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UniProtKB - O75369 (FLNB_HUMAN)

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Protein

Filamin-B

Gene

FLNB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • actin binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • RNA binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • cytoskeletal anchoring at plasma membrane Source: ProtInc
  • epithelial cell morphogenesis Source: Ensembl
  • keratinocyte development Source: Ensembl
  • signal transduction Source: ProtInc
  • skeletal muscle tissue development Source: Ensembl
Complete GO annotation...

Keywordsi

Molecular functionActin-binding, Developmental protein
Biological processDifferentiation, Myogenesis

Enzyme and pathway databases

ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
SignaLinkiO75369.

Protein family/group databases

TCDBi8.A.66.1.5. the dystrophin (dystrophin) family.

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3755. FLNB.

Subcellular locationi

Isoform 1 :
Isoform 2 :
Isoform 3 :
Isoform 6 :

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • brush border Source: Ensembl
  • cell cortex Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: HPA
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • neuron projection Source: Ensembl
  • nucleus Source: Ensembl
  • plasma membrane Source: HPA
  • stress fiber Source: Ensembl
  • Z disc Source: UniProtKB-SubCell
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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:108720
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033072173A → V in AO1. 1 Publication1
Natural variantiVAR_033073188S → P in AO1. 1 Publication1
Natural variantiVAR_033074202M → V in AO1 and AO3. 1 Publication1
Atelosteogenesis 3 (AO3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:108721
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033074202M → V in AO1 and AO3. 1 Publication1
Natural variantiVAR_033080751G → R in AO3. 1 PublicationCorresponds to variant dbSNP:rs28937587Ensembl.1
Boomerang dysplasia (BOOMD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:112310
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033071171L → R in BOOMD. 1 PublicationCorresponds to variant dbSNP:rs80356494Ensembl.1
Natural variantiVAR_033077235S → P in BOOMD. 1 PublicationCorresponds to variant dbSNP:rs121908896Ensembl.1
Larsen syndrome (LRS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:150250
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033069161F → C in LRS. 2 PublicationsCorresponds to variant dbSNP:rs80356506Ensembl.1
Natural variantiVAR_033070168G → S in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356504Ensembl.1
Natural variantiVAR_033075227E → K in LRS. 2 PublicationsCorresponds to variant dbSNP:rs80356508Ensembl.1
Natural variantiVAR_033076234L → V in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356507Ensembl.1
Natural variantiVAR_033078361G → S in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356509Ensembl.1
Natural variantiVAR_033079363G → E in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356510Ensembl.1
Natural variantiVAR_0330811431L → R in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356511Ensembl.1
Natural variantiVAR_0330821571Missing in LRS. 2 Publications1
Natural variantiVAR_0330831586G → R in LRS. 2 PublicationsCorresponds to variant dbSNP:rs28939706Ensembl.1
Natural variantiVAR_0330841592V → D in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356514Ensembl.1
Natural variantiVAR_0330851603P → L in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356515Ensembl.1
Natural variantiVAR_0330861691G → S in LRS. 2 PublicationsCorresponds to variant dbSNP:rs80356503Ensembl.1
Natural variantiVAR_0330871834G → R in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356516Ensembl.1
Spondylocarpotarsal synostosis syndrome (SCT)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionDisorder characterized by short stature and vertebral, carpal and tarsal fusions.
See also OMIM:272460

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2468K → R: Cytoplasmic localization. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi2317.
MalaCardsiFLNB.
MIMi108720. phenotype.
108721. phenotype.
112310. phenotype.
150250. phenotype.
272460. phenotype.
OpenTargetsiENSG00000136068.
Orphaneti1190. Atelosteogenesis type I.
56305. Atelosteogenesis type III.
503. Autosomal dominant Larsen syndrome.
1263. Boomerang dysplasia.
3275. Spondylocarpotarsal synostosis.
PharmGKBiPA28173.

