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Protein

Filamin-binding LIM protein 1

Gene

FBLIM1

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

Functioni

Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin-containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion.4 Publications

GO - Molecular functioni

  • filamin binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell junction assembly Source: Reactome
  • regulation of cell shape Source: UniProtKB-KW
  • regulation of integrin activation Source: UniProtKB
  • single organismal cell-cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Cell shape

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-446353. Cell-extracellular matrix interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Filamin-binding LIM protein 1
Short name:
FBLP-1
Alternative name(s):
Migfilin
Mitogen-inducible 2-interacting protein
Short name:
MIG2-interacting protein
Gene namesi
Name:FBLIM1
Synonyms:FBLP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24686. FBLIM1.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • focal adhesion Source: UniProtKB
  • stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 82KR → TG: Localizes to cell-ECM adhesions; abolishes FLNA and FLNC interactions; failed to decorate actin filaments. 1 Publication

Organism-specific databases

PharmGKBiPA142671776.

Polymorphism and mutation databases

BioMutaiFBLIM1.
DMDMi125987829.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373Filamin-binding LIM protein 1PRO_0000075732Add
BLAST

Proteomic databases

EPDiQ8WUP2.
MaxQBiQ8WUP2.
PaxDbiQ8WUP2.
PeptideAtlasiQ8WUP2.
PRIDEiQ8WUP2.

PTM databases

iPTMnetiQ8WUP2.
PhosphoSiteiQ8WUP2.
SwissPalmiQ8WUP2.

Expressioni

Tissue specificityi

Isoform 1 and isoform 3 are expressed in heart, kidney, lung, pancreas, placenta and platelets. Isoform 2 is expressed in brain, heart, kidney, lung, pancreas, placenta, skeletal muscle and platelets.1 Publication

Gene expression databases

BgeeiQ8WUP2.
CleanExiHS_FBLIM1.
ExpressionAtlasiQ8WUP2. baseline and differential.
GenevisibleiQ8WUP2. HS.

Organism-specific databases

HPAiHPA025287.

Interactioni

Subunit structurei

Interacts with NKX2-5 (By similarity). Isoform 1 and isoform 3 interact with FERMT2, FLNA, FLNB and FLNC. Isoform 2 interacts with FLNB.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUTAO608883EBI-3864120,EBI-1051556
HIST1H3DP684313EBI-3864120,EBI-79722
LMO3Q8TAP43EBI-3864120,EBI-742259

GO - Molecular functioni

  • filamin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120128. 10 interactions.
IntActiQ8WUP2. 5 interactions.
STRINGi9606.ENSP00000416387.

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi9 – 168Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K9UNMR-B1-24[»]
2W0PX-ray1.90C5-19[»]
4P3WX-ray2.00G/H/I/J/K/L5-28[»]
ProteinModelPortaliQ8WUP2.
SMRiQ8WUP2. Positions 183-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WUP2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini181 – 24262LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini243 – 30058LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini301 – 37070LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8585Intrinsically disorderedAdd
BLAST
Regioni1 – 7070Filamin-bindingAdd
BLAST
Regioni276 – 37398FERMT2-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 173132Pro-richAdd
BLAST

Domaini

The N-terminal region is intrinsically disordered.1 Publication

Sequence similaritiesi

Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiKOG1701. Eukaryota.
ENOG410Y3GP. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000007533.
HOVERGENiHBG051561.
InParanoidiQ8WUP2.
OMAiNRLFCKP.
PhylomeDBiQ8WUP2.
TreeFamiTF320310.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 3 hits.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 3 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WUP2-1) [UniParc]FASTAAdd to basket

Also known as: FBLP-1A

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
MASKPEKRVA SSVFITLAPP RRDVAVAEEV RQAVCEARRG RPWEAPAPMK
60 70 80 90 100
TPEAGLAGRP SPWTTPGRAA ATVPAAPMQL FNGGCPPPPP VLDGEDVLPD
110 120 130 140 150
LDLLPPPPPP PPVLLPSEEE APAPMGASLI ADLEQLHLSP PPPPPQAPAE
160 170 180 190 200
GPSVQPGPLR PMEEELPPPP AEPVEKGAST DICAFCHKTV SPRELAVEAM
210 220 230 240 250
KRQYHAQCFT CRTCRRQLAG QSFYQKDGRP LCEPCYQDTL ERCGKCGEVV
260 270 280 290 300
RDHIIRALGQ AFHPSCFTCV TCARCIGDES FALGSQNEVY CLDDFYRKFA
310 320 330 340 350
PVCSICENPI IPRDGKDAFK IECMGRNFHE NCYRCEDCRI LLSVEPTDQG
360 370
CYPLNNHLFC KPCHVKRSAA GCC
Length:373
Mass (Da):40,670
Last modified:February 6, 2007 - v2
Checksum:i06B8FB911FCCB194
GO
Isoform 2 (identifier: Q8WUP2-2) [UniParc]FASTAAdd to basket

