVS ARGPGLEPVG NVANKPTYFD
410 420 430 440 450
IYTAGAGTGD VAVVIVDPQG RRDTVEVALE DKGDNTFRCT YRPVMEGPHT
460 470 480 490 500
VHVAFAGAPI TRSPFPVHVA EACNPNACRA SGRGLQPKGV RVKEVADFKV
510 520 530 540 550
FTKGAGSGEL KVTVKGPKGT EEPVKVREAG DGVFECEYYP VVPGKYVVTI
560 570 580 590 600
TWGGYAIPRS PFEVQVSPEA GAQKVRAWGP GLETGQVGKS ADFVVEAIGT
610 620 630 640 650
EVGTLGFSIE GPSQAKIECD DKGDGSCDVR YWPTEPGEYA VHVICDDEDI
660 670 680 690 700
RDSPFIAHIQ PAPPDCFPDK VKAFGPGLEP TGCIVDRPAE FTIDARAAGK
710 720 730 740 750
GDLKLYAQDA DGCPIDIKVI PNGDGTFRCS YVPTKPIKHT IIVSWGGVNV
760 770 780 790 800
PKSPFRVNVG EGSHPERVKV YGPGVEKTGL KANEPTYFTV DCSEAGQGDV
810 820 830 840 850
SIGIKCAPGV VGPVEADIDF DIIKNDNDTF TVKYTPPGAG HYTIMVLFAN
860 870 880 890 900
QEIPASPFHI KVDPSHDASK VKAEGPGLSR TGVEVGKPTH FTVLTKGAGK
910 920 930 940 950
AKLDVHFAGA AKGEAVRDFE IIDNHDYSYT VKYTAVQQGN MAVTVTYGGD
960 970 980 990 1000
PVPKSPFVVN VAPPLDLSKV KVQGLNSKVA VGQEQAFSVN TRGAGGQGQL
1010 1020 1030 1040 1050
DVRMTSPSRR PIPCKLEPGG GAEAQAVRYM PPEEGPYKVD ITYDGHPVPG
1060 1070 1080 1090 1100
SPFAVEGVLP PDPSKVCAYG PGLKGGLVGT PAPFSIDTKG AGTGGLGLTV
1110 1120 1130 1140 1150
EGPCEAKIEC QDNGDGSCAV SYLPTEPGEY TINILFAEAH IPGSPFKATI
1160 1170 1180 1190 1200
QPVFDPSKVR ASGPGLERGK AGEAATFTVD CSEAGEAELT IEILSDAGVK
1210 1220 1230 1240 1250
AEVLIQNNAD GTYHITYSPA FPGTYTITIK YGGHPIPKFP TRVHVQPAVD
1260 1270 1280 1290 1300
TSGIKVSGPG VEPHGVLREV TTEFTVDARS LTATGGNHVT ARVLNPSGAK
1310 1320 1330 1340 1350
TDTYVTDNGD GTYRVQYTAY EEGVHLVEVL YDEVAVPKSP FRVGVTEGCD
1360 1370 1380 1390 1400
PTRVRAFGPG LEGGLVNKAN RFTVETRGAG TGGLGLAIEG PSEAKMSCKD
1410 1420 1430 1440 1450
NKDGSCTVEY IPFTPGDYDV NITFGGQPIP GSPFRVPVKD VVDPGKVKCS
1460 1470 1480 1490 1500
GPGLGTGVRA RVPQTFTVDC SQAGRAPLQV AVLGPTGVAE PVEVRDNGDG
1510 1520 1530 1540 1550
THTVHYTPAT DGPYTVAVKY ADQEVPRSPF KIKVLPSHDA SKVRASGPGL
1560 1570 1580 1590 1600
NASGIPASLP VEFTIDARDA GQGLLTVQIL DPEGKPKKAN IRDNGDGTYT
1610 1620 1630 1640 1650
VSYLPDMSGR YTITIKYGGD EIPYSPFRIH ALPTGDASKC LVTVSIGGHG
1660 1670 1680 1690 1700
LGACLGPRIQ IGEETVITVD AKAAGKGKVT CTVSTPDGAE LDVDVVENHD
1710 1720 1730 1740 1750
GTFDIYYTAP EPGKYVITIR FGGEHIPNSP FHVLACDPLP HVEEPAEMLQ
1760 1770 1780 1790 1800
