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Q14192

- FHL2_HUMAN

UniProt

Q14192 - FHL2_HUMAN

Protein

Four and a half LIM domains protein 2

Gene

FHL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation.3 Publications

    Regions

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

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. transcription coactivator activity Source: UniProtKB
    5. transcription factor binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. atrial cardiac muscle cell development Source: Ensembl
    3. cellular lipid metabolic process Source: Reactome
    4. heart trabecula formation Source: Ensembl
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. osteoblast differentiation Source: Ensembl
    8. positive regulation of transcription, DNA-templated Source: UniProtKB
    9. response to hormone Source: BHF-UCL
    10. small molecule metabolic process Source: Reactome
    11. transcription, DNA-templated Source: UniProtKB-KW
    12. ventricular cardiac muscle cell development Source: Ensembl

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_116145. PPARA activates gene expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Four and a half LIM domains protein 2
    Short name:
    FHL-2
    Alternative name(s):
    LIM domain protein DRAL
    Skeletal muscle LIM-protein 3
    Short name:
    SLIM-3
    Gene namesi
    Name:FHL2
    Synonyms:DRAL, SLIM3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3703. FHL2.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. focal adhesion Source: HPA
    3. M band Source: Ensembl
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA
    6. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti154. Familial isolated dilated cardiomyopathy.
    PharmGKBiPA164.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 279279Four and a half LIM domains protein 2PRO_0000075737Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei238 – 2381Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14192.
    PaxDbiQ14192.
    PRIDEiQ14192.

    2D gel databases

    UCD-2DPAGEQ14192.

    PTM databases

    PhosphoSiteiQ14192.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle and heart.1 Publication

    Gene expression databases

    ArrayExpressiQ14192.
    BgeeiQ14192.
    CleanExiHS_FHL2.
    GenevestigatoriQ14192.

    Organism-specific databases

    HPAiCAB008368.
    HPA005922.
    HPA006028.

    Interactioni

    Subunit structurei

    Interacts with ZNF638 and TTN/titin. Interacts with E4F1. Interacts with GRB7. Interacts with SIRT1 and FOXO1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-701903,EBI-701903
    ATF3P188473EBI-701903,EBI-712767
    BRCA1P383986EBI-701903,EBI-349905
    FOXO1Q127788EBI-701903,EBI-1108782
    SIRT1Q96EB62EBI-701903,EBI-1802965
    SPHK1Q9NYA17EBI-701903,EBI-985303
    ZNF408Q9H9D43EBI-701903,EBI-347633

    Protein-protein interaction databases

    BioGridi108565. 64 interactions.
    DIPiDIP-5980N.
    IntActiQ14192. 61 interactions.
    MINTiMINT-120725.
    STRINGi9606.ENSP00000322909.

    Structurei

    Secondary structure

    1
    279
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 103
    Beta strandi20 – 223
    Beta strandi25 – 273
    Helixi29 – 368
    Turni41 – 433
    Beta strandi45 – 473
    Beta strandi53 – 564
    Beta strandi59 – 624
    Turni63 – 653
    Turni69 – 713
    Beta strandi76 – 783
    Helixi90 – 978
    Beta strandi101 – 1044
    Beta strandi110 – 1123
    Beta strandi114 – 1174
    Beta strandi120 – 1234
    Turni124 – 1274
    Beta strandi130 – 1323
    Beta strandi138 – 1447
    Beta strandi147 – 1504
    Helixi151 – 1577
    Beta strandi163 – 1653
    Beta strandi171 – 18212
    Turni183 – 1853
    Beta strandi189 – 1913
    Beta strandi201 – 2088
    Helixi210 – 2167
    Turni222 – 2254
    Beta strandi231 – 2333
    Turni246 – 2483
    Beta strandi252 – 2543
    Beta strandi267 – 2715
    Helixi273 – 2775

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X4KNMR-A101-159[»]
    1X4LNMR-A221-279[»]
    2D8ZNMR-A162-218[»]
    2MIUNMR-A1-98[»]
    ProteinModelPortaliQ14192.
    SMRiQ14192. Positions 1-159, 162-218, 225-279.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14192.

    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
    Domaini221 – 27555LIM zinc-binding 4PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The third LIM zinc-binding mediates interaction with E4F1.

    Sequence similaritiesi

    Contains 4 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.
    HOGENOMiHOG000231075.
    HOVERGENiHBG074526.
    InParanoidiQ14192.
    KOiK14380.
    OrthoDBiEOG7P8P7M.
    PhylomeDBiQ14192.
    TreeFamiTF321684.

