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Q13642

- FHL1_HUMAN

UniProt

Q13642 - FHL1_HUMAN

Protein

Four and a half LIM domains protein 1

Gene

FHL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    May have an involvement in muscle development or hypertrophy.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri7 – 3125C4-typeSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. ion channel binding Source: BHF-UCL
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. muscle organ development Source: UniProtKB
    3. negative regulation of cell growth Source: UniProtKB
    4. negative regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
    5. negative regulation of G2/M transition of mitotic cell cycle Source: UniProtKB
    6. organ morphogenesis Source: UniProtKB
    7. positive regulation of potassium ion transport Source: BHF-UCL
    8. regulation of membrane depolarization Source: BHF-UCL
    9. regulation of potassium ion transmembrane transporter activity Source: BHF-UCL

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Four and a half LIM domains protein 1
    Short name:
    FHL-1
    Alternative name(s):
    Skeletal muscle LIM-protein 1
    Short name:
    SLIM
    Short name:
    SLIM-1
    Gene namesi
    Name:FHL1
    Synonyms:SLIM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3702. FHL1.

    Subcellular locationi

    Isoform 2 : Nucleus. Cytoplasmcytosol
    Note: Predominantly nuclear in myoblasts but is cytosolic in differentiated myotubes.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Scapuloperoneal myopathy, X-linked dominant (SPM) [MIM:300695]: A disease characterized by progressive muscle weakness and wasting, upper and lower limbs weakness, foot drop, scapular winging, and myopathic changes on muscle biopsy. Most affected individuals become wheelchair-bound.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti122 – 1221W → S in SPM. 1 Publication
    VAR_042603
    Myopathy, X-linked, with postural muscle atrophy (XMPMA) [MIM:300696]: A progressive muscular dystrophy with onset in adulthood. Affected individuals develop a proximal myopathy characterized by specific atrophy of postural muscles, limited neck flexion, bent spine, contractures of the Achilles tendon, respiratory problems, and cardiomyopathy. Patients may show muscle hypertrophy in the early stages of the disorder.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281T → TI in XMPMA. 1 Publication
    VAR_042604
    Natural varianti224 – 2241C → W in XMPMA. 1 Publication
    VAR_042605
    Myopathy, reducing body, X-linked, early-onset, severe (RBM) [MIM:300717]: A rare myopathy clinically characterized by rapidly progressive muscular weakness, and pathologically by the presence of intracytoplasmic inclusion bodies strongly stained by menadione-linked alpha-glycerophosphate dehydrogenase in the absence of substrate, alpha-glycerophosphate. The term 'reducing body' refers to the reducing activity of the inclusions to nitroblue tetrazolium in the absence of substrate. This condition is also commonly associated with rimmed vacuoles and cytoplasmic bodies. Death in childhood is frequent in the severe form of the disease, due to respiratory failure.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti123 – 1231H → Y in RBM; X-linked severe early-onset; the mutant protein initiates aggregation of the FHL1 protein, forms reducing bodies and traps wild-type FHL1 into the inclusion bodies; consistent with a dominant-negative effect. 1 Publication
    VAR_045999
    Natural varianti132 – 1321C → F in RBM; X-linked severe early-onset; the mutant protein initiates aggregation of the FHL1 protein, forms reducing bodies and traps wild-type FHL1 into the inclusion bodies; consistent with a dominant-negative effect. 1 Publication
    VAR_046000
    Natural varianti153 – 1531C → R in RBM; X-linked childhood-onset. 1 Publication
    VAR_046001
    Natural varianti153 – 1531C → Y in RBM; X-linked childhood-onset. 1 Publication
    VAR_046002
    Myopathy, reducing body, X-linked, childhood-onset (CO-RBM) [MIM:300718]: A rare myopathy clinically characterized by rapidly progressive muscular weakness, and pathologically by the presence of intracytoplasmic inclusion bodies strongly stained by menadione-linked alpha-glycerophosphate dehydrogenase in the absence of substrate, alpha-glycerophosphate. The term 'reducing body' refers to the reducing activity of the inclusions to nitroblue tetrazolium in the absence of substrate. This condition is also commonly associated with rimmed vacuoles and cytoplasmic bodies.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi300695. phenotype.
    300696. phenotype.
    300717. phenotype.
    300718. phenotype.
    Orphaneti155. Familial isolated hypertrophic cardiomyopathy.
    97239. Reducing body myopathy.
    98863. X-linked Emery-Dreifuss muscular dystrophy.
    178461. X-linked myopathy with postural muscle atrophy.
    PharmGKBiPA28141.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 323322Four and a half LIM domains protein 1PRO_0000075735Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ13642.
    PaxDbiQ13642.
    PRIDEiQ13642.

