Associated with
Cells (max top 100)
(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)
- Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 360.6668
Cell Significance Index: -56.1000 - Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 216.5245
Cell Significance Index: -54.9200 - Cell Name: embryonic stem cell (CL0002322)
Fold Change: 143.8775
Cell Significance Index: -59.2700 - Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 132.6992
Cell Significance Index: -53.9100 - Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 128.9919
Cell Significance Index: -60.9000 - Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 113.1448
Cell Significance Index: -58.2000 - Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 56.8949
Cell Significance Index: -54.3200 - Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 45.6545
Cell Significance Index: -56.2900 - Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 20.0720
Cell Significance Index: -53.7700 - Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 14.4474
Cell Significance Index: -57.0100 - Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 13.7231
Cell Significance Index: -42.1500 - Cell Name: enteric smooth muscle cell (CL0002504)
Fold Change: 7.4914
Cell Significance Index: 39.4200 - Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 6.8372
Cell Significance Index: 126.3700 - Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 3.0537
Cell Significance Index: 89.6900 - Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: 2.1515
Cell Significance Index: 57.5500 - Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 2.1425
Cell Significance Index: 100.7000 - Cell Name: granulosa cell (CL0000501)
Fold Change: 1.6878
Cell Significance Index: 44.3800 - Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 1.5978
Cell Significance Index: 219.4200 - Cell Name: odontoblast (CL0000060)
Fold Change: 1.4904
Cell Significance Index: 191.0600 - Cell Name: early pro-B cell (CL0002046)
Fold Change: 1.3912
Cell Significance Index: 89.7600 - Cell Name: cell in vitro (CL0001034)
Fold Change: 1.2098
Cell Significance Index: 660.6900 - Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 1.1453
Cell Significance Index: 32.8300 - Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 1.0739
Cell Significance Index: 12.2000 - Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.9476
Cell Significance Index: 72.7200 - Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.9279
Cell Significance Index: 410.2500 - Cell Name: oral mucosa squamous cell (CL1001576)
Fold Change: 0.8891
Cell Significance Index: 7.6400 - Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 0.7978
Cell Significance Index: 21.7200 - Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.7267
Cell Significance Index: 138.3000 - Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 0.6220
Cell Significance Index: 13.0200 - Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 0.5501
Cell Significance Index: 7.0500 - Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.5272
Cell Significance Index: 364.6500 - Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: 0.5131
Cell Significance Index: 4.3100 - Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.4286
Cell Significance Index: 30.3100 - Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.4031
Cell Significance Index: 49.5600 - Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.3836
Cell Significance Index: 174.1100 - Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.3078
Cell Significance Index: 277.9500 - Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.3069
Cell Significance Index: 61.5600 - Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.2464
Cell Significance Index: 463.9500 - Cell Name: lactocyte (CL0002325)
Fold Change: 0.1472
Cell Significance Index: 19.0200 - Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.1216
Cell Significance Index: 21.9200 - Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.0832
Cell Significance Index: 13.5400 - Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.0696
Cell Significance Index: 24.9600 - Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: 0.0667
Cell Significance Index: 6.9400 - Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.0514
Cell Significance Index: 10.2100 - Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.0369
Cell Significance Index: 27.9000 - Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.0110
Cell Significance Index: 1.0900 - Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0052
Cell Significance Index: -7.0400 - Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0098
Cell Significance Index: -15.0300 - Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0148
Cell Significance Index: -27.2600 - Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0309
Cell Significance Index: -19.6400 - Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0369
Cell Significance Index: -27.3000 - Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0396
Cell Significance Index: -4.0500 - Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0427
Cell Significance Index: -31.3100 - Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.0467
Cell Significance Index: -1.6400 - Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0485
Cell Significance Index: -30.2800 - Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.0534
Cell Significance Index: -9.1200 - Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.0586
Cell Significance Index: -6.7100 - Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0808
Cell Significance Index: -45.5800 - Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: -0.0845
Cell Significance Index: -9.9600 - Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: -0.1249
Cell Significance Index: -13.5900 - Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -0.1808
Cell Significance Index: -4.5200 - Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.2069
Cell Significance Index: -59.5400 - Cell Name: preadipocyte (CL0002334)
Fold Change: -0.2080
Cell Significance Index: -4.0600 - Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.2272
Cell Significance Index: -47.8600 - Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.2547
Cell Significance Index: -37.0300 - Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -0.2597
Cell Significance Index: -11.7700 - Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.2601
Cell Significance Index: -7.2700 - Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: -0.2943
Cell Significance Index: -5.2000 - Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.3397
Cell Significance Index: -39.5900 - Cell Name: lung endothelial cell (CL1001567)
Fold Change: -0.3421
Cell Significance Index: -17.8200 - Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.3469
Cell Significance Index: -39.6000 - Cell Name: Sertoli cell (CL0000216)
Fold Change: -0.3558
Cell Significance Index: -4.9900 - Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.4087
Cell Significance Index: -25.1200 - Cell Name: gut absorptive cell (CL0000677)
Fold Change: -0.4544
Cell Significance Index: -27.2800 - Cell Name: basal cell of epidermis (CL0002187)
Fold Change: -0.4662
Cell Significance Index: -7.0800 - Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.5013
Cell Significance Index: -8.3900 - Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.5105
Cell Significance Index: -11.0600 - Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.5645
Cell Significance Index: -42.0700 - Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.6114
Cell Significance Index: -34.3100 - Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.6493
Cell Significance Index: -39.8100 - Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: -0.6525
Cell Significance Index: -18.8000 - Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -0.6813
Cell Significance Index: -47.1200 - Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.7012
Cell Significance Index: -55.5400 - Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.7809
Cell Significance Index: -52.5100 - Cell Name: placental villous trophoblast (CL2000060)
Fold Change: -0.7947
Cell Significance Index: -21.2200 - Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.8261
Cell Significance Index: -26.4600 - Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.8588
Cell Significance Index: -40.0400 - Cell Name: monocyte-derived dendritic cell (CL0011031)
Fold Change: -0.8979
Cell Significance Index: -15.4300 - Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.9077
Cell Significance Index: -40.1500 - Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: -0.9097
Cell Significance Index: -9.8900 - Cell Name: peg cell (CL4033014)
Fold Change: -0.9148
Cell Significance Index: -21.1400 - Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.9509
Cell Significance Index: -59.9300 - Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.9700
Cell Significance Index: -50.3900 - Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: -1.0507
Cell Significance Index: -36.5100 - Cell Name: glycinergic neuron (CL1001509)
Fold Change: -1.0802
Cell Significance Index: -56.7200 - Cell Name: lens fiber cell (CL0011004)
Fold Change: -1.1325
Cell Significance Index: -35.8200 - Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -1.1340
Cell Significance Index: -42.9400 - Cell Name: pro-T cell (CL0000827)
Fold Change: -1.1434
Cell Significance Index: -29.2100 - Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -1.3487
Cell Significance Index: -49.5100 - Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -1.3678
Cell Significance Index: -35.1600
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Other Information
Genular Protein ID: 1992089835
Symbol: FLNA_HUMAN
Name: Filamin-A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 2391361
Title: Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring.
PubMed ID: 2391361
PubMed ID: 8088819
Title: The exon-intron organization of the human X-linked gene (FLN1) encoding actin-binding protein 280.
PubMed ID: 8088819
PubMed ID: 8733135
Title: 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.
PubMed ID: 8733135
DOI: 10.1093/hmg/5.5.659
PubMed ID: 20736409
Title: Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins.
PubMed ID: 20736409
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 21697133
Title: Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method.
PubMed ID: 21697133
DOI: 10.1167/iovs.11-7479
PubMed ID: 15772651
PubMed ID: 2248958
Title: Purification of human smooth muscle filamin and characterization of structural domains and functional sites.
PubMed ID: 2248958
DOI: 10.1021/bi00492a019
PubMed ID: 7689010
Title: Mapping of two genes encoding isoforms of the actin binding protein ABP-280, a dystrophin like protein, to Xq28 and to chromosome 7.
PubMed ID: 7689010
DOI: 10.1093/hmg/2.6.761
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
PubMed ID: 9437013
Title: Interaction of presenilins with the filamin family of actin-binding proteins.
PubMed ID: 9437013
PubMed ID: 11102480
Title: Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin.
PubMed ID: 11102480
PubMed ID: 11739414
Title: The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin.
PubMed ID: 11739414
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
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
PubMed ID: 11252955
Title: Filamins as integrators of cell mechanics and signalling.
PubMed ID: 11252955
DOI: 10.1038/35052082
PubMed ID: 16291724
Title: CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration.
