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P21333 (FLNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2647 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Involved in ciliogenesis. Ref.41

Subunit structure

Homodimer. Interacts with PDLIM2 By similarity. 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. Interacts with TMEM67 (via C-terminus) and MKS1. Interacts (via actin-binding domain) with MICALL2 (via CH domain). Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.23 Ref.26 Ref.27 Ref.38 Ref.41 Ref.42 Ref.45

Subcellular location

Cytoplasmcell cortex. Cytoplasmcytoskeleton.

Tissue specificity

Ubiquitous.

Domain

Comprised of a NH2-terminal actin-binding domain, 24 immunoglobulin-like internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation.

Post-translational modification

Phosphorylation extent changes in response to cell activation.

Involvement in disease

Periventricular nodular heterotopia 1 (PVNH1) [MIM:300049]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.47 Ref.48 Ref.49 Ref.51

Periventricular nodular heterotopia 4 (PVNH4) [MIM:300537]: A disorder characterized by nodular brain heterotopia, joint hypermobility and development of aortic dilation in early adulthood.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.54 Ref.56

Otopalatodigital syndrome 1 (OPD1) [MIM:311300]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.50 Ref.53

Otopalatodigital syndrome 2 (OPD2) [MIM:304120]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.50 Ref.57

Frontometaphyseal dysplasia (FMD) [MIM:305620]: Congenital bone disease characterized by supraorbital hyperostosis, deafness and digital anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.50 Ref.55

Melnick-Needles syndrome (MNS) [MIM:309350]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.50

Intestinal pseudoobstruction, neuronal, chronic idiopathic, X-linked (IPOX) [MIM:300048]: A disease 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

FG syndrome 2 (FGS2) [MIM:300321]: FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.58

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.60

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.59

Defects in FLNA may be a cause of macrothrombocytopenia, a disorder characterized by subnormal levels of blood platelets. Blood platelets are abnormally enlarged.

Congenital short bowel syndrome, X-linked (CSBSX) [MIM:300048]: A disease characterized by a shortened small intestine, and malabsorption. The mean length of the small intestine in affected individuals is approximately 50 cm, compared with a normal length at birth of 190-280 cm. It is associated with significant mortality and morbidity. Infants usually present with failure to thrive, recurrent vomiting, and diarrhea.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.43

Sequence similarities

Belongs to the filamin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 24 filamin repeats.

Caution

Variant Thr-1764 has been originally associated with periventricular nodular heterotopia (Ref.50). It has been subsequently reported as a benign polymorphism (Ref.50).

Sequence caution

The sequence BAC03408.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin crosslink formation

Inferred from direct assay PubMed 10051605. Source: BHF-UCL

actin cytoskeleton reorganization

Inferred from direct assay PubMed 10051605. Source: BHF-UCL

adenylate cyclase-inhibiting dopamine receptor signaling pathway

Inferred from mutant phenotype PubMed 10692483. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

cilium assembly

Inferred from mutant phenotype Ref.41. Source: UniProtKB

cytoplasmic sequestering of protein

Inferred from mutant phenotype PubMed 17536008. Source: BHF-UCL

early endosome to late endosome transport

Inferred from electronic annotation. Source: Ensembl

epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

establishment of protein localization

Inferred from direct assay Ref.27. Source: BHF-UCL

mRNA transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein catabolic process

Inferred from mutant phenotype Ref.27. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15684392. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

positive regulation of transcription factor import into nucleus

Inferred from mutant phenotype PubMed 15684392. Source: UniProtKB

protein localization to cell surface

Inferred from direct assay Ref.27. Source: BHF-UCL

protein stabilization

Inferred from mutant phenotype Ref.27. Source: BHF-UCL

receptor clustering

Inferred from direct assay PubMed 10692483. Source: BHF-UCL

spindle assembly involved in mitosis

Inferred from direct assay PubMed 18548008. Source: MGI

   Cellular_componentMyb complex

Inferred from direct assay PubMed 18548008. Source: MGI

actin cytoskeleton

Inferred by curator Ref.1. Source: BHF-UCL

actin filament

Inferred from electronic annotation. Source: Ensembl

apical dendrite

Inferred from electronic annotation. Source: Ensembl

cortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 15684392. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendritic shaft

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 15684392. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.27. Source: BHF-UCL

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionFc-gamma receptor I complex binding

Inferred from direct assay PubMed 1833070. Source: BHF-UCL

Rac GTPase binding

Inferred from direct assay PubMed 10051605. Source: BHF-UCL

Ral GTPase binding

Inferred from direct assay PubMed 10051605. Source: BHF-UCL

Rho GTPase binding

Inferred from direct assay PubMed 10051605. Source: BHF-UCL

actin filament binding

Inferred from direct assay Ref.1PubMed 3138234PubMed 4044584. Source: BHF-UCL

glycoprotein binding

Inferred from direct assay PubMed 1833070PubMed 3138234. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.1. Source: BHF-UCL

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

small GTPase binding

Inferred from direct assay PubMed 10051605. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction PubMed 15684392. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 26472646Filamin-A
PRO_0000087296

Regions

Domain2 – 274273Actin-binding
Domain43 – 149107CH 1
Domain166 – 266101CH 2
Repeat276 – 37499Filamin 1
Repeat376 – 47499Filamin 2
Repeat475 – 57096Filamin 3
Repeat571 – 66393Filamin 4
Repeat667 – 76397Filamin 5
Repeat764 – 866103Filamin 6
Repeat867 – 96599Filamin 7
Repeat966 – 106196Filamin 8
Repeat1062 – 115493Filamin 9
Repeat1155 – 124995Filamin 10
Repeat1250 – 1349100Filamin 11
Repeat1350 – 144293Filamin 12
Repeat1443 – 153997Filamin 13
Repeat1540 – 163697Filamin 14
Repeat1649 – 174092Filamin 15
Repeat1779 – 186082Filamin 16
Repeat1861 – 195090Filamin 17
Repeat1951 – 203989Filamin 18
Repeat2042 – 213190Filamin 19
Repeat2132 – 223099Filamin 20
Repeat2233 – 232593Filamin 21
Repeat2327 – 242094Filamin 22
Repeat2424 – 251693Filamin 23
Repeat2552 – 264695Filamin 24
Region1490 – 1607118Interaction with furin By similarity
Region1741 – 177838Hinge 1
Region2517 – 2647131Self-association site, tail
Region2517 – 255135Hinge 2

Sites

Site1761 – 17622Cleavage; by calpain

Amino acid modifications

Modified residue21N-acetylserine Ref.9 Ref.33
Modified residue111Phosphoserine Ref.40
Modified residue3761N6-acetyllysine By similarity
Modified residue5081N6-acetyllysine Ref.35
Modified residue7001N6-acetyllysine Ref.35
Modified residue7811N6-acetyllysine Ref.35
Modified residue8371N6-acetyllysine Ref.35
Modified residue8651N6-acetyllysine By similarity
Modified residue9061N6-acetyllysine By similarity
Modified residue10711N6-acetyllysine; alternate By similarity
Modified residue10711N6-succinyllysine; alternate By similarity
Modified residue10811Phosphoserine Ref.31 Ref.36 Ref.40
Modified residue10841Phosphoserine Ref.22 Ref.25 Ref.28 Ref.30 Ref.32 Ref.34 Ref.36 Ref.40
Modified residue10891Phosphothreonine Ref.20
Modified residue13381Phosphoserine Ref.32
Modified residue13721N6-acetyllysine By similarity
Modified residue14591Phosphoserine Ref.20 Ref.22 Ref.29 Ref.30 Ref.32 Ref.36 Ref.40
Modified residue15331Phosphoserine Ref.32 Ref.36
Modified residue15381N6-acetyllysine By similarity
Modified residue16301Phosphoserine Ref.32
Modified residue17341Phosphoserine Ref.36
Modified residue20531Phosphoserine Ref.32 Ref.36
Modified residue21521Phosphoserine Ref.20 Ref.30 Ref.32 Ref.36 Ref.40
Modified residue21581Phosphoserine Ref.30
Modified residue22841Phosphoserine Ref.20 Ref.36
Modified residue23271Phosphoserine Ref.32 Ref.36 Ref.40
Modified residue23361Phosphothreonine Ref.36
Modified residue24141Phosphoserine Ref.32 Ref.36
Modified residue25101Phosphoserine Ref.32
Modified residue25691N6-acetyllysine; alternate By similarity
Modified residue25691N6-succinyllysine; alternate By similarity
Modified residue25751N6-acetyllysine By similarity
Modified residue26071N6-acetyllysine Ref.35
Modified residue26211N6-acetyllysine Ref.35

Natural variations

Alternative sequence1649 – 16568Missing in isoform 2.
VSP_035454
Natural variant391A → G in PVNH4. Ref.54
VAR_022734
Natural variant821E → V in PVNH1. Ref.49
Corresponds to variant rs28935169 [ dbSNP | Ensembl ].
VAR_015699
Natural variant1021M → V in PVNH1. Ref.51
VAR_031305
Natural variant1281A → V in PVNH4. Ref.56
VAR_031306
Natural variant1491S → F in PVNH1. Ref.51
VAR_031307
Natural variant1701Q → P in OPD2. Ref.50
VAR_015713
Natural variant1721L → F in OPD1. Ref.50
VAR_015714
Natural variant1961R → G in OPD2. Ref.50
VAR_015715
Natural variant1961R → W in OPD1. Ref.50
VAR_015716
Natural variant2001A → S in OPD2. Ref.50
VAR_015717
Natural variant2031D → Y in OPD1. Ref.53
VAR_031308
Natural variant2071P → L in OPD1. Ref.50
Corresponds to variant rs28935469 [ dbSNP | Ensembl ].
VAR_015700
Natural variant2101C → F in OPD2. Ref.57
VAR_058720
Natural variant2541E → K in OPD2. Ref.50
Corresponds to variant rs28935470 [ dbSNP | Ensembl ].
VAR_015701
Natural variant2731A → P in OPD2. Ref.50
VAR_015718
Natural variant2881G → R in CVDX. Ref.59
VAR_064156
Natural variant3201V → A.
Corresponds to variant rs1064816 [ dbSNP | Ensembl ].
VAR_012831
Natural variant3701F → L.
Corresponds to variant rs1064817 [ dbSNP | Ensembl ].
VAR_012832
Natural variant4291T → M. Ref.50
VAR_069803
Natural variant5281V → M in PVNH1. Ref.48
Corresponds to variant rs143873938 [ dbSNP | Ensembl ].
VAR_031309
Natural variant5521V → A.
Corresponds to variant rs730319 [ dbSNP | Ensembl ].
VAR_012833
Natural variant5551T → K in OPD2. Ref.50
VAR_015719
Natural variant6371P → Q in CVDX. Ref.59
VAR_064157
Natural variant6561L → F in PVNH1. Ref.47
VAR_012834
Natural variant7111V → D in CVDX. Ref.59
VAR_064158
Natural variant10121S → L.
Corresponds to variant rs17091204 [ dbSNP | Ensembl ].
VAR_031310
Natural variant11591D → A in FMD; does not inhibit interaction with MIS18BP1. Ref.38 Ref.50
Corresponds to variant rs28935471 [ dbSNP | Ensembl ].
VAR_015702
Natural variant11841D → E in MNS. Ref.50
VAR_015720
Natural variant11861S → L in FMD. Ref.50 Ref.55
VAR_015721
Natural variant11881A → T in MNS; does not inhibit interaction with MIS18BP1. Ref.38 Ref.50
Corresponds to variant rs28935472 [ dbSNP | Ensembl ].
VAR_015703
Natural variant11991S → L in MNS; does not inhibit interaction with MIS18BP1. Ref.38 Ref.50
Corresponds to variant rs28935473 [ dbSNP | Ensembl ].
VAR_015704
Natural variant12911P → L in FGS2. Ref.58
VAR_058721
Natural variant14191A → G.
Corresponds to variant rs35504556 [ dbSNP | Ensembl ].
VAR_032083
Natural variant16201Missing in FMD. Ref.50
VAR_015722
Natural variant1635 – 16373Missing in otopalatodigital spectrum disorder.
VAR_031311
Natural variant16451C → F in OPD2. Ref.50
VAR_015723
Natural variant1724 – 173916Missing in TOD.
VAR_064159
Natural variant17281G → C in FMD. Ref.55
VAR_031312
Natural variant17641A → T. Ref.47 Ref.50
Corresponds to variant rs57108893 [ dbSNP | Ensembl ].
VAR_012835
Natural variant18031E → K Probable disease-associated mutation found in a patient with macrothrombocytopenia. Ref.39
VAR_067251

Experimental info

Sequence conflict441I → T AA sequence Ref.10
Sequence conflict17721A → G in CAA49687. Ref.11
Sequence conflict23411Q → R in BAC03408. Ref.5
Sequence conflict26341D → H in CAA37495. Ref.2

Secondary structure

............................................................................................................................................................................................. 2647
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6C1A07041DF50142

FASTA2,647280,739
        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 

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Isoform 2 [UniParc].

Checksum: 862625C6FEA39075
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FASTA2,639280,018

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Spleen.
[6]"Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , 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].
[9]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[10]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-54; 917-940; 1037-1050; 1754-1783 AND 2148-2168.
[11]"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 [GENOMIC DNA] OF 1658-1772.
[12]"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: SIMILARITY TO OTHER MEMBERS OF THE FAMILY.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSEN1 AND PSEN2.
[14]"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.
[15]"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.
[16]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLNB.
[17]"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 MYOT AND MYOZ1.
[18]"Structural and functional aspects of filamins."
van der Flier A., Sonnenberg A.
Biochim. Biophys. Acta 1538:99-117(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[19]"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.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1089; SER-1459; SER-2152 AND SER-2284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084 AND SER-1459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP24.
[24]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IPOX.
[25]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ECSCR.
[27]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCGR1A.
[28]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[30]"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-1084; SER-1459; SER-2152 AND SER-2158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[31]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[35]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-508; LYS-700; LYS-781; LYS-837; LYS-2607 AND LYS-2621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081; SER-1084; SER-1459; SER-1533; SER-1734; SER-2053; SER-2152; SER-2284; SER-2327; THR-2336 AND SER-2414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"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].
[38]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAF1B AND MIS18BP1, CHARACTERIZATION OF VARIANTS ALA-1159; THR-1188 AND LEU-1199.
[39]"Thrombocytopenia resulting from mutations in filamin A can be expressed as an isolated syndrome."
Nurden P., Debili N., Coupry I., Bryckaert M., Youlyouz-Marfak I., Sole G., Pons A.C., Berrou E., Adam F., Kauskot A., Lamaziere J.M., Rameau P., Fergelot P., Rooryck C., Cailley D., Arveiler B., Lacombe D., Vainchenker W., Nurden A., Goizet C.
Blood 118:5928-5937(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MACROTHROMBOCYTOPENIA, VARIANT LYS-1803.
[40]"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-11; SER-1081; SER-1084; SER-1459; SER-2152 AND SER-2327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"A meckelin-filamin A interaction mediates ciliogenesis."
Adams M., Simms R.J., Abdelhamed Z., Dawe H.R., Szymanska K., Logan C.V., Wheway G., Pitt E., Gull K., Knowles M.A., Blair E., Cross S.H., Sayer J.A., Johnson C.A.
Hum. Mol. Genet. 21:1272-1286(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CILIOGENESIS, INTERACTION WITH TMEM67 AND MKS1.
[42]"Junctional Rab13-binding protein (JRAB) regulates cell spreading via filamins."
Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T., Imoto I., Matsushita N., Sasaki T.
Genes Cells 18:810-822(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICALL2.
[43]"Congenital short bowel syndrome as the presenting symptom in male patients with FLNA mutations."
van der Werf C.S., Sribudiani Y., Verheij J.B., Carroll M., O'Loughlin E., Chen C.H., Brooks A.S., Liszewski M.K., Atkinson J.P., Hofstra R.M.
Genet. Med. 15:310-313(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CSBSX.
[44]"Structure of three tandem filamin domains reveals auto-inhibition of ligand binding."
Lad Y., Kiema T., Jiang P., Pentikainen O.T., Coles C.H., Campbell I.D., Calderwood D.A., Ylanne J.
EMBO J. 26:3993-4004(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2045-2329.
[45]"Structure of the human filamin A actin-binding domain."
Ruskamo S., Ylanne J.
Acta Crystallogr. D 65:1217-1221(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-278, ACTIN-BINDING REGION, SUBUNIT.
[46]"Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin."
Heikkinen O.K., Ruskamo S., Konarev P.V., Svergun D.I., Iivanainen T., Heikkinen S.M., Permi P., Koskela H., Kilpelainen I., Ylanne J.
J. Biol. Chem. 284:25450-25458(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1772-1956 AND 1954-2141.
[47]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: VARIANT PVNH1 PHE-656, VARIANT THR-1764.
[48]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PVNH1 MET-528.
[49]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PVNH1 VAL-82.
[50]"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] [Europe PMC] [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, VARIANTS MET-429 AND THR-1764.
[51]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS PVNH1 VAL-102 AND PHE-149.
[52]"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] [Europe PMC] [Abstract]
Cited for: VARIANT OTOPALATODIGITAL SPECTRUM DISORDER 1635-ARG--VAL-1637 DEL.
[53]"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] [Europe PMC] [Abstract]
Cited for: VARIANT OPD1 TYR-203.
[54]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: VARIANT PVNH4 GLY-39.
[55]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS FMD LEU-1186 AND CYS-1728.
[56]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PVNH4 VAL-128.
[57]"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] [Europe PMC] [Abstract]
Cited for: VARIANT OPD2 PHE-210.
[58]"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] [Europe PMC] [Abstract]
Cited for: VARIANT FGS2 LEU-1291.
[59]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS CVDX ARG-288; GLN-637 AND ASP-711.
[60]"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] [Europe PMC] [Abstract]
Cited for: VARIANT TOD 1724-VAL--THR-1739 DEL.
+Additional computationally mapped references.

Web resources

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.
GU727643 mRNA. Translation: ADU87644.1.
AK090427 mRNA. Translation: BAC03408.2. Different initiation.
AB593010 mRNA. Translation: BAJ83965.1.
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.
PIRA37098.
RefSeqNP_001104026.1. NM_001110556.1.
NP_001447.2. NM_001456.3.
UniGeneHs.195464.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AAVNMR-A1863-1955[»]
2BP3X-ray2.32A/B1863-1956[»]
2BRQX-ray2.10A/B2236-2329[»]
2J3SX-ray2.50A/B2045-2329[»]
2JF1X-ray2.20A2236-2329[»]
2K3TNMR-A2427-2522[»]
2K7PNMR-A1772-1956[»]
2K7QNMR-A1954-2141[»]
2W0PX-ray1.90A/B2236-2329[»]
2WFNX-ray3.20A/B1-278[»]
3CNKX-ray1.65A/B2559-2647[»]
3HOCX-ray2.30A/B2-269[»]
3HOPX-ray2.30A/B2-269[»]
3HORX-ray2.70A/B2-269[»]
3ISWX-ray2.80A/B2236-2329[»]
3RGHX-ray2.44A/B1158-1252[»]
4M9PX-ray1.72A478-766[»]
ProteinModelPortalP21333.
SMRP21333. Positions 39-2647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108605. 102 interactions.
DIPDIP-1136N.
IntActP21333. 55 interactions.
MINTMINT-118283.
STRING9606.ENSP00000358866.

PTM databases

PhosphoSiteP21333.

Polymorphism databases

DMDM116241365.

2D gel databases

OGPP21333.

Proteomic databases

PaxDbP21333.
PRIDEP21333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360319; ENSP00000353467; ENSG00000196924. [P21333-2]
ENST00000369850; ENSP00000358866; ENSG00000196924. [P21333-1]
ENST00000422373; ENSP00000416926; ENSG00000196924. [P21333-2]
ENST00000596447; ENSP00000469433; ENSG00000269329. [P21333-2]
ENST00000597475; ENSP00000471999; ENSG00000269329. [P21333-2]
ENST00000600520; ENSP00000472325; ENSG00000269329. [P21333-1]
GeneID2316.
KEGGhsa:2316.
UCSCuc004fkk.2. human. [P21333-1]
uc010nuu.1. human. [P21333-2]

Organism-specific databases

CTD2316.
GeneCardsGC0XM153576.
H-InvDBHIX0017150.
HGNCHGNC:3754. FLNA.
HPACAB000356.
HPA000368.
HPA001115.
HPA002925.
MIM300017. gene.
300048. phenotype.
300049. phenotype.
300244. phenotype.
300321. phenotype.
300537. phenotype.
304120. phenotype.
305620. phenotype.
309350. phenotype.
311300. phenotype.
314400. phenotype.
neXtProtNX_P21333.
Orphanet2978. Chronic intestinal pseudo-obstruction.
2301. Congenital short bowel syndrome.
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.
90652. Otopalatodigital syndrome type 2.
98892. Periventricular nodular heterotopia.
88630. Terminal osseous dysplasia - pigmentary defects.
PharmGKBPA28172.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000044235.
HOVERGENHBG004163.
InParanoidP21333.
KOK04437.
OMAPGVAKTG.
PhylomeDBP21333.
TreeFamTF313685.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_604. Hemostasis.
SignaLinkP21333.

Gene expression databases

ArrayExpressP21333.
BgeeP21333.
CleanExHS_FLNA.
GenevestigatorP21333.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR028559. FLN.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR11915:SF173. PTHR11915:SF173. 1 hit.
PfamPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFLNA. human.
EvolutionaryTraceP21333.
GeneWikiFLNA.
GenomeRNAi2316.
NextBio9405.
PMAP-CutDBP21333.
PROP21333.
SOURCESearch...

Entry information

Entry nameFLNA_HUMAN
AccessionPrimary (citable) accession number: P21333
Secondary accession number(s): E9KL45 expand/collapse secondary AC list , Q5HY53, Q5HY55, Q8NF52
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 185 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM