Gene FLNB - ENSG00000136068 | NCBI Gene ID: 2317

Details for: FLNB

Gene ID: 2317

Symbol: FLNB

Ensembl ID: ENSG00000136068

Description: filamin B

Associated with

Antiviral mechanism by ifn-stimulated genes
(R-HSA-1169410)
Cytokine signaling in immune system
(R-HSA-1280215)
Immune system
(R-HSA-168256)
Interferon signaling
(R-HSA-913531)
Isg15 antiviral mechanism
(R-HSA-1169408)
Actin binding
(GO:0003779)
Actin cytoskeleton
(GO:0015629)
Actin cytoskeleton organization
(GO:0030036)
Actin filament binding
(GO:0051015)
Brush border
(GO:0005903)
Cadherin binding
(GO:0045296)
Cell cortex
(GO:0005938)
Cellular response to type ii interferon
(GO:0071346)
Cytoplasm
(GO:0005737)
Cytosol
(GO:0005829)
Epithelial cell morphogenesis
(GO:0003382)
Extracellular exosome
(GO:0070062)
Focal adhesion
(GO:0005925)
Identical protein binding
(GO:0042802)
Keratinocyte development
(GO:0003334)
Membrane
(GO:0016020)
Phagocytic vesicle
(GO:0045335)
Plasma membrane
(GO:0005886)
Protein binding
(GO:0005515)
Rna binding
(GO:0003723)
Signal transduction
(GO:0007165)
Skeletal muscle tissue development
(GO:0007519)
Stress fiber
(GO:0001725)
Z disc
(GO:0030018)