PubMed ID: 16291724
DOI: 10.1242/jcs.02660
PubMed ID: 15684392
Title: FOXC1 transcriptional regulatory activity is impaired by PBX1 in a filamin A-mediated manner.
PubMed ID: 15684392
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16299064
Title: A filamin A splice mutation resulting in a syndrome of facial dysmorphism, periventricular nodular heterotopia, and severe constipation reminiscent of cerebro-fronto-facial syndrome.
PubMed ID: 16299064
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: 16862148
Title: FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling.
PubMed ID: 16862148
DOI: 10.1038/ncb1437
PubMed ID: 17357080
Title: Filamin A is mutated in X-linked chronic idiopathic intestinal pseudo-obstruction with central nervous system involvement.
PubMed ID: 17357080
DOI: 10.1086/513321
PubMed ID: 17924679
Title: 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.
PubMed ID: 17924679
DOI: 10.1021/pr070152u
PubMed ID: 18556573
Title: ECSM2, an endothelial specific filamin a binding protein that mediates chemotaxis.
PubMed ID: 18556573
PubMed ID: 18322202
Title: Filamin A stabilizes FcgammaRI surface expression and prevents its lysosomal routing.
PubMed ID: 18322202
PubMed ID: 18220336
Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
PubMed ID: 18220336
DOI: 10.1021/pr0705441
PubMed ID: 19367720
Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.
PubMed ID: 19367720
DOI: 10.1021/pr800500r
PubMed ID: 18088087
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19828450
Title: Identification and characterization of multiple similar ligand-binding repeats in filamin: implication on filamin-mediated receptor clustering and cross-talk.
PubMed ID: 19828450
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20713593
Title: A novel interaction between FlnA and Syk regulates platelet ITAM-mediated receptor signaling and function.
PubMed ID: 20713593
DOI: 10.1084/jem.20100222
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21524097
Title: Evidence for multisite ligand binding and stretching of filamin by integrin and migfilin.
PubMed ID: 21524097
DOI: 10.1021/bi2003229
PubMed ID: 21228480
Title: Identification of novel nuclear protein interactions with the N-terminal part of filamin A.
PubMed ID: 21228480
DOI: 10.1271/bbb.100567
PubMed ID: 21960593
Title: Thrombocytopenia resulting from mutations in filamin A can be expressed as an isolated syndrome.
PubMed ID: 21960593
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22121117
Title: A meckelin-filamin A interaction mediates ciliogenesis.
PubMed ID: 22121117
DOI: 10.1093/hmg/ddr557
PubMed ID: 23890175
Title: Junctional Rab13-binding protein (JRAB) regulates cell spreading via filamins.
PubMed ID: 23890175
DOI: 10.1111/gtc.12078
PubMed ID: 23037936
Title: Congenital short bowel syndrome as the presenting symptom in male patients with FLNA mutations.
PubMed ID: 23037936
DOI: 10.1038/gim.2012.123
PubMed ID: 24052262
Title: ASB2alpha, an E3 ubiquitin ligase specificity subunit, regulates cell spreading and triggers proteasomal degradation of filamins by targeting the filamin calponin homology 1 domain.
PubMed ID: 24052262
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
PubMed ID: 25358863
Title: Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to mediate Sema3A signalling.
PubMed ID: 25358863
DOI: 10.1038/ncomms6325
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 26460884
Title: G Protein-Coupled Receptors Directly Bind Filamin A with High Affinity and Promote Filamin Phosphorylation.
PubMed ID: 26460884
PubMed ID: 25772364
Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.
PubMed ID: 25772364
PubMed ID: 25666618
Title: A mechanism of global shape-dependent recognition and phosphorylation of filamin by protein kinase A.
PubMed ID: 25666618
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 25944712
Title: N-terminome analysis of the human mitochondrial proteome.
PubMed ID: 25944712
PubMed ID: 26766444
Title: Endothelial RSPO3 controls vascular stability and pruning through non-canonical WNT/Ca(2+)/NFAT signaling.
PubMed ID: 26766444
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 30500825
Title: De novo mutations in the GTP/GDP-binding region of RALA, a RAS-like small GTPase, cause intellectual disability and developmental delay.
PubMed ID: 30500825
PubMed ID: 17690686
Title: Structure of three tandem filamin domains reveals auto-inhibition of ligand binding.
PubMed ID: 17690686
PubMed ID: 19923718
Title: Structure of the human filamin A actin-binding domain.
PubMed ID: 19923718
PubMed ID: 19622754
Title: Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin.
PubMed ID: 19622754
PubMed ID: 11532987
Title: Mutations in the X-linked filamin 1 gene cause periventricular nodular heterotopia in males as well as in females.
PubMed ID: 11532987
PubMed ID: 12410386
Title: Bilateral periventricular nodular heterotopia due to filamin 1 gene mutation: widespread glomeruloid microvascular anomaly and dysplastic cytoarchitecture in the cerebral cortex.
PubMed ID: 12410386
PubMed ID: 11914408
Title: Familial periventricular heterotopia: missense and distal truncating mutations of the FLN1 gene.
PubMed ID: 11914408
DOI: 10.1212/wnl.58.6.916
PubMed ID: 12612583
Title: Localized mutations in the gene encoding the cytoskeletal protein filamin A cause diverse malformations in humans.
PubMed ID: 12612583
DOI: 10.1038/ng1119
PubMed ID: 15249610
Title: Germline and mosaic mutations of FLN1 in men with periventricular heterotopia.
PubMed ID: 15249610
PubMed ID: 15654694
Title: A novel 9 bp deletion in the filamin A gene causes an otopalatodigital-spectrum disorder with a variable, intermediate phenotype.
PubMed ID: 15654694
DOI: 10.1002/ajmg.a.30484
PubMed ID: 15940695
Title: A novel filamin A D203Y mutation in a female patient with otopalatodigital type 1 syndrome and extremely skewed X chromosome inactivation.
PubMed ID: 15940695
DOI: 10.1002/ajmg.a.30792
PubMed ID: 15668422
Title: Filamin A mutations cause periventricular heterotopia with Ehlers-Danlos syndrome.
PubMed ID: 15668422
PubMed ID: 16596676
Title: Genotype-epigenotype-phenotype correlations in females with frontometaphyseal dysplasia.
PubMed ID: 16596676
DOI: 10.1002/ajmg.a.31213
PubMed ID: 15994863
Title: Ehlers-Danlos syndrome and periventricular nodular heterotopia in a Spanish family with a single FLNA mutation.
PubMed ID: 15994863
PubMed ID: 17431908
Title: Otopalatodigital syndrome type 2 in two siblings with a novel filamin A 629G>T mutation: clinical, pathological, and molecular findings.
PubMed ID: 17431908
DOI: 10.1002/ajmg.a.31696
PubMed ID: 17632775
Title: Filamin A mutation is one cause of FG syndrome.
PubMed ID: 17632775
DOI: 10.1002/ajmg.a.31751
PubMed ID: 17190868
Title: Mutations in the gene encoding filamin A as a cause for familial cardiac valvular dystrophy.
PubMed ID: 17190868
PubMed ID: 20598277
Title: Terminal osseous dysplasia is caused by a single recurrent mutation in the FLNA gene.
PubMed ID: 20598277
PubMed ID: 20844545
Title: FLNA p.V528M substitution is neither associated with bilateral periventricular nodular heterotopia nor with macrothrombocytopenia.
PubMed ID: 20844545
DOI: 10.1038/jhg.2010.114
PubMed ID: 27193221
Title: Otopalatodigital spectrum disorders: refinement of the phenotypic and mutational spectrum.
PubMed ID: 27193221
DOI: 10.1038/jhg.2016.37
Sequence Information:
- Length: 2647
- Mass: 280739
- Checksum: 6C1A07041DF50142
- Sequence:
MSSSHSRAGQ SAAGAAPGGG VDTRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK LVSIDSKAIV DGNLKLILGL IWTLILHYSI SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL PQLPITNFSR DWQSGRALGA LVDSCAPGLC PDWDSWDASK PVTNAREAMQ QADDWLGIPQ VITPEEIVDP NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV TGTHKVTVLF AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK TTYFEIFTAG AGTGEVEVVI QDPMGQKGTV EPQLEARGDS TYRCSYQPTM EGVHTVHVTF AGVPIPRSPY TVTVGQACNP SACRAVGRGL QPKGVRVKET ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF EYYPMVPGTY IVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGV VGKSADFVVE AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN SEDIRLSPFM ADIRDAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK HGGKAPLRVQ VQDNEGCPVE ALVKDNGNGT YSCSYVPRKP VKHTAMVSWG GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA KTGLKAHEPT YFTVDCAEAG QGDVSIGIKC APGVVGPAEA DIDFDIIRND NDTFTVKYTP RGAGSYTIMV LFADQATPTS PIRVKVEPSH DASKVKAEGP GLSRTGVELG KPTHFTVNAK AAGKGKLDVQ FSGLTKGDAV RDVDIIDHHD NTYTVKYTPV QQGPVGVNVT YGGDPIPKSP FSVAVSPSLD LSKIKVSGLG EKVDVGKDQE FTVKSKGAGG QGKVASKIVG PSGAAVPCKV EPGLGADNSV VRFLPREEGP YEVEVTYDGV PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG SAGSPARFTI DTKGAGTGGL GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF ADTHIPGSPF KAHVVPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE PAVDTSGVQC YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP SGNLTETYVQ DRGDGMYKVE YTPYEEGLHS VDVTYDGSPV PSSPFQVPVT EGCDPSRVRV HGPGIQSGTT NKPNKFTVET RGAGTGGLGL AVEGPSEAKM SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV PVHDVTDASK VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV DNADGTQTVN YVPSREGPYS ISVLYGDEEV PRSPFKVKVL PTHDASKVKA SGPGLNTTGV PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH DGTYTVAYVP DVTGRYTILI KYGGDEIPFS PYRVRAVPTG DASKCTVTVS IGGHGLGAGI GPTIQIGEET VITVDTKAAG KGKVTCTVCT PDGSEVDVDV VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA LAGDQPSVQP PLRSQQLAPQ YTYAQGGQQT WAPERPLVGV NGLDVTSLRP FDLVIPFTIK KGEITGEVRM PSGKVAQPTI TDNKDGTVTV RYAPSEAGLH EMDIRYDNMH IPGSPLQFYV DYVNCGHVTA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL AIEGPSKAEI SCTDNQDGTC SVSYLPVLPG DYSILVKYNE QHVPGSPFTA RVTGDDSMRM SHLKVGSAAD IPINISETDL SLLTATVVPP SGREEPCLLK RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS QSEIGDASRV RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA PSVANVGSHC DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI RFVPAEMGTH TVSVKYKGQH VPGSPFQFTV GPLGEGGAHK VRAGGPGLER AEAGVPAEFS IWTREAGAGG LAIAVEGPSK AEISFEDRKD GSCGVAYVVQ EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL QESGLKVNQP ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGVY LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGNPAEF VVNTSNAGAG ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK YGGPYHIGGS PFKAKVTGPR LVSNHSLHET SSVFVDSLTK ATCAPQHGAP GPGPADASKV VAKGLGLSKA YVGQKSSFTV DCSKAGNNML LVGVHGPRTP CEEILVKHVG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS PYRVVVP
Genular Protein ID: 955271859
Symbol: Q6NXF2_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
Sequence Information:
- Length: 983
- Mass: 104164
- Checksum: 8B944332B1AC27F3
- Sequence:
QIGEETVITV DTKAAGKGKV TCTVCTPDGS EVDVDVVENE DGTFDIFYTA PQPGKYVICV RFGGEHVPNS PFQVTALAGD QPSVQPPLRS QQLAPQYTYA QGGQQTWAPE RPLVGVNGLD VTSLRPFDLV IPFTIKKGEI TGEVRMPSGK VAQPTITDNK DGTVTVRYAP SEAGLHEMDI RYDNMHIPGS PLQFYVDYVN CGHVTAYGPG LTHGVVNKPA TFTVNTKDAG EGGLSLAIEG PSKAEISCTD NQDGTCSVSY LPVLPGDYSI LVKYNEQHVP GSPFTARVTG DDSMRMSHLK VGSAADIPIN ISETDLSLLT ATVVPPSGRE EPCLLKRLRN GHVGISFVPK ETGEHLVHVK KNGQHVASSP IPVVISQSEI GDASRVRVSG QGLHEGHTFE PAEFIIDTRD AGYGGLSLSI EGPSKVDINT EDLEDGTCRV TYCPTEPGNY IINIKFADQH VPGSPFSVKV TGEGRVKESI TRRRRAPSVA NVGSHCDLSL KIPEISIQDM TAQVTSPSGK THEAEIVEGE NHTYCIRFVP AEMGTHTVSV KYKGQHVPGS PFQFTVGPLG EGGAHKVRAG GPGLERAEAG VPAEFSIWTR EAGAGGLAIA VEGPSKAEIS FEDRKDGSCG VAYVVQEPGD YEVSVKFNEE HIPDSPFVVP VASPSGDARR LTVSSLQESG LKVNQPASFA VSLNGAKGAI DAKVHSPSGA LEECYVTEID QDKYAVRFIP RENGVYLIDV KFNGTHIPGS PFKIRVGEPG HGGDPGLVSA YGAGLEGGVT GNPAEFVVNT SNAGAGALSV TIDGPSKVKM DCQECPEGYR VTYTPMAPGS YLISIKYGGP YHIGGSPFKA KVTGPRLVSN HSLHETSSVF VDSLTKATCA PQHGAPGPGP ADASKVVAKG LGLSKAYVGQ KSSFTVDCSK AGNNMLLVGV HGPRTPCEEI LVKHVGSRLY SVSYLLKDKG EYTLVVKWGD EHIPGSPYRV VVP
Genular Protein ID: 3313069639
Symbol: Q60FE5_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 11237011
Title: Initial sequencing and analysis of the human genome.
PubMed ID: 11237011
DOI: 10.1038/35057062
PubMed ID: 15496913
Title: Finishing the euchromatic sequence of the human genome.
PubMed ID: 15496913
DOI: 10.1038/nature03001
PubMed ID: 16106752
Title: Vector-capping: a simple method for preparing a high-quality full-length cDNA library.
PubMed ID: 16106752
PubMed ID: 15772651
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
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: 17924679
Title: 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.
PubMed ID: 17924679
DOI: 10.1021/pr070152u
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
PubMed ID: 18088087
PubMed ID: 18220336
Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
PubMed ID: 18220336
DOI: 10.1021/pr0705441
PubMed ID: 19367720
Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.
PubMed ID: 19367720
DOI: 10.1021/pr800500r
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 25772364
Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.
PubMed ID: 25772364
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 25944712
Title: N-terminome analysis of the human mitochondrial proteome.
PubMed ID: 25944712
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
Sequence Information:
- Length: 2620
- Mass: 278226
- Checksum: 9C1ABFC44B1B32B4
- Sequence:
MPATEKDLAE DAPWKKIQQN TFTRWCNEHL KCVSKRIANL QTDLSDGLRL IALLEVLSQK KMHRKHNQRP TFRQMQLENV SVALEFLDRE SIKLVSIDSK AIVDGNLKLI LGLIWTLILH YSISMPMWDE EEDEEAKKQT PKQRLLGWIQ NKLPQLPITN FSRDWQSGRA LGALVDSCAP GLCPDWDSWD ASKPVTNARE AMQQADDWLG IPQVITPEEI VDPNVDEHSV MTYLSQFPKA KLKPGAPLRP KLNPKKARAY GPGIEPTGNM VKKRAEFTVE TRSAGQGEVL VYVEDPAGHQ EEAKVTANND KNRTFSVWYV PEVTGTHKVT VLFAGQHIAK SPFEVYVDKS QGDASKVTAQ GPGLEPSGNI ANKTTYFEIF TAGAGTGEVE VVIQDPMGQK GTVEPQLEAR GDSTYRCSYQ PTMEGVHTVH VTFAGVPIPR SPYTVTVGQA CNPSACRAVG RGLQPKGVRV KETADFKVYT KGAGSGELKV TVKGPKGEER VKQKDLGDGV YGFEYYPMVP GTYIVTITWG GQNIGRSPFE VKVGTECGNQ KVRAWGPGLE GGVVGKSADF VVEAIGDDVG TLGFSVEGPS QAKIECDDKG DGSCDVRYWP QEAGEYAVHV LCNSEDIRLS PFMADIRDAP QDFHPDRVKA RGPGLEKTGV AVNKPAEFTV DAKHGGKAPL RVQVQDNEGC PVEALVKDNG NGTYSCSYVP RKPVKHTAMV SWGGVSIPNS PFRVNVGAGS HPNKVKVYGP GVAKTGLKAH EPTYFTVDCA