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Q14315

- FLNC_HUMAN

UniProt

Q14315 - FLNC_HUMAN

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Protein

Filamin-C

Gene
FLNC, ABPL, FLN2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers.

GO - Molecular functioni

  1. ankyrin binding Source: BHF-UCL
  2. cytoskeletal protein binding Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. cell junction assembly Source: Reactome
  2. muscle fiber development Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_20649. 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
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:3756. FLNC.

Subcellular locationi

Cytoplasm. Membrane; Peripheral membrane protein. Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ line
Note: A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z lines, while a minor fraction localizes with subsarcolemme. Targeting to developing and mature Z lines is mediated by the intradomain insert.1 Publication

GO - Cellular componenti

  1. costamere Source: BHF-UCL
  2. cytoplasm Source: HPA
  3. cytoskeleton Source: UniProtKB-SubCell
  4. cytosol Source: Reactome
  5. plasma membrane Source: HPA
  6. sarcolemma Source: BHF-UCL
  7. sarcoplasm Source: Ensembl
  8. Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Myopathy, myofibrillar, 5 (MFM5) [MIM:609524]: A neuromuscular disorder, usually with an adult onset, characterized by focal myofibrillar destruction, pathological cytoplasmic protein aggregations, and clinical features of a limb-girdle myopathy.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Myopathy, distal, 4 (MPD4) [MIM:614065]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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
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
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

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

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 residuei1161 – 11611Phosphoserine1 Publication
Modified residuei2233 – 22331Phosphoserine3 Publications

Post-translational modificationi

Ubiquitinated by FBXL22, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14315.
PaxDbiQ14315.
PRIDEiQ14315.

PTM databases

PhosphoSiteiQ14315.

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

ArrayExpressiQ14315.
BgeeiQ14315.
CleanExiHS_FLNC.
GenevestigatoriQ14315.

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 ANK3.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-489954,EBI-375543
CRKP461082EBI-489954,EBI-886
DYSFO759233EBI-489954,EBI-2799016
GRB2P629932EBI-489954,EBI-401755
MYOTQ9UBF96EBI-489954,EBI-296701

Protein-protein interaction databases

BioGridi108607. 58 interactions.
DIPiDIP-33398N.
IntActiQ14315. 37 interactions.
MINTiMINT-5004555.
STRINGi9606.ENSP00000327145.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 22-2725.

Miscellaneous databases

EvolutionaryTraceiQ14315.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 259259Actin-bindingAdd
BLAST
Domaini36 – 142107CH 1Add
BLAST
Domaini159 – 259101CH 2Add
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, tail By similarityAdd
BLAST
Regioni2593 – 262937Hinge 2Add
BLAST

Sequence similaritiesi

Belongs to the filamin family.
Contains 24 filamin repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
HOVERGENiHBG004163.
InParanoidiQ14315.
KOiK04437.
OMAiEPTGCIV.
OrthoDBiEOG76T9QC.
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.
IPR003961. Fibronectin_type3.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR028559. FLN.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11915:SF173. PTHR11915:SF173. 1 hit.
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00060. FN3. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: 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

MMNNSGYSDA GLGLGDETDE MPSTEKDLAE DAPWKKIQQN TFTRWCNEHL     50
KCVGKRLTDL QRDLSDGLRL IALLEVLSQK RMYRKFHPRP NFRQMKLENV 100
SVALEFLERE HIKLVSIDSK AIVDGNLKLI LGLIWTLILH YSISMPMWED 150
EDDEDARKQT PKQRLLGWIQ NKVPQLPITN FNRDWQDGKA LGALVDNCAP 200
GLCPDWEAWD PNQPVENARE AMQQADDWLG VPQVIAPEEI VDPNVDEHSV 250
MTYLSQFPKA KLKPGAPVRS KQLNPKKAIA YGPGIEPQGN TVLQPAHFTV 300
QTVDAGVGEV LVYIEDPEGH TEEAKVVPNN DKDRTYAVSY VPKVAGLHKV 350
TVLFAGQNIE RSPFEVNVGM ALGDANKVSA RGPGLEPVGN VANKPTYFDI 400
YTAGAGTGDV AVVIVDPQGR RDTVEVALED KGDSTFRCTY RPAMEGPHTV 450
HVAFAGAPIT RSPFPVHVSE ACNPNACRAS GRGLQPKGVR VKEVADFKVF 500
TKGAGSGELK VTVKGPKGTE EPVKVREAGD GVFECEYYPV VPGKYVVTIT 550
WGGYAIPRSP FEVQVSPEAG VQKVRAWGPG LETGQVGKSA DFVVEAIGTE 600
VGTLGFSIEG PSQAKIECDD KGDGSCDVRY WPTEPGEYAV HVICDDEDIR 650
DSPFIAHILP APPDCFPDKV KAFGPGLEPT GCIVDKPAEF TIDARAAGKG 700
DLKLYAQDAD GCPIDIKVIP NGDGTFRCSY VPTKPIKHTI IISWGGVNVP 750
KSPFRVNVGE GSHPERVKVY GPGVEKTGLK ANEPTYFTVD CSEAGQGDVS 800
IGIKCAPGVV GPAEADIDFD IIKNDNDTFT VKYTPPGAGR YTIMVLFANQ 850
EIPASPFHIK VDPSHDASKV KAEGPGLNRT GVEVGKPTHF TVLTKGAGKA 900
KLDVQFAGTA KGEVVRDFEI IDNHDYSYTV KYTAVQQGNM AVTVTYGGDP 950
VPKSPFVVNV APPLDLSKIK VQGLNSKVAV GQEQAFSVNT RGAGGQGQLD 1000
VRMTSPSRRP IPCKLEPGGG AEAQAVRYMP PEEGPYKVDI TYDGHPVPGS 1050
PFAVEGVLPP DPSKVCAYGP GLKGGLVGTP APFSIDTKGA GTGGLGLTVE 1100
GPCEAKIECQ DNGDGSCAVS YLPTEPGEYT INILFAEAHI PGSPFKATIR 1150
PVFDPSKVRA SGPGLERGKV GEAATFTVDC SEAGEAELTI EILSDAGVKA 1200
EVLIHNNADG TYHITYSPAF PGTYTITIKY GGHPVPKFPT RVHVQPAVDT 1250
SGVKVSGPGV EPHGVLREVT TEFTVDARSL TATGGNHVTA RVLNPSGAKT 1300
DTYVTDNGDG TYRVQYTAYE EGVHLVEVLY DEVAVPKSPF RVGVTEGCDP 1350
TRVRAFGPGL EGGLVNKANR FTVETRGAGT GGLGLAIEGP SEAKMSCKDN 1400
KDGSCTVEYI PFTPGDYDVN ITFGGRPIPG SPFRVPVKDV VDPGKVKCSG 1450
PGLGAGVRAR VPQTFTVDCS QAGRAPLQVA VLGPTGVAEP VEVRDNGDGT 1500
HTVHYTPATD GPYTVAVKYA DQEVPRSPFK IKVLPAHDAS KVRASGPGLN 1550
ASGIPASLPV EFTIDARDAG EGLLTVQILD PEGKPKKANI RDNGDGTYTV 1600
SYLPDMSGRY TITIKYGGDE IPYSPFRIHA LPTGDASKCL VTVSIGGHGL 1650
GACLGPRIQI GQETVITVDA KAAGEGKVTC TVSTPDGAEL DVDVVENHDG 1700
TFDIYYTAPE PGKYVITIRF GGEHIPNSPF HVLACDPLPH EEEPSEVPQL 1750
RQPYAPPRPG ARPTHWATEE PVVPVEPMES MLRPFNLVIP FAVQKGELTG 1800
EVRMPSGKTA RPNITDNKDG TITVRYAPTE KGLHQMGIKY DGNHIPGSPL 1850
QFYVDAINSR HVSAYGPGLS HGMVNKPATF TIVTKDAGEG GLSLAVEGPS 1900
KAEITCKDNK DGTCTVSYLP TAPGDYSIIV RFDDKHIPGS PFTAKITGDD 1950
SMRTSQLNVG TSTDVSLKIT ESDLSQLTAS IRAPSGNEEP CLLKRLPNRH 2000
IGISFTPKEV GEHVVSVRKS GKHVTNSPFK ILVGPSEIGD ASKVRVWGKG 2050
LSEGHTFQVA EFIVDTRNAG YGGLGLSIEG PSKVDINCED MEDGTCKVTY 2100
CPTEPGTYII NIKFADKHVP GSPFTVKVTG EGRMKESITR RRQAPSIATI 2150
GSTCDLNLKI PGNWFQMVSA QERLTRTFTR SSHTYTRTER TEISKTRGGE 2200
TKREVRVEES TQVGGDPFPA VFGDFLGRER LGSFGSITRQ QEGEASSQDM 2250
TAQVTSPSGK VEAAEIVEGE DSAYSVRFVP QEMGPHTVAV KYRGQHVPGS 2300
PFQFTVGPLG EGGAHKVRAG GTGLERGVAG VPAEFSIWTR EAGAGGLSIA 2350
VEGPSKAEIA FEDRKDGSCG VSYVVQEPGD YEVSIKFNDE HIPDSPFVVP 2400
VASLSDDARR LTVTSLQETG LKVNQPASFA VQLNGARGVI DARVHTPSGA 2450
VEECYVSELD SDKHTIRFIP HENGVHSIDV KFNGAHIPGS PFKIRVGEQS 2500
QAGDPGLVSA YGPGLEGGTT GVSSEFIVNT LNAGSGALSV TIDGPSKVQL 2550
DCRECPEGHV VTYTPMAPGN YLIAIKYGGP QHIVGSPFKA KVTGPRLSGG 2600
HSLHETSTVL VETVTKSSSS RGSSYSSIPK FSSDASKVVT RGPGLSQAFV 2650
GQKNSFTVDC SKAGTNMMMV GVHGPKTPCE EVYVKHMGNR VYNVTYTVKE 2700
KGDYILIVKW GDESVPGSPF KVKVP 2725
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 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.
The sequence AAD12245.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAF68195.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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
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
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. VSP_007579Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381I → T in CAB46442. 1 Publication
Sequence conflicti189 – 1891K → E in CAB46442. 1 Publication
Sequence conflicti194 – 1941L → Q in CAB46442. 1 Publication
Sequence conflicti218 – 2181A → S in AAD12245. 1 Publication
Sequence conflicti218 – 2181A → S in AAF68195. 1 Publication
Sequence conflicti233 – 2331Q → L in CAB46442. 1 Publication
Sequence conflicti484 – 4841L → P in CAB46442. 1 Publication
Sequence conflicti585 – 5851Q → V in CAA49688. 1 Publication
Sequence conflicti723 – 7231D → N in AAD12245. 1 Publication
Sequence conflicti723 – 7231D → N in AAF68195. 1 Publication
Sequence conflicti723 – 7231D → N in CAA49688. 1 Publication
Sequence conflicti1091 – 10911G → D in CAB46442. 1 Publication
Sequence conflicti1640 – 16401L → T in CAA49689. 1 Publication
Sequence conflicti1668 – 16681V → M in CAB46442. 1 Publication
Sequence conflicti2101 – 21011C → S in CAB46442. 1 Publication
Sequence conflicti2101 – 21011C → S in CAA49689. 1 Publication
Sequence conflicti2321 – 23222GT → RA in AAD12245. 1 Publication
Sequence conflicti2321 – 23222GT → RA in AAF68195. 1 Publication
Sequence conflicti2355 – 23551S → N in AAF80245. 1 Publication
Sequence conflicti2382 – 23821E → K in AAF80245. 1 Publication
Sequence conflicti2484 – 24841G → C in AAF80245. 1 Publication
Sequence conflicti2491 – 24911P → L in AAF80245. 1 Publication
Sequence conflicti2499 – 24991Q → H in AAF80245. 1 Publication
Sequence conflicti2514 – 25141G → E in AAF80245. 1 Publication
Sequence conflicti2528 – 25303VNT → DDH in AAF80245. 1 Publication
Sequence conflicti2535 – 25351S → F in AAF80245. 1 Publication
Sequence conflicti2547 – 25471K → N in AAF80245. 1 Publication
Sequence conflicti2557 – 25571E → G in AAF80245. 1 Publication
Sequence conflicti2601 – 26022HS → QH in AAF80245. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.4. human. [Q14315-1]
uc003voa.4. human. [Q14315-2]

