Q14315 (FLNC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	FLNC
Synonyms:	ABPL, FLN2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2725 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers.
Subunit structure	Homodimer. Interacts with KY. Interacts with IGFN1 By similarity. Interacts with FLNB, KCND2, ITGB1A, INPPL1, 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. Ref.4 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.30
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. Cytoplasm › cytoskeleton. Cytoplasm › myofibril › sarcomere › Z 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. Ref.11
Tissue specificity	Highly expressed in striated muscles. Weakly expressed in thyroid, fetal brain, fetal lung, retina, spinal cord and bone marrow. Not expressed in testis, pancreas, adrenal gland, placenta, liver and kidney. Ref.1 Ref.9 Ref.11
Developmental stage	Expressed in both differentiating and adult muscles.
Domain	The intradomain insert is specific to FLNC and mediates the targeting to developing and mature Z lines. Ref.11 Comprised of a N-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. Ref.11 The filamin 20 repeat mediates interaction with XIRP1. Ref.11
Post-translational modification	Ubiquitinated by FBXL22, leading to proteasomal degradation. Ref.27
Involvement in disease	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. Ref.19 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. Ref.32
Miscellaneous	Silenced in MKN28 and MKN74 gastric cancer cell lines due to aberrant methylation of the gene.
Sequence similarities	Belongs to the filamin family. Contains 1 actin-binding domain. Contains 2 CH (calponin-homology) domains. Contains 24 filamin repeats.
Sequence caution	The sequence 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. 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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Myofibrillar myopathy
Domain	Repeat
Ligand	Actin-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell junction assembly Traceable author statement. Source: Reactome muscle fiber development Inferred from electronic annotation. Source: Compara
Cellular_component	Z disc Inferred from electronic annotation. Source: UniProtKB-SubCell costamere Traceable author statement PubMed 21223964. Source: BHF-UCL cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome sarcolemma Inferred from direct assay PubMed 21223964. Source: BHF-UCL sarcoplasm Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	2	EBI-489954,EBI-375543
CRK	P46108	2	EBI-489954,EBI-886
DYSF	O75923	3	EBI-489954,EBI-2799016
GRB2	P62993	2	EBI-489954,EBI-401755
MYOT	Q9UBF9	6	EBI-489954,EBI-296701

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q14315-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q14315-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2725

2725

Filamin-C

PRO_0000087301

Regions

Domain

1 – 259

259

Actin-binding

Domain

36 – 142

107

CH 1

Domain

159 – 259

101

CH 2

Repeat

270 – 368

99

Filamin 1

Repeat

370 – 468

99

Filamin 2

Repeat

469 – 565

97

Filamin 3

Repeat

566 – 658

93

Filamin 4

Repeat

662 – 758

97

Filamin 5

Repeat

759 – 861

103

Filamin 6

Repeat

862 – 960

99

Filamin 7

Repeat

961 – 1056

96

Filamin 8

Repeat

1057 – 1149

93

Filamin 9

Repeat

1150 – 1244

95

Filamin 10

Repeat

1245 – 1344

100

Filamin 11

Repeat

1345 – 1437

93

Filamin 12

Repeat

1438 – 1533

96

Filamin 13

Repeat

1534 – 1630

97

Filamin 14

Repeat

1635 – 1734

100

Filamin 15

Repeat

1759 – 1853

95

Filamin 16

Repeat

1854 – 1946

93

Filamin 17

Repeat

1947 – 2033

87

Filamin 18

Repeat

2036 – 2128

93

Filamin 19

Repeat

2244 – 2306

63

Filamin 20

Repeat

2309 – 2401

93

Filamin 21

Repeat

2403 – 2496

94

Filamin 22

Repeat

2500 – 2592

93

Filamin 23

Repeat

2630 – 2724

95

Filamin 24

Region

1735 – 1758

24

Hinge 1

Region

2162 – 2243

82

Intradomain insert

Region

2403 – 2724

322

Interaction with INPPL1

Region

2593 – 2725

133

Self-association site, tail By similarity

Region

2593 – 2629

37

Hinge 2

Amino acid modifications

Modified residue

1161

1

Phosphoserine Ref.23

Modified residue

2233

1

Phosphoserine Ref.8 Ref.24 Ref.26

Natural variations

Alternative sequence

1734 – 1766

33

Missing in isoform 2.

