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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 neuromuscular disorder, usually with an adult onset, characterized by focal myofibrillar destruction, pathological cytoplasmic protein aggregations, and clinical features of a limb-girdle myopathy.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti193 – 1931A → 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 Publication
Corresponds to variant rs387906587 [ dbSNP | Ensembl ].
VAR_066212
Natural varianti251 – 2511M → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in the formation of intracellular protein aggregates. 1 Publication
Corresponds to variant rs387906586 [ dbSNP | Ensembl ].
VAR_066213

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2669 – 26691M → D: Abolishes dimerization. 1 Publication

Keywords - Diseasei

Disease mutation, Myofibrillar myopathy

Organism-specific databases

MalaCardsiFLNC.
MIMi609524. phenotype.
614065. phenotype.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27252725Filamin-CPRO_0000087301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei1161 – 11611PhosphoserineCombined sources
Modified residuei1338 – 13381PhosphoserineCombined sources
Modified residuei2042 – 20421PhosphoserineCombined sources
Modified residuei2233 – 22331PhosphoserineCombined sources1 Publication
Modified residuei2236 – 22361PhosphoserineCombined sources
Modified residuei2238 – 22381PhosphothreonineCombined sources
Modified residuei2586 – 25861PhosphoserineCombined sources
Modified residuei2617 – 26171PhosphoserineCombined sources
Modified residuei2620 – 26201PhosphoserineCombined sources
Modified residuei2623 – 26231PhosphoserineCombined sources
Modified residuei2632 – 26321PhosphoserineCombined sources
Modified residuei2714 – 27141PhosphoserineCombined sources
Modified residuei2718 – 27181PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated by FBXL22, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14315.
MaxQBiQ14315.
PaxDbiQ14315.
PeptideAtlasiQ14315.
PRIDEiQ14315.

PTM databases

iPTMnetiQ14315.
PhosphoSiteiQ14315.
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 interactions.
DIPiDIP-33398N.
IntActiQ14315. 44 interactions.
MINTiMINT-5004555.
STRINGi9606.ENSP00000327145.

