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Reviewed, UniProtKB/Swiss-Prot Q14315 (FLNC_HUMAN)

Last modified February 9, 2010. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Filamin-C
      Short name=FLN-C
      Short name=FLNc
Alternative name(s):
    Gamma-filamin
    Filamin-2
    Actin-binding-like protein
    ABP-L
    ABP-280-like protein
Gene names
Name: FLNC
Synonyms: ABPL, FLN2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length2725 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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-disks in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers.

Subunit structure

Homodimer. Interacts with KY By similarity. Interacts with FLNB, KCND2, ITGB1A, INPPL1, MYOT, MYOZ1 and MYOZ3. Interacts with sarcoglycans SGCD and SGCG. Ref.4 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.20 Ref.21

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Cytoplasm › cytoskeleton. Cytoplasm › myofibril › sarcomere › Z-disk. Note: A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z-disks, while a minor fraction localizes with subsarcolemme. Ref.11

Tissue specificity

Highly expressed in striated muscles. Weakly expressed in thyroid, fetal brain, fetal lung, retina, spinal cord and bone marrow. Not expressed in testis, pancreas, adrenal gland, placenta, liver and kidney. Ref.11 Ref.1 Ref.9

Developmental stage

Expressed in both differentiating and adult muscles.

Domain

The intradomain insert is specific to FLNC and mediates the targeting to developing and mature Z-disks. Ref.11

Comprised of a NH2-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. Ref.11

The filamin 20 repeat mediates interaction with XIRP1. Ref.11

Involvement in disease

Defects in FLNC are the cause of autosomal dominant filaminopathy [MIM:609524]. Myofibrillar myopathy (MFM) is a neuromuscular disorder, usually with an adult onset, characterized by focal myofibrillar destruction and pathological cytoplasmic protein aggregations. Autosomal dominant filaminopathy is a form of MFM characterized by morphological features of MFM and clinical features of a limb-girdle myopathy. A heterozygous nonsense mutation which segregates with the disease, has been identified in the FLNC gene.

Miscellaneous

Silenced in MKN28 and MKN74 gastric cancer cell lines due to aberrant methylation of the gene.

Sequence similarities

Belongs to the filamin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 24 filamin repeats.

Sequence caution

The sequence AAF80245.1 differs from that shown. Reason: Frameshift at positions 2578, 2580 and 2590.

The sequence CAA49688.1 differs from that shown. Reason: Frameshift at positions 778 and 787.

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Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentZ disc

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from Experiment. Source: Reactome

extrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14315-1)

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.
Isoform 2 (identifier: Q14315-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1734-1766: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 27252725Filamin-C
PRO_0000087301

Regions

Domain1 – 259259Actin-binding
Domain36 – 142107CH 1
Domain159 – 259101CH 2
Repeat270 – 36899Filamin 1
Repeat370 – 46899Filamin 2
Repeat469 – 56597Filamin 3
Repeat566 – 65893Filamin 4
Repeat662 – 75897Filamin 5
Repeat759 – 861103Filamin 6
Repeat862 – 96099Filamin 7
Repeat961 – 105696Filamin 8
Repeat1057 – 114993Filamin 9
Repeat1150 – 124495Filamin 10
Repeat1245 – 1344100Filamin 11
Repeat1345 – 143793Filamin 12
Repeat1438 – 153396Filamin 13
Repeat1534 – 163097Filamin 14
Repeat1635 – 1734100Filamin 15
Repeat1759 – 185395Filamin 16
Repeat1854 – 194693Filamin 17
Repeat1947 – 203387Filamin 18
Repeat2036 – 212893Filamin 19
Repeat2244 – 230663Filamin 20
Repeat2309 – 240193Filamin 21
Repeat2403 – 249694Filamin 22
Repeat2500 – 259293Filamin 23
Repeat2630 – 272495Filamin 24
Region1735 – 175824Hinge 1
Region2162 – 224382Intradomain insert
Region2403 – 2724322Interaction with INPPL1
Region2593 – 2725133Self-association site, tail By similarity
Region2593 – 262937Hinge 2