MRQPYAPLRP GTCPTHWATE EPVVPVEPLE SMLRPFNLVI PFTVQKGELT
1810 1820 1830 1840 1850
GEVRMPSGKT ARPNITDNKD GTITVRYAPT EKGLHQMGIK YDGNHIPGSP
1860 1870 1880 1890 1900
LQFYVDAINS RHVSAYGPGL SHGMVNKPAT FTIVTKDAGE GGLSLAVEGP
1910 1920 1930 1940 1950
SKAEITCKDN KDGTCTVSYL PTAPGDYSII VRFDDKHIPG SPFTAKITGD
1960 1970 1980 1990 2000
DSMRTSQLNV GTSTDVSLKI TEGDLSQLTA SIRAPSGNEE PCLLKRLPNR
2010 2020 2030 2040 2050
HIGISFTPKE VGEHVVSVRK SGKHVTNSPF KILVGPSEIG DASKVRVWGK
2060 2070 2080 2090 2100
GLSEGQTFQV AEFIVDTRNA GYGGLGLSIE GPSKVDINCE DMEDGTCKVT
2110 2120 2130 2140 2150
YCPTEPGTYI INIKFADKHV PGSPFTVKVT GEGRMKESIT RRRQAPSIAT
2160 2170 2180 2190 2200
IGSTCDLNLK IPGNWFQMVS AQERLTRTFT RSSHTYTRTE RTEISKTRGG
2210 2220 2230 2240 2250
ETKREVRVEE STQVGGDPFP AVFGDFLGRE RLGSFGSITR QQEGEASSQD
2260 2270 2280 2290 2300
MTAQVTSPSG KTEAAEIVEG EDSAYSVRFV PQEMGPHTVT VKYRGQHVPG
2310 2320 2330 2340 2350
SPFQFTVGPL GEGGAHKVRA GGTGLERGVA GVPAEFSIWT REAGAGGLSI
2360 2370 2380 2390 2400
AVEGPSKAEI AFEDRKDGSC GVSYVVQEPG DYEVSIKFND EHIPDSPFVV
2410 2420 2430 2440 2450
PVASLSDDAR RLTVTSLQET GLKVNQPASF AVQLNGARGV IDARVHTPSG
2460 2470 2480 2490 2500
AVEECYVSEL DSDKHTIRFI PHENGVHSID VKFNGAHIPG SPFKIRVGEQ
2510 2520 2530 2540 2550
SQAGDPGLVS AYGPGLEGGT TGVSSEFIVN TQNAGSGALS VTIDGPSKVQ
2560 2570 2580 2590 2600
LDCRECPEGH VVTYTPMAPG NYLIAIKYGG PQHIVGSPFK AKVTGPRLSG
2610 2620 2630 2640 2650
GHSLHETSTV LVETVTKSSS SRGASYSSIP KFSSDASKVV TRGPGLSQAF
2660 2670 2680 2690 2700
VGQKNSFTVD CSKAGTNMMM VGVHGPKTPC EEVYVKHMGN RVYNVTYTVK
2710 2720
EKGDYILIVK WGDESVPGSP FKVNVP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi Q8VHX6.
KOi K04437.
PhylomeDBi Q8VHX6.

Enzyme and pathway databases

Reactomei REACT_243772. Cell-extracellular matrix interactions.

Miscellaneous databases

NextBioi 327935.
PROi Q8VHX6.
SOURCEi Search...

Gene expression databases

Bgeei Q8VHX6.
CleanExi MM_FLNC.
ExpressionAtlasi Q8VHX6. baseline and differential.
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_A/C.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 117 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

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