Polymorphism databases

DMDMi254763419.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS43644.1. [Q14315-1 ]
CCDS47705.1. [Q14315-2 ]
PIRi S37775.
S37778.
RefSeqi NP_001120959.1. NM_001127487.1. [Q14315-2 ]
NP_001449.3. NM_001458.4. [Q14315-1 ]
UniGenei Hs.58414.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V05 X-ray 1.43 A 2633-2725 [» ]
2D7M NMR - A 1536-1637 [» ]
2D7N NMR - A 1782-1861 [» ]
2D7O NMR - A 1856-1953 [» ]
2D7P NMR - A 2405-2503 [» ]
2D7Q NMR - A 2502-2599 [» ]
2K9U NMR - A 2302-2415 [» ]
2NQC X-ray 2.05 A 2495-2598 [» ]
3V8O X-ray 2.80 A/B 569-761 [» ]
4MGX X-ray 3.16 A 572-756 [» ]
ProteinModelPortali Q14315.
SMRi Q14315. Positions 22-2725.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108607. 58 interactions.
DIPi DIP-33398N.
IntActi Q14315. 37 interactions.
MINTi MINT-5004555.
STRINGi 9606.ENSP00000327145.

PTM databases

PhosphoSitei Q14315.

Polymorphism databases

DMDMi 254763419.

Proteomic databases

MaxQBi Q14315.
PaxDbi Q14315.
PRIDEi Q14315.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325888 ; ENSP00000327145 ; ENSG00000128591 . [Q14315-1 ]
ENST00000346177 ; ENSP00000344002 ; ENSG00000128591 . [Q14315-2 ]
GeneIDi 2318.
KEGGi hsa:2318.
UCSCi uc003vnz.4. human. [Q14315-1 ]
uc003voa.4. human. [Q14315-2 ]

Organism-specific databases

CTDi 2318.
GeneCardsi GC07P128470.
GeneReviewsi FLNC.
HGNCi HGNC:3756. FLNC.
HPAi HPA006135.
MIMi 102565. gene.
609524. phenotype.
614065. phenotype.
neXtProti NX_Q14315.
Orphaneti 63273. Distal myopathy with posterior leg and anterior hand involvement.
171445. Muscle filaminopathy.
PharmGKBi PA28174.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
HOVERGENi HBG004163.
InParanoidi Q14315.
KOi K04437.
OMAi EPTGCIV.
OrthoDBi EOG76T9QC.
PhylomeDBi Q14315.
TreeFami TF313685.

Enzyme and pathway databases

Reactomei REACT_20649. Cell-extracellular matrix interactions.

Miscellaneous databases

EvolutionaryTracei Q14315.
GeneWikii FLNC_(gene).
GenomeRNAii 2318.
NextBioi 9413.
PROi Q14315.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14315.
Bgeei Q14315.
CleanExi HS_FLNC.
Genevestigatori Q14315.

Family and domain databases

Gene3Di 1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR003961. Fibronectin_type3.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR028559. FLN.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view ]
PANTHERi PTHR11915:SF173. PTHR11915:SF173. 1 hit.
Pfami PF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00060. FN3. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEi PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS GLY-1580; ALA-1599; ARG-2135 AND PRO-2203.
  4. 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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Bienvenut W.V., Pchelintsev N., Adams P.D.
    Submitted (OCT-2009) to UniProtKB
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 585-815 AND 1638-2101 (ISOFORM 2), TISSUE SPECIFICITY.
  10. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPPL1.
  15. 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] [Europe PMC] [Abstract]
    Cited for: SILENCING IN CANCER CELL LINES MKN28 AND MKN74.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MFM5.
  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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITGB1; MYOT AND MYOZ1.
  21. "The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins."
    Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.
    Cell. Mol. Life Sci. 63:723-734(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP25.
  22. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XIRP1.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C."
    Maiweilidan Y., Klauza I., Kordeli E.
    Exp. Cell Res. 317:724-736(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANK3.
  27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "F-box and leucine-rich repeat protein 22 is a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo."
    Spaich S., Will R.D., Just S., Spaich S., Kuhn C., Frank D., Berger I.M., Wiemann S., Korn B., Koegl M., Backs J., Katus H.A., Rottbauer W., Frey N.
    Circ. Res. 111:1504-1516(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY FBXL22.
  29. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 2633-2725, MUTAGENESIS OF MET-2669.
  30. "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.
  31. "Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer."
    Sjekloca L., Pudas R., Sjoblom B., Konarev P., Carugo O., Rybin V., Kiema T.R., Svergun D., Ylanne J., Djinovic Carugo K.
    J. Mol. Biol. 368:1011-1023(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2495-2598, SUBUNIT.
  32. "Migfilin, a molecular switch in regulation of integrin activation."
    Ithychanda S.S., Das M., Ma Y.Q., Ding K., Wang X., Gupta S., Wu C., Plow E.F., Qin J.
    J. Biol. Chem. 284:4713-4722(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2302-2415 IN COMPLEX WITH FBLIM1.
  33. Cited for: VARIANTS MPD4 THR-193 AND THR-251, CHARACTERIZATION OF VARIANTS MPD4 THR-193 AND THR-251.

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 3, 2014
This is version 156 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

External Data

Dasty 3

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