Amino acid modifications

Modified residue7701Phosphotyrosine Ref.24
Modified residue11611Phosphoserine Ref.23
Modified residue22331Phosphoserine Ref.8
Modified residue26831Phosphotyrosine Ref.22

Natural variations

Alternative sequence1734 – 176633Missing in isoform 2.
VSP_007579
Natural variant15671R → Q: dbSNP rs2291569.
VAR_015705
Natural variant15801D → G: dbSNP rs2643766. Ref.1 Ref.3
VAR_015706
Natural variant15991T → A: dbSNP rs2643767. Ref.1 Ref.3
VAR_015707
Natural variant21351K → R: dbSNP rs1063261. Ref.3
VAR_015708
Natural variant22031R → P: dbSNP rs1063262. Ref.1 Ref.3
VAR_015709
Natural variant26261S → N: dbSNP rs2639142.
VAR_015710
Natural variant26371K → Q: dbSNP rs2291572.
VAR_015711

Experimental info

Mutagenesis26691M → D: Abolishes dimerization. Ref.27
Sequence conflict1381I → T in CAB46442. Ref.3
Sequence conflict1891K → E in CAB46442. Ref.3
Sequence conflict1941L → Q in CAB46442. Ref.3
Sequence conflict2181A → S in AAD12245. Ref.1
Sequence conflict2181A → S in AAF68195. Ref.2
Sequence conflict2331Q → L in CAB46442. Ref.3
Sequence conflict4841L → P in CAB46442. Ref.3
Sequence conflict5851Q → V in CAA49688. Ref.9
Sequence conflict7231D → N in AAD12245. Ref.1
Sequence conflict7231D → N in AAF68195. Ref.2
Sequence conflict7231D → N in CAA49688. Ref.9
Sequence conflict10911G → D in CAB46442. Ref.3
Sequence conflict16401L → T in CAA49689. Ref.9
Sequence conflict16681V → M in CAB46442. Ref.3
Sequence conflict21011C → S in CAB46442. Ref.3
Sequence conflict21011C → S in CAA49689. Ref.9
Sequence conflict2321 – 23222GT → RA in AAD12245. Ref.1
Sequence conflict2321 – 23222GT → RA in AAF68195. Ref.2
Sequence conflict23551S → N in AAF80245. Ref.4
Sequence conflict23821E → K in AAF80245. Ref.4
Sequence conflict24841G → C in AAF80245. Ref.4
Sequence conflict24911P → L in AAF80245. Ref.4
Sequence conflict24991Q → H in AAF80245. Ref.4
Sequence conflict25141G → E in AAF80245. Ref.4
Sequence conflict2528 – 25303VNT → DDH in AAF80245. Ref.4
Sequence conflict25351S → F in AAF80245. Ref.4
Sequence conflict25471K → N in AAF80245. Ref.4
Sequence conflict25571E → G in AAF80245. Ref.4
Sequence conflict2601 – 26022HS → QH in AAF80245. Ref.4

Secondary structure

1 ............................................................................................................ 2725
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 28, 2009. Version 3.
Checksum: B7C8516C2366E75D

FASTA2,725291,022
        10         20         30         40         50         60 
MMNNSGYSDA GLGLGDETDE MPSTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVGKRLTDL 

        70         80         90        100        110        120 
QRDLSDGLRL IALLEVLSQK RMYRKFHPRP NFRQMKLENV SVALEFLERE HIKLVSIDSK 

       130        140        150        160        170        180 
AIVDGNLKLI LGLIWTLILH YSISMPMWED EDDEDARKQT PKQRLLGWIQ NKVPQLPITN 

       190        200        210        220        230        240 
FNRDWQDGKA LGALVDNCAP GLCPDWEAWD PNQPVENARE AMQQADDWLG VPQVIAPEEI 

