P21333 (FLNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Filamin-A
Short name=FLN-A

Alternative name(s):
Actin-binding protein 280
Short name=ABP-280
Alpha-filamin
Endothelial actin-binding protein
Filamin-1
Non-muscle filamin

Gene names

Name:	FLNA
Synonyms:	FLN, FLN1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2647 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking By similarity.
Subunit structure	Interacts with PDLIM2 By similarity. Homodimer. Interacts with FCGR1A, FLNB, FURIN, HSPB7, INPPL1, KCND2, MYOT, MYOZ1, ARHGAP24, PSEN1, PSEN2 and ECSCR. Interacts also with various other binding partners in addition to filamentous actin. Interacts (via N-terminus) with MIS18BP1 (via N-terminus). Interacts (via N-terminus) with TAF1B. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.23 Ref.30 Ref.31 Ref.40
Subcellular location	Cytoplasm › cell cortex. Cytoplasm › cytoskeleton.
Tissue specificity	Ubiquitous.
Domain	Comprised of a NH2-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. Phosphorylation extent changes in response to cell activation. Ref.16 Ref.19 Ref.20 Ref.22 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38
Involvement in disease	Defects in FLNA are the cause of periventricular nodular heterotopia type 1 (PVNH1) [MIM:300049]; also called nodular heterotopia, bilateral periventricular (NHBP or BPNH). PVNH is a developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant form. Heterozygous females have normal intelligence but suffer from seizures and various manifestations outside the central nervous system, especially related to the vascular system. Hemizygous affected males die in the prenatal or perinatal period. Ref.21 Ref.42 Ref.43 Ref.44 Ref.46 Defects in FLNA are the cause of periventricular nodular heterotopia type 4 (PVNH4) [MIM:300537]; also known as periventricular heterotopia Ehlers-Danlos variant. PVNH4 is characterized by nodular brain heterotopia, joint hypermobility and development of aortic dilation in early adulthood. Defects in FLNA are the cause of otopalatodigital syndrome type 1 (OPD1) [MIM:311300]. OPD1 is an X-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild mental retardation, hearing loss, cleft palate, and typical facial anomalies. OPD1 belongs to a group of X-linked skeletal dysplasias known as oto-palato-digital syndrome spectrum disorders that also include OPD2, Melnick-Needles syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. FLNA is a widely expressed protein that regulates re-organization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes and second messengers. Males with OPD1 have cleft palate, malformations of the ossicles causing deafness and milder bone and limb defects than those associated with OPD2. Obligate female carriers of mutations causing both OPD1 and OPD2 have variable (often milder) expression of a similar phenotypic spectrum. Ref.45 Ref.48 Defects in FLNA are the cause of otopalatodigital syndrome type 2 (OPD2) [MIM:304120]; also known as cranioorodigital syndrome. OPD2 is a congenital bone disorder that is characterized by abnormally modeled, bowed bones, small or absent first digits and, more variably, cleft palate, posterior fossa brain anomalies, omphalocele and cardiac defects. Defects in FLNA are the cause of frontometaphyseal dysplasia (FMD) [MIM:305620]. FMD is a congenital bone disease characterized by supraorbital hyperostosis, deafness and digital anomalies. Ref.45 Ref.50 Defects in FLNA are the cause of Melnick-Needles syndrome (MNS) [MIM:309350]. MNS is a severe congenital bone disorder characterized by typical facies (exophthalmos, full cheeks, micrognathia and malalignment of teeth), flaring of the metaphyses of long bones, s-like curvature of bones of legs, irregular constrictions in the ribs, and sclerosis of base of skull. Ref.45 Defects in FLNA are the cause of X-linked congenital idiopathic intestinal pseudoobstruction (CIIPX) [MIM:300048]. CIIPX is characterized by a severe abnormality of gastrointestinal motility due to primary qualitative defects of enteric ganglia and nerve fibers. Affected individuals manifest recurrent signs of intestinal obstruction in the absence of any mechanical lesion. Ref.25 Defects in FLNA are the cause of FG syndrome type 2 (FGS2) [MIM:300321]. FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation. Ref.53 Defects in FLNA are the cause of terminal osseous dysplasia (TOD) [MIM:300244]. A rare X-linked dominant male-lethal disease characterized by skeletal dysplasia of the limbs, pigmentary defects of the skin and recurrent digital fibroma during infancy. A significant phenotypic variability is observed in affected females. Ref.55 Defects in FLNA are the cause of cardiac valvular dysplasia X-linked (CVDX) [MIM:314400]. A rare X-linked heart disease characterized by mitral and/or aortic valve regurgitation. The histologic features include fragmentation of collagenous bundles within the valve fibrosa and accumulation of proteoglycans, which produces excessive valve tissue leading to billowing of the valve leaflets. Ref.54
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 BAC03408.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	actin crosslink formation Inferred from direct assay. Source: BHF-UCL actin cytoskeleton reorganization Inferred from direct assay. Source: BHF-UCL cell junction assembly Traceable author statement. Source: Reactome cytoplasmic sequestering of protein Inferred from mutant phenotype. Source: BHF-UCL establishment of protein localization Inferred from direct assay Ref.31. Source: BHF-UCL inhibition of adenylate cyclase activity by dopamine receptor signaling pathway Inferred from mutant phenotype. Source: BHF-UCL negative regulation of protein catabolic process Inferred from mutant phenotype Ref.31. Source: BHF-UCL negative regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype. Source: UniProtKB positive regulation of transcription factor import into nucleus Inferred from mutant phenotype. Source: UniProtKB protein localization at cell surface Inferred from direct assay Ref.31. Source: BHF-UCL protein stabilization Inferred from mutant phenotype Ref.31. Source: BHF-UCL receptor clustering Inferred from direct assay. Source: BHF-UCL
Cellular component	actin cytoskeleton Inferred by curator Ref.1. Source: BHF-UCL cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay Ref.31. Source: BHF-UCL
Molecular function	Fc-gamma receptor I complex binding Inferred from direct assay. Source: BHF-UCL GTP-Ral binding Inferred from direct assay. Source: BHF-UCL Rac GTPase binding Inferred from direct assay. Source: BHF-UCL actin filament binding Inferred from direct assay Ref.1. Source: BHF-UCL glycoprotein binding Inferred from direct assay. Source: BHF-UCL protein homodimerization activity Inferred from direct assay Ref.1. Source: BHF-UCL signal transducer activity Inferred from mutant phenotype. Source: UniProtKB transcription factor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARHGAP24	Q8N264	6	EBI-350432,EBI-988764
CRK	P46108	2	EBI-350432,EBI-886
FLNB	O75369	5	EBI-350432,EBI-352089
GRB2	P62993	2	EBI-350432,EBI-401755

Alternative products

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

Isoform 1 (identifier: P21333-1)

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: P21333-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1649-1656: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 2647

2646

Filamin-A

PRO_0000087296

Regions

Domain

2 – 274

273

Actin-binding

Domain

43 – 149

107

CH 1

Domain

166 – 266

101

CH 2

Repeat

276 – 374

99

Filamin 1

Repeat

376 – 474

99

Filamin 2

Repeat

475 – 570

96

Filamin 3

Repeat

571 – 663

93

Filamin 4

Repeat

667 – 763

97

Filamin 5

Repeat

764 – 866

103

Filamin 6

Repeat

867 – 965

99

Filamin 7

Repeat

966 – 1061

96

Filamin 8

Repeat

1062 – 1154

93

Filamin 9

Repeat

1155 – 1249

95

Filamin 10

Repeat

1250 – 1349

100

Filamin 11

Repeat

1350 – 1442

93

Filamin 12

Repeat

1443 – 1539

97

Filamin 13

Repeat

1540 – 1636

97

Filamin 14

Repeat

1649 – 1740

92

Filamin 15

Repeat

1779 – 1860

82

Filamin 16

Repeat

1861 – 1950

90

Filamin 17

Repeat

1951 – 2039

89

Filamin 18

Repeat

2042 – 2131

90

Filamin 19

Repeat

2132 – 2230

99

Filamin 20

Repeat

2233 – 2325

93

Filamin 21

Repeat

2327 – 2420

94

Filamin 22

Repeat

2424 – 2516

93

Filamin 23

Repeat

2552 – 2646

95

Filamin 24

Region

1490 – 1607

118

Interaction with furin By similarity

Region

1741 – 1778

38

Hinge 1

Region

2517 – 2647

131

Self-association site, tail

Region

2517 – 2551

35

Hinge 2

Sites

Site

1761 – 1762

2

Cleavage; by calpain

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.7

Modified residue

373

1

Phosphotyrosine Ref.26

Modified residue

504

1

N6-acetyllysine Ref.39

Modified residue

508

1

N6-acetyllysine Ref.39

Modified residue

700

1

N6-acetyllysine Ref.39

Modified residue

781

1

N6-acetyllysine Ref.39

Modified residue

837

1

N6-acetyllysine Ref.39

Modified residue

891

1

N6-acetyllysine Ref.39

Modified residue

994

1

N6-acetyllysine Ref.39

Modified residue

1047

1

Phosphotyrosine Ref.16

Modified residue

1081

1

Phosphoserine Ref.35

Modified residue

1084

1

Phosphoserine Ref.19 Ref.22 Ref.24 Ref.27 Ref.28 Ref.29 Ref.32 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38

Modified residue

1089

1

Phosphothreonine Ref.20

Modified residue

1286

1

Phosphothreonine By similarity

Modified residue

1338

1

Phosphoserine Ref.36

Modified residue

1459

1

Phosphoserine Ref.19 Ref.20 Ref.22 Ref.29 Ref.32 Ref.34 Ref.35 Ref.36

Modified residue

1533

1

Phosphoserine Ref.20 Ref.36

Modified residue

1538

1

N6-acetyllysine Ref.39

Modified residue

1604

1

Phosphotyrosine Ref.26

Modified residue

1630

1

Phosphoserine Ref.36

Modified residue

2053

1

Phosphoserine Ref.36

Modified residue

2152

1

Phosphoserine Ref.20 Ref.29 Ref.32 Ref.36 Ref.38

Modified residue

2158

1

Phosphoserine Ref.32

Modified residue

2284

1

Phosphoserine Ref.20

Modified residue

2327

1

Phosphoserine Ref.20 Ref.36

Modified residue

2388

1

Phosphotyrosine Ref.26

Modified residue

2414

1

Phosphoserine Ref.36

Modified residue

2510

1

Phosphoserine Ref.36

Modified residue

2607

1

N6-acetyllysine Ref.39

Modified residue

2621

1

N6-acetyllysine Ref.39

Natural variations

Alternative sequence

1649 – 1656

8

Missing in isoform 2.

VSP_035454

Natural variant

39

1

A → G in PVNH4. Ref.49

VAR_022734

Natural variant

82

1

E → V in PVNH1. Ref.44
Corresponds to variant rs28935169 [ dbSNP | Ensembl ].

VAR_015699

Natural variant

102

1

M → V in PVNH1. Ref.46

VAR_031305

Natural variant

128

1

A → V in PVNH4. Ref.51

VAR_031306

Natural variant

149

1

S → F in PVNH1. Ref.46

VAR_031307

Natural variant

170

1

Q → P in OPD2. Ref.45

VAR_015713

Natural variant

172

1

L → F in OPD1. Ref.45

VAR_015714

Natural variant

196

1

R → G in OPD2. Ref.45

VAR_015715

Natural variant

196

1

R → W in OPD1. Ref.45

VAR_015716

Natural variant

200

1

A → S in OPD2. Ref.45

VAR_015717

Natural variant

203

1

D → Y in OPD1. Ref.48

VAR_031308

Natural variant

207

1

P → L in OPD1. Ref.45
Corresponds to variant rs28935469 [ dbSNP | Ensembl ].

