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Protein

Filamin-C

Gene

FLNC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

  • ankyrin binding Source: BHF-UCL
  • cytoskeletal protein binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-446353. Cell-extracellular matrix interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Filamin-C
Short name:
FLN-C
Short name:
FLNc
Alternative name(s):
ABP-280-like protein
ABP-L
Actin-binding-like protein
Filamin-2
Gamma-filamin
Gene namesi
Name:FLNC
Synonyms:ABPL, FLN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:3756. FLNC.

Subcellular locationi

GO - Cellular componenti

  • costamere Source: BHF-UCL
  • cytoplasm Source: HPA
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • focal adhesion Source: UniProtKB
  • plasma membrane Source: HPA
  • sarcolemma Source: BHF-UCL
  • sarcoplasm Source: Ensembl
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Myopathy, myofibrillar, 5 (MFM5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disc and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM5 is characterized by onset in adulthood, clinical features of a limb-girdle myopathy, and focal myofibrillar destruction.
See also OMIM:609524
Myopathy, distal, 4 (MPD4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA slowly progressive muscular disorder characterized by distal muscle weakness and atrophy affecting the upper and lower limbs. Onset occurs around the third to fourth decades of life, and patients remain ambulatory even after long disease duration. Muscle biopsy shows non-specific changes with no evidence of rods, necrosis, or inflammation.
See also OMIM:614065
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066212193A → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in significantly decreased nuclear localization with formation of intracellular protein aggregates. 1 PublicationCorresponds to variant rs387906587dbSNPEnsembl.1
Natural variantiVAR_066213251M → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in the formation of intracellular protein aggregates. 1 PublicationCorresponds to variant rs387906586dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2669M → D: Abolishes dimerization. 1 Publication1

Keywords - Diseasei

Disease mutation, Myofibrillar myopathy

Organism-specific databases

DisGeNETi2318.
MalaCardsiFLNC.
MIMi609524. phenotype.
614065. phenotype.
OpenTargetsiENSG00000128591.
Orphaneti63273. Distal myopathy with posterior leg and anterior hand involvement.
171445. Muscle filaminopathy.
PharmGKBiPA28174.

Polymorphism and mutation databases

BioMutaiFLNC.
DMDMi254763419.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000873011 – 2725Filamin-CAdd BLAST2725

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphoserineCombined sources1
Modified residuei1002Omega-N-methylarginineBy similarity1
Modified residuei1161PhosphoserineCombined sources1
Modified residuei1338PhosphoserineCombined sources1
Modified residuei2042PhosphoserineCombined sources1
Modified residuei2233PhosphoserineCombined sources1 Publication1
Modified residuei2236PhosphoserineCombined sources1
Modified residuei2238PhosphothreonineCombined sources1
Modified residuei2586PhosphoserineCombined sources1
Modified residuei2617PhosphoserineCombined sources1
Modified residuei2620PhosphoserineCombined sources1
Modified residuei2623PhosphoserineCombined sources1
Modified residuei2632PhosphoserineCombined sources1
Modified residuei2714PhosphoserineCombined sources1
Modified residuei2718PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated by FBXL22, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14315.
MaxQBiQ14315.
PaxDbiQ14315.
PeptideAtlasiQ14315.
PRIDEiQ14315.

PTM databases

iPTMnetiQ14315.
PhosphoSitePlusiQ14315.
SwissPalmiQ14315.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

Expressed in both differentiating and adult muscles.

Gene expression databases

BgeeiENSG00000128591.
CleanExiHS_FLNC.
GenevisibleiQ14315. HS.

Organism-specific databases

HPAiHPA006135.

Interactioni

Subunit structurei

Homodimer; the filamin repeat 24 and the second hinge domain are important for dimer formation. 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. Interacts with XIRP1; this interaction is mediated by filamin 20 repeat. Interacts with KY. Interacts with IGFN1 (By similarity). Interacts with MICALL2 (By similarity). Interacts with ANK3.By similarity14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-489954,EBI-375543
Ank3O70511-72EBI-489954,EBI-9663485From a different organism.
CRKP461082EBI-489954,EBI-886
DYSFO759233EBI-489954,EBI-2799016
GRB2P629932EBI-489954,EBI-401755
MYOTQ9UBF96EBI-489954,EBI-296701
XIRP1Q702N84EBI-489954,EBI-7851194

GO - Molecular functioni

  • ankyrin binding Source: BHF-UCL
  • cytoskeletal protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108607. 92 interactors.
DIPiDIP-33398N.
IntActiQ14315. 46 interactors.
MINTiMINT-5004555.
STRINGi9606.ENSP00000327145.

Structurei

Secondary structure

12725
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi574 – 578Combined sources5
Helixi579 – 581Combined sources3
Beta strandi583 – 585Combined sources3
Beta strandi590 – 599Combined sources10
Helixi601 – 603Combined sources3
Beta strandi604 – 612Combined sources9
Beta strandi617 – 620Combined sources4
Beta strandi622 – 630Combined sources9
Beta strandi636 – 644Combined sources9
Beta strandi653 – 659Combined sources7
Helixi667 – 669Combined sources3
Beta strandi671 – 674Combined sources4
Helixi675 – 677Combined sources3
Beta strandi678 – 680Combined sources3
Beta strandi688 – 693Combined sources6
Beta strandi697 – 699Combined sources3
Beta strandi702 – 708Combined sources7
Beta strandi717 – 720Combined sources4
Beta strandi722 – 730Combined sources9
Beta strandi734 – 744Combined sources11
Beta strandi753 – 759Combined sources7
Helixi1539 – 1541Combined sources3
Beta strandi1542 – 1547Combined sources6
Beta strandi1554 – 1558Combined sources5
Beta strandi1560 – 1569Combined sources10
Beta strandi1574 – 1579Combined sources6
Beta strandi1588 – 1592Combined sources5
Beta strandi1594 – 1596Combined sources3
Beta strandi1598 – 1602Combined sources5
Beta strandi1608 – 1618Combined sources11
Beta strandi1625 – 1631Combined sources7
Beta strandi1785 – 1789Combined sources5
Beta strandi1794 – 1796Combined sources3
Beta strandi1798 – 1803Combined sources6
Beta strandi1813 – 1816Combined sources4
Beta strandi1818 – 1820Combined sources3
Beta strandi1822 – 1826Combined sources5
Beta strandi1832 – 1843Combined sources12
Beta strandi1849 – 1854Combined sources6
Beta strandi1863 – 1866Combined sources4
Helixi1867 – 1870Combined sources4
Beta strandi1871 – 1873Combined sources3
Beta strandi1878 – 1883Combined sources6
Turni1885 – 1887Combined sources3
Beta strandi1895 – 1900Combined sources6
Beta strandi1910 – 1918Combined sources9
Beta strandi1924 – 1929Combined sources6
Beta strandi1931 – 1934Combined sources4
Beta strandi1941 – 1947Combined sources7
Beta strandi2303 – 2308Combined sources6
Turni2313 – 2316Combined sources4
Beta strandi2318 – 2322Combined sources5
Turni2323 – 2325Combined sources3
Beta strandi2332 – 2338Combined sources7
Beta strandi2344 – 2355Combined sources12
Beta strandi2358 – 2362Combined sources5
Beta strandi2365 – 2374Combined sources10
Beta strandi2377 – 2389Combined sources13
Beta strandi2396 – 2404Combined sources9
Helixi2407 – 2410Combined sources4
Beta strandi2427 – 2432Combined sources6
Beta strandi2440 – 2445Combined sources6
Beta strandi2447 – 2449Combined sources3
Beta strandi2463 – 2468Combined sources6
Beta strandi2474 – 2484Combined sources11
Beta strandi2491 – 2496Combined sources6
Helixi2505 – 2507Combined sources3
Beta strandi2509 – 2512Combined sources4
Helixi2513 – 2515Combined sources3
Beta strandi2517 – 2519Combined sources3
Beta strandi2524 – 2529Combined sources6
Turni2531 – 2533Combined sources3
Beta strandi2538 – 2546Combined sources9
Beta strandi2549 – 2555Combined sources7
Beta strandi2558 – 2564Combined sources7
Beta strandi2569 – 2580Combined sources12
Beta strandi2587 – 2594Combined sources8
Helixi2635 – 2637Combined sources3
Beta strandi2639 – 2642Combined sources4
Helixi2643 – 2645Combined sources3
Beta strandi2654 – 2659Combined sources6
Beta strandi2663 – 2665Combined sources3
Beta strandi2668 – 2673Combined sources6
Beta strandi2675 – 2677Combined sources3
Beta strandi2680 – 2686Combined sources7
Beta strandi2691 – 2697Combined sources7
Beta strandi2702 – 2710Combined sources9
Beta strandi2719 – 2724Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V05X-ray1.43A2633-2725[»]
2D7MNMR-A1536-1637[»]
2D7NNMR-A1782-1861[»]
2D7ONMR-A1856-1953[»]
2D7PNMR-A2405-2503[»]
2D7QNMR-A2502-2599[»]
2K9UNMR-A2302-2415[»]
2NQCX-ray2.05A2495-2598[»]
3V8OX-ray2.80A/B569-761[»]
4MGXX-ray3.16A572-756[»]
ProteinModelPortaliQ14315.
SMRiQ14315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14315.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 259Actin-bindingAdd BLAST259
Domaini36 – 142CH 1PROSITE-ProRule annotationAdd BLAST107
Domaini159 – 259CH 2PROSITE-ProRule annotationAdd BLAST101
Repeati270 – 368Filamin 1Add BLAST99
Repeati370 – 468Filamin 2Add BLAST99
Repeati469 – 565Filamin 3Add BLAST97
Repeati566 – 658Filamin 4Add BLAST93
Repeati662 – 758Filamin 5Add BLAST97
Repeati759 – 861Filamin 6Add BLAST103
Repeati862 – 960Filamin 7Add BLAST99
Repeati961 – 1056Filamin 8Add BLAST96
Repeati1057 – 1149Filamin 9Add BLAST93
Repeati1150 – 1244Filamin 10Add BLAST95
Repeati1245 – 1344Filamin 11Add BLAST100
Repeati1345 – 1437Filamin 12Add BLAST93
Repeati1438 – 1533Filamin 13Add BLAST96
Repeati1534 – 1630Filamin 14Add BLAST97
Repeati1635 – 1734Filamin 15Add BLAST100
Repeati1759 – 1853Filamin 16Add BLAST95
Repeati1854 – 1946Filamin 17Add BLAST93
Repeati1947 – 2033Filamin 18Add BLAST87
Repeati2036 – 2128Filamin 19Add BLAST93
Repeati2244 – 2306Filamin 20; mediates interaction with XIRP1Add BLAST63
Repeati2309 – 2401Filamin 21Add BLAST93
Repeati2403 – 2496Filamin 22Add BLAST94
Repeati2500 – 2592Filamin 23Add BLAST93
Repeati2630 – 2724Filamin 24Add BLAST95