Polymorphism and mutation databases

BioMutaiFLNB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000872981 – 2602Filamin-BAdd BLAST2602

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei216PhosphothreonineCombined sources1
Modified residuei519PhosphothreonineCombined sources1
Modified residuei681N6-acetyllysineCombined sources1
Modified residuei730PhosphoserineCombined sources1
Modified residuei886PhosphoserineCombined sources1
Modified residuei932PhosphoserineCombined sources1
Modified residuei983PhosphoserineCombined sources1
Modified residuei1028PhosphoserineCombined sources1
Modified residuei1307PhosphothreonineCombined sources1
Modified residuei1316PhosphoserineCombined sources1
Modified residuei1433PhosphoserineCombined sources1
Modified residuei1505PhosphoserineCombined sources1
Modified residuei1602PhosphoserineCombined sources1
Modified residuei1780N6-acetyllysineBy similarity1
Modified residuei2083PhosphoserineCombined sources1
Modified residuei2107PhosphoserineCombined sources1
Modified residuei2113PhosphoserineCombined sources1
Modified residuei2369PhosphoserineCombined sources1
Modified residuei2465PhosphoserineCombined sources1
Cross-linki2468Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)1 Publication
Modified residuei2478PhosphoserineCombined sources1
Modified residuei2481PhosphoserineCombined sources1
Modified residuei2492PhosphoserineCombined sources1
Modified residuei2518N6-succinyllysineBy similarity1
Modified residuei2524N6-succinyllysineBy similarity1
Modified residuei2576N6-acetyllysineCombined sources1
Isoform 8 (identifier: O75369-8)
Modified residuei1474PhosphoserineCombined sources1

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

EPDiO75369.
MaxQBiO75369.
PaxDbiO75369.
PeptideAtlasiO75369.
PRIDEiO75369.

PTM databases

iPTMnetiO75369.
PhosphoSitePlusiO75369.
SwissPalmiO75369.

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

BgeeiENSG00000136068.
ExpressionAtlasiO75369. baseline and differential.
GenevisibleiO75369. HS.

Organism-specific databases

HPAiCAB019322.
HPA004747.
HPA004886.

Interactioni

Subunit structurei

Homodimer. Interacts with MICALL2 (By similarity). Interacts with RFLNA and RFLNB (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

Show more details

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL
  • identical protein binding Source: IntAct
Complete GO annotation...

Protein-protein interaction databases

BioGridi108606. 104 interactors.
IntActiO75369. 53 interactors.
MINTiMINT-4998813.
STRINGi9606.ENSP00000420213.