       250        260        270        280        290        300 
VDPNVDEHSV MTYLSQFPKA KLKPGAPVRS KQLNPKKAIA YGPGIEPQGN TVLQPAHFTV 

       310        320        330        340        350        360 
QTVDAGVGEV LVYIEDPEGH TEEAKVVPNN DKDRTYAVSY VPKVAGLHKV TVLFAGQNIE 

       370        380        390        400        410        420 
RSPFEVNVGM ALGDANKVSA RGPGLEPVGN VANKPTYFDI YTAGAGTGDV AVVIVDPQGR 

       430        440        450        460        470        480 
RDTVEVALED KGDSTFRCTY RPAMEGPHTV HVAFAGAPIT RSPFPVHVSE ACNPNACRAS 

       490        500        510        520        530        540 
GRGLQPKGVR VKEVADFKVF TKGAGSGELK VTVKGPKGTE EPVKVREAGD GVFECEYYPV 

       550        560        570        580        590        600 
VPGKYVVTIT WGGYAIPRSP FEVQVSPEAG VQKVRAWGPG LETGQVGKSA DFVVEAIGTE 

       610        620        630        640        650        660 
VGTLGFSIEG PSQAKIECDD KGDGSCDVRY WPTEPGEYAV HVICDDEDIR DSPFIAHILP 

       670        680        690        700        710        720 
APPDCFPDKV KAFGPGLEPT GCIVDKPAEF TIDARAAGKG DLKLYAQDAD GCPIDIKVIP 

       730        740        750        760        770        780 
NGDGTFRCSY VPTKPIKHTI IISWGGVNVP KSPFRVNVGE GSHPERVKVY GPGVEKTGLK 

       790        800        810        820        830        840 
ANEPTYFTVD CSEAGQGDVS IGIKCAPGVV GPAEADIDFD IIKNDNDTFT VKYTPPGAGR 

       850        860        870        880        890        900 
YTIMVLFANQ EIPASPFHIK VDPSHDASKV KAEGPGLNRT GVEVGKPTHF TVLTKGAGKA 

       910        920        930        940        950        960 
KLDVQFAGTA KGEVVRDFEI IDNHDYSYTV KYTAVQQGNM AVTVTYGGDP VPKSPFVVNV 

       970        980        990       1000       1010       1020 
APPLDLSKIK VQGLNSKVAV GQEQAFSVNT RGAGGQGQLD VRMTSPSRRP IPCKLEPGGG 

      1030       1040       1050       1060       1070       1080 
AEAQAVRYMP PEEGPYKVDI TYDGHPVPGS PFAVEGVLPP DPSKVCAYGP GLKGGLVGTP 

      1090       1100       1110       1120       1130       1140 
APFSIDTKGA GTGGLGLTVE GPCEAKIECQ DNGDGSCAVS YLPTEPGEYT INILFAEAHI 

      1150       1160       1170       1180       1190       1200 
PGSPFKATIR PVFDPSKVRA SGPGLERGKV GEAATFTVDC SEAGEAELTI EILSDAGVKA 

      1210       1220       1230       1240       1250       1260 
EVLIHNNADG TYHITYSPAF PGTYTITIKY GGHPVPKFPT RVHVQPAVDT SGVKVSGPGV 

      1270       1280       1290       1300       1310       1320 
EPHGVLREVT TEFTVDARSL TATGGNHVTA RVLNPSGAKT DTYVTDNGDG TYRVQYTAYE 

      1330       1340       1350       1360       1370       1380 
EGVHLVEVLY DEVAVPKSPF RVGVTEGCDP TRVRAFGPGL EGGLVNKANR FTVETRGAGT 

      1390       1400       1410       1420       1430       1440 
GGLGLAIEGP SEAKMSCKDN KDGSCTVEYI PFTPGDYDVN ITFGGRPIPG SPFRVPVKDV 