Structurei

Secondary structure

1
2725
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi574 – 5785Combined sources
Helixi579 – 5813Combined sources
Beta strandi583 – 5853Combined sources
Beta strandi590 – 59910Combined sources
Helixi601 – 6033Combined sources
Beta strandi604 – 6129Combined sources
Beta strandi617 – 6204Combined sources
Beta strandi622 – 6309Combined sources
Beta strandi636 – 6449Combined sources
Beta strandi653 – 6597Combined sources
Helixi667 – 6693Combined sources
Beta strandi671 – 6744Combined sources
Helixi675 – 6773Combined sources
Beta strandi678 – 6803Combined sources
Beta strandi688 – 6936Combined sources
Beta strandi697 – 6993Combined sources
Beta strandi702 – 7087Combined sources
Beta strandi717 – 7204Combined sources
Beta strandi722 – 7309Combined sources
Beta strandi734 – 74411Combined sources
Beta strandi753 – 7597Combined sources
Helixi1539 – 15413Combined sources
Beta strandi1542 – 15476Combined sources
Beta strandi1554 – 15585Combined sources
Beta strandi1560 – 156910Combined sources
Beta strandi1574 – 15796Combined sources
Beta strandi1588 – 15925Combined sources
Beta strandi1594 – 15963Combined sources
Beta strandi1598 – 16025Combined sources
Beta strandi1608 – 161811Combined sources
Beta strandi1625 – 16317Combined sources
Beta strandi1785 – 17895Combined sources
Beta strandi1794 – 17963Combined sources
Beta strandi1798 – 18036Combined sources
Beta strandi1813 – 18164Combined sources
Beta strandi1818 – 18203Combined sources
Beta strandi1822 – 18265Combined sources
Beta strandi1832 – 184312Combined sources
Beta strandi1849 – 18546Combined sources
Beta strandi1863 – 18664Combined sources
Helixi1867 – 18704Combined sources
Beta strandi1871 – 18733Combined sources
Beta strandi1878 – 18836Combined sources
Turni1885 – 18873Combined sources
Beta strandi1895 – 19006Combined sources
Beta strandi1910 – 19189Combined sources
Beta strandi1924 – 19296Combined sources
Beta strandi1931 – 19344Combined sources
Beta strandi1941 – 19477Combined sources
Beta strandi2303 – 23086Combined sources
Turni2313 – 23164Combined sources
Beta strandi2318 – 23225Combined sources
Turni2323 – 23253Combined sources
Beta strandi2332 – 23387Combined sources
Beta strandi2344 – 235512Combined sources
Beta strandi2358 – 23625Combined sources
Beta strandi2365 – 237410Combined sources
Beta strandi2377 – 238913Combined sources
Beta strandi2396 – 24049Combined sources
Helixi2407 – 24104Combined sources
Beta strandi2427 – 24326Combined sources
Beta strandi2440 – 24456Combined sources
Beta strandi2447 – 24493Combined sources
Beta strandi2463 – 24686Combined sources
Beta strandi2474 – 248411Combined sources
Beta strandi2491 – 24966Combined sources
Helixi2505 – 25073Combined sources
Beta strandi2509 – 25124Combined sources
Helixi2513 – 25153Combined sources
Beta strandi2517 – 25193Combined sources
Beta strandi2524 – 25296Combined sources
Turni2531 – 25333Combined sources
Beta strandi2538 – 25469Combined sources
Beta strandi2549 – 25557Combined sources
Beta strandi2558 – 25647Combined sources
Beta strandi2569 – 258012Combined sources
Beta strandi2587 – 25948Combined sources
Helixi2635 – 26373Combined sources
Beta strandi2639 – 26424Combined sources
Helixi2643 – 26453Combined sources
Beta strandi2654 – 26596Combined sources
Beta strandi2663 – 26653Combined sources
Beta strandi2668 – 26736Combined sources
Beta strandi2675 – 26773Combined sources
Beta strandi2680 – 26867Combined sources
Beta strandi2691 – 26977Combined sources
Beta strandi2702 – 27109Combined sources
Beta strandi2719 – 27246Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 22-368, 472-761, 1039-1637, 1767-2135, 2248-2598, 2633-2725.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14315.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 259259Actin-bindingAdd
BLAST
Domaini36 – 142107CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini159 – 259101CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati270 – 36899Filamin 1Add
BLAST
Repeati370 – 46899Filamin 2Add
BLAST
Repeati469 – 56597Filamin 3Add
BLAST
Repeati566 – 65893Filamin 4Add
BLAST
Repeati662 – 75897Filamin 5Add
BLAST
Repeati759 – 861103Filamin 6Add
BLAST
Repeati862 – 96099Filamin 7Add
BLAST
Repeati961 – 105696Filamin 8Add
BLAST
Repeati1057 – 114993Filamin 9Add
BLAST
Repeati1150 – 124495Filamin 10Add
BLAST
Repeati1245 – 1344100Filamin 11Add
BLAST
Repeati1345 – 143793Filamin 12Add
BLAST
Repeati1438 – 153396Filamin 13Add
BLAST
Repeati1534 – 163097Filamin 14Add
BLAST
Repeati1635 – 1734100Filamin 15Add
BLAST
Repeati1759 – 185395Filamin 16Add
BLAST
Repeati1854 – 194693Filamin 17Add
BLAST
Repeati1947 – 203387Filamin 18Add
BLAST
Repeati2036 – 212893Filamin 19Add
BLAST
Repeati2244 – 230663Filamin 20; mediates interaction with XIRP1Add
BLAST
Repeati2309 – 240193Filamin 21Add
BLAST
Repeati2403 – 249694Filamin 22Add
BLAST
Repeati2500 – 259293Filamin 23Add
BLAST
Repeati2630 – 272495Filamin 24Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1735 – 175824Hinge 1Add
BLAST
Regioni2162 – 224382Intradomain insert; mediate targeting to Z linesAdd
BLAST
Regioni2403 – 2724322Interaction with INPPL1Add
BLAST
Regioni2593 – 2725133Self-association site, tailBy similarityAdd
BLAST
Regioni2593 – 262937Hinge 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

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

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381I → T in CAB46442 (PubMed:10658210).Curated
Sequence conflicti189 – 1891K → E in CAB46442 (PubMed:10658210).Curated
Sequence conflicti194 – 1941L → Q in CAB46442 (PubMed:10658210).Curated
Sequence conflicti218 – 2181A → S in AAD12245 (PubMed:9791010).Curated
Sequence conflicti218 – 2181A → S in AAF68195 (PubMed:11153914).Curated
Sequence conflicti233 – 2331Q → L in CAB46442 (PubMed:10658210).Curated
Sequence conflicti484 – 4841L → P in CAB46442 (PubMed:10658210).Curated
Sequence conflicti585 – 5851Q → V in CAA49688 (PubMed:7689010).Curated
Sequence conflicti723 – 7231D → N in AAD12245 (PubMed:9791010).Curated
Sequence conflicti723 – 7231D → N in AAF68195 (PubMed:11153914).Curated
Sequence conflicti723 – 7231D → N in CAA49688 (PubMed:7689010).Curated
Sequence conflicti1091 – 10911G → D in CAB46442 (PubMed:10658210).Curated
Sequence conflicti1640 – 16401L → T in CAA49689 (PubMed:7689010).Curated
Sequence conflicti1668 – 16681V → M in CAB46442 (PubMed:10658210).Curated
Sequence conflicti2101 – 21011C → S in CAB46442 (PubMed:10658210).Curated
Sequence conflicti2101 – 21011C → S in CAA49689 (PubMed:7689010).Curated
Sequence conflicti2321 – 23222GT → RA in AAD12245 (PubMed:9791010).Curated
Sequence conflicti2321 – 23222GT → RA in AAF68195 (PubMed:11153914).Curated
Sequence conflicti2355 – 23551S → N in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2382 – 23821E → K in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2484 – 24841G → C in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2491 – 24911P → L in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2499 – 24991Q → H in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2514 – 25141G → E in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2528 – 25303VNT → DDH in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2535 – 25351S → F in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2547 – 25471K → N in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2557 – 25571E → G in AAF80245 (PubMed:10629222).Curated
Sequence conflicti2601 – 26022HS → QH in AAF80245 (PubMed:10629222).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti193 – 1931A → 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 Publication
Corresponds to variant rs387906587 [ dbSNP | Ensembl ].
VAR_066212
Natural varianti251 – 2511M → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in the formation of intracellular protein aggregates. 1 Publication
Corresponds to variant rs387906586 [ dbSNP | Ensembl ].
VAR_066213
Natural varianti1567 – 15671R → Q.
Corresponds to variant rs2291569 [ dbSNP | Ensembl ].
VAR_015705
Natural varianti1580 – 15801D → G.2 Publications
Corresponds to variant rs2643766 [ dbSNP | Ensembl ].
VAR_015706
Natural varianti1599 – 15991T → A.2 Publications
Corresponds to variant rs2643767 [ dbSNP | Ensembl ].
VAR_015707
Natural varianti2135 – 21351K → R.1 Publication
Corresponds to variant rs1063261 [ dbSNP | Ensembl ].
VAR_015708
Natural varianti2203 – 22031R → P.2 Publications
Corresponds to variant rs1063262 [ dbSNP | Ensembl ].
VAR_015709
Natural varianti2626 – 26261S → N.
Corresponds to variant rs2639142 [ dbSNP | Ensembl ].
VAR_015710
Natural varianti2637 – 26371K → Q.
Corresponds to variant rs2291572 [ dbSNP | Ensembl ].
VAR_015711

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1734 – 176633Missing in isoform 2. 3 PublicationsVSP_007579Add
BLAST

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
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. Positions 22-368, 472-761, 1039-1637, 1767-2135, 2248-2598, 2633-2725.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108607. 92 interactions.
DIPiDIP-33398N.
IntActiQ14315. 44 interactions.
MINTiMINT-5004555.
STRINGi9606.ENSP00000327145.

PTM databases

iPTMnetiQ14315.
PhosphoSiteiQ14315.
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.
GeneCardsiFLNC.
GeneReviewsiFLNC.
HGNCiHGNC:3756. FLNC.
HPAiHPA006135.
MalaCardsiFLNC.
MIMi102565. gene.
609524. phenotype.
614065. phenotype.
neXtProtiNX_Q14315.
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

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: September 7, 2016
This is version 179 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.