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 3.32
Marker Score: 7295
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 3.09
Marker Score: 54820
Cell Name: anterior lens cell (CL0002223)
Fold Change: 2.91
Marker Score: 3911
Cell Name: taste receptor cell (CL0000209)
Fold Change: 2.27
Marker Score: 1957
Cell Name: epithelial cell of prostate (CL0002231)
Fold Change: 2.22
Marker Score: 1544
Cell Name: colon epithelial cell (CL0011108)
Fold Change: 2.18
Marker Score: 6842
Cell Name: cerebral cortex endothelial cell (CL1001602)
Fold Change: 2.11
Marker Score: 1258
Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
Fold Change: 2.1
Marker Score: 2247
Cell Name: lung goblet cell (CL1000143)
Fold Change: 2.01
Marker Score: 580
Cell Name: caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 2
Marker Score: 7728
Cell Name: luminal cell of prostate epithelium (CL0002340)
Fold Change: 2
Marker Score: 1163
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 1.93
Marker Score: 2845.5
Cell Name: enterocyte (CL0000584)
Fold Change: 1.92
Marker Score: 9209
Cell Name: endothelial cell of vascular tree (CL0002139)
Fold Change: 1.9
Marker Score: 2764
Cell Name: nasal mucosa goblet cell (CL0002480)
Fold Change: 1.89
Marker Score: 1266
Cell Name: foveolar cell of stomach (CL0002179)
Fold Change: 1.89
Marker Score: 12074
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 1.89
Marker Score: 2283
Cell Name: P/D1 enteroendocrine cell (CL0002268)
Fold Change: 1.87
Marker Score: 698
Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
Fold Change: 1.84
Marker Score: 17323
Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
Fold Change: 1.82
Marker Score: 27202.5
Cell Name: renal alpha-intercalated cell (CL0005011)
Fold Change: 1.8
Marker Score: 948
Cell Name: vip GABAergic cortical interneuron (CL4023016)
Fold Change: 1.77
Marker Score: 67285
Cell Name: sncg GABAergic cortical interneuron (CL4023015)
Fold Change: 1.76
Marker Score: 13497
Cell Name: renal principal cell (CL0005009)
Fold Change: 1.75
Marker Score: 1350
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: 1.75
Marker Score: 1815
Cell Name: neuron (CL0000540)
Fold Change: 1.73
Marker Score: 7025
Cell Name: luminal epithelial cell of mammary gland (CL0002326)
Fold Change: 1.72
Marker Score: 3042
Cell Name: preosteoblast (CL0007010)
Fold Change: 1.71
Marker Score: 484.5
Cell Name: ciliated columnar cell of tracheobronchial tree (CL0002145)
Fold Change: 1.71
Marker Score: 14845
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.71
Marker Score: 104883.5
Cell Name: Sertoli cell (CL0000216)
Fold Change: 1.71
Marker Score: 10115
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 1.71
Marker Score: 17609
Cell Name: corneal endothelial cell (CL0000132)
Fold Change: 1.69
Marker Score: 982
Cell Name: hepatoblast (CL0005026)
Fold Change: 1.66
Marker Score: 5428
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: 1.65
Marker Score: 14199
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 1.64
Marker Score: 14395.5
Cell Name: Leydig cell (CL0000178)
Fold Change: 1.63
Marker Score: 1754
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: 1.61
Marker Score: 15319
Cell Name: kidney interstitial fibroblast (CL1000692)
Fold Change: 1.6
Marker Score: 3073
Cell Name: smooth muscle cell of prostate (CL1000487)
Fold Change: 1.6
Marker Score: 406
Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
Fold Change: 1.58
Marker Score: 3721
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 1.58
Marker Score: 461
Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
Fold Change: 1.55
Marker Score: 1670
Cell Name: type A enteroendocrine cell (CL0002067)
Fold Change: 1.53
Marker Score: 615
Cell Name: basal cell (CL0000646)
Fold Change: 1.52
Marker Score: 1966
Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
Fold Change: 1.52
Marker Score: 4073
Cell Name: medullary thymic epithelial cell (CL0002365)
Fold Change: 1.52
Marker Score: 2489
Cell Name: papillary tips cell (CL1000597)
Fold Change: 1.52
Marker Score: 306
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 1.51
Marker Score: 1593
Cell Name: parietal epithelial cell (CL1000452)
Fold Change: 1.5
Marker Score: 545
Cell Name: cerebellar granule cell precursor (CL0002362)
Fold Change: 1.49
Marker Score: 837
Cell Name: lung ciliated cell (CL1000271)
Fold Change: 1.49
Marker Score: 708
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 1.49
Marker Score: 3398
Cell Name: type EC enteroendocrine cell (CL0000577)
Fold Change: 1.48
Marker Score: 1390
Cell Name: basal epithelial cell of prostatic duct (CL0002236)
Fold Change: 1.47
Marker Score: 1303
Cell Name: kidney collecting duct principal cell (CL1001431)
Fold Change: 1.46
Marker Score: 3689
Cell Name: kidney capillary endothelial cell (CL1000892)
Fold Change: 1.46
Marker Score: 458
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: 1.46
Marker Score: 9393
Cell Name: mural cell (CL0008034)
Fold Change: 1.46
Marker Score: 166969
Cell Name: respiratory goblet cell (CL0002370)
Fold Change: 1.45
Marker Score: 418
Cell Name: endothelial cell of uterus (CL0009095)
Fold Change: 1.45
Marker Score: 2888
Cell Name: type I pneumocyte (CL0002062)
Fold Change: 1.43
Marker Score: 1721
Cell Name: retinal blood vessel endothelial cell (CL0002585)
Fold Change: 1.43
Marker Score: 343
Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
Fold Change: 1.43
Marker Score: 1446
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: 1.41
Marker Score: 445
Cell Name: duct epithelial cell (CL0000068)
Fold Change: 1.41
Marker Score: 658
Cell Name: brainstem motor neuron (CL2000047)
Fold Change: 1.41
Marker Score: 816
Cell Name: pulmonary artery endothelial cell (CL1001568)
Fold Change: 1.4
Marker Score: 1209
Cell Name: vein endothelial cell (CL0002543)
Fold Change: 1.38
Marker Score: 1247
Cell Name: kidney collecting duct intercalated cell (CL1001432)
Fold Change: 1.37
Marker Score: 2271
Cell Name: endothelial cell of sinusoid (CL0002262)
Fold Change: 1.36
Marker Score: 331
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 1.36
Marker Score: 338
Cell Name: sst GABAergic cortical interneuron (CL4023017)
Fold Change: 1.35
Marker Score: 26861.5
Cell Name: lung microvascular endothelial cell (CL2000016)
Fold Change: 1.35
Marker Score: 287
Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
Fold Change: 1.35
Marker Score: 2082
Cell Name: pyramidal neuron (CL0000598)
Fold Change: 1.35
Marker Score: 2260
Cell Name: midzonal region hepatocyte (CL0019028)
Fold Change: 1.34
Marker Score: 5799
Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
Fold Change: 1.34
Marker Score: 49548
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 1.34
Marker Score: 5177.5
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: 1.33
Marker Score: 7176.5
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 1.33
Marker Score: 780
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 1.33
Marker Score: 20773
Cell Name: enteric smooth muscle cell (CL0002504)
Fold Change: 1.31
Marker Score: 3086.5
Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
Fold Change: 1.31
Marker Score: 1386
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: 1.28
Marker Score: 633
Cell Name: cholangiocyte (CL1000488)
Fold Change: 1.28
Marker Score: 478
Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
Fold Change: 1.27
Marker Score: 5257
Cell Name: ciliated epithelial cell (CL0000067)
Fold Change: 1.25
Marker Score: 573
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 1.25
Marker Score: 1244.5
Cell Name: bronchial goblet cell (CL1000312)
Fold Change: 1.25
Marker Score: 615
Cell Name: endothelial cell (CL0000115)
Fold Change: 1.25
Marker Score: 1117
Cell Name: basal cell of epithelium of trachea (CL1000348)
Fold Change: 1.24
Marker Score: 9247
Cell Name: intestine goblet cell (CL0019031)
Fold Change: 1.24
Marker Score: 1188
Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
Fold Change: 1.24
Marker Score: 340
Cell Name: cell in vitro (CL0001034)
Fold Change: 1.23
Marker Score: 42753
Cell Name: secretory cell (CL0000151)
Fold Change: 1.22
Marker Score: 2233
Cell Name: kidney connecting tubule epithelial cell (CL1000768)
Fold Change: 1.22
Marker Score: 1722
Cell Name: endocardial cell (CL0002350)
Fold Change: 1.21
Marker Score: 686
Cell Name: neuron associated cell (sensu Vertebrata) (CL0000123)
Fold Change: 1.21
Marker Score: 6339
Cell Name: epithelial cell of lower respiratory tract (CL0002632)
Fold Change: 1.21
Marker Score: 5036

Hover over a box to see details here...

**Key characteristics:** * FLNB is a large protein (170 kDa) that is composed of three domains: FLN1, FLN2, and FLN3. * It is a transmembrane protein that is expressed on the surface of various cell types. * It is a key component of the microfilaments, which are responsible for providing structural support and shape to the cell. * It is also involved in the regulation of cell migration, adhesion, and signaling. **Pathways and functions:** * FLNB is involved in a wide range of cellular processes, including cell migration, adhesion, and signaling. * It plays a crucial role in the organization of the actin cytoskeleton, which is essential for the proper function of various cellular structures, such as the cell membrane, the nucleus, and the extracellular matrix. * It is also involved in the regulation of cell migration, adhesion, and signaling pathways. * It is a key regulator of epithelial cell morphogenesis, which is the process by which cells acquire their final cell fate and structure. * It is also involved in the immune response, where it acts as an receptor for type II interferons. * It is involved in the regulation of stress fiber development and maintenance. **Clinical significance:** * Mutations in the FLNB gene have been linked to several human diseases, including alkaptonuria, ichthyosis, and leukemogenesis. * In alkaptonuria, mutations in FLNB lead to the accumulation of a toxic metabolite called alkapton in the body. This can cause severe kidney damage and death. * In ichthyosis, mutations in FLNB lead to the formation of a protein called filamin A, which is a mutant form of filamin B. This protein is expressed in the skin and can cause a condition called ichthyosis. * In leukemogenesis, mutations in FLNB are associated with the development of leukemia. **Conclusion:** The FLNB gene is a critical component of the actin cytoskeleton, which is essential for the proper function of various cellular structures. Mutations in the FLNB gene have been linked to several human diseases, highlighting its importance in human health.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Filamin-B

Genular Protein ID: 252061028

Symbol: FLNB_HUMAN

Name: Filamin-B

UniProtKB Accession Codes:

O75369 B2ZZ83 B2ZZ84 B2ZZ85 C9JKE6 C9JMC4 Q13706 Q59EC2 Q60FE7 Q6MZJ1 Q8WXS9 Q8WXT0 Q8WXT1 Q8WXT2 Q8WXT3 Q9NRB5 Q9NT26 Q9UEV9

Database IDs:

Citations:

PubMed ID: 9651345

Title: Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha.

PubMed ID: 9651345

DOI: 10.1074/jbc.273.28.17531

PubMed ID: 9694715

Title: A novel human actin-binding protein homologue that binds to platelet glycoprotein Ibalpha.

PubMed ID: 9694715

PubMed ID: 11807098

Title: Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits.

PubMed ID: 11807098

DOI: 10.1083/jcb.200103037

PubMed ID: 11153914

Title: Genomic structure and fine mapping of the two human filamin gene paralogues FLNB and FLNC and comparative analysis of the filamin gene family.

PubMed ID: 11153914

DOI: 10.1007/s004390000414

PubMed ID: 18487259

Title: Fine expression profiling of full-length transcripts using a size-unbiased cDNA library prepared with the vector-capping method.

PubMed ID: 18487259

DOI: 10.1093/dnares/dsn010

PubMed ID: 16106752

Title: Vector-capping: a simple method for preparing a high-quality full-length cDNA library.

PubMed ID: 16106752

DOI: 10.1093/dnares/12.1.53

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 16641997

Title: The DNA sequence, annotation and analysis of human chromosome 3.

PubMed ID: 16641997

DOI: 10.1038/nature04728

PubMed ID: 11739414

Title: The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin.

PubMed ID: 11739414

DOI: 10.1083/jcb.200104005

PubMed ID: 11230166

Title: Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.

PubMed ID: 11230166

DOI: 10.1101/gr.gr1547r

PubMed ID: 9437013

Title: Interaction of presenilins with the filamin family of actin-binding proteins.

PubMed ID: 9437013

DOI: 10.1523/jneurosci.18-03-00914.1998

PubMed ID: 8327473

Title: Cloning from the thyroid of a protein related to actin binding protein that is recognized by Graves disease immunoglobulins.

PubMed ID: 8327473

DOI: 10.1073/pnas.90.13.5994

PubMed ID: 10754391

Title: Hepatitis B virus core protein interacts with the C-terminal region of actin-binding protein.

PubMed ID: 10754391

DOI: 10.1159/000025442

PubMed ID: 12393796

Title: Filamin A and filamin B are co-expressed within neurons during periods of neuronal migration and can physically interact.

PubMed ID: 12393796

DOI: 10.1093/hmg/11.23.2845

PubMed ID: 12496242

Title: A new member of the LIM protein family binds to filamin B and localizes at stress fibers.

PubMed ID: 12496242

DOI: 10.1074/jbc.m209339200

PubMed ID: 12525170

Title: The limits of promiscuity: isoform-specific dimerization of filamins.

PubMed ID: 12525170

DOI: 10.1021/bi026501+

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 16076904

Title: The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins.

PubMed ID: 16076904

DOI: 10.1242/jcs.02484

PubMed ID: 11336782

Title: Structural and functional aspects of filamins.

PubMed ID: 11336782

DOI: 10.1016/s0167-4889(01)00072-6

PubMed ID: 11252955

Title: Filamins as integrators of cell mechanics and signalling.

PubMed ID: 11252955

DOI: 10.1038/35052082

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19300455

Title: The E3 ubiquitin ligase specificity subunit ASB2beta is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation.

PubMed ID: 19300455

DOI: 10.1038/cdd.2009.27

PubMed ID: 19270716

Title: ISG15 modification of filamin B negatively regulates the type I interferon-induced JNK signalling pathway.

PubMed ID: 19270716

DOI: 10.1038/embor.2009.23

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 19505475

Title: Disease-associated substitutions in the filamin B actin binding domain confer enhanced actin binding affinity in the absence of major structural disturbance: Insights from the crystal structures of filamin B actin binding domains.

PubMed ID: 19505475

DOI: 10.1016/j.jmb.2009.06.009

PubMed ID: 14991055

Title: Mutations in the gene encoding filamin B disrupt vertebral segmentation, joint formation and skeletogenesis.

PubMed ID: 14991055

DOI: 10.1038/ng1319

PubMed ID: 15994868

Title: Mutations in FLNB cause boomerang dysplasia.

PubMed ID: 15994868

DOI: 10.1136/jmg.2004.029967

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

PubMed ID: 16801345

Title: A molecular and clinical study of Larsen syndrome caused by mutations in FLNB.

PubMed ID: 16801345

DOI: 10.1136/jmg.2006.043687

Sequence Information:

Length: 2602
Mass: 278164
Checksum: 1BF5C64C86360C6A
Sequence:

MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK 
RMYRKYHQRP TFRQMQLENV SVALEFLDRE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH 
YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP 
GLCPDWESWD PQKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA 
KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK 
EEAQVTPDSD KNKTYSVEYL PKVTGLHKVT VLFAGQHISK SPFEVSVDKA QGDASKVTAK 
GPGLEAVGNI ANKPTYFDIY TAGAGVGDIG VEVEDPQGKN TVELLVEDKG NQVYRCVYKP 
MQPGPHVVKI FFAGDTIPKS PFVVQVGEAC NPNACRASGR GLQPKGVRIR ETTDFKVDTK 
AAGSGELGVT MKGPKGLEEL VKQKDFLDGV YAFEYYPSTP GRYSIAITWG GHHIPKSPFE 
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG SLGFAIEGPS QAKIEYNDQN 
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GGYNPDLVRA YGPGLEKSGC 
IVNNLAEFTV DPKDAGKAPL KIFAQDGEGQ RIDIQMKNRM DGTYACSYTP VKAIKHTIAV 
VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG 
IKCDARVLSE DEEDVDFDII HNANDTFTVK YVPPAAGRYT IKVLFASQEI PASPFRVKVD 
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV YTKGAGKAPL NVQFNSPLPG DAVKDLDIID 
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKLN GLENRVEVGK 
DQEFTVDTRG AGGQGKLDVT ILSPSRKVVP CLVTPVTGRE NSTAKFIPRE EGLYAVDVTY 
DGHPVPGSPY TVEASLPPDP SKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP 
CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG 
PGLEHGKVGE AGLLSVDCSE AGPGALGLEA VSDSGTKAEV SIQNNKDGTY AVTYVPLTAG 
MYTLTMKYGG ELVPHFPARV KVEPAVDTSR IKVFGPGIEG KDVFREATTD FTVDSRPLTQ 
VGGDHIKAHI ANPSGASTEC FVTDNADGTY QVEYTPFEKG LHVVEVTYDD VPIPNSPFKV 
AVTEGCQPSR VQAQGPGLKE AFTNKPNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD 
GSCSAEYIPF APGDYDVNIT YGGAHIPGSP FRVPVKDVVD PSKVKIAGPG LGSGVRARVL 
QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YMVSVKYADE 
EIPRSPFKVK VLPTYDASKV TASGPGLSSY GVPASLPVDF AIDARDAGEG LLAVQITDQE 
GKPKRAIVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDDIP LSPYRIRATQ TGDASKCLAT 
GPGIASTVKT GEEVGFVVDA KTAGKGKVTC TVLTPDGTEA EADVIENEDG TYDIFYTAAK 
PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AVEEAPVNAC PPGFRPWVTE EAYVPVSDMN 
GLGFKPFDLV IPFAVRKGEI TGEVHMPSGK TATPEIVDNK DGTVTVRYAP TEVGLHEMHI 
KYMGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG 
PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DSRRCSQVKL 
GSAADFLLDI SETDLSSLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK 
NGNHVANSPV SIMVVQSEIG DARRAKVYGR GLSEGRTFEM SDFIVDTRDA GYGGISLAVE 
GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVKESIT 
RTSRAPSVAT VGSICDLNLK IPEINSSDMS AHVTSPSGRV TEAEIVPMGK NSHCVRFVPQ 
EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGV PAEFSIWTRE 
AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPESPYLVPV 
IAPSDDARRL TVMSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP 
DKYAVRFIPH ENGVHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GTGLEGGTTG 
IQSEFFINTT RAGPGTLSVT IEGPSKVKMD CQETPEGYKV MYTPMAPGNY LISVKYGGPN 
HIVGSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKASS DASKVTSKGA 
GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGNQQYN VTYVVKERGD 
YVLAVKWGEE HIPGSPFHVT VP

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.

Details for: FLNB

Associated with

Cells (max top 100)

Other Information

Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha. PubMed ID: 9651345

A novel human actin-binding protein homologue that binds to platelet glycoprotein Ibalpha. PubMed ID: 9694715

Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits. PubMed ID: 11807098

Genomic structure and fine mapping of the two human filamin gene paralogues FLNB and FLNC and comparative analysis of the filamin gene family. PubMed ID: 11153914

Fine expression profiling of full-length transcripts using a size-unbiased cDNA library prepared with the vector-capping method. PubMed ID: 18487259

Vector-capping: a simple method for preparing a high-quality full-length cDNA library. PubMed ID: 16106752

The full-ORF clone resource of the German cDNA consortium. PubMed ID: 17974005

The DNA sequence, annotation and analysis of human chromosome 3. PubMed ID: 16641997

The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. PubMed ID: 11739414

Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. PubMed ID: 11230166

Interaction of presenilins with the filamin family of actin-binding proteins. PubMed ID: 9437013

Cloning from the thyroid of a protein related to actin binding protein that is recognized by Graves disease immunoglobulins. PubMed ID: 8327473

Hepatitis B virus core protein interacts with the C-terminal region of actin-binding protein. PubMed ID: 10754391

Filamin A and filamin B are co-expressed within neurons during periods of neuronal migration and can physically interact. PubMed ID: 12393796

A new member of the LIM protein family binds to filamin B and localizes at stress fibers. PubMed ID: 12496242

The limits of promiscuity: isoform-specific dimerization of filamins. PubMed ID: 12525170

Proteomic characterization of the human centrosome by protein correlation profiling. PubMed ID: 14654843

The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins. PubMed ID: 16076904

Structural and functional aspects of filamins. PubMed ID: 11336782

Filamins as integrators of cell mechanics and signalling. PubMed ID: 11252955

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

The E3 ubiquitin ligase specificity subunit ASB2beta is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation. PubMed ID: 19300455

ISG15 modification of filamin B negatively regulates the type I interferon-induced JNK signalling pathway. PubMed ID: 19270716

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Disease-associated substitutions in the filamin B actin binding domain confer enhanced actin binding affinity in the absence of major structural disturbance: Insights from the crystal structures of filamin B actin binding domains. PubMed ID: 19505475

Mutations in the gene encoding filamin B disrupt vertebral segmentation, joint formation and skeletogenesis. PubMed ID: 14991055

Mutations in FLNB cause boomerang dysplasia. PubMed ID: 15994868

The consensus coding sequences of human breast and colorectal cancers. PubMed ID: 16959974

A molecular and clinical study of Larsen syndrome caused by mutations in FLNB. PubMed ID: 16801345