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Q14315

- FLNC_HUMAN

UniProt

Q14315 - FLNC_HUMAN

Protein

Filamin-C

Gene

FLNC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers.

    GO - Molecular functioni

    1. ankyrin binding Source: BHF-UCL
    2. cytoskeletal protein binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell junction assembly Source: Reactome
    2. muscle fiber development Source: Ensembl

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_20649. Cell-extracellular matrix interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Filamin-C
    Short name:
    FLN-C
    Short name:
    FLNc
    Alternative name(s):
    ABP-280-like protein
    ABP-L
    Actin-binding-like protein
    Filamin-2
    Gamma-filamin
    Gene namesi
    Name:FLNC
    Synonyms:ABPL, FLN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:3756. FLNC.

    Subcellular locationi

    Cytoplasm 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasmcytoskeleton 1 Publication. CytoplasmmyofibrilsarcomereZ line 1 Publication
    Note: A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z lines, while a minor fraction localizes with subsarcolemme. Targeting to developing and mature Z lines is mediated by the intradomain insert.

    GO - Cellular componenti

    1. costamere Source: BHF-UCL
    2. cytoplasm Source: HPA
    3. cytoskeleton Source: UniProtKB-SubCell
    4. cytosol Source: Reactome
    5. plasma membrane Source: HPA
    6. sarcolemma Source: BHF-UCL
    7. sarcoplasm Source: Ensembl
    8. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Myopathy, myofibrillar, 5 (MFM5) [MIM:609524]: A neuromuscular disorder, usually with an adult onset, characterized by focal myofibrillar destruction, pathological cytoplasmic protein aggregations, and clinical features of a limb-girdle myopathy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Myopathy, distal, 4 (MPD4) [MIM:614065]: A slowly progressive muscular disorder characterized by distal muscle weakness and atrophy affecting the upper and lower limbs. Onset occurs around the third to fourth decades of life, and patients remain ambulatory even after long disease duration. Muscle biopsy shows non-specific changes with no evidence of rods, necrosis, or inflammation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti193 – 1931A → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in significantly decreased nuclear localization with formation of intracellular protein aggregates. 1 Publication
    VAR_066212
    Natural varianti251 – 2511M → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in the formation of intracellular protein aggregates. 1 Publication
    VAR_066213

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2669 – 26691M → D: Abolishes dimerization. 1 Publication

    Keywords - Diseasei

    Disease mutation, Myofibrillar myopathy

    Organism-specific databases

    MIMi609524. phenotype.
    614065. phenotype.
    Orphaneti63273. Distal myopathy with posterior leg and anterior hand involvement.
    171445. Muscle filaminopathy.
    PharmGKBiPA28174.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 27252725Filamin-CPRO_0000087301Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1161 – 11611Phosphoserine1 Publication
    Modified residuei2233 – 22331Phosphoserine3 Publications

    Post-translational modificationi

    Ubiquitinated by FBXL22, leading to proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14315.
    PaxDbiQ14315.
    PRIDEiQ14315.

    PTM databases

    PhosphoSiteiQ14315.

    Expressioni

    Tissue specificityi

    Highly expressed in striated muscles. Weakly expressed in thyroid, fetal brain, fetal lung, retina, spinal cord and bone marrow. Not expressed in testis, pancreas, adrenal gland, placenta, liver and kidney.3 Publications

    Developmental stagei

    Expressed in both differentiating and adult muscles.

    Gene expression databases

    ArrayExpressiQ14315.
    BgeeiQ14315.
    CleanExiHS_FLNC.
    GenevestigatoriQ14315.

    Organism-specific databases

    HPAiHPA006135.

    Interactioni

    Subunit structurei

    Homodimer; the filamin repeat 24 and the second hinge domain are important for dimer formation. Interacts with FLNB, INPPL1, ITGB1A, KCND2, MYOT, MYOZ1 and MYOZ3. Interacts with sarcoglycans SGCD and SGCG. Interacts (via filament repeats 17-18, 20-21 and 24) with USP25 (isoform USP25m only). Interacts with FBLIM1. Interacts with XIRP1; this interaction is mediated by filamin 20 repeat. Interacts with KY. Interacts with IGFN1 By similarity. Interacts with MICALL2 By similarity. Interacts with ANK3.By similarity14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005192EBI-489954,EBI-375543
    CRKP461082EBI-489954,EBI-886
    DYSFO759233EBI-489954,EBI-2799016
    GRB2P629932EBI-489954,EBI-401755
    MYOTQ9UBF96EBI-489954,EBI-296701
    XIRP1Q702N84EBI-489954,EBI-7851194

    Protein-protein interaction databases

    BioGridi108607. 58 interactions.
    DIPiDIP-33398N.
    IntActiQ14315. 38 interactions.
    MINTiMINT-5004555.
    STRINGi9606.ENSP00000327145.

    Structurei

    Secondary structure

    1
    2725
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi574 – 5785
    Helixi579 – 5813
    Beta strandi583 – 5853
    Beta strandi590 – 59910
    Helixi601 – 6033
    Beta strandi604 – 6129
    Beta strandi617 – 6204
    Beta strandi622 – 6309
    Beta strandi636 – 6449
    Beta strandi653 – 6597
    Helixi667 – 6693
    Beta strandi671 – 6744
    Helixi675 – 6773
    Beta strandi678 – 6803
    Beta strandi688 – 6936
    Beta strandi697 – 6993
    Beta strandi702 – 7087
    Beta strandi717 – 7204
    Beta strandi722 – 7309
    Beta strandi734 – 74411
    Beta strandi753 – 7597
    Helixi1539 – 15413
    Beta strandi1542 – 15476
    Beta strandi1554 – 15585
    Beta strandi1560 – 156910
    Beta strandi1574 – 15796
    Beta strandi1588 – 15925
    Beta strandi1594 – 15963
    Beta strandi1598 – 16025
    Beta strandi1608 – 161811
    Beta strandi1625 – 16317
    Beta strandi1785 – 17895
    Beta strandi1794 – 17963
    Beta strandi1798 – 18036
    Beta strandi1813 – 18164
    Beta strandi1818 – 18203
    Beta strandi1822 – 18265
    Beta strandi1832 – 184312
    Beta strandi1849 – 18546
    Beta strandi1863 – 18664
    Helixi1867 – 18704
    Beta strandi1871 – 18733
    Beta strandi1878 – 18836
    Turni1885 – 18873
    Beta strandi1895 – 19006
    Beta strandi1910 – 19189
    Beta strandi1924 – 19296
    Beta strandi1931 – 19344
    Beta strandi1941 – 19477
    Beta strandi2303 – 23086
    Turni2313 – 23164
    Beta strandi2318 – 23225
    Turni2323 – 23253
    Beta strandi2332 – 23387
    Beta strandi2344 – 235512
    Beta strandi2358 – 23625
    Beta strandi2365 – 237410
    Beta strandi2377 – 238913
    Beta strandi2396 – 24049
    Helixi2407 – 24104
    Beta strandi2427 – 24326
    Beta strandi2440 – 24456
    Beta strandi2447 – 24493
    Beta strandi2463 – 24686
    Beta strandi2474 – 248411
    Beta strandi2491 – 24966
    Helixi2505 – 25073
    Beta strandi2509 – 25124
    Helixi2513 – 25153
    Beta strandi2517 – 25193
    Beta strandi2524 – 25296
    Turni2531 – 25333
    Beta strandi2538 – 25469
    Beta strandi2549 – 25557
    Beta strandi2558 – 25647
    Beta strandi2569 – 258012
    Beta strandi2587 – 25948
    Helixi2635 – 26373
    Beta strandi2639 – 26424
    Helixi2643 – 26453
    Beta strandi2654 – 26596
    Beta strandi2663 – 26653
    Beta strandi2668 – 26736
    Beta strandi2675 – 26773
    Beta strandi2680 – 26867
    Beta strandi2691 – 26977
    Beta strandi2702 – 27109
    Beta strandi2719 – 27246