      1450       1460       1470       1480       1490       1500 
VDPGKVKCSG PGLGAGVRAR VPQTFTVDCS QAGRAPLQVA VLGPTGVAEP VEVRDNGDGT 

      1510       1520       1530       1540       1550       1560 
HTVHYTPATD GPYTVAVKYA DQEVPRSPFK IKVLPAHDAS KVRASGPGLN ASGIPASLPV 

      1570       1580       1590       1600       1610       1620 
EFTIDARDAG EGLLTVQILD PEGKPKKANI RDNGDGTYTV SYLPDMSGRY TITIKYGGDE 

      1630       1640       1650       1660       1670       1680 
IPYSPFRIHA LPTGDASKCL VTVSIGGHGL GACLGPRIQI GQETVITVDA KAAGEGKVTC 

      1690       1700       1710       1720       1730       1740 
TVSTPDGAEL DVDVVENHDG TFDIYYTAPE PGKYVITIRF GGEHIPNSPF HVLACDPLPH 

      1750       1760       1770       1780       1790       1800 
EEEPSEVPQL RQPYAPPRPG ARPTHWATEE PVVPVEPMES MLRPFNLVIP FAVQKGELTG 

      1810       1820       1830       1840       1850       1860 
EVRMPSGKTA RPNITDNKDG TITVRYAPTE KGLHQMGIKY DGNHIPGSPL QFYVDAINSR 

      1870       1880       1890       1900       1910       1920 
HVSAYGPGLS HGMVNKPATF TIVTKDAGEG GLSLAVEGPS KAEITCKDNK DGTCTVSYLP 

      1930       1940       1950       1960       1970       1980 
TAPGDYSIIV RFDDKHIPGS PFTAKITGDD SMRTSQLNVG TSTDVSLKIT ESDLSQLTAS 

      1990       2000       2010       2020       2030       2040 
IRAPSGNEEP CLLKRLPNRH IGISFTPKEV GEHVVSVRKS GKHVTNSPFK ILVGPSEIGD 

      2050       2060       2070       2080       2090       2100 
ASKVRVWGKG LSEGHTFQVA EFIVDTRNAG YGGLGLSIEG PSKVDINCED MEDGTCKVTY 

      2110       2120       2130       2140       2150       2160 
CPTEPGTYII NIKFADKHVP GSPFTVKVTG EGRMKESITR RRQAPSIATI GSTCDLNLKI 

      2170       2180       2190       2200       2210       2220 
PGNWFQMVSA QERLTRTFTR SSHTYTRTER TEISKTRGGE TKREVRVEES TQVGGDPFPA 

      2230       2240       2250       2260       2270       2280 
VFGDFLGRER LGSFGSITRQ QEGEASSQDM TAQVTSPSGK VEAAEIVEGE DSAYSVRFVP 

      2290       2300       2310       2320       2330       2340 
QEMGPHTVAV KYRGQHVPGS PFQFTVGPLG EGGAHKVRAG GTGLERGVAG VPAEFSIWTR 

      2350       2360       2370       2380       2390       2400 
EAGAGGLSIA VEGPSKAEIA FEDRKDGSCG VSYVVQEPGD YEVSIKFNDE HIPDSPFVVP 

      2410       2420       2430       2440       2450       2460 
VASLSDDARR LTVTSLQETG LKVNQPASFA VQLNGARGVI DARVHTPSGA VEECYVSELD 

      2470       2480       2490       2500       2510       2520 
SDKHTIRFIP HENGVHSIDV KFNGAHIPGS PFKIRVGEQS QAGDPGLVSA YGPGLEGGTT 

      2530       2540       2550       2560       2570       2580 
GVSSEFIVNT LNAGSGALSV TIDGPSKVQL DCRECPEGHV VTYTPMAPGN YLIAIKYGGP 

      2590       2600       2610       2620       2630       2640 
QHIVGSPFKA KVTGPRLSGG HSLHETSTVL VETVTKSSSS RGSSYSSIPK FSSDASKVVT 

      2650       2660       2670       2680       2690       2700 
RGPGLSQAFV GQKNSFTVDC SKAGTNMMMV GVHGPKTPCE EVYVKHMGNR VYNVTYTVKE 

      2710       2720 
KGDYILIVKW GDESVPGSPF KVKVP

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Isoform 2.