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1735 – 1758Hinge 1Add BLAST24
Regioni2162 – 2243Intradomain insert; mediate targeting to Z linesAdd BLAST82
Regioni2403 – 2724Interaction with INPPL11 PublicationAdd BLAST322
Regioni2593 – 2725Self-association site, tailBy similarityAdd BLAST133
Regioni2593 – 2629Hinge 2Add BLAST37

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

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00660000095431.
HOVERGENiHBG004163.
InParanoidiQ14315.
KOiK04437.
OMAiAEPMESM.
OrthoDBiEOG091G00U5.
PhylomeDBiQ14315.
TreeFamiTF313685.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR032461. FLN_C.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11915:SF210. PTHR11915:SF210. 2 hits.
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTiSM00033. CH. 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. AlignAdd to basket

Isoform 1 (identifier: Q14315-1) [UniParc]FASTAAdd to basket

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
MMNNSGYSDA GLGLGDETDE MPSTEKDLAE DAPWKKIQQN TFTRWCNEHL
60 70 80 90 100
KCVGKRLTDL QRDLSDGLRL IALLEVLSQK RMYRKFHPRP NFRQMKLENV
110 120 130 140 150
SVALEFLERE HIKLVSIDSK AIVDGNLKLI LGLIWTLILH YSISMPMWED
160 170 180 190 200
EDDEDARKQT PKQRLLGWIQ NKVPQLPITN FNRDWQDGKA LGALVDNCAP
210 220 230 240 250
GLCPDWEAWD PNQPVENARE AMQQADDWLG VPQVIAPEEI VDPNVDEHSV
260 270 280 290 300
MTYLSQFPKA KLKPGAPVRS KQLNPKKAIA YGPGIEPQGN TVLQPAHFTV
310 320 330 340 350
QTVDAGVGEV LVYIEDPEGH TEEAKVVPNN DKDRTYAVSY VPKVAGLHKV
360 370 380 390 400
TVLFAGQNIE RSPFEVNVGM ALGDANKVSA RGPGLEPVGN VANKPTYFDI
410 420 430 440 450
YTAGAGTGDV AVVIVDPQGR RDTVEVALED KGDSTFRCTY RPAMEGPHTV
460 470 480 490 500
HVAFAGAPIT RSPFPVHVSE ACNPNACRAS GRGLQPKGVR VKEVADFKVF
510 520 530 540 550
TKGAGSGELK VTVKGPKGTE EPVKVREAGD GVFECEYYPV VPGKYVVTIT
560 570 580 590 600
WGGYAIPRSP FEVQVSPEAG VQKVRAWGPG LETGQVGKSA DFVVEAIGTE
610 620 630 640 650
VGTLGFSIEG PSQAKIECDD KGDGSCDVRY WPTEPGEYAV HVICDDEDIR
660 670 680 690 700
DSPFIAHILP APPDCFPDKV KAFGPGLEPT GCIVDKPAEF TIDARAAGKG
710 720 730 740 750
DLKLYAQDAD GCPIDIKVIP NGDGTFRCSY VPTKPIKHTI IISWGGVNVP
760 770 780 790 800
KSPFRVNVGE GSHPERVKVY GPGVEKTGLK ANEPTYFTVD CSEAGQGDVS
810 820 830 840 850
IGIKCAPGVV GPAEADIDFD IIKNDNDTFT VKYTPPGAGR YTIMVLFANQ
860 870 880 890 900
EIPASPFHIK VDPSHDASKV KAEGPGLNRT GVEVGKPTHF TVLTKGAGKA
910 920 930 940 950
KLDVQFAGTA KGEVVRDFEI IDNHDYSYTV KYTAVQQGNM AVTVTYGGDP
960 970 980 990 1000
VPKSPFVVNV APPLDLSKIK VQGLNSKVAV GQEQAFSVNT RGAGGQGQLD
1010 1020 1030 1040 1050
VRMTSPSRRP IPCKLEPGGG AEAQAVRYMP PEEGPYKVDI TYDGHPVPGS
1060 1070 1080 1090 1100
PFAVEGVLPP DPSKVCAYGP GLKGGLVGTP APFSIDTKGA GTGGLGLTVE
1110 1120 1130 1140 1150
GPCEAKIECQ DNGDGSCAVS YLPTEPGEYT INILFAEAHI PGSPFKATIR