    Expressioni

    Tissue specificityi

    Isoform 1 is highly expressed in skeletal muscle and to a lesser extent in heart, placenta, ovary, prostate, testis, small intestine, colon and spleen. Expression is barely detectable in brain, lung, liver, kidney, pancreas, thymus and peripheral blood leukocytes. Isoform 2 is expressed in brain, skeletal muscle and to a lesser extent in heart, colon, prostate and small intestine. Isoform 3 is expressed in testis, heart and skeletal muscle.5 Publications

    Developmental stagei

    Elevated levels during postnatal muscle growth.1 Publication

    Gene expression databases

    ArrayExpressiQ13642.
    BgeeiQ13642.
    GenevestigatoriQ13642.

    Organism-specific databases

    HPAiCAB020817.
    HPA001040.
    HPA001391.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NRIP1P485526EBI-912547,EBI-746484
    PPP2CBP627143EBI-8477209,EBI-1044367

    Protein-protein interaction databases

    BioGridi108564. 29 interactions.
    IntActiQ13642. 27 interactions.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi41 – 433
    Beta strandi49 – 513
    Beta strandi53 – 564
    Beta strandi59 – 624
    Turni63 – 653
    Beta strandi69 – 713
    Beta strandi81 – 833
    Beta strandi86 – 883
    Helixi90 – 934
    Beta strandi102 – 1043
    Beta strandi110 – 1123
    Beta strandi114 – 1163
    Beta strandi121 – 1233
    Turni124 – 1263
    Beta strandi130 – 1323
    Beta strandi141 – 1444
    Beta strandi147 – 1504
    Helixi151 – 1577
    Beta strandi163 – 1653
    Beta strandi174 – 1763
    Beta strandi179 – 1813
    Turni183 – 1864
    Turni189 – 1913
    Beta strandi200 – 2023
    Beta strandi207 – 2093
    Helixi210 – 2178

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X63NMR-A91-159[»]
    2CUPNMR-A40-127[»]
    2CURNMR-A162-217[»]
    2EGQNMR-A211-280[»]
    ProteinModelPortaliQ13642.
    SMRiQ13642. Positions 1-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13642.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 9253LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini101 – 15353LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini162 – 21251LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri7 – 3125C4-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    LIM domain, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG314122.
    HOVERGENiHBG074526.
    InParanoidiQ13642.
    KOiK14365.
    OMAiPEMSAEF.
    OrthoDBiEOG7P8P7M.
    PhylomeDBiQ13642.
    TreeFamiTF318571.

    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 (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q13642-2) [UniParc]FASTAAdd to Basket

    Also known as: FHL1B, SLIMMER

    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

    MAEKFDCHYC RDPLQGKKYV QKDGHHCCLK CFDKFCANTC VECRKPIGAD    50
    SKEVHYKNRF WHDTCFRCAK CLHPLANETF VAKDNKILCN KCTTREDSPK 100
    CKGCFKAIVA GDQNVEYKGT VWHKDCFTCS NCKQVIGTGS FFPKGEDFYC 150
    VTCHETKFAK HCVKCNKAIT SGGITYQDQP WHADCFVCVT CSKKLAGQRF 200
    TAVEDQYYCV DCYKNFVAKK CAGCKNPITG KRTVSRVSHP VSKARKPPVC 250
    HGKRLPLTLF PSANLRGRHP GGERTCPSWV VVLYRKNRSL AAPRGPGLVK 300
    APVWWPMKDN PGTTTASTAK NAP 323
    Length:323
    Mass (Da):36,263
    Last modified:January 23, 2007 - v4
    Checksum:i50FD17F7B2606823
    GO
    Isoform 1 (identifier: Q13642-1) [UniParc]FASTAAdd to Basket

    Also known as: FHL1, FHL1A, SLIM1

    The sequence of this isoform differs from the canonical sequence as follows:
         231-323: KRTVSRVSHP...TTASTAKNAP → FGKGSSVVAY...VYCPDCAKKL

    Show »
    Length:280
    Mass (Da):31,895
    Checksum:i2FC873D70E62834D
    GO
    Isoform 3 (identifier: Q13642-3) [UniParc]FASTAAdd to Basket

    Also known as: FHL1C

    The sequence of this isoform differs from the canonical sequence as follows:
         168-296: Missing.

    Show »
    Length:194
    Mass (Da):22,017
    Checksum:i2DBD610944FFE5EC
    GO
    Isoform 4 (identifier: Q13642-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTFYVASLALELIWMLSSPAGPSSYKVGTM
         231-323: KRTVSRVSHP...TTASTAKNAP → FGKGSSVVAY...VYCPDCAKKL

    Note: No experimental confirmation available.

    Show »
    Length:309
    Mass (Da):34,997
    Checksum:i70D165A814166097
    GO
    Isoform 5 (identifier: Q13642-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MASHRHSGPSSYKVGTM
         231-323: KRTVSRVSHP...TTASTAKNAP → FGKGSSVVAY...VYCPDCAKKL

    Note: No experimental confirmation available.

    Show »
    Length:296
    Mass (Da):33,579
    Checksum:i24EAD21C9DEF4DAD
    GO

    Sequence cautioni

    The sequence AAH88369.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI41055.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731H → Q in AAC52021. (PubMed:8753811)Curated
    Sequence conflicti81 – 9111VAKDNKILCNK → CGQGQQRSCAQ in AAD21579. (PubMed:10352231)CuratedAdd
    BLAST
    Sequence conflicti98 – 981S → F(PubMed:8753811)Curated
    Sequence conflicti98 – 981S → F(PubMed:10352231)Curated
    Sequence conflicti158 – 1581F → L(PubMed:8753811)Curated
    Sequence conflicti158 – 1581F → L(PubMed:7626119)Curated
    Sequence conflicti239 – 2391H → R in AAC72390. (PubMed:10524257)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti122 – 1221W → S in SPM. 1 Publication
    VAR_042603
    Natural varianti123 – 1231H → Y in RBM; X-linked severe early-onset; the mutant protein initiates aggregation of the FHL1 protein, forms reducing bodies and traps wild-type FHL1 into the inclusion bodies; consistent with a dominant-negative effect. 1 Publication
    VAR_045999
    Natural varianti128 – 1281T → TI in XMPMA. 1 Publication
    VAR_042604
    Natural varianti132 – 1321C → F in RBM; X-linked severe early-onset; the mutant protein initiates aggregation of the FHL1 protein, forms reducing bodies and traps wild-type FHL1 into the inclusion bodies; consistent with a dominant-negative effect. 1 Publication
    VAR_046000
    Natural varianti153 – 1531C → R in RBM; X-linked childhood-onset. 1 Publication
    VAR_046001
    Natural varianti153 – 1531C → Y in RBM; X-linked childhood-onset. 1 Publication
    VAR_046002
    Natural varianti224 – 2241C → W in XMPMA. 1 Publication
    VAR_042605