VAR_015700

Natural variant

210

1

C → F in OPD2. Ref.52

VAR_058720

Natural variant

254

1

E → K in OPD2. Ref.45
Corresponds to variant rs28935470 [ dbSNP | Ensembl ].

VAR_015701

Natural variant

273

1

A → P in OPD2. Ref.45

VAR_015718

Natural variant

288

1

G → R in CVDX. Ref.54

VAR_064156

Natural variant

320

1

V → A.
Corresponds to variant rs1064816 [ dbSNP | Ensembl ].

VAR_012831

Natural variant

370

1

F → L.
Corresponds to variant rs1064817 [ dbSNP | Ensembl ].

VAR_012832

Natural variant

528

1

V → M in PVNH1. Ref.43

VAR_031309

Natural variant

552

1

V → A.
Corresponds to variant rs730319 [ dbSNP | Ensembl ].

VAR_012833

Natural variant

555

1

T → K in OPD2. Ref.45

VAR_015719

Natural variant

637

1

P → Q in CVDX. Ref.54

VAR_064157

Natural variant

656

1

L → F in PVNH1. Ref.42

VAR_012834

Natural variant

711

1

V → D in CVDX. Ref.54

VAR_064158

Natural variant

1012

1

S → L.
Corresponds to variant rs17091204 [ dbSNP | Ensembl ].

VAR_031310

Natural variant

1159

1

D → A in FMD; does not inhibit interaction with MIS18BP1. Ref.40 Ref.45
Corresponds to variant rs28935471 [ dbSNP | Ensembl ].

VAR_015702

Natural variant

1184

1

D → E in MNS. Ref.45

VAR_015720

Natural variant

1186

1

S → L in FMD. Ref.45 Ref.50

VAR_015721

Natural variant

1188

1

A → T in MNS; does not inhibit interaction with MIS18BP1. Ref.40 Ref.45
Corresponds to variant rs28935472 [ dbSNP | Ensembl ].

VAR_015703

Natural variant

1199

1

S → L in MNS; does not inhibit interaction with MIS18BP1. Ref.40 Ref.45
Corresponds to variant rs28935473 [ dbSNP | Ensembl ].

VAR_015704

Natural variant

1291

1

P → L in FGS2. Ref.53

VAR_058721

Natural variant

1419

1

A → G.
Corresponds to variant rs35504556 [ dbSNP | Ensembl ].

VAR_032083

Natural variant

1620

1

Missing in FMD.

VAR_015722

Natural variant

1635 – 1637

3

Missing in otopalatodigital spectrum disorder.

VAR_031311

Natural variant

1645

1

C → F in OPD2. Ref.45

VAR_015723

Natural variant

1724 – 1739

16

Missing in TOD.

VAR_064159

Natural variant

1728

1

G → C in FMD. Ref.50

VAR_031312

Natural variant

1764

1

A → T in PVNH1. Ref.42
Corresponds to variant rs57108893 [ dbSNP | Ensembl ].

VAR_012835

Experimental info

Sequence conflict

44

1

I → T AA sequence Ref.8

Sequence conflict

1772

1

A → G in CAA49687. Ref.9

Sequence conflict

2341

1

Q → R in BAC03408. Ref.4

Sequence conflict

2634

1

D → H in CAA37495. Ref.2

Secondary structure

1

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2647

Helix Strand Turn

Details...