VSP_007579

Natural variant

193

1

A → 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. Ref.32

VAR_066212

Natural variant

251

1

M → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in the formation of intracellular protein aggregates. Ref.32

VAR_066213

Natural variant

1567

1

R → Q.
Corresponds to variant rs2291569 [ dbSNP | Ensembl ].

VAR_015705

Natural variant

1580

1

D → G. Ref.1 Ref.3
Corresponds to variant rs2643766 [ dbSNP | Ensembl ].

VAR_015706

Natural variant

1599

1

T → A. Ref.1 Ref.3
Corresponds to variant rs2643767 [ dbSNP | Ensembl ].

VAR_015707

Natural variant

2135

1

K → R. Ref.3
Corresponds to variant rs1063261 [ dbSNP | Ensembl ].

VAR_015708

Natural variant

2203

1

R → P. Ref.1 Ref.3
Corresponds to variant rs1063262 [ dbSNP | Ensembl ].

VAR_015709

Natural variant

2626

1

S → N.
Corresponds to variant rs2639142 [ dbSNP | Ensembl ].

VAR_015710

Natural variant

2637

1

K → Q.
Corresponds to variant rs2291572 [ dbSNP | Ensembl ].

VAR_015711

Experimental info

Mutagenesis

2669

1

M → D: Abolishes dimerization. Ref.28

Sequence conflict

138

1

I → T in CAB46442. Ref.3

Sequence conflict

189

1

K → E in CAB46442. Ref.3

Sequence conflict

194

1

L → Q in CAB46442. Ref.3

Sequence conflict

218

1

A → S in AAD12245. Ref.1

Sequence conflict

218

1

A → S in AAF68195. Ref.2

Sequence conflict

233

1

Q → L in CAB46442. Ref.3

Sequence conflict

484

1

L → P in CAB46442. Ref.3

Sequence conflict

585

1

Q → V in CAA49688. Ref.9

Sequence conflict

723

1

D → N in AAD12245. Ref.1

Sequence conflict

723

1

D → N in AAF68195. Ref.2

Sequence conflict

723

1

D → N in CAA49688. Ref.9

Sequence conflict

1091

1

G → D in CAB46442. Ref.3

Sequence conflict

1640

1

L → T in CAA49689. Ref.9

Sequence conflict

1668

1

V → M in CAB46442. Ref.3

Sequence conflict

2101

1

C → S in CAB46442. Ref.3

Sequence conflict

2101

1

C → S in CAA49689. Ref.9

Sequence conflict

2321 – 2322

2

GT → RA in AAD12245. Ref.1

Sequence conflict

2321 – 2322

2

GT → RA in AAF68195. Ref.2

Sequence conflict

2355

1

S → N in AAF80245. Ref.4

Sequence conflict

2382

1

E → K in AAF80245. Ref.4

Sequence conflict

2484

1

G → C in AAF80245. Ref.4

Sequence conflict

2491

1

P → L in AAF80245. Ref.4

Sequence conflict

2499

1

Q → H in AAF80245. Ref.4

Sequence conflict

2514

1

G → E in AAF80245. Ref.4

Sequence conflict

2528 – 2530

3

VNT → DDH in AAF80245. Ref.4

Sequence conflict

2535

1

S → F in AAF80245. Ref.4

Sequence conflict

2547

1

K → N in AAF80245. Ref.4

Sequence conflict

2557

1

E → G in AAF80245. Ref.4

Sequence conflict

2601 – 2602

2

HS → QH in AAF80245. Ref.4

Secondary structure

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2725

Helix Strand Turn

Details...

Helix

1539 – 1541

3

Beta strand

1542 – 1547

6

Beta strand

1554 – 1558

5

Beta strand

1560 – 1569

10

Beta strand

1574 – 1579

6

Beta strand

1588 – 1592

5

Beta strand

1594 – 1596

3

Beta strand

1598 – 1602

5

Beta strand

1608 – 1618

11

Beta strand

1625 – 1631

7

Beta strand

1785 – 1789

5

Beta strand

1794 – 1796

3

Beta strand

1798 – 1803

6

Beta strand

1813 – 1816

4

Beta strand

1818 – 1820

3

Beta strand

1822 – 1826

5

Beta strand

1832 – 1843

12

Beta strand

1849 – 1854

6

Beta strand

1863 – 1866

4

Helix

1867 – 1870

4

Beta strand

1871 – 1873

3

Beta strand

1878 – 1883

6

Turn

1885 – 1887

3

Beta strand

1895 – 1900

6

Beta strand

1910 – 1918

9

Beta strand

1924 – 1929

6

Beta strand

1931 – 1934

4

Beta strand

1941 – 1947

7

Beta strand

2303 – 2308

6

Turn

2313 – 2316

4

Beta strand

2318 – 2322

5

Turn

2323 – 2325

3

Beta strand

2332 – 2338

7

Beta strand

2344 – 2355

12

Beta strand

2358 – 2362

5

Beta strand

2365 – 2374

10

Beta strand

2377 – 2389

13

Beta strand

2396 – 2404

9

Helix

2407 – 2410

4

Beta strand

2427 – 2432

6

Beta strand

2440 – 2445

6

Beta strand

2447 – 2449

3

Beta strand

2463 – 2468

6

Beta strand

2474 – 2484

11

Beta strand

2491 – 2496

6

Helix

2505 – 2507

3

Beta strand

2509 – 2512

4

Helix

2513 – 2515

3

Beta strand

2517 – 2519

3

Beta strand

2524 – 2529

6

Turn

2531 – 2533

3

Beta strand

2538 – 2546

9

Beta strand

2549 – 2555

7

Beta strand

2558 – 2564

7

Beta strand

2569 – 2580

12

Beta strand

2587 – 2594

8

Helix

2635 – 2637

3

Beta strand

2639 – 2642

4

Helix

2643 – 2645

3

Beta strand

2654 – 2659

6

Beta strand

2663 – 2665

3

Beta strand

2668 – 2673

6

Beta strand

2675 – 2677

3

Beta strand

2680 – 2686

7

Beta strand

2691 – 2697

7

Beta strand

2702 – 2710

9

Beta strand

2719 – 2724

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 28, 2009. Version 3. Checksum: B7C8516C2366E75D	FASTA	2,725	291,022
	10 20 30 40 50 60 MMNNSGYSDA GLGLGDETDE MPSTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVGKRLTDL 70 80 90 100 110 120 QRDLSDGLRL IALLEVLSQK RMYRKFHPRP NFRQMKLENV SVALEFLERE HIKLVSIDSK 130 140 150 160 170 180 AIVDGNLKLI LGLIWTLILH YSISMPMWED EDDEDARKQT PKQRLLGWIQ NKVPQLPITN 190 200 210 220 230 240 FNRDWQDGKA LGALVDNCAP GLCPDWEAWD PNQPVENARE AMQQADDWLG VPQVIAPEEI 250 260 270 280 290 300 VDPNVDEHSV MTYLSQFPKA KLKPGAPVRS KQLNPKKAIA YGPGIEPQGN TVLQPAHFTV 310 320 330 340 350 360 QTVDAGVGEV LVYIEDPEGH TEEAKVVPNN DKDRTYAVSY VPKVAGLHKV TVLFAGQNIE 370 380 390 400 410 420 RSPFEVNVGM ALGDANKVSA RGPGLEPVGN VANKPTYFDI YTAGAGTGDV AVVIVDPQGR 430 440 450 460 470 480 RDTVEVALED KGDSTFRCTY RPAMEGPHTV HVAFAGAPIT RSPFPVHVSE ACNPNACRAS 490 500 510 520 530 540 GRGLQPKGVR VKEVADFKVF TKGAGSGELK VTVKGPKGTE EPVKVREAGD GVFECEYYPV 550 560 570 580 590 600 VPGKYVVTIT WGGYAIPRSP FEVQVSPEAG VQKVRAWGPG LETGQVGKSA DFVVEAIGTE 610 620 630 640 650 660 VGTLGFSIEG PSQAKIECDD KGDGSCDVRY WPTEPGEYAV HVICDDEDIR DSPFIAHILP 670 680 690 700 710 720 APPDCFPDKV KAFGPGLEPT GCIVDKPAEF TIDARAAGKG DLKLYAQDAD GCPIDIKVIP 730 740 750 760 770 780 NGDGTFRCSY VPTKPIKHTI IISWGGVNVP KSPFRVNVGE GSHPERVKVY GPGVEKTGLK 790 800 810 820 830 840 ANEPTYFTVD CSEAGQGDVS IGIKCAPGVV GPAEADIDFD IIKNDNDTFT VKYTPPGAGR 850 860 870 880 890 900 YTIMVLFANQ EIPASPFHIK VDPSHDASKV KAEGPGLNRT GVEVGKPTHF TVLTKGAGKA 910 920 930 940 950 960 KLDVQFAGTA KGEVVRDFEI IDNHDYSYTV KYTAVQQGNM AVTVTYGGDP VPKSPFVVNV 970 980 990 1000 1010 1020 APPLDLSKIK VQGLNSKVAV GQEQAFSVNT RGAGGQGQLD VRMTSPSRRP IPCKLEPGGG 1030 1040 1050 1060 1070 1080 AEAQAVRYMP PEEGPYKVDI TYDGHPVPGS PFAVEGVLPP DPSKVCAYGP GLKGGLVGTP 1090 1100 1110 1120 1130 1140 APFSIDTKGA GTGGLGLTVE GPCEAKIECQ DNGDGSCAVS YLPTEPGEYT INILFAEAHI 1150 1160 1170 1180 1190 1200 PGSPFKATIR PVFDPSKVRA SGPGLERGKV GEAATFTVDC SEAGEAELTI EILSDAGVKA 1210 1220 1230 1240 1250 1260 EVLIHNNADG TYHITYSPAF PGTYTITIKY GGHPVPKFPT RVHVQPAVDT SGVKVSGPGV 1270 1280 1290 1300 1310 1320 EPHGVLREVT TEFTVDARSL TATGGNHVTA RVLNPSGAKT DTYVTDNGDG TYRVQYTAYE 1330 1340 1350 1360 1370 1380 EGVHLVEVLY DEVAVPKSPF RVGVTEGCDP TRVRAFGPGL EGGLVNKANR FTVETRGAGT 1390 1400 1410 1420 1430 1440 GGLGLAIEGP SEAKMSCKDN KDGSCTVEYI PFTPGDYDVN ITFGGRPIPG SPFRVPVKDV 1450 1460 1470 1480 1490 1500 VDPGKVKCSG PGLGAGVRAR VPQTFTVDCS QAGRAPLQVA VLGPTGVAEP VEVRDNGDGT 1510 1520 1530 1540 1550 1560 HTVHYTPATD GPYTVAVKYA DQEVPRSPFK IKVLPAHDAS KVRASGPGLN ASGIPASLPV 1570 1580 1590 1600 1610 1620 EFTIDARDAG EGLLTVQILD PEGKPKKANI RDNGDGTYTV SYLPDMSGRY TITIKYGGDE 1630 1640 1650 1660 1670 1680 IPYSPFRIHA LPTGDASKCL VTVSIGGHGL GACLGPRIQI GQETVITVDA KAAGEGKVTC 1690 1700 1710 1720 1730 1740 TVSTPDGAEL DVDVVENHDG TFDIYYTAPE PGKYVITIRF GGEHIPNSPF HVLACDPLPH 1750 1760 1770 1780 1790 1800 EEEPSEVPQL RQPYAPPRPG ARPTHWATEE PVVPVEPMES MLRPFNLVIP FAVQKGELTG 1810 1820 1830 1840 1850 1860 EVRMPSGKTA RPNITDNKDG TITVRYAPTE KGLHQMGIKY DGNHIPGSPL QFYVDAINSR 1870 1880 1890 1900 1910 1920 HVSAYGPGLS HGMVNKPATF TIVTKDAGEG GLSLAVEGPS KAEITCKDNK DGTCTVSYLP 1930 1940 1950 1960 1970 1980 TAPGDYSIIV RFDDKHIPGS PFTAKITGDD SMRTSQLNVG TSTDVSLKIT ESDLSQLTAS 1990 2000 2010 2020 2030 2040 IRAPSGNEEP CLLKRLPNRH IGISFTPKEV GEHVVSVRKS GKHVTNSPFK ILVGPSEIGD 2050 2060 2070 2080 2090 2100 ASKVRVWGKG LSEGHTFQVA EFIVDTRNAG YGGLGLSIEG PSKVDINCED MEDGTCKVTY 2110 2120 2130 2140 2150 2160 CPTEPGTYII NIKFADKHVP GSPFTVKVTG EGRMKESITR RRQAPSIATI GSTCDLNLKI 2170 2180 2190 2200 2210 2220 PGNWFQMVSA QERLTRTFTR SSHTYTRTER TEISKTRGGE TKREVRVEES TQVGGDPFPA 2230 2240 2250 2260 2270 2280 VFGDFLGRER LGSFGSITRQ QEGEASSQDM TAQVTSPSGK VEAAEIVEGE DSAYSVRFVP 2290 2300 2310 2320 2330 2340 QEMGPHTVAV KYRGQHVPGS PFQFTVGPLG EGGAHKVRAG GTGLERGVAG VPAEFSIWTR 2350 2360 2370 2380 2390 2400 EAGAGGLSIA VEGPSKAEIA FEDRKDGSCG VSYVVQEPGD YEVSIKFNDE HIPDSPFVVP 2410 2420 2430 2440 2450 2460 VASLSDDARR LTVTSLQETG LKVNQPASFA VQLNGARGVI DARVHTPSGA VEECYVSELD 2470 2480 2490 2500 2510 2520 SDKHTIRFIP HENGVHSIDV KFNGAHIPGS PFKIRVGEQS QAGDPGLVSA YGPGLEGGTT 2530 2540 2550 2560 2570 2580 GVSSEFIVNT LNAGSGALSV TIDGPSKVQL DCRECPEGHV VTYTPMAPGN YLIAIKYGGP 2590 2600 2610 2620 2630 2640 QHIVGSPFKA KVTGPRLSGG HSLHETSTVL VETVTKSSSS RGSSYSSIPK FSSDASKVVT 2650 2660 2670 2680 2690 2700 RGPGLSQAFV GQKNSFTVDC SKAGTNMMMV GVHGPKTPCE EVYVKHMGNR VYNVTYTVKE 2710 2720 KGDYILIVKW GDESVPGSPF KVKVP
	Isoform 2 [UniParc]. Checksum: 7C07C97B4A882CF2	FASTA	2,692	287,281
	10 20 30 40 50 60 MMNNSGYSDA GLGLGDETDE MPSTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVGKRLTDL 70 80 90 100 110 120 QRDLSDGLRL IALLEVLSQK RMYRKFHPRP NFRQMKLENV SVALEFLERE HIKLVSIDSK 130 140 150 160 170 180 AIVDGNLKLI LGLIWTLILH YSISMPMWED EDDEDARKQT PKQRLLGWIQ NKVPQLPITN 190 200 210 220 230 240 FNRDWQDGKA LGALVDNCAP GLCPDWEAWD PNQPVENARE AMQQADDWLG VPQVIAPEEI 250 260 270 280 290 300 VDPNVDEHSV MTYLSQFPKA KLKPGAPVRS KQLNPKKAIA YGPGIEPQGN TVLQPAHFTV 310 320 330 340 350 360 QTVDAGVGEV LVYIEDPEGH TEEAKVVPNN DKDRTYAVSY VPKVAGLHKV TVLFAGQNIE 370 380 390 400 410 420 RSPFEVNVGM ALGDANKVSA RGPGLEPVGN VANKPTYFDI YTAGAGTGDV AVVIVDPQGR 430 440 450 460 470 480 RDTVEVALED KGDSTFRCTY RPAMEGPHTV HVAFAGAPIT RSPFPVHVSE ACNPNACRAS 490 500 510 520 530 540 GRGLQPKGVR VKEVADFKVF TKGAGSGELK VTVKGPKGTE EPVKVREAGD GVFECEYYPV 550 560 570 580 590 600 VPGKYVVTIT WGGYAIPRSP FEVQVSPEAG VQKVRAWGPG LETGQVGKSA DFVVEAIGTE 610 620 630 640 650 660 VGTLGFSIEG PSQAKIECDD KGDGSCDVRY WPTEPGEYAV HVICDDEDIR DSPFIAHILP 670 680 690 700 710 720 APPDCFPDKV KAFGPGLEPT GCIVDKPAEF TIDARAAGKG DLKLYAQDAD GCPIDIKVIP 730 740 750 760 770 780 NGDGTFRCSY VPTKPIKHTI IISWGGVNVP KSPFRVNVGE GSHPERVKVY GPGVEKTGLK 790 800 810 820 830 840 ANEPTYFTVD CSEAGQGDVS IGIKCAPGVV GPAEADIDFD IIKNDNDTFT VKYTPPGAGR 850 860 870 880 890 900 YTIMVLFANQ EIPASPFHIK VDPSHDASKV KAEGPGLNRT GVEVGKPTHF TVLTKGAGKA 910 920 930 940 950 960 KLDVQFAGTA KGEVVRDFEI IDNHDYSYTV KYTAVQQGNM AVTVTYGGDP VPKSPFVVNV 970 980 990 1000 1010 1020 APPLDLSKIK VQGLNSKVAV GQEQAFSVNT RGAGGQGQLD VRMTSPSRRP IPCKLEPGGG 1030 1040 1050 1060 1070 1080 AEAQAVRYMP PEEGPYKVDI TYDGHPVPGS PFAVEGVLPP DPSKVCAYGP GLKGGLVGTP 1090 1100 1110 1120 1130 1140 APFSIDTKGA GTGGLGLTVE GPCEAKIECQ DNGDGSCAVS YLPTEPGEYT INILFAEAHI 1150 1160 1170 1180 1190 1200 PGSPFKATIR PVFDPSKVRA SGPGLERGKV GEAATFTVDC SEAGEAELTI EILSDAGVKA 1210 1220 1230 1240 1250 1260 EVLIHNNADG TYHITYSPAF PGTYTITIKY GGHPVPKFPT RVHVQPAVDT SGVKVSGPGV 1270 1280 1290 1300 1310 1320 EPHGVLREVT TEFTVDARSL TATGGNHVTA RVLNPSGAKT DTYVTDNGDG TYRVQYTAYE 1330 1340 1350 1360 1370 1380 EGVHLVEVLY DEVAVPKSPF RVGVTEGCDP TRVRAFGPGL EGGLVNKANR FTVETRGAGT 1390 1400 1410 1420 1430 1440 GGLGLAIEGP SEAKMSCKDN KDGSCTVEYI PFTPGDYDVN ITFGGRPIPG SPFRVPVKDV 1450 1460 1470 1480 1490 1500 VDPGKVKCSG PGLGAGVRAR VPQTFTVDCS QAGRAPLQVA VLGPTGVAEP VEVRDNGDGT 1510 1520 1530 1540 1550 1560 HTVHYTPATD GPYTVAVKYA DQEVPRSPFK IKVLPAHDAS KVRASGPGLN ASGIPASLPV 1570 1580 1590 1600 1610 1620 EFTIDARDAG EGLLTVQILD PEGKPKKANI RDNGDGTYTV SYLPDMSGRY TITIKYGGDE 1630 1640 1650 1660 1670 1680 IPYSPFRIHA LPTGDASKCL VTVSIGGHGL GACLGPRIQI GQETVITVDA KAAGEGKVTC 1690 1700 1710 1720 1730 1740 TVSTPDGAEL DVDVVENHDG TFDIYYTAPE PGKYVITIRF GGEHIPNSPF HVLATEEPVV 1750 1760 1770 1780 1790 1800 PVEPMESMLR PFNLVIPFAV QKGELTGEVR MPSGKTARPN ITDNKDGTIT VRYAPTEKGL 1810 1820 1830 1840 1850 1860 HQMGIKYDGN HIPGSPLQFY VDAINSRHVS AYGPGLSHGM VNKPATFTIV TKDAGEGGLS 1870 1880 1890 1900 1910 1920 LAVEGPSKAE ITCKDNKDGT CTVSYLPTAP GDYSIIVRFD DKHIPGSPFT AKITGDDSMR 1930 1940 1950 1960 1970 1980 TSQLNVGTST DVSLKITESD LSQLTASIRA PSGNEEPCLL KRLPNRHIGI SFTPKEVGEH 1990 2000 2010 2020 2030 2040 VVSVRKSGKH VTNSPFKILV GPSEIGDASK VRVWGKGLSE GHTFQVAEFI VDTRNAGYGG 2050 2060 2070 2080 2090 2100 LGLSIEGPSK VDINCEDMED GTCKVTYCPT EPGTYIINIK FADKHVPGSP FTVKVTGEGR 2110 2120 2130 2140 2150 2160 MKESITRRRQ APSIATIGST CDLNLKIPGN WFQMVSAQER LTRTFTRSSH TYTRTERTEI 2170 2180 2190 2200 2210 2220 SKTRGGETKR EVRVEESTQV GGDPFPAVFG DFLGRERLGS FGSITRQQEG EASSQDMTAQ 2230 2240 2250 2260 2270 2280 VTSPSGKVEA AEIVEGEDSA YSVRFVPQEM GPHTVAVKYR GQHVPGSPFQ FTVGPLGEGG 2290 2300 2310 2320 2330 2340 AHKVRAGGTG LERGVAGVPA EFSIWTREAG AGGLSIAVEG PSKAEIAFED RKDGSCGVSY 2350 2360 2370 2380 2390 2400 VVQEPGDYEV SIKFNDEHIP DSPFVVPVAS LSDDARRLTV TSLQETGLKV NQPASFAVQL 2410 2420 2430 2440 2450 2460 NGARGVIDAR VHTPSGAVEE CYVSELDSDK HTIRFIPHEN GVHSIDVKFN GAHIPGSPFK 2470 2480 2490 2500 2510 2520 IRVGEQSQAG DPGLVSAYGP GLEGGTTGVS SEFIVNTLNA GSGALSVTID GPSKVQLDCR 2530 2540 2550 2560 2570 2580 ECPEGHVVTY TPMAPGNYLI AIKYGGPQHI VGSPFKAKVT GPRLSGGHSL HETSTVLVET 2590 2600 2610 2620 2630 2640 VTKSSSSRGS SYSSIPKFSS DASKVVTRGP GLSQAFVGQK NSFTVDCSKA GTNMMMVGVH 2650 2660 2670 2680 2690 GPKTPCEEVY VKHMGNRVYN VTYTVKEKGD YILIVKWGDE SVPGSPFKVK VP