Also known as: FBLP-1

The sequence of this isoform differs from the canonical sequence as follows:
     298-373: KFAPVCSICE...HVKRSAAGCC → YEKGLCTGWG...TRSGDRDHPG

Note: May be due to competing donor splice site.
Show »
Length:374
Mass (Da):40,306
Checksum:i36BC4CED0B270C4C
GO
Isoform 3 (identifier: Q8WUP2-3) [UniParc]FASTAAdd to basket

Also known as: FBLP-1B

The sequence of this isoform differs from the canonical sequence as follows:
     84-180: Missing.

Note: May be due to exon skipping.
Show »
Length:276
Mass (Da):30,770
Checksum:i77664085430F8163
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391R → C.
Corresponds to variant rs34375304 [ dbSNP | Ensembl ].
VAR_050145
Natural varianti191 – 1911S → F.4 Publications
Corresponds to variant rs10927851 [ dbSNP | Ensembl ].
VAR_022842

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei84 – 18097Missing in isoform 3. 3 PublicationsVSP_008781Add
BLAST
Alternative sequencei298 – 37376KFAPV…AAGCC → YEKGLCTGWGAGTGRDPSRV KELSLSPGCWARVSCLLVYY KEYYRAGLGAVAHACNPSTL GGRGGWITRSGDRDHPG in isoform 2. 1 PublicationVSP_008782Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY180161 mRNA. Translation: AAO49012.1.
AF459643 mRNA. Translation: AAO15549.1.
AK027444 mRNA. Translation: BAB55115.1.
AK055259 mRNA. Translation: BAG51492.1.
AL450998 Genomic DNA. Translation: CAH70854.1.
AL450998 Genomic DNA. Translation: CAH70853.1.
BC019895 mRNA. Translation: AAH19895.1.
AL133035 mRNA. Translation: CAB61365.1.
CCDSiCCDS163.1. [Q8WUP2-1]
CCDS30609.1. [Q8WUP2-3]
CCDS44064.1. [Q8WUP2-2]
PIRiT42678.
RefSeqiNP_001019386.1. NM_001024215.1. [Q8WUP2-2]
NP_001019387.1. NM_001024216.1. [Q8WUP2-3]
NP_060026.2. NM_017556.2. [Q8WUP2-1]
XP_005245957.1. XM_005245900.1. [Q8WUP2-2]
XP_005245958.1. XM_005245901.1. [Q8WUP2-2]
XP_005245959.1. XM_005245902.1. [Q8WUP2-2]
XP_005245960.1. XM_005245903.1. [Q8WUP2-2]
XP_005245966.1. XM_005245909.2. [Q8WUP2-1]
XP_006710767.1. XM_006710704.2. [Q8WUP2-2]
XP_006710768.1. XM_006710705.1. [Q8WUP2-2]
XP_011539918.1. XM_011541616.1. [Q8WUP2-2]
XP_011539919.1. XM_011541617.1. [Q8WUP2-1]
XP_011539921.1. XM_011541619.1. [Q8WUP2-3]
UniGeneiHs.530101.

Genome annotation databases

EnsembliENST00000332305; ENSP00000364920; ENSG00000162458. [Q8WUP2-3]
ENST00000375766; ENSP00000364921; ENSG00000162458. [Q8WUP2-1]
ENST00000375771; ENSP00000364926; ENSG00000162458. [Q8WUP2-1]
ENST00000441801; ENSP00000416387; ENSG00000162458. [Q8WUP2-2]
GeneIDi54751.
KEGGihsa:54751.
UCSCiuc001axd.2. human. [Q8WUP2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY180161 mRNA. Translation: AAO49012.1.
AF459643 mRNA. Translation: AAO15549.1.
AK027444 mRNA. Translation: BAB55115.1.
AK055259 mRNA. Translation: BAG51492.1.
AL450998 Genomic DNA. Translation: CAH70854.1.
AL450998 Genomic DNA. Translation: CAH70853.1.
BC019895 mRNA. Translation: AAH19895.1.
AL133035 mRNA. Translation: CAB61365.1.
CCDSiCCDS163.1. [Q8WUP2-1]
CCDS30609.1. [Q8WUP2-3]
CCDS44064.1. [Q8WUP2-2]
PIRiT42678.
RefSeqiNP_001019386.1. NM_001024215.1. [Q8WUP2-2]
NP_001019387.1. NM_001024216.1. [Q8WUP2-3]
NP_060026.2. NM_017556.2. [Q8WUP2-1]
XP_005245957.1. XM_005245900.1. [Q8WUP2-2]
XP_005245958.1. XM_005245901.1. [Q8WUP2-2]
XP_005245959.1. XM_005245902.1. [Q8WUP2-2]
XP_005245960.1. XM_005245903.1. [Q8WUP2-2]
XP_005245966.1. XM_005245909.2. [Q8WUP2-1]
XP_006710767.1. XM_006710704.2. [Q8WUP2-2]
XP_006710768.1. XM_006710705.1. [Q8WUP2-2]
XP_011539918.1. XM_011541616.1. [Q8WUP2-2]
XP_011539919.1. XM_011541617.1. [Q8WUP2-1]
XP_011539921.1. XM_011541619.1. [Q8WUP2-3]
UniGeneiHs.530101.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K9UNMR-B1-24[»]
2W0PX-ray1.90C5-19[»]
4P3WX-ray2.00G/H/I/J/K/L5-28[»]
ProteinModelPortaliQ8WUP2.
SMRiQ8WUP2. Positions 183-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120128. 10 interactions.
IntActiQ8WUP2. 5 interactions.
STRINGi9606.ENSP00000416387.