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V05X-ray1.43A2633-2725[»]
    2D7MNMR-A1536-1637[»]
    2D7NNMR-A1782-1861[»]
    2D7ONMR-A1856-1953[»]
    2D7PNMR-A2405-2503[»]
    2D7QNMR-A2502-2599[»]
    2K9UNMR-A2302-2415[»]
    2NQCX-ray2.05A2495-2598[»]
    3V8OX-ray2.80A/B569-761[»]
    4MGXX-ray3.16A572-756[»]
    ProteinModelPortaliQ14315.
    SMRiQ14315. Positions 22-2725.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14315.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 259259Actin-bindingAdd
    BLAST
    Domaini36 – 142107CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini159 – 259101CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati270 – 36899Filamin 1Add
    BLAST
    Repeati370 – 46899Filamin 2Add
    BLAST
    Repeati469 – 56597Filamin 3Add
    BLAST
    Repeati566 – 65893Filamin 4Add
    BLAST
    Repeati662 – 75897Filamin 5Add
    BLAST
    Repeati759 – 861103Filamin 6Add
    BLAST
    Repeati862 – 96099Filamin 7Add
    BLAST
    Repeati961 – 105696Filamin 8Add
    BLAST
    Repeati1057 – 114993Filamin 9Add
    BLAST
    Repeati1150 – 124495Filamin 10Add
    BLAST
    Repeati1245 – 1344100Filamin 11Add
    BLAST
    Repeati1345 – 143793Filamin 12Add
    BLAST
    Repeati1438 – 153396Filamin 13Add
    BLAST
    Repeati1534 – 163097Filamin 14Add
    BLAST
    Repeati1635 – 1734100Filamin 15Add
    BLAST
    Repeati1759 – 185395Filamin 16Add
    BLAST
    Repeati1854 – 194693Filamin 17Add
    BLAST
    Repeati1947 – 203387Filamin 18Add
    BLAST
    Repeati2036 – 212893Filamin 19Add
    BLAST
    Repeati2244 – 230663Filamin 20; mediates interaction with XIRP1Add
    BLAST
    Repeati2309 – 240193Filamin 21Add
    BLAST
    Repeati2403 – 249694Filamin 22Add
    BLAST
    Repeati2500 – 259293Filamin 23Add
    BLAST
    Repeati2630 – 272495Filamin 24Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1735 – 175824Hinge 1Add
    BLAST
    Regioni2162 – 224382Intradomain insert; mediate targeting to Z linesAdd
    BLAST
    Regioni2403 – 2724322Interaction with INPPL1Add
    BLAST
    Regioni2593 – 2725133Self-association site, tailBy similarityAdd
    BLAST
    Regioni2593 – 262937Hinge 2Add
    BLAST

    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.
    HOVERGENiHBG004163.
    InParanoidiQ14315.
    KOiK04437.
    OMAiEPTGCIV.
    OrthoDBiEOG76T9QC.
    PhylomeDBiQ14315.
    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.
    IPR003961. Fibronectin_type3.
    IPR017868. Filamin/ABP280_repeat-like.
    IPR001298. Filamin/ABP280_rpt.
    IPR028559. FLN.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view]
    PANTHERiPTHR11915:SF173. PTHR11915:SF173. 1 hit.
    PfamiPF00307. CH. 2 hits.
    PF00630. Filamin. 23 hits.
    [Graphical view]
    SMARTiSM00033. CH. 2 hits.
    SM00060. FN3. 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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14315-1) [UniParc]FASTAAdd to Basket