1160 1170 1180 1190 1200
PVFDPSKVRA SGPGLERGKV GEAATFTVDC SEAGEAELTI EILSDAGVKA
1210 1220 1230 1240 1250
EVLIHNNADG TYHITYSPAF PGTYTITIKY GGHPVPKFPT RVHVQPAVDT
1260 1270 1280 1290 1300
SGVKVSGPGV EPHGVLREVT TEFTVDARSL TATGGNHVTA RVLNPSGAKT
1310 1320 1330 1340 1350
DTYVTDNGDG TYRVQYTAYE EGVHLVEVLY DEVAVPKSPF RVGVTEGCDP
1360 1370 1380 1390 1400
TRVRAFGPGL EGGLVNKANR FTVETRGAGT GGLGLAIEGP SEAKMSCKDN
1410 1420 1430 1440 1450
KDGSCTVEYI PFTPGDYDVN ITFGGRPIPG SPFRVPVKDV VDPGKVKCSG
1460 1470 1480 1490 1500
PGLGAGVRAR VPQTFTVDCS QAGRAPLQVA VLGPTGVAEP VEVRDNGDGT
1510 1520 1530 1540 1550
HTVHYTPATD GPYTVAVKYA DQEVPRSPFK IKVLPAHDAS KVRASGPGLN
1560 1570 1580 1590 1600
ASGIPASLPV EFTIDARDAG EGLLTVQILD PEGKPKKANI RDNGDGTYTV
1610 1620 1630 1640 1650
SYLPDMSGRY TITIKYGGDE IPYSPFRIHA LPTGDASKCL VTVSIGGHGL
1660 1670 1680 1690 1700
GACLGPRIQI GQETVITVDA KAAGEGKVTC TVSTPDGAEL DVDVVENHDG
1710 1720 1730 1740 1750
TFDIYYTAPE PGKYVITIRF GGEHIPNSPF HVLACDPLPH EEEPSEVPQL
1760 1770 1780 1790 1800
RQPYAPPRPG ARPTHWATEE PVVPVEPMES MLRPFNLVIP FAVQKGELTG
1810 1820 1830 1840 1850
EVRMPSGKTA RPNITDNKDG TITVRYAPTE KGLHQMGIKY DGNHIPGSPL
1860 1870 1880 1890 1900
QFYVDAINSR HVSAYGPGLS HGMVNKPATF TIVTKDAGEG GLSLAVEGPS
1910 1920 1930 1940 1950
KAEITCKDNK DGTCTVSYLP TAPGDYSIIV RFDDKHIPGS PFTAKITGDD
1960 1970 1980 1990 2000
SMRTSQLNVG TSTDVSLKIT ESDLSQLTAS IRAPSGNEEP CLLKRLPNRH
2010 2020 2030 2040 2050
IGISFTPKEV GEHVVSVRKS GKHVTNSPFK ILVGPSEIGD ASKVRVWGKG
2060 2070 2080 2090 2100
LSEGHTFQVA EFIVDTRNAG YGGLGLSIEG PSKVDINCED MEDGTCKVTY
2110 2120 2130 2140 2150
CPTEPGTYII NIKFADKHVP GSPFTVKVTG EGRMKESITR RRQAPSIATI
2160 2170 2180 2190 2200
GSTCDLNLKI PGNWFQMVSA QERLTRTFTR SSHTYTRTER TEISKTRGGE
2210 2220 2230 2240 2250
TKREVRVEES TQVGGDPFPA VFGDFLGRER LGSFGSITRQ QEGEASSQDM
2260 2270 2280 2290 2300
TAQVTSPSGK VEAAEIVEGE DSAYSVRFVP QEMGPHTVAV KYRGQHVPGS
2310 2320 2330 2340 2350
PFQFTVGPLG EGGAHKVRAG GTGLERGVAG VPAEFSIWTR EAGAGGLSIA
2360 2370 2380 2390 2400
VEGPSKAEIA FEDRKDGSCG VSYVVQEPGD YEVSIKFNDE HIPDSPFVVP
2410 2420 2430 2440 2450
VASLSDDARR LTVTSLQETG LKVNQPASFA VQLNGARGVI DARVHTPSGA
2460 2470 2480 2490 2500
VEECYVSELD SDKHTIRFIP HENGVHSIDV KFNGAHIPGS PFKIRVGEQS
2510 2520 2530 2540 2550
QAGDPGLVSA YGPGLEGGTT GVSSEFIVNT LNAGSGALSV TIDGPSKVQL
2560 2570 2580 2590 2600
DCRECPEGHV VTYTPMAPGN YLIAIKYGGP QHIVGSPFKA KVTGPRLSGG
2610 2620 2630 2640 2650
HSLHETSTVL VETVTKSSSS RGSSYSSIPK FSSDASKVVT RGPGLSQAFV
2660 2670 2680 2690 2700
GQKNSFTVDC SKAGTNMMMV GVHGPKTPCE EVYVKHMGNR VYNVTYTVKE
2710 2720
KGDYILIVKW GDESVPGSPF KVKVP
Length:2,725
Mass (Da):291,022
Last modified:July 28, 2009 - v3
Checksum:iB7C8516C2366E75D
GO
Isoform 2 (identifier: Q14315-2) [UniParc]FASTAAdd to basket