Checksum: 7C07C97B4A882CF2
Show »

FASTA2,692287,281

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References

« Hide 'large scale' references
[1]"Molecular cloning of human ABPL, an actin-binding protein homologue."
Xie Z.-W., Xu W.-F., Davie E.W., Chung D.W.
Biochem. Biophys. Res. Commun. 251:914-919(1998) [PubMed: 9791010] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS GLY-1580; ALA-1599 AND PRO-2203.
Tissue: Heart.
[2]"Genomic structure and fine mapping of the two human filamin gene paralogues FLNB and FLNC and comparative analysis of the filamin gene family."
Chakarova C., Wehnert M.S., Uhl K., Sakthivel S., Vosberg H.-P., van der Ven P.F.M., Fuerst D.O.
Hum. Genet. 107:597-611(2000) [PubMed: 11153914] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), GENE ORGANIZATION, SIMILARITY TO OTHER MEMBERS OF THE FAMILY.
[3]"Characterization of muscle filamin isoforms suggests a possible role of gamma-filamin/ABP-L in sarcomeric Z-disc formation."
van der Ven P.F.M., Obermann W.M.J., Lemke B., Gautel M., Weber K., Fuerst D.O.
Cell Motil. Cytoskeleton 45:149-162(2000) [PubMed: 10658210] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS GLY-1580; ALA-1599; ARG-2135 AND PRO-2203.
[4]"Filamin 2 (FLN2): a muscle-specific sarcoglycan interacting protein."
Thompson T.G., Chan Y.-M., Hack A.A., Brosius M., Rajala M., Lidov H.G.W., McNally E.M., Watkins S., Kunkel L.M.
J. Cell Biol. 148:115-126(2000) [PubMed: 10629222] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SGCD AND SGCG.
Tissue: Skeletal muscle.
[5]Kato S.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Bienvenut W.V., Pchelintsev N., Adams P.D.
Submitted (OCT-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 70-81; 165-183; 335-343; 350-377; 422-437; 559-573; 576-588; 718-727; 880-895; 900-911; 917-968; 978-991; 1015-1027; 1074-1088; 1147-1157; 1242-1278; 1300-1313; 1355-1367; 1377-1394; 1475-1494; 1568-1586; 1616-1627; 1658-1671; 1714-1719; 1809-1825; 1840-1860; 1886-1901; 1932-1945; 1954-1968; 2000-2008; 2031-2043; 2050-2083; 2114-2127; 2231-2291; 2294-2316; 2327-2356; 2411-2437; 2577-2589; 2597-2616; 2642-2653 AND 2691-2699, PHOSPHORYLATION AT SER-2233, MASS SPECTROMETRY.
Tissue: Lung fibroblast.
[9]"Mapping of two genes encoding isoforms of the actin binding protein ABP-280, a dystrophin like protein, to Xq28 and to chromosome 7."
Maestrini E., Patrosso C., Mancini M., Rivella S., Rocchi M., Repetto M., Villa A., Frattini A., Zoppe M., Vezzoni P., Toniolo D.
Hum. Mol. Genet. 2:761-766(1993) [PubMed: 7689010] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 585-815 AND 1638-2101 (ISOFORM 2), TISSUE SPECIFICITY.
[10]"FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle."
Faulkner G., Pallavicini A., Comelli A., Salamon M., Bortoletto G., Ievolella C., Trevisan S., Kojic' S., Dalla Vecchia F., Laveder P., Valle G., Lanfranchi G.
J. Biol. Chem. 275:41234-41242(2000) [PubMed: 10984498] [Abstract]
Cited for: INTERACTION WITH MYOZ1.
[11]"Indications for a novel muscular dystrophy pathway: gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin."
van der Ven P.F.M., Wiesner S., Salmikangas P., Auerbach D., Himmel M., Kempa S., Hayess K., Pacholsky D., Taivainen A., Schroeder R., Carpen O., Fuerst D.O.
J. Cell Biol. 151:235-248(2000) [PubMed: 11038172] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH MYOT.