    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

    MMNNSGYSDA GLGLGDETDE MPSTEKDLAE DAPWKKIQQN TFTRWCNEHL     50
    KCVGKRLTDL QRDLSDGLRL IALLEVLSQK RMYRKFHPRP NFRQMKLENV 100
    SVALEFLERE HIKLVSIDSK AIVDGNLKLI LGLIWTLILH YSISMPMWED 150
    EDDEDARKQT PKQRLLGWIQ NKVPQLPITN FNRDWQDGKA LGALVDNCAP 200
    GLCPDWEAWD PNQPVENARE AMQQADDWLG VPQVIAPEEI VDPNVDEHSV 250
    MTYLSQFPKA KLKPGAPVRS KQLNPKKAIA YGPGIEPQGN TVLQPAHFTV 300
    QTVDAGVGEV LVYIEDPEGH TEEAKVVPNN DKDRTYAVSY VPKVAGLHKV 350
    TVLFAGQNIE RSPFEVNVGM ALGDANKVSA RGPGLEPVGN VANKPTYFDI 400
    YTAGAGTGDV AVVIVDPQGR RDTVEVALED KGDSTFRCTY RPAMEGPHTV 450
    HVAFAGAPIT RSPFPVHVSE ACNPNACRAS GRGLQPKGVR VKEVADFKVF 500
    TKGAGSGELK VTVKGPKGTE EPVKVREAGD GVFECEYYPV VPGKYVVTIT 550
    WGGYAIPRSP FEVQVSPEAG VQKVRAWGPG LETGQVGKSA DFVVEAIGTE 600
    VGTLGFSIEG PSQAKIECDD KGDGSCDVRY WPTEPGEYAV HVICDDEDIR 650
    DSPFIAHILP APPDCFPDKV KAFGPGLEPT GCIVDKPAEF TIDARAAGKG 700
    DLKLYAQDAD GCPIDIKVIP NGDGTFRCSY VPTKPIKHTI IISWGGVNVP 750
    KSPFRVNVGE GSHPERVKVY GPGVEKTGLK ANEPTYFTVD CSEAGQGDVS 800
    IGIKCAPGVV GPAEADIDFD IIKNDNDTFT VKYTPPGAGR YTIMVLFANQ 850
    EIPASPFHIK VDPSHDASKV KAEGPGLNRT GVEVGKPTHF TVLTKGAGKA 900
    KLDVQFAGTA KGEVVRDFEI IDNHDYSYTV KYTAVQQGNM AVTVTYGGDP 950
    VPKSPFVVNV APPLDLSKIK VQGLNSKVAV GQEQAFSVNT RGAGGQGQLD 1000
    VRMTSPSRRP IPCKLEPGGG AEAQAVRYMP PEEGPYKVDI TYDGHPVPGS 1050
    PFAVEGVLPP DPSKVCAYGP GLKGGLVGTP APFSIDTKGA GTGGLGLTVE 1100
    GPCEAKIECQ DNGDGSCAVS YLPTEPGEYT INILFAEAHI PGSPFKATIR 1150
    PVFDPSKVRA SGPGLERGKV GEAATFTVDC SEAGEAELTI EILSDAGVKA 1200
    EVLIHNNADG TYHITYSPAF PGTYTITIKY GGHPVPKFPT RVHVQPAVDT 1250
    SGVKVSGPGV EPHGVLREVT TEFTVDARSL TATGGNHVTA RVLNPSGAKT 1300
    DTYVTDNGDG TYRVQYTAYE EGVHLVEVLY DEVAVPKSPF RVGVTEGCDP 1350
    TRVRAFGPGL EGGLVNKANR FTVETRGAGT GGLGLAIEGP SEAKMSCKDN 1400
    KDGSCTVEYI PFTPGDYDVN ITFGGRPIPG SPFRVPVKDV VDPGKVKCSG 1450
    PGLGAGVRAR VPQTFTVDCS QAGRAPLQVA VLGPTGVAEP VEVRDNGDGT 1500
    HTVHYTPATD GPYTVAVKYA DQEVPRSPFK IKVLPAHDAS KVRASGPGLN 1550
    ASGIPASLPV EFTIDARDAG EGLLTVQILD PEGKPKKANI RDNGDGTYTV 1600
    SYLPDMSGRY TITIKYGGDE IPYSPFRIHA LPTGDASKCL VTVSIGGHGL 1650
    GACLGPRIQI GQETVITVDA KAAGEGKVTC TVSTPDGAEL DVDVVENHDG 1700
    TFDIYYTAPE PGKYVITIRF GGEHIPNSPF HVLACDPLPH EEEPSEVPQL 1750
    RQPYAPPRPG ARPTHWATEE PVVPVEPMES MLRPFNLVIP FAVQKGELTG 1800
    EVRMPSGKTA RPNITDNKDG TITVRYAPTE KGLHQMGIKY DGNHIPGSPL 1850
    QFYVDAINSR HVSAYGPGLS HGMVNKPATF TIVTKDAGEG GLSLAVEGPS 1900
    KAEITCKDNK DGTCTVSYLP TAPGDYSIIV RFDDKHIPGS PFTAKITGDD 1950
    SMRTSQLNVG TSTDVSLKIT ESDLSQLTAS IRAPSGNEEP CLLKRLPNRH 2000
    IGISFTPKEV GEHVVSVRKS GKHVTNSPFK ILVGPSEIGD ASKVRVWGKG 2050
    LSEGHTFQVA EFIVDTRNAG YGGLGLSIEG PSKVDINCED MEDGTCKVTY 2100
    CPTEPGTYII NIKFADKHVP GSPFTVKVTG EGRMKESITR RRQAPSIATI 2150
    GSTCDLNLKI PGNWFQMVSA QERLTRTFTR SSHTYTRTER TEISKTRGGE 2200
    TKREVRVEES TQVGGDPFPA VFGDFLGRER LGSFGSITRQ QEGEASSQDM 2250
    TAQVTSPSGK VEAAEIVEGE DSAYSVRFVP QEMGPHTVAV KYRGQHVPGS 2300
    PFQFTVGPLG EGGAHKVRAG GTGLERGVAG VPAEFSIWTR EAGAGGLSIA 2350
    VEGPSKAEIA FEDRKDGSCG VSYVVQEPGD YEVSIKFNDE HIPDSPFVVP 2400
    VASLSDDARR LTVTSLQETG LKVNQPASFA VQLNGARGVI DARVHTPSGA 2450
    VEECYVSELD SDKHTIRFIP HENGVHSIDV KFNGAHIPGS PFKIRVGEQS 2500
    QAGDPGLVSA YGPGLEGGTT GVSSEFIVNT LNAGSGALSV TIDGPSKVQL 2550
    DCRECPEGHV VTYTPMAPGN YLIAIKYGGP QHIVGSPFKA KVTGPRLSGG 2600
    HSLHETSTVL VETVTKSSSS RGSSYSSIPK FSSDASKVVT RGPGLSQAFV 2650
    GQKNSFTVDC SKAGTNMMMV GVHGPKTPCE EVYVKHMGNR VYNVTYTVKE 2700
    KGDYILIVKW GDESVPGSPF KVKVP 2725
    Length:2,725
    Mass (Da):291,022
    Last modified:July 28, 2009 - v3
    Checksum:iB7C8516C2366E75D
    GO
    Isoform 2 (identifier: Q14315-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1734-1766: Missing.

    Show »
    Length:2,692
    Mass (Da):287,281
    Checksum:i7C07C97B4A882CF2
    GO

    Sequence cautioni

    The sequence AAF80245.1 differs from that shown. Reason: Frameshift at positions 2578, 2580 and 2590.
    The sequence CAA49688.1 differs from that shown. Reason: Frameshift at positions 778 and 787.
    The sequence AAD12245.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAF68195.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381I → T in CAB46442. (PubMed:10658210)Curated
    Sequence conflicti189 – 1891K → E in CAB46442. (PubMed:10658210)Curated
    Sequence conflicti194 – 1941L → Q in CAB46442. (PubMed:10658210)Curated
    Sequence conflicti218 – 2181A → S in AAD12245. (PubMed:9791010)Curated
    Sequence conflicti218 – 2181A → S in AAF68195. (PubMed:11153914)Curated
    Sequence conflicti233 – 2331Q → L in CAB46442. (PubMed:10658210)Curated
    Sequence conflicti484 – 4841L → P in CAB46442. (PubMed:10658210)Curated
    Sequence conflicti585 – 5851Q → V in CAA49688. (PubMed:7689010)Curated
    Sequence conflicti723 – 7231D → N in AAD12245. (PubMed:9791010)Curated
    Sequence conflicti723 – 7231D → N in AAF68195. (PubMed:11153914)Curated
    Sequence conflicti723 – 7231D → N in CAA49688. (PubMed:7689010)Curated
    Sequence conflicti1091 – 10911G → D in CAB46442. (PubMed:10658210)Curated
    Sequence conflicti1640 – 16401L → T in CAA49689. (PubMed:7689010)Curated
    Sequence conflicti1668 – 16681V → M in CAB46442. (PubMed:10658210)Curated
    Sequence conflicti2101 – 21011C → S in CAB46442. (PubMed:10658210)Curated
    Sequence conflicti2101 – 21011C → S in CAA49689. (PubMed:7689010)Curated
    Sequence conflicti2321 – 23222GT → RA in AAD12245. (PubMed:9791010)Curated
    Sequence conflicti2321 – 23222GT → RA in AAF68195. (PubMed:11153914)Curated
    Sequence conflicti2355 – 23551S → N in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2382 – 23821E → K in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2484 – 24841G → C in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2491 – 24911P → L in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2499 – 24991Q → H in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2514 – 25141G → E in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2528 – 25303VNT → DDH in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2535 – 25351S → F in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2547 – 25471K → N in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2557 – 25571E → G in AAF80245. (PubMed:10629222)Curated
    Sequence conflicti2601 – 26022HS → QH in AAF80245. (PubMed:10629222)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti193 – 1931A → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in significantly decreased nuclear localization with formation of intracellular protein aggregates. 1 Publication
    VAR_066212
    Natural varianti251 – 2511M → T in MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in the formation of intracellular protein aggregates. 1 Publication
    VAR_066213
    Natural varianti1567 – 15671R → Q.
    Corresponds to variant rs2291569 [ dbSNP | Ensembl ].
    VAR_015705
    Natural varianti1580 – 15801D → G.2 Publications
    Corresponds to variant rs2643766 [ dbSNP | Ensembl ].
    VAR_015706
    Natural varianti1599 – 15991T → A.2 Publications
    Corresponds to variant rs2643767 [ dbSNP | Ensembl ].
    VAR_015707
    Natural varianti2135 – 21351K → R.1 Publication
    Corresponds to variant rs1063261 [ dbSNP | Ensembl ].
    VAR_015708
    Natural varianti2203 – 22031R → P.2 Publications
    Corresponds to variant rs1063262 [ dbSNP | Ensembl ].
    VAR_015709
    Natural varianti2626 – 26261S → N.
    Corresponds to variant rs2639142 [ dbSNP | Ensembl ].
    VAR_015710
    Natural varianti2637 – 26371K → Q.
    Corresponds to variant rs2291572 [ dbSNP | Ensembl ].
    VAR_015711

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1734 – 176633Missing in isoform 2. 3 PublicationsVSP_007579Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF089841 mRNA. Translation: AAD12245.1. Different initiation.
    AF184126
    , AF184119, AF184120, AF184121, AF184122, AF184123, AF184124, AF184125 Genomic DNA. Translation: AAF68195.1. Different initiation.
    AF252549 Genomic DNA. Translation: AAF67190.1.
    AJ132990 Genomic DNA. Translation: CAB51535.1.
    AJ012737 mRNA. Translation: CAB46442.1.
    AB371585 mRNA. Translation: BAG48314.1.
    AC025594 Genomic DNA. No translation available.
    CH471070 Genomic DNA. Translation: EAW83691.1.
    AF146692 mRNA. Translation: AAF80245.1. Frameshift.
    X70083 mRNA. Translation: CAA49688.1. Frameshift.
    X70084 mRNA. Translation: CAA49689.1.
    CCDSiCCDS43644.1. [Q14315-1]
    CCDS47705.1. [Q14315-2]
    PIRiS37775.
    S37778.
    RefSeqiNP_001120959.1. NM_001127487.1. [Q14315-2]
    NP_001449.3. NM_001458.4. [Q14315-1]
    UniGeneiHs.58414.

    Genome annotation databases

    EnsembliENST00000325888; ENSP00000327145; ENSG00000128591. [Q14315-1]
    ENST00000346177; ENSP00000344002; ENSG00000128591. [Q14315-2]
    GeneIDi2318.
    KEGGihsa:2318.
    UCSCiuc003vnz.4. human. [Q14315-1]
    uc003voa.4. human. [Q14315-2]

    Polymorphism databases

    DMDMi254763419.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF089841 mRNA. Translation: AAD12245.1 . Different initiation.
    AF184126
    , AF184119 , AF184120 , AF184121 , AF184122 , AF184123 , AF184124 , AF184125 Genomic DNA. Translation: AAF68195.1 . Different initiation.
    AF252549 Genomic DNA. Translation: AAF67190.1 .
    AJ132990 Genomic DNA. Translation: CAB51535.1 .
    AJ012737 mRNA. Translation: CAB46442.1 .
    AB371585 mRNA. Translation: BAG48314.1 .
    AC025594 Genomic DNA. No translation available.
    CH471070 Genomic DNA. Translation: EAW83691.1 .
    AF146692 mRNA. Translation: AAF80245.1 . Frameshift.
    X70083 mRNA. Translation: CAA49688.1 . Frameshift.
    X70084 mRNA. Translation: CAA49689.1 .
    CCDSi CCDS43644.1. [Q14315-1 ]
    CCDS47705.1. [Q14315-2 ]
    PIRi S37775.
    S37778.
    RefSeqi NP_001120959.1. NM_001127487.1. [Q14315-2 ]
    NP_001449.3. NM_001458.4. [Q14315-1 ]
    UniGenei Hs.58414.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V05 X-ray 1.43 A 2633-2725 [» ]
    2D7M NMR - A 1536-1637 [» ]
    2D7N NMR - A 1782-1861 [» ]
    2D7O NMR - A 1856-1953 [» ]
    2D7P NMR - A 2405-2503 [» ]
    2D7Q NMR - A 2502-2599 [» ]
    2K9U NMR - A 2302-2415 [» ]
    2NQC X-ray 2.05 A 2495-2598 [» ]
    3V8O X-ray 2.80 A/B 569-761 [» ]
    4MGX X-ray 3.16 A 572-756 [» ]
    ProteinModelPortali Q14315.
    SMRi Q14315. Positions 22-2725.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108607. 58 interactions.
    DIPi DIP-33398N.
    IntActi Q14315. 38 interactions.
    MINTi MINT-5004555.
    STRINGi 9606.ENSP00000327145.

    PTM databases

    PhosphoSitei Q14315.

    Polymorphism databases

    DMDMi 254763419.

    Proteomic databases

    MaxQBi Q14315.
    PaxDbi Q14315.
    PRIDEi Q14315.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325888 ; ENSP00000327145 ; ENSG00000128591 . [Q14315-1 ]
    ENST00000346177 ; ENSP00000344002 ; ENSG00000128591 . [Q14315-2 ]
    GeneIDi 2318.
    KEGGi hsa:2318.
    UCSCi uc003vnz.4. human. [Q14315-1 ]
    uc003voa.4. human. [Q14315-2 ]

    Organism-specific databases

    CTDi 2318.
    GeneCardsi GC07P128470.
    GeneReviewsi FLNC.
    HGNCi HGNC:3756. FLNC.
    HPAi HPA006135.
    MIMi 102565. gene.
    609524. phenotype.
    614065. phenotype.
    neXtProti NX_Q14315.
    Orphaneti 63273. Distal myopathy with posterior leg and anterior hand involvement.
    171445. Muscle filaminopathy.
    PharmGKBi PA28174.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOVERGENi HBG004163.
    InParanoidi Q14315.
    KOi K04437.
    OMAi EPTGCIV.
    OrthoDBi EOG76T9QC.
    PhylomeDBi Q14315.
    TreeFami TF313685.

    Enzyme and pathway databases

    Reactomei REACT_20649. Cell-extracellular matrix interactions.

    Miscellaneous databases

    EvolutionaryTracei Q14315.
    GeneWikii FLNC_(gene).
    GenomeRNAii 2318.
    NextBioi 9413.
    PROi Q14315.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14315.
    Bgeei Q14315.
    CleanExi HS_FLNC.
    Genevestigatori Q14315.