References

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[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]	"Filamin 2 (FLN2): a muscle-specific sarcoglycan interacting protein." Thompson T.G., Chan Y.-M., Hack A.A., Brosius M., Rajala M., Lidov H.G.W., McNally E.M., Watkins S., Kunkel L.M. J. Cell Biol. 148:115-126(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SGCD AND SGCG. Tissue: Skeletal muscle.
[5]	Kato S. Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Bienvenut W.V., Pchelintsev N., Adams P.D. Submitted (OCT-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 70-81; 165-183; 335-343; 350-377; 422-437; 559-573; 576-588; 718-727; 880-895; 900-911; 917-968; 978-991; 1015-1027; 1074-1088; 1147-1157; 1242-1278; 1300-1313; 1355-1367; 1377-1394; 1475-1494; 1568-1586; 1616-1627; 1658-1671; 1714-1719; 1809-1825; 1840-1860; 1886-1901; 1932-1945; 1954-1968; 2000-2008; 2031-2043; 2050-2083; 2114-2127; 2231-2291; 2294-2316; 2327-2356; 2411-2437; 2577-2589; 2597-2616; 2642-2653 AND 2691-2699, PHOSPHORYLATION AT SER-2233, MASS SPECTROMETRY. Tissue: Lung fibroblast.
[9]	"Mapping of two genes encoding isoforms of the actin binding protein ABP-280, a dystrophin like protein, to Xq28 and to chromosome 7." Maestrini E., Patrosso C., Mancini M., Rivella S., Rocchi M., Repetto M., Villa A., Frattini A., Zoppe M., Vezzoni P., Toniolo D. Hum. Mol. Genet. 2:761-766(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 585-815 AND 1638-2101 (ISOFORM 2), TISSUE SPECIFICITY.
[10]	"FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle." Faulkner G., Pallavicini A., Comelli A., Salamon M., Bortoletto G., Ievolella C., Trevisan S., Kojic' S., Dalla Vecchia F., Laveder P., Valle G., Lanfranchi G. J. Biol. Chem. 275:41234-41242(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYOZ1.
[11]	"Indications for a novel muscular dystrophy pathway: gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin." van der Ven P.F.M., Wiesner S., Salmikangas P., Auerbach D., Himmel M., Kempa S., Hayess K., Pacholsky D., Taivainen A., Schroeder R., Carpen O., Fuerst D.O. J. Cell Biol. 151:235-248(2000) [PubMed] [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]	"Filamins as integrators of cell mechanics and signalling." Stossel T.P., Condeelis J., Cooley L., Hartwig J.H., Noegel A., Schleicher M., Shapiro S.S. Nat. Rev. Mol. Cell Biol. 2:138-145(2001) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[16]	"Identification of silencing of nine genes in human gastric cancers." Kaneda A., Kaminishi M., Yanagihara K., Sugimura T., Ushijima T. Cancer Res. 62:6645-6650(2002) [PubMed] [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]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161, MASS SPECTROMETRY. Tissue: Platelet.
[24]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2233, MASS SPECTROMETRY.
[25]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"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, MASS SPECTROMETRY.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"Mutations in the N-terminal actin-binding domain of filamin C cause a distal myopathy." Duff R.M., Tay V., Hackman P., Ravenscroft G., McLean C., Kennedy P., Steinbach A., Schoffler W., van der Ven P.F., Furst D.O., Song J., Djinovic-Carugo K., Penttila S., Raheem O., Reardon K., Malandrini A., Gambelli S., Villanova M. , Nowak K.J., Williams D.R., Landers J.E., Brown R.H. Jr., Udd B., Laing N.G. Am. J. Hum. Genet. 88:729-740(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPD4 THR-193 AND THR-251, CHARACTERIZATION OF VARIANTS MPD4 THR-193 AND THR-251.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00178352.
IPI00413958.