PTM databases

iPTMnetiQ8WUP2.
PhosphoSiteiQ8WUP2.
SwissPalmiQ8WUP2.

Polymorphism and mutation databases

BioMutaiFBLIM1.
DMDMi125987829.

Proteomic databases

EPDiQ8WUP2.
MaxQBiQ8WUP2.
PaxDbiQ8WUP2.
PeptideAtlasiQ8WUP2.
PRIDEiQ8WUP2.

Protocols and materials databases

DNASUi54751.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332305; ENSP00000364920; ENSG00000162458. [Q8WUP2-3]
ENST00000375766; ENSP00000364921; ENSG00000162458. [Q8WUP2-1]
ENST00000375771; ENSP00000364926; ENSG00000162458. [Q8WUP2-1]
ENST00000441801; ENSP00000416387; ENSG00000162458. [Q8WUP2-2]
GeneIDi54751.
KEGGihsa:54751.
UCSCiuc001axd.2. human. [Q8WUP2-1]

Organism-specific databases

CTDi54751.
GeneCardsiFBLIM1.
HGNCiHGNC:24686. FBLIM1.
HPAiHPA025287.
MIMi607747. gene.
neXtProtiNX_Q8WUP2.
PharmGKBiPA142671776.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1701. Eukaryota.
ENOG410Y3GP. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000007533.
HOVERGENiHBG051561.
InParanoidiQ8WUP2.
OMAiNRLFCKP.
PhylomeDBiQ8WUP2.
TreeFamiTF320310.

Enzyme and pathway databases

ReactomeiR-HSA-446353. Cell-extracellular matrix interactions.

Miscellaneous databases

ChiTaRSiFBLIM1. human.
EvolutionaryTraceiQ8WUP2.
GeneWikiiFBLIM1.
GenomeRNAii54751.
PROiQ8WUP2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WUP2.
CleanExiHS_FBLIM1.
ExpressionAtlasiQ8WUP2. baseline and differential.
GenevisibleiQ8WUP2. HS.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 3 hits.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 3 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation."
    Tu Y., Wu S., Shi X., Chen K., Wu C.
    Cell 113:37-47(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANT PHE-191, FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, INTERACTION WITH FERMT2; FLNA AND FLNC, MUTAGENESIS OF 7-LYS-ARG-8.
    Tissue: Lung.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT PHE-191, FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH FNLB.
    Tissue: Placenta.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT PHE-191.
    Tissue: Brain and Teratocarcinoma.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PHE-191.
    Tissue: Cervix adenocarcinoma.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-373 (ISOFORM 1).
    Tissue: Testis.
  7. "Structural basis of the migfilin-filamin interaction and competition with integrin beta tails."
    Lad Y., Jiang P., Ruskamo S., Harburger D.S., Ylanne J., Campbell I.D., Calderwood D.A.
    J. Biol. Chem. 283:35154-35163(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-19 IN COMPLEX WITH FLNA, INTERACTION WITH FLNA; FLNB AND FLNC, FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
  8. "Migfilin, a molecular switch in regulation of integrin activation."
    Ithychanda S.S., Das M., Ma Y.Q., Ding K., Wang X., Gupta S., Wu C., Plow E.F., Qin J.
    J. Biol. Chem. 284:4713-4722(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-24 IN COMPLEX WITH FLNC, INTERACTION WITH FLNA AND FLNC, FUNCTION.

Entry informationi

Entry nameiFBLI1_HUMAN
AccessioniPrimary (citable) accession number: Q8WUP2
Secondary accession number(s): B3KNY0
, Q5VVE0, Q5VVE1, Q8IX23, Q96T00, Q9UFD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: February 6, 2007
Last modified: July 6, 2016
This is version 147 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 1
    Human chromosome 1: 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

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.