Beta strand

1869 – 1872

4

Helix

1873 – 1875

3

Beta strand

1877 – 1879

3

Beta strand

1884 – 1889

6

Beta strand

1895 – 1906

12

Beta strand

1909 – 1914

6

Beta strand

1916 – 1925

10

Beta strand

1930 – 1938

9

Beta strand

1947 – 1953

7

Helix

2047 – 2049

3

Beta strand

2051 – 2054

4

Helix

2055 – 2057

3

Beta strand

2059 – 2061

3

Beta strand

2066 – 2071

6

Beta strand

2075 – 2077

3

Beta strand

2080 – 2088

9

Beta strand

2091 – 2096

6

Beta strand

2100 – 2107

8

Beta strand

2112 – 2120

9

Beta strand

2129 – 2136

8

Beta strand

2139 – 2148

10

Beta strand

2174 – 2179

6

Beta strand

2185 – 2189

5

Beta strand

2208 – 2216

9

Beta strand

2225 – 2231

7

Helix

2238 – 2240

3

Beta strand

2242 – 2245

4

Helix

2246 – 2248

3

Beta strand

2257 – 2262

6

Beta strand

2268 – 2279

12

Beta strand

2281 – 2286

6

Beta strand

2291 – 2301

11

Beta strand

2303 – 2311

9

Beta strand

2320 – 2326

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 6C1A07041DF50142	FASTA	2,647	280,739
	10 20 30 40 50 60 MSSSHSRAGQ SAAGAAPGGG VDTRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV 70 80 90 100 110 120 SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK 130 140 150 160 170 180 LVSIDSKAIV DGNLKLILGL IWTLILHYSI SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL 190 200 210 220 230 240 PQLPITNFSR DWQSGRALGA LVDSCAPGLC PDWDSWDASK PVTNAREAMQ QADDWLGIPQ 250 260 270 280 290 300 VITPEEIVDP NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK 310 320 330 340 350 360 RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV TGTHKVTVLF 370 380 390 400 410 420 AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK TTYFEIFTAG AGTGEVEVVI 430 440 450 460 470 480 QDPMGQKGTV EPQLEARGDS TYRCSYQPTM EGVHTVHVTF AGVPIPRSPY TVTVGQACNP 490 500 510 520 530 540 SACRAVGRGL QPKGVRVKET ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF 550 560 570 580 590 600 EYYPMVPGTY IVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGV VGKSADFVVE 610 620 630 640 650 660 AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN SEDIRLSPFM 670 680 690 700 710 720 ADIRDAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK HGGKAPLRVQ VQDNEGCPVE 730 740 750 760 770 780 ALVKDNGNGT YSCSYVPRKP VKHTAMVSWG GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA 790 800 810 820 830 840 KTGLKAHEPT YFTVDCAEAG QGDVSIGIKC APGVVGPAEA DIDFDIIRND NDTFTVKYTP 850 860 870 880 890 900 RGAGSYTIMV LFADQATPTS PIRVKVEPSH DASKVKAEGP GLSRTGVELG KPTHFTVNAK 910 920 930 940 950 960 AAGKGKLDVQ FSGLTKGDAV RDVDIIDHHD NTYTVKYTPV QQGPVGVNVT YGGDPIPKSP 970 980 990 1000 1010 1020 FSVAVSPSLD LSKIKVSGLG EKVDVGKDQE FTVKSKGAGG QGKVASKIVG PSGAAVPCKV 1030 1040 1050 1060 1070 1080 EPGLGADNSV VRFLPREEGP YEVEVTYDGV PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG 1090 1100 1110 1120 1130 1140 SAGSPARFTI DTKGAGTGGL GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF 1150 1160 1170 1180 1190 1200 ADTHIPGSPF KAHVVPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE 1210 1220 1230 1240 1250 1260 AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE PAVDTSGVQC 1270 1280 1290 1300 1310 1320 YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP SGNLTETYVQ DRGDGMYKVE 1330 1340 1350 1360 1370 1380 YTPYEEGLHS VDVTYDGSPV PSSPFQVPVT EGCDPSRVRV HGPGIQSGTT NKPNKFTVET 1390 1400 1410 1420 1430 1440 RGAGTGGLGL AVEGPSEAKM SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV 1450 1460 1470 1480 1490 1500 PVHDVTDASK VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV 1510 1520 1530 1540 1550 1560 DNADGTQTVN YVPSREGPYS ISVLYGDEEV PRSPFKVKVL PTHDASKVKA SGPGLNTTGV 1570 1580 1590 1600 1610 1620 PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH DGTYTVAYVP DVTGRYTILI 1630 1640 1650 1660 1670 1680 KYGGDEIPFS PYRVRAVPTG DASKCTVTVS IGGHGLGAGI GPTIQIGEET VITVDTKAAG 1690 1700 1710 1720 1730 1740 KGKVTCTVCT PDGSEVDVDV VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA 1750 1760 1770 1780 1790 1800 LAGDQPSVQP PLRSQQLAPQ YTYAQGGQQT WAPERPLVGV NGLDVTSLRP FDLVIPFTIK 1810 1820 1830 1840 1850 1860 KGEITGEVRM PSGKVAQPTI TDNKDGTVTV RYAPSEAGLH EMDIRYDNMH IPGSPLQFYV 1870 1880 1890 1900 1910 1920 DYVNCGHVTA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL AIEGPSKAEI SCTDNQDGTC 1930 1940 1950 1960 1970 1980 SVSYLPVLPG DYSILVKYNE QHVPGSPFTA RVTGDDSMRM SHLKVGSAAD IPINISETDL 1990 2000 2010 2020 2030 2040 SLLTATVVPP SGREEPCLLK RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS 2050 2060 2070 2080 2090 2100 QSEIGDASRV RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG 2110 2120 2130 2140 2150 2160 TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA PSVANVGSHC 2170 2180 2190 2200 2210 2220 DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI RFVPAEMGTH TVSVKYKGQH 2230 2240 2250 2260 2270 2280 VPGSPFQFTV GPLGEGGAHK VRAGGPGLER AEAGVPAEFS IWTREAGAGG LAIAVEGPSK 2290 2300 2310 2320 2330 2340 AEISFEDRKD GSCGVAYVVQ EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL 2350 2360 2370 2380 2390 2400 QESGLKVNQP ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGVY 2410 2420 2430 2440 2450 2460 LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGNPAEF VVNTSNAGAG 2470 2480 2490 2500 2510 2520 ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK YGGPYHIGGS PFKAKVTGPR 2530 2540 2550 2560 2570 2580 LVSNHSLHET SSVFVDSLTK ATCAPQHGAP GPGPADASKV VAKGLGLSKA YVGQKSSFTV 2590 2600 2610 2620 2630 2640 DCSKAGNNML LVGVHGPRTP CEEILVKHVG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS PYRVVVP