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

Show »
Length:2,692
Mass (Da):287,281
Checksum:i7C07C97B4A882CF2
GO

Sequence cautioni

The sequence AAD12245 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF68195 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF80245 differs from that shown. Reason: Frameshift at positions 2578, 2580 and 2590.Curated
The sequence CAA49688 differs from that shown. Reason: Frameshift at positions 778 and 787.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti138I → T in CAB46442 (PubMed:10658210).Curated1
Sequence conflicti189K → E in CAB46442 (PubMed:10658210).Curated1
Sequence conflicti194L → Q in CAB46442 (PubMed:10658210).Curated1
Sequence conflicti218A → S in AAD12245 (PubMed:9791010).Curated1
Sequence conflicti218A → S in AAF68195 (PubMed:11153914).Curated1
Sequence conflicti233Q → L in CAB46442 (PubMed:10658210).Curated1
Sequence conflicti484L → P in CAB46442 (PubMed:10658210).Curated1
Sequence conflicti585Q → V in CAA49688 (PubMed:7689010).Curated1
Sequence conflicti723D → N in AAD12245 (PubMed:9791010).Curated1
Sequence conflicti723D → N in AAF68195 (PubMed:11153914).Curated1
Sequence conflicti723D → N in CAA49688 (PubMed:7689010).Curated1
Sequence conflicti1091G → D in CAB46442 (PubMed:10658210).Curated1
Sequence conflicti1640L → T in CAA49689 (PubMed:7689010).Curated1
Sequence conflicti1668V → M in CAB46442 (PubMed:10658210).Curated1
Sequence conflicti2101C → S in CAB46442 (PubMed:10658210).Curated1
Sequence conflicti2101C → S in CAA49689 (PubMed:7689010).Curated1
Sequence conflicti2321 – 2322GT → RA in AAD12245 (PubMed:9791010).Curated2
Sequence conflicti2321 – 2322GT → RA in AAF68195 (PubMed:11153914).Curated2
Sequence conflicti2355S → N in AAF80245 (PubMed:10629222).Curated1
Sequence conflicti2382E → K in AAF80245 (PubMed:10629222).Curated1
Sequence conflicti2484G → C in AAF80245 (PubMed:10629222).Curated1
Sequence conflicti2491P → L in AAF80245 (PubMed:10629222).Curated1
Sequence conflicti2499Q → H in AAF80245 (PubMed:10629222).Curated1
Sequence conflicti2514G → E in AAF80245 (PubMed:10629222).Curated1
Sequence conflicti2528 – 2530VNT → DDH in AAF80245 (PubMed:10629222).Curated3
Sequence conflicti2535S → F in AAF80245 (PubMed:10629222).Curated1
Sequence conflicti2547K → N in AAF80245 (PubMed:10629222).Curated1
Sequence conflicti2557E → G in AAF80245 (PubMed:10629222).Curated1
Sequence conflicti2601 – 2602HS → QH in AAF80245 (PubMed:10629222).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066212193A → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in significantly decreased nuclear localization with formation of intracellular protein aggregates. 1 PublicationCorresponds to variant rs387906587dbSNPEnsembl.1
Natural variantiVAR_066213251M → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in the formation of intracellular protein aggregates. 1 PublicationCorresponds to variant rs387906586dbSNPEnsembl.1
Natural variantiVAR_0157051567R → Q.Corresponds to variant rs2291569dbSNPEnsembl.1
Natural variantiVAR_0157061580D → G.2 PublicationsCorresponds to variant rs2643766dbSNPEnsembl.1
Natural variantiVAR_0157071599T → A.2 PublicationsCorresponds to variant rs2643767dbSNPEnsembl.1
Natural variantiVAR_0157082135K → R.1 PublicationCorresponds to variant rs1063261dbSNPEnsembl.1
Natural variantiVAR_0157092203R → P.2 PublicationsCorresponds to variant rs1063262dbSNPEnsembl.1
Natural variantiVAR_0157102626S → N.Corresponds to variant rs2639142dbSNPEnsembl.1
Natural variantiVAR_0157112637K → Q.Corresponds to variant rs2291572dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0075791734 – 1766Missing in isoform 2. 3 PublicationsAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF089841 mRNA. Translation: AAD12245.1. Different initiation.
AF184126
, 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.
CCDSiCCDS43644.1. [Q14315-1]
CCDS47705.1. [Q14315-2]
PIRiS37775.
S37778.
RefSeqiNP_001120959.1. NM_001127487.1. [Q14315-2]
NP_001449.3. NM_001458.4. [Q14315-1]
UniGeneiHs.58414.