PIR

S37775.
S37778.

RefSeq

NP_001120959.1. NM_001127487.1.
NP_001449.3. NM_001458.4.

UniGene

Hs.58414.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2405-2500	[»]
2D7Q	NMR	-	A	2502-2599	[»]
2K9U	NMR	-	A	2302-2415	[»]
2NQC	X-ray	2.05	A	2495-2598	[»]

ProteinModelPortal

Q14315.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33398N.

IntAct

Q14315. 32 interactions.

MINT

MINT-5004555.

STRING

9606.ENSP00000327145.

PTM databases

PhosphoSite

Q14315.

Polymorphism databases

DMDM

254763419.

Proteomic databases

PaxDb

Q14315.

PRIDE

Q14315.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325888; ENSP00000327145; ENSG00000128591.
ENST00000346177; ENSP00000344002; ENSG00000128591.

GeneID

2318.

KEGG

hsa:2318.

UCSC

uc003vnz.4. human.
uc003voa.4. human.

Organism-specific databases

CTD

2318.

GeneCards

GC07P128470.

HGNC

HGNC:3756. FLNC.

HPA

HPA006135.

MIM

102565. gene.
609524. phenotype.
614065. phenotype.

neXtProt

NX_Q14315.

Orphanet

63273. Distal myopathy with posterior leg and anterior hand involvement.
171445. Muscle filaminopathy.

PharmGKB

PA28174.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5069.

HOVERGEN

HBG004163.

InParanoid

Q14315.

KO

K04437.

OMA

EPTGCIV.

OrthoDB

EOG4JWVCJ.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

Q14315.

Bgee

Q14315.

CleanEx

HS_FLNC.

Genevestigator

Q14315.

GermOnline

ENSG00000128591. Homo sapiens.

Family and domain databases

Gene3D

1.10.418.10. 2 hits.
2.60.40.10. 24 hits.

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR003961. Fibronectin_type3.
IPR001298. Filamin.
IPR017868. Filamin/ABP280_repeat-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]

Pfam

PF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]

SMART

SM00033. CH. 2 hits.
SM00060. FN3. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.
SSF81296. Ig_E-set. 24 hits.

PROSITE

PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q14315.

GenomeRNAi

2318.

NextBio

9413.

SOURCE

Search...

Entry information

Entry name

FLNC_HUMAN

Accession

Primary (citable) accession number: Q14315
Secondary accession number(s): B2ZZ88 , O95303, Q07985, Q9NS12, Q9NYE5, Q9UMR8, Q9Y503

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	July 28, 2009
Last modified:	May 1, 2013
This is version 145 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.