    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.
    IPR003961. Fibronectin_type3.
    IPR017868. Filamin/ABP280_repeat-like.
    IPR001298. Filamin/ABP280_rpt.
    IPR028559. FLN.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    [Graphical view ]
    PANTHERi PTHR11915:SF173. PTHR11915:SF173. 1 hit.
    Pfami PF00307. CH. 2 hits.
    PF00630. Filamin. 23 hits.
    [Graphical view ]
    SMARTi SM00033. CH. 2 hits.
    SM00060. FN3. 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of human ABPL, an actin-binding protein homologue."
      Xie Z.-W., Xu W.-F., Davie E.W., Chung D.W.
      Biochem. Biophys. Res. Commun. 251:914-919(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS GLY-1580; ALA-1599 AND PRO-2203.
      Tissue: Heart.
    2. "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] (ISOFORM 1), GENE ORGANIZATION, SIMILARITY TO OTHER MEMBERS OF THE FAMILY.
    3. "Characterization of muscle filamin isoforms suggests a possible role of gamma-filamin/ABP-L in sarcomeric Z-disc formation."
      van der Ven P.F.M., Obermann W.M.J., Lemke B., Gautel M., Weber K., Fuerst D.O.
      Cell Motil. Cytoskeleton 45:149-162(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS GLY-1580; ALA-1599; ARG-2135 AND PRO-2203.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SGCD AND SGCG.
      Tissue: Skeletal muscle.
    5. Kato S.
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Bienvenut W.V., Pchelintsev N., Adams P.D.
      Submitted (OCT-2009) to UniProtKB
      Tissue: Lung fibroblast.
    9. "Mapping of two genes encoding isoforms of the actin binding protein ABP-280, a dystrophin like protein, to Xq28 and to chromosome 7."
      Maestrini E., Patrosso C., Mancini M., Rivella S., Rocchi M., Repetto M., Villa A., Frattini A., Zoppe M., Vezzoni P., Toniolo D.
      Hum. Mol. Genet. 2:761-766(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 585-815 AND 1638-2101 (ISOFORM 2), TISSUE SPECIFICITY.
    10. Cited for: INTERACTION WITH MYOZ1.
    11. "Indications for a novel muscular dystrophy pathway: gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin."
      van der Ven P.F.M., Wiesner S., Salmikangas P., Auerbach D., Himmel M., Kempa S., Hayess K., Pacholsky D., Taivainen A., Schroeder R., Carpen O., Fuerst D.O.
      J. Cell Biol. 151:235-248(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH MYOT.
    12. "Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin."
      Petrecca K., Miller D.M., Shrier A.
      J. Neurosci. 20:8736-8744(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCND2.
    13. "Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines."
      Takada F., Vander Woude D.L., Tong H.-Q., Thompson T.G., Watkins S.C., Kunkel L.M., Beggs A.H.
      Proc. Natl. Acad. Sci. U.S.A. 98:1595-1600(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYOZ1.
    14. "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: INTERACTION WITH INPPL1.
    15. Cited for: REVIEW.
    16. "Identification of silencing of nine genes in human gastric cancers."
      Kaneda A., Kaminishi M., Yanagihara K., Sugimura T., Ushijima T.
      Cancer Res. 62:6645-6650(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SILENCING IN CANCER CELL LINES MKN28 AND MKN74.
    17. "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins."
      Frey N., Olson E.N.
      J. Biol. Chem. 277:13998-14004(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYOZ3.
    18. "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 FLNB.
    19. "A mutation in the dimerization domain of filamin C causes a novel type of autosomal dominant myofibrillar myopathy."
      Vorgerd M., van der Ven P.F.M., Bruchertseifer V., Loewe T., Kley R.A., Schroeder R., Lochmueller H., Himmel M., Koehler K., Fuerst D.O., Huebner A.
      Am. J. Hum. Genet. 77:297-304(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MFM5.
    20. "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.
    21. "The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins."
      Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.
      Cell. Mol. Life Sci. 63:723-734(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP25.
    22. "Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP."
      van der Ven P.F.M., Ehler E., Vakeel P., Eulitz S., Schenk J.A., Milting H., Micheel B., Fuerst D.O.
      Exp. Cell Res. 312:2154-2167(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XIRP1.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C."
      Maiweilidan Y., Klauza I., Kordeli E.
      Exp. Cell Res. 317:724-736(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANK3.
    27. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "F-box and leucine-rich repeat protein 22 is a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo."
      Spaich S., Will R.D., Just S., Spaich S., Kuhn C., Frank D., Berger I.M., Wiemann S., Korn B., Koegl M., Backs J., Katus H.A., Rottbauer W., Frey N.
      Circ. Res. 111:1504-1516(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY FBXL22.
    29. "Structural basis for vertebrate filamin dimerization."
      Pudas R., Kiema T.-R., Butler P.J.G., Stewart M., Ylaenne J.
      Structure 13:111-119(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 2633-2725, MUTAGENESIS OF MET-2669.
    30. "Solution structure of the filamin domains from human filamin C."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1536-2599.
    31. "Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer."
      Sjekloca L., Pudas R., Sjoblom B., Konarev P., Carugo O., Rybin V., Kiema T.R., Svergun D., Ylanne J., Djinovic Carugo K.
      J. Mol. Biol. 368:1011-1023(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2495-2598, SUBUNIT.
    32. "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 2302-2415 IN COMPLEX WITH FBLIM1.
    33. Cited for: VARIANTS MPD4 THR-193 AND THR-251, CHARACTERIZATION OF VARIANTS MPD4 THR-193 AND THR-251.

    Entry informationi

    Entry nameiFLNC_HUMAN
    AccessioniPrimary (citable) accession number: Q14315
    Secondary accession number(s): B2ZZ88
    , O95303, Q07985, Q9NS12, Q9NYE5, Q9UMR8, Q9Y503
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2003
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 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

    Miscellaneous

    Silenced in MKN28 and MKN74 gastric cancer cell lines due to aberrant methylation of the gene.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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

    Dasty 3