    Family and domain databases

    Gene3Di2.10.110.10. 5 hits.
    InterProiIPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00412. LIM. 4 hits.
    [Graphical view]
    SMARTiSM00132. LIM. 4 hits.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q14192-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTERFDCHHC NESLFGKKYI LREESPYCVV CFETLFANTC EECGKPIGCD    50
    CKDLSYKDRH WHEACFHCSQ CRNSLVDKPF AAKEDQLLCT DCYSNEYSSK 100
    CQECKKTIMP GTRKMEYKGS SWHETCFICH RCQQPIGTKS FIPKDNQNFC 150
    VPCYEKQHAM QCVQCKKPIT TGGVTYREQP WHKECFVCTA CRKQLSGQRF 200
    TARDDFAYCL NCFCDLYAKK CAGCTNPISG LGGTKYISFE ERQWHNDCFN 250
    CKKCSLSLVG RGFLTERDDI LCPDCGKDI 279
    Length:279
    Mass (Da):32,193
    Last modified:October 17, 2006 - v3
    Checksum:iE94E3A7F6601F9F3
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671K → M.3 Publications
    Corresponds to variant rs1127588 [ dbSNP | Ensembl ].
    VAR_067455

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42176 mRNA. Translation: AAA85333.1.
    U29332 mRNA. Translation: AAC52073.1.
    AB038794 Genomic DNA. Translation: BAA92253.1.
    DQ307067 mRNA. Translation: ABC25549.1.
    BC014397 mRNA. Translation: AAH14397.1.
    U60117 mRNA. Translation: AAC50794.1.
    CCDSiCCDS2070.1.
    PIRiJC6565.
    RefSeqiNP_001034581.1. NM_001039492.2.
    NP_001441.4. NM_001450.3.
    NP_963849.1. NM_201555.1.
    NP_963851.2. NM_201557.3.
    XP_005263961.1. XM_005263904.1.
    XP_005263963.1. XM_005263906.1.
    UniGeneiHs.443687.

    Genome annotation databases

    EnsembliENST00000322142; ENSP00000322909; ENSG00000115641.
    ENST00000358129; ENSP00000350846; ENSG00000115641.
    ENST00000393352; ENSP00000377020; ENSG00000115641.
    ENST00000393353; ENSP00000377021; ENSG00000115641.
    ENST00000408995; ENSP00000386633; ENSG00000115641.
    ENST00000409807; ENSP00000386665; ENSG00000115641.
    GeneIDi2274.
    KEGGihsa:2274.
    UCSCiuc002tct.3. human.

    Polymorphism databases

    DMDMi116241364.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42176 mRNA. Translation: AAA85333.1 .
    U29332 mRNA. Translation: AAC52073.1 .
    AB038794 Genomic DNA. Translation: BAA92253.1 .
    DQ307067 mRNA. Translation: ABC25549.1 .
    BC014397 mRNA. Translation: AAH14397.1 .
    U60117 mRNA. Translation: AAC50794.1 .
    CCDSi CCDS2070.1.
    PIRi JC6565.
    RefSeqi NP_001034581.1. NM_001039492.2.
    NP_001441.4. NM_001450.3.
    NP_963849.1. NM_201555.1.
    NP_963851.2. NM_201557.3.
    XP_005263961.1. XM_005263904.1.
    XP_005263963.1. XM_005263906.1.
    UniGenei Hs.443687.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X4K NMR - A 101-159 [» ]
    1X4L NMR - A 221-279 [» ]
    2D8Z NMR - A 162-218 [» ]
    2MIU NMR - A 1-98 [» ]
    ProteinModelPortali Q14192.
    SMRi Q14192. Positions 1-159, 162-218, 225-279.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108565. 64 interactions.
    DIPi DIP-5980N.
    IntActi Q14192. 61 interactions.
    MINTi MINT-120725.
    STRINGi 9606.ENSP00000322909.

    PTM databases

    PhosphoSitei Q14192.

    Polymorphism databases

    DMDMi 116241364.

    2D gel databases

    UCD-2DPAGE Q14192.

    Proteomic databases

    MaxQBi Q14192.
    PaxDbi Q14192.
    PRIDEi Q14192.

    Protocols and materials databases

    DNASUi 2274.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322142 ; ENSP00000322909 ; ENSG00000115641 .
    ENST00000358129 ; ENSP00000350846 ; ENSG00000115641 .
    ENST00000393352 ; ENSP00000377020 ; ENSG00000115641 .
    ENST00000393353 ; ENSP00000377021 ; ENSG00000115641 .
    ENST00000408995 ; ENSP00000386633 ; ENSG00000115641 .
    ENST00000409807 ; ENSP00000386665 ; ENSG00000115641 .
    GeneIDi 2274.
    KEGGi hsa:2274.
    UCSCi uc002tct.3. human.

    Organism-specific databases

    CTDi 2274.
    GeneCardsi GC02M105974.
    HGNCi HGNC:3703. FHL2.
    HPAi CAB008368.
    HPA005922.
    HPA006028.
    MIMi 602633. gene.
    neXtProti NX_Q14192.
    Orphaneti 154. Familial isolated dilated cardiomyopathy.
    PharmGKBi PA164.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314122.
    HOGENOMi HOG000231075.
    HOVERGENi HBG074526.
    InParanoidi Q14192.
    KOi K14380.
    OrthoDBi EOG7P8P7M.
    PhylomeDBi Q14192.
    TreeFami TF321684.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.

    Miscellaneous databases

    ChiTaRSi FHL2. human.
    EvolutionaryTracei Q14192.
    GeneWikii FHL2.
    GenomeRNAii 2274.
    NextBioi 9247.
    PROi Q14192.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14192.
    Bgeei Q14192.
    CleanExi HS_FHL2.
    Genevestigatori Q14192.

    Family and domain databases

    Gene3Di 2.10.110.10. 5 hits.
    InterProi IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 4 hits.
    [Graphical view ]
    SMARTi SM00132. LIM. 4 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Subtractive cloning and characterization of DRAL, a novel LIM-domain protein down-regulated in rhabdomyosarcoma."
      Genini M., Schwalbe P., Scholl F.A., Remppis A., Mattei M.-G., Schaefer B.W.
      DNA Cell Biol. 16:433-442(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skeletal muscle.
    2. "Molecular cloning and characterization of FHL2, a novel LIM domain protein preferentially expressed in human heart."
      Chan K.K., Tsui S.K.W., Lee S.M.Y., Luk S.C.W., Liew C.C., Fung K.P., Waye M.M.Y., Lee C.Y.
      Gene 210:345-350(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-167.
      Tissue: Heart.
    3. "Alzheimer's disease-associated presenilin 2 interacts with DRAL, an LIM-domain protein."
      Tanahashi H., Tabira T.
      Hum. Mol. Genet. 9:2281-2289(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Leukocyte.
    4. "The FHL2 LIM-domain protein is implicated in hematopoiesis and leukemogenesis."
      Qian Z., Mao L., Fernald A., Yu H., Luo R., Anastasi J., Le Beau M.M.
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-167.
      Tissue: Bone marrow.
    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].
      Tissue: Placenta.
    6. "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] OF 127-279, VARIANT MET-167.
      Tissue: Heart muscle.
    7. "Interaction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220."
      Ng E.K.O., Chan K.K., Wong C.H., Tsui S.K.W., Ngai S.M., Lee S.M.Y., Kotaka M., Lee C.Y., Waye M.M.Y., Fung K.P.
      J. Cell. Biochem. 84:556-566(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ZNF638.
    8. "Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2."
      Lange S., Auerbach D., McLoughlin P., Perriard E., Schafer B.W., Perriard J.-C., Ehler E.
      J. Cell Sci. 115:4925-4936(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TTN.
    9. "Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation."
      Yang Y., Hou H., Haller E.M., Nicosia S.V., Bai W.
      EMBO J. 24:1021-1032(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SIRT1 AND FOXO1.
    10. Cited for: FUNCTION, INTERACTION WITH E4F1, SUBCELLULAR LOCATION.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "The cell migration protein Grb7 associates with transcriptional regulator FHL2 in a Grb7 phosphorylation-dependent manner."
      Siamakpour-Reihani S., Argiros H.J., Wilmeth L.J., Haas L.L., Peterson T.A., Johnson D.L., Shuster C.B., Lyons B.A.
      J. Mol. Recognit. 22:9-17(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GRB7.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structure of LIM domains in LIM-protein 3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 98-279.

    Entry informationi

    Entry nameiFHL2_HUMAN
    AccessioniPrimary (citable) accession number: Q14192
    Secondary accession number(s): Q13229
    , Q13644, Q2I5I4, Q9P294
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 141 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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