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MTFYVASLALELIWMLSSPA GPSSYKVGTM in isoform 4. 1 PublicationVSP_043162
    Alternative sequencei1 – 11M → MASHRHSGPSSYKVGTM in isoform 5. 1 PublicationVSP_043404
    Alternative sequencei168 – 296129Missing in isoform 3. 1 PublicationVSP_010693Add
    BLAST
    Alternative sequencei231 – 32393KRTVS…AKNAP → FGKGSSVVAYEGQSWHDYCF HCKKCSVNLANKRFVFHQEQ VYCPDCAKKL in isoform 1, isoform 4 and isoform 5. 6 PublicationsVSP_010694Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U60115 mRNA. Translation: AAC52021.1.
    U29538 mRNA. Translation: AAC35421.1.
    AF110763 Genomic DNA. Translation: AAD21579.1.
    AF098518 mRNA. Translation: AAC72390.1.
    AF063002 mRNA. Translation: AAC72886.1.
    AF220153 mRNA. Translation: AAF32351.1.
    AK122708 mRNA. Translation: BAG53680.1.
    AK289411 mRNA. Translation: BAF82100.1.
    AK299381 mRNA. Translation: BAH13020.1.
    AK301642 mRNA. Translation: BAH13529.1.
    CR456974 mRNA. Translation: CAG33255.1.
    AL078638 Genomic DNA. Translation: CAC18881.1.
    AL078638 Genomic DNA. Translation: CAI41062.1.
    AL078638 Genomic DNA. Translation: CAI41055.1. Different initiation.
    CH471150 Genomic DNA. Translation: EAW88476.1.
    CH471150 Genomic DNA. Translation: EAW88478.1.
    CH471150 Genomic DNA. Translation: EAW88479.1.
    BC010998 mRNA. Translation: AAH10998.1.
    BC088369 mRNA. Translation: AAH88369.1. Different initiation.
    U60118 mRNA. Translation: AAC50795.1.
    CCDSiCCDS14655.1. [Q13642-1]
    CCDS55505.1. [Q13642-4]
    CCDS55506.1. [Q13642-5]
    CCDS55507.1. [Q13642-2]
    PIRiG01884.
    JC4893. G02741.
    RefSeqiNP_001153171.1. NM_001159699.1. [Q13642-5]
    NP_001153172.1. NM_001159700.1. [Q13642-1]
    NP_001153173.1. NM_001159701.1. [Q13642-4]
    NP_001153174.1. NM_001159702.2. [Q13642-2]
    NP_001153175.1. NM_001159703.1. [Q13642-3]
    NP_001153176.1. NM_001159704.1. [Q13642-1]
    NP_001161291.1. NM_001167819.1. [Q13642-1]
    NP_001440.2. NM_001449.4. [Q13642-1]
    XP_006724807.1. XM_006724744.1. [Q13642-2]
    XP_006724808.1. XM_006724745.1. [Q13642-2]
    XP_006724809.1. XM_006724746.1. [Q13642-2]
    XP_006724810.1. XM_006724747.1. [Q13642-1]
    UniGeneiHs.435369.

    Genome annotation databases

    EnsembliENST00000345434; ENSP00000071281; ENSG00000022267. [Q13642-2]
    ENST00000370683; ENSP00000359717; ENSG00000022267. [Q13642-5]
    ENST00000370690; ENSP00000359724; ENSG00000022267. [Q13642-1]
    ENST00000394153; ENSP00000377709; ENSG00000022267. [Q13642-1]
    ENST00000394155; ENSP00000377710; ENSG00000022267. [Q13642-2]
    ENST00000535737; ENSP00000444815; ENSG00000022267. [Q13642-1]
    ENST00000539015; ENSP00000437673; ENSG00000022267. [Q13642-4]
    ENST00000543669; ENSP00000443333; ENSG00000022267. [Q13642-1]
    GeneIDi2273.
    KEGGihsa:2273.
    UCSCiuc004ezl.2. human. [Q13642-1]
    uc004ezo.3. human. [Q13642-2]
    uc004ezp.2. human. [Q13642-5]
    uc004ezq.2. human. [Q13642-3]
    uc011mwa.1. human. [Q13642-4]

    Polymorphism databases

    DMDMi59800384.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U60115 mRNA. Translation: AAC52021.1 .
    U29538 mRNA. Translation: AAC35421.1 .
    AF110763 Genomic DNA. Translation: AAD21579.1 .
    AF098518 mRNA. Translation: AAC72390.1 .
    AF063002 mRNA. Translation: AAC72886.1 .
    AF220153 mRNA. Translation: AAF32351.1 .
    AK122708 mRNA. Translation: BAG53680.1 .
    AK289411 mRNA. Translation: BAF82100.1 .
    AK299381 mRNA. Translation: BAH13020.1 .
    AK301642 mRNA. Translation: BAH13529.1 .
    CR456974 mRNA. Translation: CAG33255.1 .
    AL078638 Genomic DNA. Translation: CAC18881.1 .
    AL078638 Genomic DNA. Translation: CAI41062.1 .
    AL078638 Genomic DNA. Translation: CAI41055.1 . Different initiation.
    CH471150 Genomic DNA. Translation: EAW88476.1 .
    CH471150 Genomic DNA. Translation: EAW88478.1 .
    CH471150 Genomic DNA. Translation: EAW88479.1 .
    BC010998 mRNA. Translation: AAH10998.1 .
    BC088369 mRNA. Translation: AAH88369.1 . Different initiation.
    U60118 mRNA. Translation: AAC50795.1 .
    CCDSi CCDS14655.1. [Q13642-1 ]
    CCDS55505.1. [Q13642-4 ]
    CCDS55506.1. [Q13642-5 ]
    CCDS55507.1. [Q13642-2 ]
    PIRi G01884.
    JC4893. G02741.
    RefSeqi NP_001153171.1. NM_001159699.1. [Q13642-5 ]
    NP_001153172.1. NM_001159700.1. [Q13642-1 ]
    NP_001153173.1. NM_001159701.1. [Q13642-4 ]
    NP_001153174.1. NM_001159702.2. [Q13642-2 ]
    NP_001153175.1. NM_001159703.1. [Q13642-3 ]
    NP_001153176.1. NM_001159704.1. [Q13642-1 ]
    NP_001161291.1. NM_001167819.1. [Q13642-1 ]
    NP_001440.2. NM_001449.4. [Q13642-1 ]
    XP_006724807.1. XM_006724744.1. [Q13642-2 ]
    XP_006724808.1. XM_006724745.1. [Q13642-2 ]
    XP_006724809.1. XM_006724746.1. [Q13642-2 ]
    XP_006724810.1. XM_006724747.1. [Q13642-1 ]
    UniGenei Hs.435369.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X63 NMR - A 91-159 [» ]
    2CUP NMR - A 40-127 [» ]
    2CUR NMR - A 162-217 [» ]
    2EGQ NMR - A 211-280 [» ]
    ProteinModelPortali Q13642.
    SMRi Q13642. Positions 1-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108564. 29 interactions.
    IntActi Q13642. 27 interactions.

    Polymorphism databases

    DMDMi 59800384.

    Proteomic databases

    MaxQBi Q13642.
    PaxDbi Q13642.
    PRIDEi Q13642.

    Protocols and materials databases

    DNASUi 2273.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345434 ; ENSP00000071281 ; ENSG00000022267 . [Q13642-2 ]
    ENST00000370683 ; ENSP00000359717 ; ENSG00000022267 . [Q13642-5 ]
    ENST00000370690 ; ENSP00000359724 ; ENSG00000022267 . [Q13642-1 ]
    ENST00000394153 ; ENSP00000377709 ; ENSG00000022267 . [Q13642-1 ]
    ENST00000394155 ; ENSP00000377710 ; ENSG00000022267 . [Q13642-2 ]
    ENST00000535737 ; ENSP00000444815 ; ENSG00000022267 . [Q13642-1 ]
    ENST00000539015 ; ENSP00000437673 ; ENSG00000022267 . [Q13642-4 ]
    ENST00000543669 ; ENSP00000443333 ; ENSG00000022267 . [Q13642-1 ]
    GeneIDi 2273.
    KEGGi hsa:2273.
    UCSCi uc004ezl.2. human. [Q13642-1 ]
    uc004ezo.3. human. [Q13642-2 ]
    uc004ezp.2. human. [Q13642-5 ]
    uc004ezq.2. human. [Q13642-3 ]
    uc011mwa.1. human. [Q13642-4 ]

    Organism-specific databases

    CTDi 2273.
    GeneCardsi GC0XP135229.
    GeneReviewsi FHL1.
    HGNCi HGNC:3702. FHL1.
    HPAi CAB020817.
    HPA001040.
    HPA001391.
    MIMi 300163. gene.
    300695. phenotype.
    300696. phenotype.
    300717. phenotype.
    300718. phenotype.
    neXtProti NX_Q13642.
    Orphaneti 155. Familial isolated hypertrophic cardiomyopathy.
    97239. Reducing body myopathy.
    98863. X-linked Emery-Dreifuss muscular dystrophy.
    178461. X-linked myopathy with postural muscle atrophy.
    PharmGKBi PA28141.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314122.
    HOVERGENi HBG074526.
    InParanoidi Q13642.
    KOi K14365.
    OMAi PEMSAEF.
    OrthoDBi EOG7P8P7M.
    PhylomeDBi Q13642.
    TreeFami TF318571.

    Miscellaneous databases

    ChiTaRSi FHL1. human.
    EvolutionaryTracei Q13642.
    GeneWikii FHL1.
    GenomeRNAii 2273.
    NextBioi 9243.
    PROi Q13642.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13642.
    Bgeei Q13642.
    Genevestigatori Q13642.

    Family and domain databases

    Gene3Di 2.10.110.10. 3 hits.
    InterProi IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 3 hits.
    [Graphical view ]
    SMARTi SM00132. LIM. 3 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 3 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Slim defines a novel family of LIM-proteins expressed in skeletal muscle."
      Morgan M.J., Madgwick A.J.A.
      Biochem. Biophys. Res. Commun. 225:632-638(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skeletal muscle.
    2. Morgan M.J.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Chromosomal mapping, tissue distribution and cDNA sequence of four-and-a-half LIM domain protein 1 (FHL1)."
      Lee S.M.Y., Tsui S.K.W., Chan K.K., Garcia-Barcelo M., Waye M.M.Y., Fung K.P., Liew C.C., Lee C.Y.
      Gene 216:163-170(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Heart.
    4. "Genomic structure, tissue expression and chromosomal location of the LIM-only gene, SLIM1."
      Greene W.K., Baker E., Rabbitts T.H., Kees U.R.
      Gene 232:203-207(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY.
    5. "Characterization of a brain-specific nuclear LIM domain protein (FHL1B) which is an alternatively spliced variant of FHL1."
      Lee S.M.Y., Li H.-Y., Ng E.K.O., Or S.M.W., Chan K.K., Kotaka M., Chim S.S.C., Tsui S.K.W., Waye M.M.Y., Fung K.-P., Lee C.-Y.
      Gene 237:253-263(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    6. "Characterization of two isoforms of the skeletal muscle LIM protein 1, SLIM1. Localization of SLIM1 at focal adhesions and the isoform slimmer in the nucleus of myoblasts and cytoplasm of myotubes suggests distinct roles in the cytoskeleton and in nuclear-cytoplasmic communication."
      Brown S., McGrath M.J., Ooms L.M., Gurung R., Maimone M.M., Mitchell C.A.
      J. Biol. Chem. 274:27083-27091(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Bone marrow.
    7. "Characterization of tissue-specific LIM domain protein (FHL1C) which is an alternatively spliced isoform of a human LIM-only protein (FHL1)."
      Ng E.K.O., Lee S.M.Y., Li H.-Y., Ngai S.-M., Tsui S.K.W., Waye M.M.Y., Lee C.-Y., Fung K.-P.
      J. Cell. Biochem. 82:1-10(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Testis.
    8. "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; 4 AND 5).
      Tissue: Esophagus, Thalamus and Tongue.
    9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    10. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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).
      Tissue: Lung and Muscle.
    13. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-255 (ISOFORM 1), DEVELOPMENTAL STAGE.
      Tissue: Muscle.
    14. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Tissue: Platelet.
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Solution structure of LIM domains from human four and a half LIM domains 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 40-280 IN COMPLEXES WITH ZINC IONS.
    18. "An X-linked myopathy with postural muscle atrophy and generalized hypertrophy, termed XMPMA, is caused by mutations in FHL1."
      Windpassinger C., Schoser B., Straub V., Hochmeister S., Noor A., Lohberger B., Farra N., Petek E., Schwarzbraun T., Ofner L., Loescher W.N., Wagner K., Lochmueller H., Vincent J.B., Quasthoff S.
      Am. J. Hum. Genet. 82:88-99(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS XMPMA ILE-128 INS AND TRP-224.
    19. "X-linked dominant scapuloperoneal myopathy is due to a mutation in the gene encoding four-and-a-half-LIM protein 1."
      Quinzii C.M., Vu T.H., Min K.C., Tanji K., Barral S., Grewal R.P., Kattah A., Camano P., Otaegui D., Kunimatsu T., Blake D.M., Wilhelmsen K.C., Rowland L.P., Hays A.P., Bonilla E., Hirano M.
      Am. J. Hum. Genet. 82:208-213(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPM SER-122.
    20. Cited for: VARIANTS RBM TYR-123; PHE-132; TYR-153 AND ARG-153.

    Entry informationi

    Entry nameiFHL1_HUMAN
    AccessioniPrimary (citable) accession number: Q13642
    Secondary accession number(s): B7Z5T4
    , B7Z793, O95212, Q13230, Q13645, Q5JXI7, Q5M7Y6, Q6IB30, Q9NZ40, Q9UKZ8, Q9Y630
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 148 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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