[12]"Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin."
Petrecca K., Miller D.M., Shrier A.
J. Neurosci. 20:8736-8744(2000) [PubMed: 11102480] [Abstract]
Cited for: INTERACTION WITH KCND2.
[13]"Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines."
Takada F., Vander Woude D.L., Tong H.-Q., Thompson T.G., Watkins S.C., Kunkel L.M., Beggs A.H.
Proc. Natl. Acad. Sci. U.S.A. 98:1595-1600(2001) [PubMed: 11171996] [Abstract]
Cited for: INTERACTION WITH MYOZ1.
[14]"The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin."
Dyson J.M., O'Malley C.J., Becanovic J., Munday A.D., Berndt M.C., Coghill I.D., Nandurkar H.H., Ooms L.M., Mitchell C.A.
J. Cell Biol. 155:1065-1079(2001) [PubMed: 11739414] [Abstract]
Cited for: INTERACTION WITH INPPL1.
[15]"Filamins as integrators of cell mechanics and signalling."
Stossel T.P., Condeelis J., Cooley L., Hartwig J.H., Noegel A., Schleicher M., Shapiro S.S.
Nat. Rev. Mol. Cell Biol. 2:138-145(2001) [PubMed: 11252955] [Abstract]
Cited for: REVIEW.
[16]"Identification of silencing of nine genes in human gastric cancers."
Kaneda A., Kaminishi M., Yanagihara K., Sugimura T., Ushijima T.
Cancer Res. 62:6645-6650(2002) [PubMed: 12438262] [Abstract]
Cited for: SILENCING IN MKN28 AND MKN74 CANCER CELL LINES.
[17]"Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins."
Frey N., Olson E.N.
J. Biol. Chem. 277:13998-14004(2002) [PubMed: 11842093] [Abstract]
Cited for: INTERACTION WITH MYOZ3.
[18]"The limits of promiscuity: isoform-specific dimerization of filamins."
Himmel M., van der Ven P.F.M., Stoecklein W., Fuerst D.O.
Biochemistry 42:430-439(2003) [PubMed: 12525170] [Abstract]
Cited for: DIMERIZATION, INTERACTION WITH FLNB.
[19]"A mutation in the dimerization domain of filamin C causes a novel type of autosomal dominant myofibrillar myopathy."
Vorgerd M., van der Ven P.F.M., Bruchertseifer V., Loewe T., Kley R.A., Schroeder R., Lochmueller H., Himmel M., Koehler K., Fuerst D.O., Huebner A.
Am. J. Hum. Genet. 77:297-304(2005) [PubMed: 15929027] [Abstract]
Cited for: INVOLVEMENT IN AUTOSOMAL DOMINANT MYOFIBRILLAR MYOPATHY.
[20]"The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins."
Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A., Carpen O., Faulkner G., Borradori L.
J. Cell Sci. 118:3739-3749(2005) [PubMed: 16076904] [Abstract]
Cited for: INTERACTION WITH ITGB1; MYOT AND MYOZ1.
[21]"Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP."
van der Ven P.F.M., Ehler E., Vakeel P., Eulitz S., Schenk J.A., Milting H., Micheel B., Fuerst D.O.
Exp. Cell Res. 312:2154-2167(2006) [PubMed: 16631741] [Abstract]
Cited for: INTERACTION WITH XIRP1.
[22]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2683, MASS SPECTROMETRY.
[23]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161, MASS SPECTROMETRY.
Tissue: Platelet.
[24]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-770, MASS SPECTROMETRY.
[25]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2233, MASS SPECTROMETRY.
[27]"Structural basis for vertebrate filamin dimerization."
Pudas R., Kiema T.-R., Butler P.J.G., Stewart M., Ylaenne J.
Structure 13:111-119(2005) [PubMed: 15642266] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 2633-2725, MUTAGENESIS OF MET-2669.
[28]"Solution structure of the filamin domains from human filamin C."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1536-2599.
+Additional computationally mapped references.