Structurei

Secondary structure

12602
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 10Combined sources6
Helixi13 – 16Combined sources4
Helixi17 – 30Combined sources14
Helixi31 – 33Combined sources3
Turni40 – 46Combined sources7
Helixi48 – 58Combined sources11
Helixi73 – 89Combined sources17
Helixi99 – 103Combined sources5
Helixi107 – 122Combined sources16
Helixi141 – 152Combined sources12
Helixi163 – 165Combined sources3
Helixi169 – 178Combined sources10
Helixi186 – 188Combined sources3
Helixi194 – 208Combined sources15
Helixi217 – 220Combined sources4
Helixi227 – 234Combined sources8
Helixi236 – 239Combined sources4
Helixi254 – 256Combined sources3
Beta strandi258 – 261Combined sources4
Helixi262 – 264Combined sources3
Beta strandi265 – 267Combined sources3
Beta strandi275 – 280Combined sources6
Turni282 – 284Combined sources3
Beta strandi289 – 294Combined sources6
Beta strandi300 – 302Combined sources3
Beta strandi304 – 309Combined sources6
Beta strandi313 – 319Combined sources7
Beta strandi323 – 333Combined sources11
Beta strandi342 – 347Combined sources6
Helixi1040 – 1042Combined sources3
Beta strandi1044 – 1047Combined sources4
Helixi1048 – 1051Combined sources4
Beta strandi1052 – 1054Combined sources3
Beta strandi1059 – 1064Combined sources6
Turni1066 – 1068Combined sources3
Beta strandi1073 – 1077Combined sources5
Beta strandi1079 – 1081Combined sources3
Beta strandi1084 – 1089Combined sources6
Beta strandi1091 – 1100Combined sources10
Beta strandi1102 – 1115Combined sources14
Beta strandi1122 – 1128Combined sources7
Helixi1133 – 1135Combined sources3
Beta strandi1136 – 1140Combined sources5
Helixi1141 – 1143Combined sources3
Beta strandi1154 – 1160Combined sources7
Beta strandi1166 – 1172Combined sources7
Turni1173 – 1175Combined sources3
Beta strandi1179 – 1184Combined sources6
Beta strandi1188 – 1195Combined sources8
Beta strandi1200 – 1208Combined sources9
Beta strandi1217 – 1223Combined sources7
Beta strandi1232 – 1235Combined sources4
Helixi1236 – 1239Combined sources4
Beta strandi1249 – 1254Combined sources6
Beta strandi1256 – 1258Combined sources3
Beta strandi1273 – 1275Combined sources3
Beta strandi1281 – 1284Combined sources4
Beta strandi1286 – 1294Combined sources9
Beta strandi1300 – 1310Combined sources11
Beta strandi1317 – 1321Combined sources5
Beta strandi1332 – 1335Combined sources4
Helixi1336 – 1339Combined sources4
Beta strandi1347 – 1352Combined sources6
Turni1354 – 1356Combined sources3
Beta strandi1361 – 1369Combined sources9
Beta strandi1374 – 1377Combined sources4
Beta strandi1379 – 1381Combined sources3
Beta strandi1383 – 1387Combined sources5
Beta strandi1393 – 1401Combined sources9
Beta strandi1410 – 1416Combined sources7
Beta strandi1425 – 1428Combined sources4
Turni1429 – 1431Combined sources3
Beta strandi1441 – 1446Combined sources6
Turni1448 – 1450Combined sources3
Beta strandi1455 – 1460Combined sources6
Beta strandi1462 – 1464Combined sources3
Beta strandi1475 – 1483Combined sources9
Beta strandi1489 – 1501Combined sources13
Beta strandi1506 – 1512Combined sources7
Helixi1517 – 1519Combined sources3
Beta strandi1520 – 1524Combined sources5
Helixi1525 – 1527Combined sources3
Beta strandi1538 – 1546Combined sources9
Beta strandi1566 – 1570Combined sources5
Beta strandi1573 – 1580Combined sources8
Beta strandi1586 – 1590Combined sources5
Beta strandi1593 – 1596Combined sources4
Beta strandi1603 – 1609Combined sources7
Beta strandi1618 – 1621Combined sources4
Helixi1622 – 1624Combined sources3
Beta strandi1625 – 1639Combined sources15
Beta strandi1641 – 1643Combined sources3
Beta strandi1648 – 1653Combined sources6
Beta strandi1663 – 1666Combined sources4
Beta strandi1672 – 1677Combined sources6
Beta strandi1682 – 1692Combined sources11
Beta strandi1699 – 1705Combined sources7
Beta strandi1747 – 1751Combined sources5
Beta strandi1760 – 1765Combined sources6
Beta strandi1775 – 1779Combined sources5
Turni1780 – 1782Combined sources3
Beta strandi1783 – 1788Combined sources6
Beta strandi1794 – 1802Combined sources9
Beta strandi1811 – 1816Combined sources6
Beta strandi1825 – 1828Combined sources4
Helixi1829 – 1831Combined sources3
Beta strandi1833 – 1835Combined sources3
Beta strandi1840 – 1845Combined sources6
