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O75369

- FLNB_HUMAN

UniProt

O75369 - FLNB_HUMAN

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Protein

Filamin-B

Gene

FLNB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: ProtInc
  2. cell differentiation Source: UniProtKB-KW
  3. cytokine-mediated signaling pathway Source: Reactome
  4. cytoskeletal anchoring at plasma membrane Source: ProtInc
  5. signal transduction Source: ProtInc
  6. skeletal muscle tissue development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Myogenesis

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
SignaLinkiO75369.

Names & Taxonomyi

Protein namesi
Recommended name:
Filamin-B
Short name:
FLN-B
Alternative name(s):
ABP-278
ABP-280 homolog
Actin-binding-like protein
Beta-filamin
Filamin homolog 1
Short name:
Fh1
Filamin-3
Thyroid autoantigen
Truncated actin-binding protein
Short name:
Truncated ABP
Gene namesi
Name:FLNB
Synonyms:FLN1L, FLN3, TABP, TAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:3755. FLNB.

Subcellular locationi

Isoform 1 : Cytoplasmcell cortex. Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ line
Note: In differentiating myotubes, isoform 1, isoform 2 and isoform 3 are localized diffusely throughout the cytoplasm with regions of enrichment at the longitudinal actin stress fiber. In differentiated tubes, isoform 1 is also detected within the Z-lines.
Isoform 2 : Cytoplasmcytoskeleton
Note: Predominantly localized at actin stress fibers.
Isoform 3 : Cytoplasmcytoskeleton
Note: Predominantly localized at actin stress fibers.
Isoform 6 : Cytoplasmcytoskeleton
Note: Polarized at the periphery of myotubes.

GO - Cellular componenti

  1. actin cytoskeleton Source: ProtInc
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. integral component of membrane Source: UniProtKB
  7. plasma membrane Source: HPA
  8. stress fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Interaction with FLNA may compensate for dysfunctional FLNA homodimer in the periventricular nodular heterotopia (PVNH) disorder.
Atelosteogenesis 1 (AO1) [MIM:108720]: A lethal chondrodysplasia characterized by distal hypoplasia of the humeri and femurs, hypoplasia of the mid-thoracic spine, occasionally complete lack of ossification of single hand bones, and the finding in cartilage of multiple degenerated chondrocytes which are encapsulated in fibrous tissue.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731A → V in AO1. 1 Publication
Corresponds to variant rs28937586 [ dbSNP | Ensembl ].
VAR_033072
Natural varianti188 – 1881S → P in AO1. 1 Publication
VAR_033073
Natural varianti202 – 2021M → V in AO1 and AO3. 1 Publication
Corresponds to variant rs28939707 [ dbSNP | Ensembl ].
VAR_033074
Atelosteogenesis 3 (AO3) [MIM:108721]: A short-limb lethal skeletal dysplasia with vertebral abnormalities, disharmonious skeletal maturation, poorly modeled long bones and joint dislocations. Recurrent respiratory insufficiency and/or infections usually result in early death.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti202 – 2021M → V in AO1 and AO3. 1 Publication
Corresponds to variant rs28939707 [ dbSNP | Ensembl ].
VAR_033074
Natural varianti751 – 7511G → R in AO3. 1 Publication
Corresponds to variant rs28937587 [ dbSNP | Ensembl ].
VAR_033080
Boomerang dysplasia (BOOMD) [MIM:112310]: A perinatal lethal osteochondrodysplasia characterized by absence or underossification of the limb bones and vertebrae. Patients manifest dwarfism with short, bowed, rigid limbs and characteristic facies. Boomerang dysplasia is distinguished from atelosteogenesis on the basis of a more severe defect in mineralization, with complete absence of ossification in some limb elements and vertebral segments.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711L → R in BOOMD. 1 Publication
VAR_033071
Natural varianti235 – 2351S → P in BOOMD. 1 Publication
VAR_033077
Larsen syndrome (LRS) [MIM:150250]: An osteochondrodysplasia characterized by large-joint dislocations and characteristic craniofacial abnormalities. The cardinal features of the condition are dislocations of the hip, knee and elbow joints, with equinovarus or equinovalgus foot deformities. Spatula-shaped fingers, most marked in the thumb, are also present. Craniofacial anomalies include hypertelorism, prominence of the forehead, a depressed nasal bridge, and a flattened midface. Cleft palate and short stature are often associated features. Spinal anomalies include scoliosis and cervical kyphosis. Hearing loss is a well-recognized complication.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti161 – 1611F → C in LRS. 2 Publications
VAR_033069
Natural varianti168 – 1681G → S in LRS. 1 Publication
VAR_033070
Natural varianti227 – 2271E → K in LRS. 2 Publications
VAR_033075
Natural varianti234 – 2341L → V in LRS. 1 Publication
VAR_033076
Natural varianti361 – 3611G → S in LRS. 1 Publication
VAR_033078
Natural varianti363 – 3631G → E in LRS. 1 Publication
VAR_033079
Natural varianti1431 – 14311L → R in LRS. 1 Publication
VAR_033081
Natural varianti1571 – 15711Missing in LRS. 2 Publications
VAR_033082
Natural varianti1586 – 15861G → R in LRS. 2 Publications
Corresponds to variant rs28939706 [ dbSNP | Ensembl ].
VAR_033083
Natural varianti1592 – 15921V → D in LRS. 1 Publication
VAR_033084
Natural varianti1603 – 16031P → L in LRS. 1 Publication
VAR_033085
Natural varianti1691 – 16911G → S in LRS. 2 Publications
VAR_033086
Natural varianti1834 – 18341G → R in LRS. 1 Publication
VAR_033087
Spondylocarpotarsal synostosis syndrome (SCT) [MIM:272460]: Disorder characterized by short stature and vertebral, carpal and tarsal fusions.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2468 – 24681K → R: Cytoplasmic localization. 1 Publication

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi108720. phenotype.
108721. phenotype.
112310. phenotype.
150250. phenotype.
272460. phenotype.
Orphaneti1190. Atelosteogenesis type I.
56305. Atelosteogenesis type III.
503. Autosomal dominant Larsen syndrome.
1263. Boomerang dysplasia.
3275. Spondylocarpotarsal synostosis.
PharmGKBiPA28173.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26022602Filamin-BPRO_0000087298Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei519 – 5191Phosphothreonine2 Publications
Modified residuei681 – 6811N6-acetyllysine1 Publication
Modified residuei730 – 7301Phosphoserine1 Publication
Modified residuei886 – 8861Phosphoserine1 Publication
Modified residuei932 – 9321Phosphoserine1 Publication
Modified residuei983 – 9831Phosphoserine4 Publications
Modified residuei1028 – 10281Phosphoserine1 Publication
Modified residuei1316 – 13161Phosphoserine2 Publications
Modified residuei1433 – 14331Phosphoserine1 Publication
Modified residuei1505 – 15051Phosphoserine1 Publication
Modified residuei1602 – 16021Phosphoserine1 Publication
Modified residuei1780 – 17801N6-acetyllysineBy similarity
Modified residuei2083 – 20831Phosphoserine1 Publication
Modified residuei2107 – 21071Phosphoserine1 Publication
Modified residuei2369 – 23691Phosphoserine1 Publication
Modified residuei2465 – 24651Phosphoserine1 Publication
Cross-linki2468 – 2468Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
Modified residuei2478 – 24781Phosphoserine3 Publications
Modified residuei2481 – 24811Phosphoserine1 Publication
Modified residuei2518 – 25181N6-succinyllysineBy similarity
Modified residuei2524 – 25241N6-succinyllysineBy similarity
Modified residuei2576 – 25761N6-acetyllysine1 Publication

Post-translational modificationi

ISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling.1 Publication
Ubiquitination by a SCF-like complex containing ASB2 isoform 2 leads to proteasomal degradation which promotes muscle differentiation.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO75369.
PaxDbiO75369.
PRIDEiO75369.

PTM databases

PhosphoSiteiO75369.

Expressioni

Tissue specificityi

Ubiquitous. Isoform 1 and isoform 2 are expressed in placenta, bone marrow, brain, umbilical vein endothelial cells (HUVEC), retina and skeletal muscle. Isoform 1 is predominantly expressed in prostate, uterus, liver, thyroid, stomach, lymph node, small intestine, spleen, skeletal muscle, kidney, placenta, pancreas, heart, lung, platelets, endothelial cells, megakaryocytic and erythroleukemic cell lines. Isoform 2 is predominantly expressed in spinal cord, platelet and Daudi cells. Also expressed in thyroid adenoma, neurofibrillary tangles (NFT), senile plaques in the hippocampus and cerebral cortex in Alzheimer disease (AD). Isoform 3 and isoform 6 are expressed predominantly in lung, heart, skeletal muscle, testis, spleen, thymus and leukocytes. Isoform 4 and isoform 5 are expressed in heart.4 Publications

Gene expression databases

BgeeiO75369.
ExpressionAtlasiO75369. baseline and differential.
GenevestigatoriO75369.

Organism-specific databases

HPAiCAB019322.
HPA004747.
HPA004886.

Interactioni

Subunit structurei

Homodimer. Interacts with MICALL2 By similarity. Isoform 1 interacts with FBLP1, FLNA, FLNC, GP1BA, INPPL1, ITGB1A, PSEN1 and PSEN2. Isoform 3 interacts with ITGB1A, ITGB1D, ITGB3 and ITGB6. Interacts with MYOT and MYOZ1. Interacts with HBV capsid protein.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-352089,EBI-352089
FLNAP213335EBI-352089,EBI-350432
GRB2P629932EBI-352089,EBI-401755
ISG15P051614EBI-352089,EBI-746466
MAP3K1Q132332EBI-352089,EBI-49776
MAP3K4Q9Y6R42EBI-352089,EBI-448104
NCK1P163333EBI-352089,EBI-389883
RAC1P630002EBI-352089,EBI-413628

Protein-protein interaction databases

BioGridi108606. 54 interactions.
IntActiO75369. 29 interactions.
MINTiMINT-4998813.

Structurei

Secondary structure

1
2602
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 106
Helixi13 – 164
Helixi17 – 3014
Helixi31 – 333
Turni40 – 467
Helixi48 – 5811
Helixi73 – 8917
Helixi99 – 1035
Helixi107 – 12216
Helixi141 – 15212
Helixi163 – 1653
Helixi169 – 17810
Helixi186 – 1883
Helixi194 – 20815
Helixi217 – 2204
Helixi227 – 2348
Helixi236 – 2394
Helixi254 – 2563
Beta strandi258 – 2614
Helixi262 – 2643
Beta strandi265 – 2673
Beta strandi275 – 2806
Turni282 – 2843
Beta strandi289 – 2946
Beta strandi300 – 3023
Beta strandi304 – 3096
Beta strandi313 – 3197
Beta strandi323 – 33311
Beta strandi342 – 3476
Helixi1040 – 10423
Beta strandi1044 – 10474
Helixi1048 – 10514
Beta strandi1052 – 10543
Beta strandi1059 – 10646
Turni1066 – 10683
Beta strandi1073 – 10775
Beta strandi1079 – 10813
Beta strandi1084 – 10896
Beta strandi1091 – 110010
Beta strandi1102 – 111514
Beta strandi1122 – 11287
Helixi1133 – 11353
Beta strandi1136 – 11405
Helixi1141 – 11433
Beta strandi1154 – 11607
Beta strandi1166 – 11727
Turni1173 – 11753
Beta strandi1179 – 11846
Beta strandi1188 – 11958
Beta strandi1200 – 12089
Beta strandi1217 – 12237
Beta strandi1232 – 12354
Helixi1236 – 12394
Beta strandi1249 – 12546
Beta strandi1256 – 12583
Beta strandi1273 – 12753
Beta strandi1281 – 12844
Beta strandi1286 – 12949
Beta strandi1300 – 131011
Beta strandi1317 – 13215
Beta strandi1332 – 13354
Helixi1336 – 13394
Beta strandi1347 – 13526
Turni1354 – 13563
Beta strandi1361 – 13699
Beta strandi1374 – 13774
Beta strandi1379 – 13813
Beta strandi1383 – 13875
Beta strandi1393 – 14019
Beta strandi1410 – 14167
Beta strandi1425 – 14284
Turni1429 – 14313
Beta strandi1441 – 14466
Turni1448 – 14503
Beta strandi1455 – 14606
Beta strandi1462 – 14643
Beta strandi1475 – 14839
Beta strandi1489 – 150113
Beta strandi1506 – 15127
Helixi1517 – 15193
Beta strandi1520 – 15245
Helixi1525 – 15273
Beta strandi1538 – 15469
Beta strandi1566 – 15705
Beta strandi1573 – 15808
Beta strandi1586 – 15905
Beta strandi1593 – 15964
Beta strandi1603 – 16097
Beta strandi1618 – 16214
Helixi1622 – 16243
Beta strandi1625 – 163915
Beta strandi1641 – 16433
Beta strandi1648 – 16536
Beta strandi1663 – 16664
Beta strandi1672 – 16776
Beta strandi1682 – 169211
Beta strandi1699 – 17057
Beta strandi1748 – 17503
Beta strandi1759 – 17657
Beta strandi1775 – 17784
Beta strandi1780 – 17823
Beta strandi1784 – 17874
Beta strandi1792 – 180413
Beta strandi1811 – 18166
Beta strandi1825 – 18284
Helixi1829 – 18324
Beta strandi1833 – 18353
Beta strandi1840 – 18456
Beta strandi1854 – 18629
Beta strandi1872 – 188110
Beta strandi1888 – 189811
Beta strandi1903 – 19097
Beta strandi1924 – 19274
Beta strandi1941 – 19433
Beta strandi1952 – 19576
Turni1958 – 19603
Beta strandi1961 – 19666
Beta strandi1972 – 19776
Beta strandi1979 – 19846
Beta strandi1989 – 19946
Beta strandi1997 – 19993
Helixi2002 – 20043
Beta strandi2006 – 20105
Turni2011 – 20133
Beta strandi2014 – 20163
Beta strandi2021 – 20266
Turni2028 – 20303
Beta strandi2035 – 20439
Beta strandi2057 – 20615
Beta strandi2067 – 207711
Beta strandi2084 – 20907
Beta strandi2111 – 21133
Beta strandi2118 – 21203
Helixi2126 – 21283
Beta strandi2130 – 21345
Beta strandi2140 – 21423
Beta strandi2144 – 21474
Beta strandi2149 – 21579
Beta strandi2164 – 217512
Beta strandi2180 – 21856
Helixi2193 – 21953
Turni2201 – 22033
Beta strandi2206 – 22083
Beta strandi2210 – 22145
Beta strandi2219 – 22213
Beta strandi2226 – 22349
Beta strandi2236 – 22405
Beta strandi2250 – 22567
Beta strandi2258 – 22669
Beta strandi2275 – 22817
Beta strandi2288 – 22947
Beta strandi2306 – 23149
Beta strandi2320 – 23245
Beta strandi2330 – 23323
Beta strandi2334 – 23374
Beta strandi2340 – 23478
Beta strandi2352 – 236514
Beta strandi2370 – 23756
Turni2384 – 23863
Beta strandi2388 – 23925
Turni2393 – 23953
Beta strandi2403 – 24086
Turni2410 – 24123
Beta strandi2417 – 24259
Beta strandi2430 – 24334
Beta strandi2435 – 24428
Beta strandi2448 – 245912
Beta strandi2466 – 24738
Turni2512 – 25143
Beta strandi2516 – 25194
Helixi2520 – 25234
Beta strandi2531 – 25366
Turni2538 – 25403
Beta strandi2545 – 25473
Beta strandi2557 – 25659
Beta strandi2568 – 25747
Beta strandi2579 – 25835
Beta strandi2585 – 25917
Beta strandi2596 – 26016

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DI8NMR-A1999-2096[»]
2DI9NMR-A1017-1134[»]
2DIANMR-A1130-1229[»]
2DIBNMR-A1215-1329[»]
2DICNMR-A1325-1422[»]
2DJ4NMR-A1418-1518[»]
2DLGNMR-A2104-2192[»]
2DMBNMR-A1611-1721[»]
2DMCNMR-A1899-2001[»]
2E9INMR-A2094-2192[»]
2E9JNMR-A1504-1615[»]
2EE6NMR-A2190-2287[»]
2EE9NMR-A1736-1823[»]
2EEANMR-A1808-1915[»]
2EEBNMR-A2284-2382[»]
2EECNMR-A2371-2488[»]
2EEDNMR-A2509-2602[»]
2WA5X-ray1.90A2-242[»]
2WA6X-ray1.95A2-242[»]
2WA7X-ray1.85A2-242[»]
3FERX-ray2.40A/B/C/D1-252[»]
4B7LX-ray2.05A/B1-347[»]
ProteinModelPortaliO75369.
SMRiO75369. Positions 13-347, 450-739, 1017-1723, 1735-2488, 2511-2602.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75369.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 239239Actin-bindingAdd
BLAST
Domaini16 – 122107CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini139 – 239101CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati249 – 34799Filamin 1Add
BLAST
Repeati349 – 44698Filamin 2Add
BLAST
Repeati447 – 54397Filamin 3Add
BLAST
Repeati544 – 63693Filamin 4Add
BLAST
Repeati640 – 73697Filamin 5Add
BLAST
Repeati737 – 839103Filamin 6Add
BLAST
Repeati840 – 93899Filamin 7Add
BLAST
Repeati939 – 103496Filamin 8Add
BLAST
Repeati1035 – 112793Filamin 9Add
BLAST
Repeati1128 – 122295Filamin 10Add
BLAST
Repeati1223 – 1322100Filamin 11Add
BLAST
Repeati1323 – 141593Filamin 12Add
BLAST
Repeati1416 – 151196Filamin 13Add
BLAST
Repeati1512 – 160897Filamin 14Add
BLAST
Repeati1609 – 170496Filamin 15Add
BLAST
Repeati1729 – 181385Filamin 16Add
BLAST
Repeati1816 – 190893Filamin 17Add
BLAST
Repeati1919 – 199476Filamin 18Add
BLAST
Repeati1997 – 208993Filamin 19Add
BLAST
Repeati2091 – 218595Filamin 20Add
BLAST
Repeati2188 – 228093Filamin 21Add
BLAST
Repeati2282 – 237594Filamin 22Add
BLAST
Repeati2379 – 247193Filamin 23Add
BLAST
Repeati2507 – 260195Filamin 24Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1128 – 1511384Interaction with FBLP1Add
BLAST
Regioni1705 – 172824Hinge 1By similarityAdd
BLAST
Regioni1862 – 2148287Interaction with the cytoplasmic tail of GP1BAAdd
BLAST
Regioni2060 – 2225166Interaction with FLNA 1Add
BLAST
Regioni2130 – 2602473Interaction with INPPL1Add
BLAST
Regioni2472 – 2602131Self-association site, tailBy similarityAdd
BLAST
Regioni2472 – 250635Hinge 2By similarityAdd
BLAST
Regioni2507 – 260296Interaction with FLNA 2Add
BLAST

Domaini

Comprised of a NH2-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. The first hinge region prevents binding to ITGA and ITGB subunits.

Sequence similaritiesi

Belongs to the filamin family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 24 filamin repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00660000095431.
HOGENOMiHOG000044235.
HOVERGENiHBG004163.
InParanoidiO75369.
KOiK04437.
OMAiDQEGKPK.
OrthoDBiEOG76T9QC.
PhylomeDBiO75369.
TreeFamiTF313685.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75369-1) [UniParc]FASTAAdd to Basket

Also known as: ABP-278

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.

« Hide

        10         20         30         40         50
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL
60 70 80 90 100
IALLEVLSQK RMYRKYHQRP TFRQMQLENV SVALEFLDRE SIKLVSIDSK
110 120 130 140 150
AIVDGNLKLI LGLVWTLILH YSISMPVWED EGDDDAKKQT PKQRLLGWIQ
160 170 180 190 200
NKIPYLPITN FNQNWQDGKA LGALVDSCAP GLCPDWESWD PQKPVDNARE
210 220 230 240 250
AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA KLKPGAPLKP
260 270 280 290 300
KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK
310 320 330 340 350
EEAQVTPDSD KNKTYSVEYL PKVTGLHKVT VLFAGQHISK SPFEVSVDKA
360 370 380 390 400
QGDASKVTAK GPGLEAVGNI ANKPTYFDIY TAGAGVGDIG VEVEDPQGKN
410 420 430 440 450
TVELLVEDKG NQVYRCVYKP MQPGPHVVKI FFAGDTIPKS PFVVQVGEAC
460 470 480 490 500
NPNACRASGR GLQPKGVRIR ETTDFKVDTK AAGSGELGVT MKGPKGLEEL
510 520 530 540 550
VKQKDFLDGV YAFEYYPSTP GRYSIAITWG GHHIPKSPFE VQVGPEAGMQ
560 570 580 590 600
KVRAWGPGLH GGIVGRSADF VVESIGSEVG SLGFAIEGPS QAKIEYNDQN
610 620 630 640 650
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GGYNPDLVRA
660 670 680 690 700
YGPGLEKSGC IVNNLAEFTV DPKDAGKAPL KIFAQDGEGQ RIDIQMKNRM
710 720 730 740 750
DGTYACSYTP VKAIKHTIAV VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP
760 770 780 790 800
GVERSGLKAN EPTHFTVDCT EAGEGDVSVG IKCDARVLSE DEEDVDFDII
810 820 830 840 850
HNANDTFTVK YVPPAAGRYT IKVLFASQEI PASPFRVKVD PSHDASKVKA
860 870 880 890 900
EGPGLSKAGV ENGKPTHFTV YTKGAGKAPL NVQFNSPLPG DAVKDLDIID
910 920 930 940 950
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKLN
960 970 980 990 1000
GLENRVEVGK DQEFTVDTRG AGGQGKLDVT ILSPSRKVVP CLVTPVTGRE
1010 1020 1030 1040 1050
NSTAKFIPRE EGLYAVDVTY DGHPVPGSPY TVEASLPPDP SKVKAHGPGL
1060 1070 1080 1090 1100
EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP CEAKIECSDN GDGTCSVSYL
1110 1120 1130 1140 1150
PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG PGLEHGKVGE
1160 1170 1180 1190 1200
AGLLSVDCSE AGPGALGLEA VSDSGTKAEV SIQNNKDGTY AVTYVPLTAG
1210 1220 1230 1240 1250
MYTLTMKYGG ELVPHFPARV KVEPAVDTSR IKVFGPGIEG KDVFREATTD
1260 1270 1280 1290 1300
FTVDSRPLTQ VGGDHIKAHI ANPSGASTEC FVTDNADGTY QVEYTPFEKG
1310 1320 1330 1340 1350
LHVVEVTYDD VPIPNSPFKV AVTEGCQPSR VQAQGPGLKE AFTNKPNVFT
1360 1370 1380 1390 1400
VVTRGAGIGG LGITVEGPSE SKINCRDNKD GSCSAEYIPF APGDYDVNIT
1410 1420 1430 1440 1450
YGGAHIPGSP FRVPVKDVVD PSKVKIAGPG LGSGVRARVL QSFTVDSSKA
1460 1470 1480 1490 1500
GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YMVSVKYADE
1510 1520 1530 1540 1550
EIPRSPFKVK VLPTYDASKV TASGPGLSSY GVPASLPVDF AIDARDAGEG
1560 1570 1580 1590 1600
LLAVQITDQE GKPKRAIVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDDIP
1610 1620 1630 1640 1650
LSPYRIRATQ TGDASKCLAT GPGIASTVKT GEEVGFVVDA KTAGKGKVTC
1660 1670 1680 1690 1700
TVLTPDGTEA EADVIENEDG TYDIFYTAAK PGTYVIYVRF GGVDIPNSPF
1710 1720 1730 1740 1750
TVMATDGEVT AVEEAPVNAC PPGFRPWVTE EAYVPVSDMN GLGFKPFDLV
1760 1770 1780 1790 1800
IPFAVRKGEI TGEVHMPSGK TATPEIVDNK DGTVTVRYAP TEVGLHEMHI
1810 1820 1830 1840 1850
KYMGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG
1860 1870 1880 1890 1900
EGGLDLAIEG PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP
1910 1920 1930 1940 1950
GSPFTAKITD DSRRCSQVKL GSAADFLLDI SETDLSSLTA SIKAPSGRDE
1960 1970 1980 1990 2000
PCLLKRLPNN HIGISFIPRE VGEHLVSIKK NGNHVANSPV SIMVVQSEIG
2010 2020 2030 2040 2050
DARRAKVYGR GLSEGRTFEM SDFIVDTRDA GYGGISLAVE GPSKVDIQTE
2060 2070 2080 2090 2100
DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVKESIT
2110 2120 2130 2140 2150
RTSRAPSVAT VGSICDLNLK IPEINSSDMS AHVTSPSGRV TEAEIVPMGK
2160 2170 2180 2190 2200
NSHCVRFVPQ EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG
2210 2220 2230 2240 2250
PGLERGEAGV PAEFSIWTRE AGAGGLSIAV EGPSKAEITF DDHKNGSCGV
2260 2270 2280 2290 2300
SYIAQEPGNY EVSIKFNDEH IPESPYLVPV IAPSDDARRL TVMSLQESGL
2310 2320 2330 2340 2350
KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP DKYAVRFIPH
2360 2370 2380 2390 2400
ENGVHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GTGLEGGTTG
2410 2420 2430 2440 2450
IQSEFFINTT RAGPGTLSVT IEGPSKVKMD CQETPEGYKV MYTPMAPGNY
2460 2470 2480 2490 2500
LISVKYGGPN HIVGSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET
2510 2520 2530 2540 2550
CYSAIPKASS DASKVTSKGA GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH
2560 2570 2580 2590 2600
GPTTPCEEVS MKHVGNQQYN VTYVVKERGD YVLAVKWGEE HIPGSPFHVT

VP
Length:2,602
Mass (Da):278,164
Last modified:May 18, 2010 - v2
Checksum:i1BF5C64C86360C6A
GO
Isoform 2 (identifier: O75369-2) [UniParc]FASTAAdd to Basket

Also known as: ABP-276

The sequence of this isoform differs from the canonical sequence as follows:
     1704-1727: Missing.

Note: May be due to exon skipping.

Show »
Length:2,578
Mass (Da):275,668
Checksum:i4E51115028A676F8
GO
Isoform 3 (identifier: O75369-3) [UniParc]FASTAAdd to Basket

Also known as: Var-1

The sequence of this isoform differs from the canonical sequence as follows:
     2081-2121: Missing.

Note: May be due to exon skipping.

Show »
Length:2,561
Mass (Da):273,909
Checksum:iA367021E1BCF1EF1
GO
Isoform 7 (identifier: O75369-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: Missing.
     170-181: ALGALVDSCAPG → MQEHSTRRRSLS
     1717-1727: Missing.

Show »
Length:2,422
Mass (Da):257,551
Checksum:i8BB43D0D58E153B1
GO
Isoform 4 (identifier: O75369-4) [UniParc]FASTAAdd to Basket

Also known as: Var-3

The sequence of this isoform differs from the canonical sequence as follows:
     2123-2150: EINSSDMSAHVTSPSGRVTEAEIVPMGK → GVRVMNCSAQILWGWRVQFHTGSRNQQQ
     2151-2602: Missing.

Show »
Length:2,150
Mass (Da):230,788
Checksum:iB1FDAE6F0E99947C
GO
Isoform 5 (identifier: O75369-5) [UniParc]FASTAAdd to Basket

Also known as: Var-2

The sequence of this isoform differs from the canonical sequence as follows:
     2123-2146: EINSSDMSAHVTSPSGRVTEAEIV → GVRVMNCSAQILWGWRVQFHTGSR
     2147-2602: Missing.

Note: May be due to competing donor splice sites.

Show »
Length:2,146
Mass (Da):230,289
Checksum:i0E99947C9734D59E
GO
Isoform 6 (identifier: O75369-6) [UniParc]FASTAAdd to Basket

Also known as: Var-1-DeltaH1

The sequence of this isoform differs from the canonical sequence as follows:
     1704-1727: Missing.
     2081-2121: Missing.

Note: May be due to exon skipping.

Show »
Length:2,537
Mass (Da):271,413
Checksum:iDABD7554C44F38DA
GO
Isoform 8 (identifier: O75369-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1463-1463: R → RADDTDSQSWRSPLKALSEFFKGDPKGDFNKT

Show »
Length:2,633
Mass (Da):281,635
Checksum:i8D8F7817049EECA1
GO
Isoform 9 (identifier: O75369-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1717-1727: Missing.

Note: No experimental confirmation available.

Show »
Length:2,591
Mass (Da):276,939
Checksum:i2D9AF6AF4D1469EF
GO

Sequence cautioni

The sequence AAA35505.1 differs from that shown. Reason: Frameshift at positions 2432 and 2589.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti816 – 8161A → T in CAE46040. (PubMed:17974005)Curated
Sequence conflicti924 – 9241Y → H in CAE46040. (PubMed:17974005)Curated
Sequence conflicti1411 – 14111F → L in CAE46040. (PubMed:17974005)Curated
Sequence conflicti1560 – 15601E → G in CAE46040. (PubMed:17974005)Curated
Sequence conflicti1953 – 19531L → F in AAF97046. (PubMed:11153914)Curated
Sequence conflicti2006 – 20061K → R in AAC33845. (PubMed:9694715)Curated
Sequence conflicti2099 – 20991I → S in CAE46040. (PubMed:17974005)Curated
Sequence conflicti2170 – 21701K → N in AAF97046. (PubMed:11153914)Curated
Sequence conflicti2293 – 22931M → V in AAF97046. (PubMed:11153914)Curated
Sequence conflicti2293 – 22931M → V in CAE46040. (PubMed:17974005)Curated
Sequence conflicti2354 – 23541V → A in CAB70818. (PubMed:11230166)Curated
Sequence conflicti2487 – 24871S → C in AAA35505. (PubMed:8327473)Curated
Sequence conflicti2571 – 25711V → A in CAB70818. (PubMed:11230166)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti161 – 1611F → C in LRS. 2 Publications
VAR_033069
Natural varianti168 – 1681G → S in LRS. 1 Publication
VAR_033070
Natural varianti171 – 1711L → R in BOOMD. 1 Publication
VAR_033071
Natural varianti173 – 1731A → V in AO1. 1 Publication
Corresponds to variant rs28937586 [ dbSNP | Ensembl ].
VAR_033072
Natural varianti188 – 1881S → P in AO1. 1 Publication
VAR_033073
Natural varianti202 – 2021M → V in AO1 and AO3. 1 Publication
Corresponds to variant rs28939707 [ dbSNP | Ensembl ].
VAR_033074
Natural varianti227 – 2271E → K in LRS. 2 Publications
VAR_033075
Natural varianti234 – 2341L → V in LRS. 1 Publication
VAR_033076
Natural varianti235 – 2351S → P in BOOMD. 1 Publication
VAR_033077
Natural varianti361 – 3611G → S in LRS. 1 Publication
VAR_033078
Natural varianti363 – 3631G → E in LRS. 1 Publication
VAR_033079
Natural varianti566 – 5661R → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_035917
Natural varianti663 – 6631N → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035918
Natural varianti703 – 7031T → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035919
Natural varianti751 – 7511G → R in AO3. 1 Publication
Corresponds to variant rs28937587 [ dbSNP | Ensembl ].
VAR_033080
Natural varianti1018 – 10181V → M.
Corresponds to variant rs2276742 [ dbSNP | Ensembl ].
VAR_017182
Natural varianti1157 – 11571D → N.3 Publications
Corresponds to variant rs1131356 [ dbSNP | Ensembl ].
VAR_017183
Natural varianti1179 – 11791E → K.
Corresponds to variant rs17058845 [ dbSNP | Ensembl ].
VAR_031392
Natural varianti1431 – 14311L → R in LRS. 1 Publication
VAR_033081
Natural varianti1471 – 14711V → M.3 Publications
Corresponds to variant rs12632456 [ dbSNP | Ensembl ].
VAR_031393
Natural varianti1534 – 15341A → G in a breast cancer sample; somatic mutation. 1 Publication
VAR_035920
Natural varianti1571 – 15711Missing in LRS. 2 Publications
VAR_033082
Natural varianti1586 – 15861G → R in LRS. 2 Publications
Corresponds to variant rs28939706 [ dbSNP | Ensembl ].
VAR_033083
Natural varianti1592 – 15921V → D in LRS. 1 Publication
VAR_033084
Natural varianti1603 – 16031P → L in LRS. 1 Publication
VAR_033085
Natural varianti1691 – 16911G → S in LRS. 2 Publications
VAR_033086
Natural varianti1834 – 18341G → R in LRS. 1 Publication
VAR_033087

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 169169Missing in isoform 7. 1 PublicationVSP_024113Add
BLAST
Alternative sequencei170 – 18112ALGAL…SCAPG → MQEHSTRRRSLS in isoform 7. 1 PublicationVSP_024114Add
BLAST
Alternative sequencei1463 – 14631R → RADDTDSQSWRSPLKALSEF FKGDPKGDFNKT in isoform 8. 2 PublicationsVSP_043446
Alternative sequencei1704 – 172724Missing in isoform 2 and isoform 6. 3 PublicationsVSP_008773Add
BLAST
Alternative sequencei1717 – 172711Missing in isoform 7 and isoform 9. 3 PublicationsVSP_024115Add
BLAST
Alternative sequencei2081 – 212141Missing in isoform 3 and isoform 6. CuratedVSP_008774Add
BLAST
Alternative sequencei2123 – 215028EINSS…VPMGK → GVRVMNCSAQILWGWRVQFH TGSRNQQQ in isoform 4. CuratedVSP_008775Add
BLAST
Alternative sequencei2123 – 214624EINSS…EAEIV → GVRVMNCSAQILWGWRVQFH TGSR in isoform 5. CuratedVSP_008777Add
BLAST
Alternative sequencei2147 – 2602456Missing in isoform 5. CuratedVSP_008778Add
BLAST
Alternative sequencei2151 – 2602452Missing in isoform 4. CuratedVSP_008776Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF042166 mRNA. Translation: AAC39842.1.
AF043045 mRNA. Translation: AAC33845.1.
AF353666 mRNA. Translation: AAL68439.1.
AF353667 Genomic DNA. Translation: AAL68440.1.
AF353667 Genomic DNA. Translation: AAL68441.1.
AF353667 Genomic DNA. Translation: AAL68442.1.
AF353667 Genomic DNA. Translation: AAL68443.1.
AF191633
, AF191594, AF191595, AF191596, AF191597, AF191598, AF191599, AF191600, AF191601, AF191602, AF191603, AF191604, AF191605, AF191606, AF191607, AF191608, AF191609, AF191611, AF191610, AF191613, AF191612, AF191614, AF191615, AF191617, AF191616, AF191618, AF191619, AF191620, AF191621, AF191622, AF191623, AF191624, AF191625, AF191627, AF191626, AF191628, AF191629, AF191630, AF191631, AF191632 Genomic DNA. Translation: AAF72339.1.
AF238609 mRNA. Translation: AAF97046.1.
AB371580 mRNA. Translation: BAG48309.1.
AB371581 mRNA. Translation: BAG48310.1.
AB371582 mRNA. Translation: BAG48311.1.
AB191258 mRNA. Translation: BAD52434.1.
BX641085 mRNA. Translation: CAE46040.1.
AC114399 Genomic DNA. No translation available.
AC137936 Genomic DNA. No translation available.
AL137574 mRNA. Translation: CAB70818.1.
AB209889 mRNA. Translation: BAD93126.1.
M62994 mRNA. Translation: AAA35505.1. Frameshift.
CCDSiCCDS2885.1. [O75369-1]
CCDS54599.1. [O75369-8]
CCDS54600.1. [O75369-9]
CCDS54601.1. [O75369-2]
PIRiT46270.
RefSeqiNP_001157789.1. NM_001164317.1. [O75369-8]
NP_001157790.1. NM_001164318.1. [O75369-9]
NP_001157791.1. NM_001164319.1. [O75369-2]
NP_001448.2. NM_001457.3. [O75369-1]
UniGeneiHs.476448.

Genome annotation databases

EnsembliENST00000295956; ENSP00000295956; ENSG00000136068. [O75369-1]
ENST00000358537; ENSP00000351339; ENSG00000136068. [O75369-2]
ENST00000429972; ENSP00000415599; ENSG00000136068. [O75369-9]
ENST00000490882; ENSP00000420213; ENSG00000136068. [O75369-8]
GeneIDi2317.
KEGGihsa:2317.
UCSCiuc003djj.2. human. [O75369-1]
uc003djk.2. human. [O75369-9]
uc003djl.2. human. [O75369-7]
uc010hne.2. human. [O75369-8]
uc010hnf.2. human. [O75369-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF042166 mRNA. Translation: AAC39842.1 .
AF043045 mRNA. Translation: AAC33845.1 .
AF353666 mRNA. Translation: AAL68439.1 .
AF353667 Genomic DNA. Translation: AAL68440.1 .
AF353667 Genomic DNA. Translation: AAL68441.1 .
AF353667 Genomic DNA. Translation: AAL68442.1 .
AF353667 Genomic DNA. Translation: AAL68443.1 .
AF191633
, AF191594 , AF191595 , AF191596 , AF191597 , AF191598 , AF191599 , AF191600 , AF191601 , AF191602 , AF191603 , AF191604 , AF191605 , AF191606 , AF191607 , AF191608 , AF191609 , AF191611 , AF191610 , AF191613 , AF191612 , AF191614 , AF191615 , AF191617 , AF191616 , AF191618 , AF191619 , AF191620 , AF191621 , AF191622 , AF191623 , AF191624 , AF191625 , AF191627 , AF191626 , AF191628 , AF191629 , AF191630 , AF191631 , AF191632 Genomic DNA. Translation: AAF72339.1 .
AF238609 mRNA. Translation: AAF97046.1 .
AB371580 mRNA. Translation: BAG48309.1 .
AB371581 mRNA. Translation: BAG48310.1 .
AB371582 mRNA. Translation: BAG48311.1 .
AB191258 mRNA. Translation: BAD52434.1 .
BX641085 mRNA. Translation: CAE46040.1 .
AC114399 Genomic DNA. No translation available.
AC137936 Genomic DNA. No translation available.
AL137574 mRNA. Translation: CAB70818.1 .
AB209889 mRNA. Translation: BAD93126.1 .
M62994 mRNA. Translation: AAA35505.1 . Frameshift.
CCDSi CCDS2885.1. [O75369-1 ]
CCDS54599.1. [O75369-8 ]
CCDS54600.1. [O75369-9 ]
CCDS54601.1. [O75369-2 ]
PIRi T46270.
RefSeqi NP_001157789.1. NM_001164317.1. [O75369-8 ]
NP_001157790.1. NM_001164318.1. [O75369-9 ]
NP_001157791.1. NM_001164319.1. [O75369-2 ]
NP_001448.2. NM_001457.3. [O75369-1 ]
UniGenei Hs.476448.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DI8 NMR - A 1999-2096 [» ]
2DI9 NMR - A 1017-1134 [» ]
2DIA NMR - A 1130-1229 [» ]
2DIB NMR - A 1215-1329 [» ]
2DIC NMR - A 1325-1422 [» ]
2DJ4 NMR - A 1418-1518 [» ]
2DLG NMR - A 2104-2192 [» ]
2DMB NMR - A 1611-1721 [» ]
2DMC NMR - A 1899-2001 [» ]
2E9I NMR - A 2094-2192 [» ]
2E9J NMR - A 1504-1615 [» ]
2EE6 NMR - A 2190-2287 [» ]
2EE9 NMR - A 1736-1823 [» ]
2EEA NMR - A 1808-1915 [» ]
2EEB NMR - A 2284-2382 [» ]
2EEC NMR - A 2371-2488 [» ]
2EED NMR - A 2509-2602 [» ]
2WA5 X-ray 1.90 A 2-242 [» ]
2WA6 X-ray 1.95 A 2-242 [» ]
2WA7 X-ray 1.85 A 2-242 [» ]
3FER X-ray 2.40 A/B/C/D 1-252 [» ]
4B7L X-ray 2.05 A/B 1-347 [» ]
ProteinModelPortali O75369.
SMRi O75369. Positions 13-347, 450-739, 1017-1723, 1735-2488, 2511-2602.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108606. 54 interactions.
IntActi O75369. 29 interactions.
MINTi MINT-4998813.

PTM databases

PhosphoSitei O75369.

Proteomic databases

MaxQBi O75369.
PaxDbi O75369.
PRIDEi O75369.

Protocols and materials databases

DNASUi 2317.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295956 ; ENSP00000295956 ; ENSG00000136068 . [O75369-1 ]
ENST00000358537 ; ENSP00000351339 ; ENSG00000136068 . [O75369-2 ]
ENST00000429972 ; ENSP00000415599 ; ENSG00000136068 . [O75369-9 ]
ENST00000490882 ; ENSP00000420213 ; ENSG00000136068 . [O75369-8 ]
GeneIDi 2317.
KEGGi hsa:2317.
UCSCi uc003djj.2. human. [O75369-1 ]
uc003djk.2. human. [O75369-9 ]
uc003djl.2. human. [O75369-7 ]
uc010hne.2. human. [O75369-8 ]
uc010hnf.2. human. [O75369-2 ]

Organism-specific databases

CTDi 2317.
GeneCardsi GC03P057969.
GeneReviewsi FLNB.
H-InvDB HIX0003397.
HGNCi HGNC:3755. FLNB.
HPAi CAB019322.
HPA004747.
HPA004886.
MIMi 108720. phenotype.
108721. phenotype.
112310. phenotype.
150250. phenotype.
272460. phenotype.
603381. gene.
neXtProti NX_O75369.
Orphaneti 1190. Atelosteogenesis type I.
56305. Atelosteogenesis type III.
503. Autosomal dominant Larsen syndrome.
1263. Boomerang dysplasia.
3275. Spondylocarpotarsal synostosis.
PharmGKBi PA28173.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00660000095431.
HOGENOMi HOG000044235.
HOVERGENi HBG004163.
InParanoidi O75369.
KOi K04437.
OMAi DQEGKPK.
OrthoDBi EOG76T9QC.
PhylomeDBi O75369.
TreeFami TF313685.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
SignaLinki O75369.

Miscellaneous databases

ChiTaRSi FLNB. human.
EvolutionaryTracei O75369.
GeneWikii FLNB.
GenomeRNAii 2317.
NextBioi 9409.
PROi O75369.
SOURCEi Search...

Gene expression databases

Bgeei O75369.
ExpressionAtlasi O75369. baseline and differential.
Genevestigatori O75369.