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Web resources

GeneReviews

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF089841 mRNA. Translation: AAD12245.1. Different initiation.
AF184126 expand/collapse EMBL AC list , AF184119, AF184120, AF184121, AF184122, AF184123, AF184124, AF184125 Genomic DNA. Translation: AAF68195.1. Different initiation.
AF252549 Genomic DNA. Translation: AAF67190.1.
AJ132990 Genomic DNA. Translation: CAB51535.1.
AJ012737 mRNA. Translation: CAB46442.1.
AB371585 mRNA. Translation: BAG48314.1.
AC025594 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83691.1.
AF146692 mRNA. Translation: AAF80245.1. Frameshift.
X70083 mRNA. Translation: CAA49688.1. Frameshift.
X70084 mRNA. Translation: CAA49689.1.
IPIIPI00178352.
IPI00413958.
PIRS37775.
S37778.
RefSeqNP_001120959.1.
NP_001449.3.
UniGeneHs.58414

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V05X-ray1.43A2633-2725[»]
2D7MNMR-A1536-1637[»]
2D7NNMR-A1782-1861[»]
2D7ONMR-A1856-1953[»]
2D7PNMR-A2405-2500[»]
2D7QNMR-A2502-2599[»]
2NQCX-ray2.05A2495-2598[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ14315. 12 interactions.
STRINGQ14315.

PTM databases

PhosphoSiteQ14315.

Proteomic databases

PRIDEQ14315.

Genome annotation databases

EnsemblENST00000325888; ENSP00000327145; ENSG00000128591; Homo sapiens. [Genome view]
GeneID2318.
KEGGhsa:2318.
UCSCuc003vnz.2. human.
uc003voa.2. human.

Organism-specific databases

CTD2318.
GeneCardsGC07P128257.
H-InvDBHIX0007057.
HGNCHGNC:3756. FLNC.
HPAHPA006135.
MIM102565. gene.
609524. phenotype.
Orphanet171445. Muscle filaminopathy.
PharmGKBPA28174.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08886.
HOVERGENQ14315.
InParanoidQ14315.
OMACAYGPGL.
OrthoDBEOG9R52NM.

Enzyme and pathway databases

ReactomeREACT_20676. Cell junction organization.

Gene expression databases

ArrayExpressQ14315.
BgeeQ14315.
CleanExHS_FLNC.
GenevestigatorQ14315.
GermOnlineENSG00000128591. Homo sapiens.

Family and domain databases

InterProIPR001589. Actinin_actin-bd_CS.
IPR016146. Calponin-homology.
IPR001715. Calponin_act_bd.
IPR001298. Filamin.
IPR017868. Filamin/ABP280_repeat-like.
IPR003961. FN_III.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
Gene3DG3DSA:1.10.418.10. Calponin-homology. 2 hits.
G3DSA:2.60.40.10. Ig-like_fold. 24 hits.
PfamPF00307. CH. 2 hits.
PF00630. Filamin. 24 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00060. FN3. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameFLNC_HUMAN
AccessionPrimary (citable) accession number: Q14315
Secondary accession number(s): B2ZZ88 expand/collapse secondary AC list , O95303, Q07985, Q9NS12, Q9NYE5, Q9UMR8, Q9Y503
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: July 28, 2009
Last modified: February 9, 2010
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents