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Protein

Filamin-C

Gene

FLNC

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

Miscellaneous

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding

Enzyme and pathway databases

ReactomeiR-HSA-446353 Cell-extracellular matrix interactions

Protein family/group databases

TCDBi8.A.66.1.6 the dystrophin (dystrophin) family

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

EuPathDBiHostDB:ENSG00000128591.15
HGNCiHGNC:3756 FLNC
MIMi102565 gene
neXtProtiNX_Q14315

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 disk 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 dbSNP:rs387906587EnsemblClinVar.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 dbSNP:rs387906586EnsemblClinVar.1
Cardiomyopathy, familial hypertrophic 26 (CMH26)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
See also OMIM:617047
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_077036123V → A in CMH26; increased aggregation; localized in perinuclear region of cytoplasm. 1 Publication1
Natural variantiVAR_077037290N → K in CMH26; unknown pathological significance. 1 Publication1
Natural variantiVAR_0770381539A → T in CMH26; increased actin aggregation; localized in perinuclear region of cytoplasm. 1 Publication1
Natural variantiVAR_0770402133R → H in CMH26; increased aggregation; localized in perinuclear region of cytoplasm. 1 Publication1
Natural variantiVAR_0770412151G → S in CMH26; unknown pathological significance. 1 Publication1
Natural variantiVAR_0770432430A → V in CMH26; unknown pathological significance; increased aggregation; localized in perinuclear region of cytoplasm. 1 PublicationCorresponds to variant dbSNP:rs200516164EnsemblClinVar.1
Cardiomyopathy, familial restrictive 5 (RCM5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA heart disorder characterized by impaired filling of the ventricles with reduced diastolic volume, in the presence of normal or near normal wall thickness and systolic function.
See also OMIM:617047
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0770391624S → L in RCM5; increased protein aggregates; effect on cytoplasm localization; localized in perinuclear region of cytoplasm; no effect on expression. 1 PublicationCorresponds to variant dbSNP:rs879255639EnsemblClinVar.1
Natural variantiVAR_0770422160I → F in RCM5; no effect on cytoplasm localization; no effect on expression. 1 PublicationCorresponds to variant dbSNP:rs879255640EnsemblClinVar.1

Mutagenesis

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

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Myofibrillar myopathy

Organism-specific databases

DisGeNETi2318
GeneReviewsiFLNC
MalaCardsiFLNC
MIMi609524 phenotype
614065 phenotype
617047 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
ProteomicsDBi59960
59961 [Q14315-2]

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 Expressed in 214 organ(s), highest expression level in heart left ventricle
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. Interacts with SYNPO2.By similarity15 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108607, 104 interactors
DIPiDIP-33398N
IntActiQ14315, 48 interactors
MINTiQ14315
STRINGi9606.ENSP00000327145

Structurei

Secondary structure

12725
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ14315
SMRiQ14315
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14315

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 142Calponin-homology (CH) 1PROSITE-ProRule annotationAdd BLAST107
Domaini159 – 262Calponin-homology (CH) 2PROSITE-ProRule annotationAdd BLAST104
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
Regioni1 – 259Actin-bindingAdd BLAST259
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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0518 Eukaryota
COG5069 LUCA
GeneTreeiENSGT00900000140842
HOVERGENiHBG004163
InParanoidiQ14315
KOiK04437
OMAiQNIERSP
OrthoDBiEOG091G00U5
PhylomeDBiQ14315
TreeFamiTF313685

Family and domain databases

CDDicd00014 CH, 2 hits
Gene3Di1.10.418.10, 2 hits
2.60.40.10, 24 hits
InterProiView protein in InterPro
IPR001589 Actinin_actin-bd_CS
IPR001715 CH-domain
IPR036872 CH_dom_sf
IPR017868 Filamin/ABP280_repeat-like
IPR001298 Filamin/ABP280_rpt
IPR032461 FLN_C
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
PANTHERiPTHR43998:SF4 PTHR43998:SF4, 1 hit
PfamiView protein in Pfam
PF00307 CH, 2 hits
PF00630 Filamin, 23 hits
SMARTiView protein in SMART
SM00033 CH, 2 hits
SM00557 IG_FLMN, 24 hits
SUPFAMiSSF47576 SSF47576, 1 hit
SSF81296 SSF81296, 24 hits
PROSITEiView protein in PROSITE
PS00019 ACTININ_1, 1 hit
PS00020 ACTININ_2, 1 hit
PS50021 CH, 2 hits
PS50194 FILAMIN_REPEAT, 24 hits

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_077036123V → A in CMH26; increased aggregation; localized in perinuclear region of cytoplasm. 1 Publication1
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 dbSNP:rs387906587EnsemblClinVar.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 dbSNP:rs387906586EnsemblClinVar.1
Natural variantiVAR_077037290N → K in CMH26; unknown pathological significance. 1 Publication1
Natural variantiVAR_0770381539A → T in CMH26; increased actin aggregation; localized in perinuclear region of cytoplasm. 1 Publication1
Natural variantiVAR_0157051567R → Q. Corresponds to variant dbSNP:rs2291569EnsemblClinVar.1
Natural variantiVAR_0157061580D → G2 PublicationsCorresponds to variant dbSNP:rs2643766Ensembl.1
Natural variantiVAR_0157071599T → A2 PublicationsCorresponds to variant dbSNP:rs2643767Ensembl.1
Natural variantiVAR_0770391624S → L in RCM5; increased protein aggregates; effect on cytoplasm localization; localized in perinuclear region of cytoplasm; no effect on expression. 1 PublicationCorresponds to variant dbSNP:rs879255639EnsemblClinVar.1
Natural variantiVAR_0770402133R → H in CMH26; increased aggregation; localized in perinuclear region of cytoplasm. 1 Publication1
Natural variantiVAR_0157082135K → R1 PublicationCorresponds to variant dbSNP:rs1063261Ensembl.1
Natural variantiVAR_0770412151G → S in CMH26; unknown pathological significance. 1 Publication1
Natural variantiVAR_0770422160I → F in RCM5; no effect on cytoplasm localization; no effect on expression. 1 PublicationCorresponds to variant dbSNP:rs879255640EnsemblClinVar.1
Natural variantiVAR_0157092203R → P2 PublicationsCorresponds to variant dbSNP:rs1063262Ensembl.1
Natural variantiVAR_0770432430A → V in CMH26; unknown pathological significance; increased aggregation; localized in perinuclear region of cytoplasm. 1 PublicationCorresponds to variant dbSNP:rs200516164EnsemblClinVar.1
Natural variantiVAR_0157102626S → N. Corresponds to variant dbSNP:rs2639142Ensembl.1
Natural variantiVAR_0157112637K → Q. Corresponds to variant dbSNP:rs2291572Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiFLNC_HUMAN
AccessioniPrimary (citable) accession number: Q14315
Secondary accession number(s): B2ZZ88
, O95303, Q07985, Q9NS12, Q9NYE5, Q9UMR8, Q9Y503
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: July 28, 2009
Last modified: September 12, 2018
This is version 200 of the entry and version 3 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health

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