Beta strandi1855 – 1863Combined sources9
Beta strandi1868 – 1870Combined sources3
Beta strandi1872 – 1880Combined sources9
Beta strandi1886 – 1898Combined sources13
Beta strandi1903 – 1909Combined sources7
Beta strandi1924 – 1927Combined sources4
Beta strandi1941 – 1943Combined sources3
Beta strandi1952 – 1957Combined sources6
Turni1958 – 1960Combined sources3
Beta strandi1961 – 1966Combined sources6
Beta strandi1972 – 1977Combined sources6
Beta strandi1979 – 1984Combined sources6
Beta strandi1989 – 1994Combined sources6
Beta strandi1997 – 1999Combined sources3
Helixi2002 – 2004Combined sources3
Beta strandi2006 – 2010Combined sources5
Turni2011 – 2013Combined sources3
Beta strandi2014 – 2016Combined sources3
Beta strandi2021 – 2026Combined sources6
Turni2028 – 2030Combined sources3
Beta strandi2035 – 2043Combined sources9
Beta strandi2057 – 2061Combined sources5
Beta strandi2067 – 2077Combined sources11
Beta strandi2084 – 2090Combined sources7
Beta strandi2111 – 2113Combined sources3
Beta strandi2118 – 2120Combined sources3
Helixi2126 – 2128Combined sources3
Beta strandi2130 – 2134Combined sources5
Beta strandi2140 – 2142Combined sources3
Beta strandi2144 – 2147Combined sources4
Beta strandi2149 – 2157Combined sources9
Beta strandi2164 – 2175Combined sources12
Beta strandi2180 – 2185Combined sources6
Helixi2193 – 2195Combined sources3
Turni2201 – 2203Combined sources3
Beta strandi2206 – 2208Combined sources3
Beta strandi2210 – 2214Combined sources5
Beta strandi2219 – 2221Combined sources3
Beta strandi2226 – 2234Combined sources9
Beta strandi2236 – 2240Combined sources5
Beta strandi2250 – 2256Combined sources7
Beta strandi2258 – 2266Combined sources9
Beta strandi2275 – 2281Combined sources7
Beta strandi2288 – 2294Combined sources7
Beta strandi2306 – 2314Combined sources9
Beta strandi2320 – 2324Combined sources5
Beta strandi2330 – 2332Combined sources3
Beta strandi2334 – 2337Combined sources4
Beta strandi2340 – 2347Combined sources8
Beta strandi2352 – 2365Combined sources14
Beta strandi2370 – 2375Combined sources6
Turni2384 – 2386Combined sources3
Beta strandi2388 – 2392Combined sources5
Turni2393 – 2395Combined sources3
Beta strandi2403 – 2408Combined sources6
Turni2410 – 2412Combined sources3
Beta strandi2417 – 2425Combined sources9
Beta strandi2430 – 2433Combined sources4
Beta strandi2435 – 2442Combined sources8
Beta strandi2448 – 2459Combined sources12
Beta strandi2466 – 2473Combined sources8
Turni2512 – 2514Combined sources3
Beta strandi2516 – 2519Combined sources4
Helixi2520 – 2523Combined sources4
Beta strandi2531 – 2536Combined sources6
Turni2538 – 2540Combined sources3
Beta strandi2545 – 2547Combined sources3
Beta strandi2557 – 2565Combined sources9
Beta strandi2568 – 2574Combined sources7
Beta strandi2579 – 2583Combined sources5
Beta strandi2585 – 2591Combined sources7
Beta strandi2596 – 2601Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5DCPX-ray2.49A/B1737-1911[»]
ProteinModelPortaliO75369.
SMRiO75369.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75369.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 239Actin-bindingAdd BLAST239
Domaini16 – 122Calponin-homology 1PROSITE-ProRule annotationAdd BLAST107
Domaini139 – 239Calponin-homology 2PROSITE-ProRule annotationAdd BLAST101
Repeati249 – 347Filamin 1Add BLAST99
Repeati349 – 446Filamin 2Add BLAST98
Repeati447 – 543Filamin 3Add BLAST97
Repeati544 – 636Filamin 4Add BLAST93
Repeati640 – 736Filamin 5Add BLAST97
Repeati737 – 839Filamin 6Add BLAST103
Repeati840 – 938Filamin 7Add BLAST99
Repeati939 – 1034Filamin 8Add BLAST96
Repeati1035 – 1127Filamin 9Add BLAST93
Repeati1128 – 1222Filamin 10Add BLAST95
Repeati1223 – 1322Filamin 11Add BLAST100
Repeati1323 – 1415Filamin 12Add BLAST93
Repeati1416 – 1511Filamin 13Add BLAST96
Repeati1512 – 1608Filamin 14Add BLAST97
Repeati1609 – 1704Filamin 15Add BLAST96
Repeati1729 – 1813Filamin 16Add BLAST85
Repeati1816 – 1908Filamin 17Add BLAST93
Repeati1919 – 1994Filamin 18Add BLAST76
Repeati1997 – 2089Filamin 19Add BLAST93
Repeati2091 – 2185Filamin 20Add BLAST95
Repeati2188 – 2280Filamin 21Add BLAST93
Repeati2282 – 2375Filamin 22Add BLAST94
Repeati2379 – 2471Filamin 23Add BLAST93
Repeati2507 – 2601Filamin 24Add BLAST95

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1128 – 1511Interaction with FBLP11 PublicationAdd BLAST384
Regioni1705 – 1728Hinge 1By similarityAdd BLAST24
Regioni1862 – 2148Interaction with the cytoplasmic tail of GP1BAAdd BLAST287
Regioni2060 – 2225Interaction with FLNA 1Add BLAST166
Regioni2130 – 2602Interaction with INPPL11 PublicationAdd BLAST473
Regioni2472 – 2602Self-association site, tailBy similarityAdd BLAST131
Regioni2472 – 2506Hinge 2By similarityAdd BLAST35
Regioni2507 – 2602Interaction with FLNA 2Add BLAST96

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00660000095431.
HOGENOMiHOG000044235.
HOVERGENiHBG004163.
InParanoidiO75369.
KOiK04437.
OMAiGTYDIFY.
OrthoDBiEOG091G00U5.
PhylomeDBiO75369.
TreeFamiTF313685.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProiView protein in InterPro
IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR029874. FLNB.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
PANTHERiPTHR11915:SF419. PTHR11915:SF419. 1 hit.
PfamiView protein in Pfam
PF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
SMARTiView protein in SMART
SM00033. CH. 2 hits.
SM00557. IG_FLMN. 24 hits.
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEiView protein in PROSITE
PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