Family and domain databases

Gene3Di 1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view ]
Pfami PF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEi PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
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Publicationsi

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  1. "Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha."
    Takafuta T., Wu G., Murphy G.F., Shapiro S.S.
    J. Biol. Chem. 273:17531-17538(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH GP1BA, VARIANTS ASN-1157 AND MET-1471.
    Tissue: Endothelial cell and Placenta.
  2. "A novel human actin-binding protein homologue that binds to platelet glycoprotein Ibalpha."
    Xu W.-F., Xie Z.-W., Chung D.W., Davie E.W.
    Blood 92:1268-1276(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH GP1BA.
    Tissue: Placenta.
  3. "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits."
    van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A.
    J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4 AND 5), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ISOFORMS OF ITGB1.
    Tissue: Keratinocyte and Skeletal muscle.
  4. "Genomic structure and fine mapping of the two human filamin gene paralogues FLNB and FLNC and comparative analysis of the filamin gene family."
    Chakarova C., Wehnert M.S., Uhl K., Sakthivel S., Vosberg H.-P., van der Ven P.F.M., Fuerst D.O.
    Hum. Genet. 107:597-611(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), GENE ORGANIZATION, SIMILARITY TO OTHER MEMBERS OF THE FAMILY, VARIANTS ASN-1157 AND MET-1471.
  5. "Fine expression profiling of full-length transcripts using a size-unbiased cDNA library prepared with the vector-capping method."
    Oshikawa M., Sugai Y., Usami R., Ohtoko K., Toyama S., Kato S.
    DNA Res. 15:123-136(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 8 AND 9), VARIANTS ASN-1157 AND MET-1471.
  6. "Vector-capping: a simple method for preparing a high-quality full-length cDNA library."
    Kato S., Ohtoko K., Ohtake H., Kimura T.
    DNA Res. 12:53-62(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 8 AND 9).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
    Tissue: Endometrial tumor and Fetal brain.
  8. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 990-2602.
    Tissue: Aortic endothelium.
  10. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 2130-2602, INTERACTION WITH INPPL1.
    Tissue: Skeletal muscle.
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1874-2602.
    Tissue: Fetal brain.
  12. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 2311-2602, INTERACTION WITH PSEN1 AND PSEN2.
    Tissue: Fetal brain.
  13. "Cloning from the thyroid of a protein related to actin binding protein that is recognized by Graves disease immunoglobulins."
    Leedman P.J., Faulkner-Jones B., Cram D.C., Harrison P.J., West J., O'Brien E.J., Simpson R., Coppel R.L., Harrison L.C.
    Proc. Natl. Acad. Sci. U.S.A. 90:5994-5998(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2404-2602, TISSUE SPECIFICITY.
    Tissue: Thyroid.
  14. "Hepatitis B virus core protein interacts with the C-terminal region of actin-binding protein."
    Huang C.J., Chen Y.H., Ting L.P.
    J. Biomed. Sci. 7:160-168(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HBV CAPSID PROTEIN.
  15. "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 FLNA.
  16. "A new member of the LIM protein family binds to filamin B and localizes at stress fibers."
    Takafuta T., Saeki M., Fujimoto T.-T., Fujimura K., Shapiro S.S.
    J. Biol. Chem. 278:12175-12181(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBLP1.
    Tissue: Placenta.
  17. "The limits of promiscuity: isoform-specific dimerization of filamins."
    Himmel M., van der Ven P.F.M., Stoecklein W., Fuerst D.O.
    Biochemistry 42:430-439(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DIMERIZATION, INTERACTION WITH FLNC.
  18. "The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins."
    Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A., Carpen O., Faulkner G., Borradori L.
    J. Cell Sci. 118:3739-3749(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITGB1; MYOT AND MYOZ1.
  19. Cited for: REVIEW.
  20. Cited for: REVIEW.
  21. "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-983, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519; SER-983; SER-1028; SER-1316; SER-1505; SER-1602; SER-2083; SER-2107; SER-2478 AND SER-2481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "The E3 ubiquitin ligase specificity subunit ASB2beta is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation."
    Bello N.F., Lamsoul I., Heuze M.L., Metais A., Moreaux G., Calderwood D.A., Duprez D., Moog-Lutz C., Lutz P.G.
    Cell Death Differ. 16:921-932(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  25. "ISG15 modification of filamin B negatively regulates the type I interferon-induced JNK signalling pathway."
    Jeon Y.J., Choi J.S., Lee J.Y., Yu K.R., Kim S.M., Ka S.H., Oh K.H., Kim K.I., Zhang D.E., Bang O.S., Chung C.H.
    EMBO Rep. 10:374-380(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION AT LYS-2468, MUTAGENESIS OF LYS-2468.
  26. "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-983 AND SER-2478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  27. "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-681 AND LYS-2576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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 THR-519; SER-730; SER-886; SER-932; SER-983; SER-1316; SER-1433; SER-2369; SER-2465 AND SER-2478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "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."
    Sawyer G.M., Clark A.R., Robertson S.P., Sutherland-Smith A.J.
    J. Mol. Biol. 390:1030-1047(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-242.
  33. "Solution structure of the 9th through 24th filamin domains from human filamin-B."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1017-1721; 1736-2488 AND 2509-2602.
  34. Cited for: INVOLVEMENT IN SCT, VARIANTS LRS CYS-161; LYS-227; ASN-1571 DEL; ARG-1586 AND SER-1691, VARIANTS AO1 VAL-173 AND PRO-188, VARIANT AO3 ARG-751, VARIANT AO1/AO3 VAL-202.
  35. "Solution structure of filamin domains from human filamin-B."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1017-2602.
  36. Cited for: VARIANTS BOOMD ARG-171 AND PRO-235.
  37. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-566; LYS-663; LYS-703 AND GLY-1534.
  38. Cited for: VARIANTS LRS CYS-161; SER-168; LYS-227; VAL-234; SER-361; GLU-363; ARG-1431; ASN-1571 DEL; ARG-1586; ASP-1592; LEU-1603; SER-1691 AND ARG-1834.

Entry informationi

Entry nameiFLNB_HUMAN
AccessioniPrimary (citable) accession number: O75369
Secondary accession number(s): B2ZZ83
, B2ZZ84, B2ZZ85, C9JKE6, C9JMC4, Q13706, Q59EC2, Q60FE7, Q6MZJ1, Q8WXS9, Q8WXT0, Q8WXT1, Q8WXT2, Q8WXT3, Q9NRB5, Q9NT26, Q9UEV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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