	Isoform 2 [UniParc]. Checksum: 862625C6FEA39075	FASTA	2,639	280,018
	10 20 30 40 50 60 MSSSHSRAGQ SAAGAAPGGG VDTRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV 70 80 90 100 110 120 SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK 130 140 150 160 170 180 LVSIDSKAIV DGNLKLILGL IWTLILHYSI SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL 190 200 210 220 230 240 PQLPITNFSR DWQSGRALGA LVDSCAPGLC PDWDSWDASK PVTNAREAMQ QADDWLGIPQ 250 260 270 280 290 300 VITPEEIVDP NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK 310 320 330 340 350 360 RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV TGTHKVTVLF 370 380 390 400 410 420 AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK TTYFEIFTAG AGTGEVEVVI 430 440 450 460 470 480 QDPMGQKGTV EPQLEARGDS TYRCSYQPTM EGVHTVHVTF AGVPIPRSPY TVTVGQACNP 490 500 510 520 530 540 SACRAVGRGL QPKGVRVKET ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF 550 560 570 580 590 600 EYYPMVPGTY IVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGV VGKSADFVVE 610 620 630 640 650 660 AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN SEDIRLSPFM 670 680 690 700 710 720 ADIRDAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK HGGKAPLRVQ VQDNEGCPVE 730 740 750 760 770 780 ALVKDNGNGT YSCSYVPRKP VKHTAMVSWG GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA 790 800 810 820 830 840 KTGLKAHEPT YFTVDCAEAG QGDVSIGIKC APGVVGPAEA DIDFDIIRND NDTFTVKYTP 850 860 870 880 890 900 RGAGSYTIMV LFADQATPTS PIRVKVEPSH DASKVKAEGP GLSRTGVELG KPTHFTVNAK 910 920 930 940 950 960 AAGKGKLDVQ FSGLTKGDAV RDVDIIDHHD NTYTVKYTPV QQGPVGVNVT YGGDPIPKSP 970 980 990 1000 1010 1020 FSVAVSPSLD LSKIKVSGLG EKVDVGKDQE FTVKSKGAGG QGKVASKIVG PSGAAVPCKV 1030 1040 1050 1060 1070 1080 EPGLGADNSV VRFLPREEGP YEVEVTYDGV PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG 1090 1100 1110 1120 1130 1140 SAGSPARFTI DTKGAGTGGL GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF 1150 1160 1170 1180 1190 1200 ADTHIPGSPF KAHVVPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE 1210 1220 1230 1240 1250 1260 AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE PAVDTSGVQC 1270 1280 1290 1300 1310 1320 YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP SGNLTETYVQ DRGDGMYKVE 1330 1340 1350 1360 1370 1380 YTPYEEGLHS VDVTYDGSPV PSSPFQVPVT EGCDPSRVRV HGPGIQSGTT NKPNKFTVET 1390 1400 1410 1420 1430 1440 RGAGTGGLGL AVEGPSEAKM SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV 1450 1460 1470 1480 1490 1500 PVHDVTDASK VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV 1510 1520 1530 1540 1550 1560 DNADGTQTVN YVPSREGPYS ISVLYGDEEV PRSPFKVKVL PTHDASKVKA SGPGLNTTGV 1570 1580 1590 1600 1610 1620 PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH DGTYTVAYVP DVTGRYTILI 1630 1640 1650 1660 1670 1680 KYGGDEIPFS PYRVRAVPTG DASKCTVTGA GIGPTIQIGE ETVITVDTKA AGKGKVTCTV 1690 1700 1710 1720 1730 1740 CTPDGSEVDV DVVENEDGTF DIFYTAPQPG KYVICVRFGG EHVPNSPFQV TALAGDQPSV 1750 1760 1770 1780 1790 1800 QPPLRSQQLA PQYTYAQGGQ QTWAPERPLV GVNGLDVTSL RPFDLVIPFT IKKGEITGEV 1810 1820 1830 1840 1850 1860 RMPSGKVAQP TITDNKDGTV TVRYAPSEAG LHEMDIRYDN MHIPGSPLQF YVDYVNCGHV 1870 1880 1890 1900 1910 1920 TAYGPGLTHG VVNKPATFTV NTKDAGEGGL SLAIEGPSKA EISCTDNQDG TCSVSYLPVL 1930 1940 1950 1960 1970 1980 PGDYSILVKY NEQHVPGSPF TARVTGDDSM RMSHLKVGSA ADIPINISET DLSLLTATVV 1990 2000 2010 2020 2030 2040 PPSGREEPCL LKRLRNGHVG ISFVPKETGE HLVHVKKNGQ HVASSPIPVV ISQSEIGDAS 2050 2060 2070 2080 2090 2100 RVRVSGQGLH EGHTFEPAEF IIDTRDAGYG GLSLSIEGPS KVDINTEDLE DGTCRVTYCP 2110 2120 2130 2140 2150 2160 TEPGNYIINI KFADQHVPGS PFSVKVTGEG RVKESITRRR RAPSVANVGS HCDLSLKIPE 2170 2180 2190 2200 2210 2220 ISIQDMTAQV TSPSGKTHEA EIVEGENHTY CIRFVPAEMG THTVSVKYKG QHVPGSPFQF 2230 2240 2250 2260 2270 2280 TVGPLGEGGA HKVRAGGPGL ERAEAGVPAE FSIWTREAGA GGLAIAVEGP SKAEISFEDR 2290 2300 2310 2320 2330 2340 KDGSCGVAYV VQEPGDYEVS VKFNEEHIPD SPFVVPVASP SGDARRLTVS SLQESGLKVN 2350 2360 2370 2380 2390 2400 QPASFAVSLN GAKGAIDAKV HSPSGALEEC YVTEIDQDKY AVRFIPRENG VYLIDVKFNG 2410 2420 2430 2440 2450 2460 THIPGSPFKI RVGEPGHGGD PGLVSAYGAG LEGGVTGNPA EFVVNTSNAG AGALSVTIDG 2470 2480 2490 2500 2510 2520 PSKVKMDCQE CPEGYRVTYT PMAPGSYLIS IKYGGPYHIG GSPFKAKVTG PRLVSNHSLH 2530 2540 2550 2560 2570 2580 ETSSVFVDSL TKATCAPQHG APGPGPADAS KVVAKGLGLS KAYVGQKSSF TVDCSKAGNN 2590 2600 2610 2620 2630 MLLVGVHGPR TPCEEILVKH VGSRLYSVSY LLKDKGEYTL VVKWGDEHIP GSPYRVVVP

References

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[1]	"Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring." Gorlin J.B., Yamin R., Egan S., Stewart M., Stossel T.P., Kwiatkowski D.J., Hartwig J.H. J. Cell Biol. 111:1089-1105(1990) [PubMed: 2391361] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]	"The exon-intron organization of the human X-linked gene (FLN1) encoding actin-binding protein 280." Patrosso M.C., Repetto M., Villa A., Milanesi L., Frattini A., Faranda S., Mancini M., Maestrini E., Toniolo D., Vezzoni P. Genomics 21:71-76(1994) [PubMed: 8088819] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci." Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M. Hum. Mol. Genet. 5:659-668(1996) [PubMed: 8733135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Spleen.
[5]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Bienvenut W.V., Claeys D. Submitted (NOV-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-24; 44-51; 64-87; 101-127; 172-190; 300-376; 384-400; 428-437; 497-504; 581-593; 656-664; 685-700; 761-771; 774-781; 829-837; 842-900; 907-916; 959-973; 983-994; 1020-1032; 1165-1172; 1235-1294; 1297-1312; 1360-1399; 1440-1450; 1465-1486; 1492-1532; 1539-1547; 1550-1592; 1622-1633; 1636-1644; 1726-1753; 1801-1809; 1815-1831; 1892-1907; 1965-1993; 2015-2024; 2026-2049; 2202-2215; 2243-2250; 2265-2289; 2311-2333; 2335-2361; 2396-2405; 2521-2540; 2585-2598 AND 2613-2631, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Platelet.
[8]	"Purification of human smooth muscle filamin and characterization of structural domains and functional sites." Hock R.S., Davis G., Speicher D.W. Biochemistry 29:9441-9451(1990) [PubMed: 2248958] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-54; 917-940; 1037-1050; 1754-1783 AND 2148-2168.
[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: 7689010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1658-1772.
[10]	"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: 11153914] [Abstract] Cited for: SIMILARITY TO OTHER MEMBERS OF THE FAMILY.
[11]	"Interaction of presenilins with the filamin family of actin-binding proteins." Zhang W., Han S.W., McKeel D.W., Goate A., Wu J.Y. J. Neurosci. 18:914-922(1998) [PubMed: 9437013] [Abstract] Cited for: INTERACTION WITH PSEN1 AND PSEN2.
[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: 11102480] [Abstract] Cited for: INTERACTION WITH KCND2.
[13]	"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: 11739414] [Abstract] Cited for: INTERACTION WITH INPPL1.
[14]	"Filamin A and filamin B are co-expressed within neurons during periods of neuronal migration and can physically interact." Sheen V.L., Feng Y., Graham D., Takafuta T., Shapiro S.S., Walsh C.A. Hum. Mol. Genet. 11:2845-2854(2002) [PubMed: 12393796] [Abstract] Cited for: INTERACTION WITH FLNB.
[15]	"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: 16076904] [Abstract] Cited for: INTERACTION WITH MYOT AND MYOZ1.
[16]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1047, MASS SPECTROMETRY.
[17]	"Structural and functional aspects of filamins." van der Flier A., Sonnenberg A. Biochim. Biophys. Acta 1538:99-117(2001) [PubMed: 11336782] [Abstract] Cited for: REVIEW.
[18]	"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: 11252955] [Abstract] Cited for: REVIEW.
[19]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084 AND SER-1459, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1089; SER-1459; SER-1533; SER-2152; SER-2284 AND SER-2327, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"A filamin A splice mutation resulting in a syndrome of facial dysmorphism, periventricular nodular heterotopia, and severe constipation reminiscent of cerebro-fronto-facial syndrome." Hehr U., Hehr A., Uyanik G., Phelan E., Winkler J., Reardon W. J. Med. Genet. 43:541-544(2006) [PubMed: 16299064] [Abstract] Cited for: INVOLVEMENT IN PVNH1.
[22]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084 AND SER-1459, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling." Ohta Y., Hartwig J.H., Stossel T.P. Nat. Cell Biol. 8:803-814(2006) [PubMed: 16862148] [Abstract] Cited for: INTERACTION WITH ARHGAP24.
[24]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[25]	"Filamin A is mutated in X-linked chronic idiopathic intestinal pseudo-obstruction with central nervous system involvement." Gargiulo A., Auricchio R., Barone M.V., Cotugno G., Reardon W., Milla P.J., Ballabio A., Ciccodicola A., Auricchio A. Am. J. Hum. Genet. 80:751-758(2007) [PubMed: 17357080] [Abstract] Cited for: INVOLVEMENT IN CIIPX.
[26]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-373; TYR-1604 AND TYR-2388, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[27]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1459 AND SER-2152, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"ECSM2, an endothelial specific filamin a binding protein that mediates chemotaxis." Armstrong L.-J., Heath V.L., Sanderson S., Kaur S., Beesley J.F.J., Herbert J.M.J., Legg J.A., Poulsom R., Bicknell R. Arterioscler. Thromb. Vasc. Biol. 28:1640-1646(2008) [PubMed: 18556573] [Abstract] Cited for: INTERACTION WITH ECSCR.
[31]	"Filamin A stabilizes FcgammaRI surface expression and prevents its lysosomal routing." Beekman J.M., van der Poel C.E., van der Linden J.A., van den Berg D.L.C., van den Berghe P.V.E., van de Winkel J.G.J., Leusen J.H.W. J. Immunol. 180:3938-3945(2008) [PubMed: 18322202] [Abstract] Cited for: INTERACTION WITH FCGR1A.
[32]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1459; SER-2152 AND SER-2158, MASS SPECTROMETRY. Tissue: Platelet.
[33]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[34]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, MASS SPECTROMETRY. Tissue: T-cell.
[35]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081; SER-1084 AND SER-1459, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1338; SER-1459; SER-1533; SER-1630; SER-2053; SER-2152; SER-2327; SER-2414 AND SER-2510, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[37]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[38]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084 AND SER-2152, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[39]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-504; LYS-508; LYS-700; LYS-781; LYS-837; LYS-891; LYS-994; LYS-1538; LYS-2607 AND LYS-2621, MASS SPECTROMETRY.
[40]	"Identification of novel nuclear protein interactions with the N-terminal part of filamin A." Qiu H., Nomiyama R., Moriguchi K., Fukada T., Sugimoto K. Biosci. Biotechnol. Biochem. 75:145-147(2011) [PubMed: 21228480] [Abstract] Cited for: INTERACTION WITH TAF1B AND MIS18BP1, CHARACTERIZATION OF VARIANTS ALA-1159; THR-1188 AND LEU-1199.
[41]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]	"Mutations in the X-linked filamin 1 gene cause periventricular nodular heterotopia in males as well as in females." Sheen V.L., Dixon P.H., Fox J.W., Hong S.E., Kinton L., Sisodiya S.M., Duncan J.S., Dubeau F., Scheffer I.E., Schachter S.C., Wilner A., Henchy R., Crino P., Kamuro K., DiMario F., Berg M., Kuzniecky R., Cole A.J. , Bromfield E., Biber M., Schomer D., Wheless J., Silver K., Mochida G.H., Berkovic S.F., Andermann F., Andermann E., Dobyns W.B., Wood N.W., Walsh C.A. Hum. Mol. Genet. 10:1775-1783(2001) [PubMed: 11532987] [Abstract] Cited for: VARIANTS PVNH1 PHE-656 AND THR-1764.
[43]	"Bilateral periventricular nodular heterotopia due to filamin 1 gene mutation: widespread glomeruloid microvascular anomaly and dysplastic cytoarchitecture in the cerebral cortex." Kakita A., Hayashi S., Moro F., Guerrini R., Ozawa T., Ono K., Kameyama S., Walsh C.A., Takahashi H. Acta Neuropathol. 104:649-657(2002) [PubMed: 12410386] [Abstract] Cited for: VARIANT PVNH1 MET-528.
[44]	"Familial periventricular heterotopia: missense and distal truncating mutations of the FLN1 gene." Moro F., Carrozzo R., Veggiotti P., Tortorella G., Toniolo D., Volzone A., Guerrini R. Neurology 58:916-921(2002) [PubMed: 11914408] [Abstract] Cited for: VARIANT PVNH1 VAL-82.
[45]	"Localized mutations in the gene encoding the cytoskeletal protein filamin A cause diverse malformations in humans." Robertson S.P., Twigg S.R.F., Sutherland-Smith A.J., Biancalana V., Gorlin R.J., Horn D., Kenwrick S.J., Kim C.A., Morava E., Newbury-Ecob R., Oerstavik K.H., Quarrell O.W.J., Schwartz C.E., Shears D.J., Suri M., Kendrick-Jones J., Wilkie A.O.M. Nat. Genet. 33:487-491(2003) [PubMed: 12612583] [Abstract] Cited for: VARIANTS OPD1 PHE-172; TRP-196 AND LEU-207, VARIANTS OPD2 PRO-170; GLY-196; SER-200; LYS-254; PRO-273; LYS-555 AND PHE-1645, VARIANTS FMD ALA-1159; LEU-1186 AND ILE-1620 DEL, VARIANTS MNS GLU-1184; THR-1188 AND LEU-1199.
[46]	"Germline and mosaic mutations of FLN1 in men with periventricular heterotopia." Guerrini R., Mei D., Sisodiya S.M., Sicca F., Harding B., Takahashi Y., Dorn T., Yoshida A., Campistol J., Kraemer G., Moro F., Dobyns W.B., Parrini E. Neurology 63:51-56(2004) [PubMed: 15249610] [Abstract] Cited for: VARIANTS PVNH1 VAL-102 AND PHE-149.
[47]	"A novel 9 bp deletion in the filamin A gene causes an otopalatodigital-spectrum disorder with a variable, intermediate phenotype." Stefanova M., Meinecke P., Gal A., Bolz H. Am. J. Med. Genet. A 132:386-390(2005) [PubMed: 15654694] [Abstract] Cited for: VARIANT OTOPALATODIGITAL SPECTRUM DISORDER 1635-ARG--VAL-1637 DEL.
[48]	"A novel filamin A D203Y mutation in a female patient with otopalatodigital type 1 syndrome and extremely skewed X chromosome inactivation." Hidalgo-Bravo A., Pompa-Mera E.N., Kofman-Alfaro S., Gonzalez-Bonilla C.R., Zenteno J.C. Am. J. Med. Genet. A 136:190-193(2005) [PubMed: 15940695] [Abstract] Cited for: VARIANT OPD1 TYR-203.
[49]	"Filamin A mutations cause periventricular heterotopia with Ehlers-Danlos syndrome." Sheen V.L., Jansen A., Chen M.H., Parrini E., Morgan T., Ravenscroft R., Ganesh V., Underwood T., Wiley J., Leventer R., Vaid R.R., Ruiz D.E., Hutchins G.M., Menasha J., Willner J., Geng Y., Gripp K.W., Nicholson L. , Berry-Kravis E., Bodell A., Apse K., Hill R.S., Dubeau F., Andermann F., Barkovich J., Andermann E., Shugart Y.Y., Thomas P., Viri M., Veggiotti P., Robertson S., Guerrini R., Walsh C.A. Neurology 64:254-262(2005) [PubMed: 15668422] [Abstract] Cited for: VARIANT PVNH4 GLY-39.
[50]	"Genotype-epigenotype-phenotype correlations in females with frontometaphyseal dysplasia." Zenker M., Naehrlich L., Sticht H., Reis A., Horn D. Am. J. Med. Genet. A 140:1069-1073(2006) [PubMed: 16596676] [Abstract] Cited for: VARIANTS FMD LEU-1186 AND CYS-1728.
[51]	"Ehlers-Danlos syndrome and periventricular nodular heterotopia in a Spanish family with a single FLNA mutation." Gomez-Garre P., Seijo M., Gutierrez-Delicado E., Castro del Rio M., de la Torre C., Gomez-Abad C., Morales-Corraliza J., Puig M., Serratosa J.M. J. Med. Genet. 43:232-237(2006) [PubMed: 15994863] [Abstract] Cited for: VARIANT PVNH4 VAL-128.
[52]	"Otopalatodigital syndrome type 2 in two siblings with a novel filamin A 629G>T mutation: clinical, pathological, and molecular findings." Marino-Enriquez A., Lapunzina P., Robertson S.P., Rodriguez J.I. Am. J. Med. Genet. A 143:1120-1125(2007) [PubMed: 17431908] [Abstract] Cited for: VARIANT OPD2 PHE-210.
[53]	"Filamin A mutation is one cause of FG syndrome." Unger S., Mainberger A., Spitz C., Baehr A., Zeschnigk C., Zabel B., Superti-Furga A., Morris-Rosendahl D.J. Am. J. Med. Genet. A 143:1876-1879(2007) [PubMed: 17632775] [Abstract] Cited for: VARIANT FGS2 LEU-1291.
[54]	"Mutations in the gene encoding filamin A as a cause for familial cardiac valvular dystrophy." Kyndt F., Gueffet J.P., Probst V., Jaafar P., Legendre A., Le Bouffant F., Toquet C., Roy E., McGregor L., Lynch S.A., Newbury-Ecob R., Tran V., Young I., Trochu J.N., Le Marec H., Schott J.J. Circulation 115:40-49(2007) [PubMed: 17190868] [Abstract] Cited for: VARIANTS CVDX ARG-288; GLN-637 AND ASP-711.
[55]	"Terminal osseous dysplasia is caused by a single recurrent mutation in the FLNA gene." Sun Y., Almomani R., Aten E., Celli J., van der Heijden J., Venselaar H., Robertson S.P., Baroncini A., Franco B., Basel-Vanagaite L., Horii E., Drut R., Ariyurek Y., den Dunnen J.T., Breuning M.H. Am. J. Hum. Genet. 87:146-153(2010) [PubMed: 20598277] [Abstract] Cited for: VARIANT TOD 1724-VAL--THR-1739 DEL.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53416 mRNA. Translation: CAA37495.1.
L44140 Genomic DNA. Translation: AAA92644.1.
X70082 Genomic DNA. Translation: CAA49687.1.
X70085 Genomic DNA. Translation: CAA49690.1.
AK090427 mRNA. Translation: BAC03408.2. Different initiation.
BX664723, BX936346 Genomic DNA. Translation: CAI43197.1.
BX664723, BX936346 Genomic DNA. Translation: CAI43199.1.
BX936346, BX664723 Genomic DNA. Translation: CAI43225.1.
BX936346, BX664723 Genomic DNA. Translation: CAI43227.1.
CH471172 Genomic DNA. Translation: EAW72745.1.
CH471172 Genomic DNA. Translation: EAW72746.1.

IPI

IPI00302592.
IPI00333541.

PIR

A37098.

RefSeq

NP_001104026.1. NM_001110556.1.
NP_001447.2. NM_001456.3.

UniGene

Hs.195464.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AAV	NMR	-	A	1863-1955	[»]
2BP3	X-ray	2.32	A/B	1863-1956	[»]
2BRQ	X-ray	2.10	A/B	2236-2329	[»]
2J3S	X-ray	2.50	A/B	2045-2329	[»]
2JF1	X-ray	2.20	A	2236-2329	[»]
2K3T	NMR	-	A	2427-2522	[»]
2K7P	NMR	-	A	1772-1956	[»]
2K7Q	NMR	-	A	1954-2141	[»]
2W0P	X-ray	1.90	A/B	2236-2329	[»]
2WFN	X-ray	3.20	A/B	1-278	[»]
3CNK	X-ray	1.65	A/B	2559-2647	[»]
3HOC	X-ray	2.30	A/B	2-269	[»]
3HOP	X-ray	2.30	A/B	2-269	[»]
3HOR	X-ray	2.70	A/B	2-269	[»]
3ISW	X-ray	2.80	A/B	2236-2329	[»]
3RGH	X-ray	2.44	A/B	1158-1252	[»]

ProteinModelPortal

P21333.

SMR

P21333. Positions 39-2647.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1136N.

IntAct

P21333. 38 interactions.

MINT

MINT-118283.

STRING

P21333.

PTM databases

PhosphoSite

P21333.

Polymorphism databases

DMDM

116241365.

2D gel databases

OGP

P21333.

Proteomic databases

PRIDE

P21333.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369850; ENSP00000358866; ENSG00000196924.
ENST00000369863; ENSP00000358879; ENSG00000196924.

GeneID

2316.

KEGG

hsa:2316.

UCSC

uc004fkk.2. human.

Organism-specific databases

CTD

2316.

GeneCards

GC0XM153576.

H-InvDB

HIX0017150.

HGNC

HGNC:3754. FLNA.

HPA

CAB000356.
HPA001115.
HPA002925.

MIM

300017. gene.
300048. phenotype.
300049. phenotype.
300244. phenotype.
300321. phenotype.
300537. phenotype.
304120. phenotype.
305620. phenotype.
309350. phenotype.
311300. phenotype.
314400. phenotype.

neXtProt

NX_P21333.

Orphanet

2978. Chronic intestinal pseudo-obstruction.
1864. Congenital valvular dysplasia.
82004. Ehlers-Danlos syndrome with periventricular heterotopia.
323. FG syndrome.
1826. Frontometaphyseal dysplasia.
2484. Osteodysplasty, Melnick-Needles type.
90650. Otopalatodigital syndrome type 1.
98892. Periventricular nodular heterotopia.
88630. Terminal osseous dysplasia - pigmentary defects.

PharmGKB

PA28172.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04349.

HOGENOM

HBG357078.

HOVERGEN

HBG004163.

InParanoid

P21333.

OMA

MSHLKVG.

PhylomeDB

P21333.

Enzyme and pathway databases

Pathway_Interaction_DB

tcrpathway. TCR signaling in naive CD4+ T cells.

Reactome

REACT_111155. Cell-Cell communication.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P21333.

Bgee

P21333.

CleanEx

HS_FLNA.

Genevestigator

P21333.

GermOnline

ENSG00000196924. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 2 hits.
G3DSA:2.60.40.10. Ig-like_fold. 24 hits.

KO

K04437.

Pfam

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

SMART

SM00033. CH. 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

NextBio

9405.

PMAP-CutDB

P21333.

SOURCE

Search...

Entry information

Entry name

FLNA_HUMAN

Accession

Primary (citable) accession number: P21333
Secondary accession number(s): Q5HY53, Q5HY55, Q8NF52

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 160 of the entry and version 4 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.