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 differs from that shown. Reason: Frameshift at positions 2432 and 2589.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti816A → T in CAE46040 (PubMed:17974005).Curated1
Sequence conflicti924Y → H in CAE46040 (PubMed:17974005).Curated1
Sequence conflicti1411F → L in CAE46040 (PubMed:17974005).Curated1
Sequence conflicti1560E → G in CAE46040 (PubMed:17974005).Curated1
Sequence conflicti1953L → F in AAF97046 (PubMed:11153914).Curated1
Sequence conflicti2006K → R in AAC33845 (PubMed:9694715).Curated1
Sequence conflicti2099I → S in CAE46040 (PubMed:17974005).Curated1
Sequence conflicti2170K → N in AAF97046 (PubMed:11153914).Curated1
Sequence conflicti2293M → V in AAF97046 (PubMed:11153914).Curated1
Sequence conflicti2293M → V in CAE46040 (PubMed:17974005).Curated1
Sequence conflicti2354V → A in CAB70818 (PubMed:11230166).Curated1
Sequence conflicti2487S → C in AAA35505 (PubMed:8327473).Curated1
Sequence conflicti2571V → A in CAB70818 (PubMed:11230166).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033069161F → C in LRS. 2 PublicationsCorresponds to variant dbSNP:rs80356506Ensembl.1
Natural variantiVAR_033070168G → S in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356504Ensembl.1
Natural variantiVAR_033071171L → R in BOOMD. 1 PublicationCorresponds to variant dbSNP:rs80356494Ensembl.1
Natural variantiVAR_033072173A → V in AO1. 1 Publication1
Natural variantiVAR_033073188S → P in AO1. 1 Publication1
Natural variantiVAR_033074202M → V in AO1 and AO3. 1 Publication1
Natural variantiVAR_033075227E → K in LRS. 2 PublicationsCorresponds to variant dbSNP:rs80356508Ensembl.1
Natural variantiVAR_033076234L → V in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356507Ensembl.1
Natural variantiVAR_033077235S → P in BOOMD. 1 PublicationCorresponds to variant dbSNP:rs121908896Ensembl.1
Natural variantiVAR_033078361G → S in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356509Ensembl.1
Natural variantiVAR_033079363G → E in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356510Ensembl.1
Natural variantiVAR_035917566R → Q in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs150747960Ensembl.1
Natural variantiVAR_035918663N → K in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_035919703T → K in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_033080751G → R in AO3. 1 PublicationCorresponds to variant dbSNP:rs28937587Ensembl.1
Natural variantiVAR_0171821018V → M. Corresponds to variant dbSNP:rs2276742Ensembl.1
Natural variantiVAR_0171831157D → N3 PublicationsCorresponds to variant dbSNP:rs1131356Ensembl.1
Natural variantiVAR_0313921179E → K. Corresponds to variant dbSNP:rs17058845Ensembl.1
Natural variantiVAR_0330811431L → R in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356511Ensembl.1
Natural variantiVAR_0313931471V → M3 PublicationsCorresponds to variant dbSNP:rs12632456Ensembl.1
Natural variantiVAR_0359201534A → G in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0330821571Missing in LRS. 2 Publications1
Natural variantiVAR_0330831586G → R in LRS. 2 PublicationsCorresponds to variant dbSNP:rs28939706Ensembl.1
Natural variantiVAR_0330841592V → D in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356514Ensembl.1
Natural variantiVAR_0330851603P → L in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356515Ensembl.1
Natural variantiVAR_0330861691G → S in LRS. 2 PublicationsCorresponds to variant dbSNP:rs80356503Ensembl.1
Natural variantiVAR_0330871834G → R in LRS. 1 PublicationCorresponds to variant dbSNP:rs80356516Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0241131 – 169Missing in isoform 7. 1 PublicationAdd BLAST169
Alternative sequenceiVSP_024114170 – 181ALGAL…SCAPG → MQEHSTRRRSLS in isoform 7. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_0434461463R → RADDTDSQSWRSPLKALSEF FKGDPKGDFNKT in isoform 8. 2 Publications1
Alternative sequenceiVSP_0087731704 – 1727Missing in isoform 2 and isoform 6. 3 PublicationsAdd BLAST24
Alternative sequenceiVSP_0241151717 – 1727Missing in isoform 7 and isoform 9. 3 PublicationsAdd BLAST11
Alternative sequenceiVSP_0087742081 – 2121Missing in isoform 3 and isoform 6. CuratedAdd BLAST41
Alternative sequenceiVSP_0087752123 – 2150EINSS…VPMGK → GVRVMNCSAQILWGWRVQFH TGSRNQQQ in isoform 4. CuratedAdd BLAST28
Alternative sequenceiVSP_0087772123 – 2146EINSS…EAEIV → GVRVMNCSAQILWGWRVQFH TGSR in isoform 5. CuratedAdd BLAST24
Alternative sequenceiVSP_0087782147 – 2602Missing in isoform 5. CuratedAdd BLAST456
Alternative sequenceiVSP_0087762151 – 2602Missing in isoform 4. CuratedAdd BLAST452

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. human. [O75369-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

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 historyiIntegrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: May 18, 2010
Last modified: July 5, 2017
This is version 192 of the entry and version 2 of the sequence. See 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