Genome annotation databases

EnsembliENST00000325888; ENSP00000327145; ENSG00000128591. [Q14315-1]
ENST00000346177; ENSP00000344002; ENSG00000128591. [Q14315-2]
GeneIDi2318.
KEGGihsa:2318.
UCSCiuc003vnz.5. human. [Q14315-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF089841 mRNA. Translation: AAD12245.1. Different initiation.
AF184126
, 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.
CCDSiCCDS43644.1. [Q14315-1]
CCDS47705.1. [Q14315-2]
PIRiS37775.
S37778.
RefSeqiNP_001120959.1. NM_001127487.1. [Q14315-2]
NP_001449.3. NM_001458.4. [Q14315-1]
UniGeneiHs.58414.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V05X-ray1.43A2633-2725[»]
2D7MNMR-A1536-1637[»]
2D7NNMR-A1782-1861[»]
2D7ONMR-A1856-1953[»]
2D7PNMR-A2405-2503[»]
2D7QNMR-A2502-2599[»]
2K9UNMR-A2302-2415[»]
2NQCX-ray2.05A2495-2598[»]
3V8OX-ray2.80A/B569-761[»]
4MGXX-ray3.16A572-756[»]
ProteinModelPortaliQ14315.
SMRiQ14315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108607. 92 interactors.
DIPiDIP-33398N.
IntActiQ14315. 46 interactors.
MINTiMINT-5004555.
STRINGi9606.ENSP00000327145.

PTM databases

iPTMnetiQ14315.
PhosphoSitePlusiQ14315.
SwissPalmiQ14315.

Polymorphism and mutation databases

BioMutaiFLNC.
DMDMi254763419.

Proteomic databases

EPDiQ14315.
MaxQBiQ14315.
PaxDbiQ14315.
PeptideAtlasiQ14315.
PRIDEiQ14315.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325888; ENSP00000327145; ENSG00000128591. [Q14315-1]
ENST00000346177; ENSP00000344002; ENSG00000128591. [Q14315-2]
GeneIDi2318.
KEGGihsa:2318.
UCSCiuc003vnz.5. human. [Q14315-1]

Organism-specific databases

CTDi2318.
DisGeNETi2318.
GeneCardsiFLNC.
GeneReviewsiFLNC.
HGNCiHGNC:3756. FLNC.
HPAiHPA006135.
MalaCardsiFLNC.
MIMi102565. gene.
609524. phenotype.
614065. phenotype.
neXtProtiNX_Q14315.
OpenTargetsiENSG00000128591.
Orphaneti63273. Distal myopathy with posterior leg and anterior hand involvement.
171445. Muscle filaminopathy.
PharmGKBiPA28174.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00660000095431.
HOVERGENiHBG004163.
InParanoidiQ14315.
KOiK04437.
OMAiAEPMESM.
OrthoDBiEOG091G00U5.
PhylomeDBiQ14315.
TreeFamiTF313685.

Enzyme and pathway databases

ReactomeiR-HSA-446353. Cell-extracellular matrix interactions.

Miscellaneous databases

ChiTaRSiFLNC. human.
EvolutionaryTraceiQ14315.
GeneWikiiFLNC_(gene).
GenomeRNAii2318.
PROiQ14315.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000128591.
CleanExiHS_FLNC.
GenevisibleiQ14315. HS.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR032461. FLN_C.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11915:SF210. PTHR11915:SF210. 2 hits.
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTiSM00033. CH. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiFLNC_HUMAN
AccessioniPrimary (citable) accession number: Q14315
Secondary accession number(s): B2ZZ88
, O95303, Q07985, Q9NS12, Q9NYE5, Q9UMR8, Q9Y503
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: July 28, 2009
Last modified: November 30, 2016
This is version 182 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.