EAGQGDVSIG IKCAPGVVGP AEADIDFDII RNDNDTFTVK YTPRGAGSYT IMVLFADQAT PTSPIRVKVE PSHDASKVKA EGPGLSRTGV ELGKPTHFTV NAKAAGKGKL DVQFSGLTKG DAVRDVDIID HHDNTYTVKY TPVQQGPVGV NVTYGGDPIP KSPFSVAVSP SLDLSKIKVS GLGEKVDVGK DQEFTVKSKG AGGQGKVASK IVGPSGAAVP CKVEPGLGAD NSVVRFLPRE EGPYEVEVTY DGVPVPGSPF PLEAVAPTKP SKVKAFGPGL QGGSAGSPAR FTIDTKGAGT GGLGLTVEGP CEAQLECLDN GDGTCSVSYV PTEPGDYNIN ILFADTHIPG SPFKAHVVPC FDASKVKCSG PGLERATAGE VGQFQVDCSS AGSAELTIEI CSEAGLPAEV YIQDHGDGTH TITYIPLCPG AYTVTIKYGG QPVPNFPSKL QVEPAVDTSG VQCYGPGIEG QGVFREATTE FSVDARALTQ TGGPHVKARV ANPSGNLTET YVQDRGDGMY KVEYTPYEEG LHSVDVTYDG SPVPSSPFQV PVTEGCDPSR VRVHGPGIQS GTTNKPNKFT VETRGAGTGG LGLAVEGPSE AKMSCMDNKD GSCSVEYIPY EAGTYSLNVT YGGHQVPGSP FKVPVHDVTD ASKVKCSGPG LSPGMVRANL PQSFQVDTSK AGVAPLQVKV QGPKGLVEPV DVVDNADGTQ TVNYVPSREG PYSISVLYGD EEVPRSPFKV KVLPTHDASK VKASGPGLNT TGVPASLPVE FTIDAKDAGE GLLAVQITDP EGKPKKTHIQ DNHDGTYTVA YVPDVTGRYT ILIKYGGDEI PFSPYRVRAV PTGDASKCTV TVSIGGHGLG AGIGPTIQIG EETVITVDTK AAGKGKVTCT VCTPDGSEVD VDVVENEDGT FDIFYTAPQP GKYVICVRFG GEHVPNSPFQ VTALAGDQPS VQPPLRSQQL APQYTYAQGG QQTWAPERPL VGVNGLDVTS LRPFDLVIPF TIKKGEITGE VRMPSGKVAQ PTITDNKDGT VTVRYAPSEA GLHEMDIRYD NMHIPGSPLQ FYVDYVNCGH VTAYGPGLTH GVVNKPATFT VNTKDAGEGG LSLAIEGPSK AEISCTDNQD GTCSVSYLPV LPGDYSILVK YNEQHVPGSP FTARVTGDDS MRMSHLKVGS AADIPINISE TDLSLLTATV VPPSGREEPC LLKRLRNGHV GISFVPKETG EHLVHVKKNG QHVASSPIPV VISQSEIGDA SRVRVSGQGL HEGHTFEPAE FIIDTRDAGY GGLSLSIEGP SKVDINTEDL EDGTCRVTYC PTEPGNYIIN IKFADQHVPG SPFSVKVTGE GRVKESITRR RRAPSVANVG SHCDLSLKIP EISIQDMTAQ VTSPSGKTHE AEIVEGENHT YCIRFVPAEM GTHTVSVKYK GQHVPGSPFQ FTVGPLGEGG AHKVRAGGPG LERAEAGVPA EFSIWTREAG AGGLAIAVEG PSKAEISFED RKDGSCGVAY VVQEPGDYEV SVKFNEEHIP DSPFVVPVAS PSGDARRLTV SSLQESGLKV NQPASFAVSL NGAKGAIDAK VHSPSGALEE CYVTEIDQDK YAVRFIPREN GVYLIDVKFN GTHIPGSPFK IRVGEPGHGG DPGLVSAYGA GLEGGVTGNP AEFVVNTSNA GAGALSVTID GPSKVKMDCQ ECPEGYRVTY TPMAPGSYLI SIKYGGPYHI GGSPFKAKVT GPRLVSNHSL HETSSVFVDS LTKATCAPQH GAPGPGPADA SKVVAKGLGL SKAYVGQKSS FTVDCSKAGN NMLLVGVHGP RTPCEEILVK HVGSRLYSVS YLLKDKGEYT LVVKWGDEHI PGSPYRVVVP
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. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.