Tag Content
SG ID
SG00006417 
UniProt Accession
Theoretical PI
8.76  
Molecular Weight
31889 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Fhl1 
Gene Synonyms/Alias
 
Protein Name
Four and a half LIM domains protein 1 
Protein Synonyms/Alias
FHL-1 KyoT; RBP-associated molecule 14-1;RAM14-1 Skeletal muscle LIM-protein 1;SLIMSLIM-1 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:X;53984964-54046523;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.169459313 
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Description
Temporarily unavailable 
Abstract of related literatures
1. We have determined the complete mRNA sequence of FHL3 (formerly SLIM2). We have confirmed that it is a member of the family of LIM proteins that share a similar secondary protein structure, renamed as Four-and-a-Half-LIM domain (or FHL) proteins in accordance with this structure. The "half-LIM" domain is a single zinc finger domain that may represent a subfamily of LIM domains and defines this particular family of LIM proteins. The distribution of FHL mRNA expression within a variety of murine tissues is complex. Both FHL1 and FHL3 were expressed in a number of skeletal muscles while FHL2 was expressed at high levels in cardiac muscle. Localisation of FHL3 to human chromosome 1 placed this gene in the proximity of, but not overlapping with, alleles associated with muscle diseases. FHL1 and FHL3 mRNAs were reciprocally expressed in the murine C2C12 skeletal muscle cell line and this suggested that the pattern of expression was linked to key events in myogenesis. PMID: [10049693] 

2. The RBP-J/Su(H) DNA-binding protein plays a key role in transcriptional regulation by targeting Epstein-Barr virus nuclear antigen 2 (EBNA2) and the intracellular portions of Notch receptors to specific promoters. Using the yeast two-hybrid system, we isolated a LIM-only protein, KyoT, which physically interacts with RBP-J. Differential splicing gave rise to two transcripts of the KyoT gene, KyoT1 and KyoT2, that encoded proteins with four and two LIM domains, respectively. With differential splicing resulting in deletion of an exon, KyoT2 lacked two LIM domains from the C terminus and had a frameshift in the last exon, creating the RBP-J-binding region in the C terminus. KyoT1 had a negligible level of interaction with RBP-J. Strong expression of KyoT mRNAs was detected in skeletal muscle and lung, with a predominance of KyoT1 mRNA. When expressed in F9 embryonal carcinoma cells, KyoT1 and KyoT2 were localized in the cytoplasm and the nucleus, respectively. The binding site of KyoT2 on RBP-J overlaps those of EBNA2 and Notchl but is distinct from that of Hairless, the negative regulator of RBP-J-mediated transcription in Drosophila. KyoT2 but not KyoT1 repressed the RBP-J-mediated transcriptional activation by EBNA2 and Notch1 by competing with them for binding to RBP-J and by dislocating RBP-J from DNA. KyoT2 is a novel negative regulatory molecule for RBP-J-mediated transcription in mammalian systems. PMID: [9418910] 

3. LIM domain containing proteins play critical roles in animal development and cellular differentiation. Here, we describe the cloning and expression patterns of three members of the four and a half LIM domain-only protein family, FHL1, 2, and 3, from mouse. A comparison of embryonic expression patterns of these three highly-related genes indicates that they are expressed in an overlapping pattern in the developing cardiovascular system, and skeletal muscle. In adult tissues, the three genes are expressed in a predominant and overlapping manner in cardiac and skeletal muscle. Of the three genes, FHL2 appears to have the most restricted expression pattern during development, in heart, blood vessels, and skeletal muscle. Expression in heart is highest in cardiac septa and in the region adjacent to the atrio-ventricular ring, suggesting a potential role in septation or conduction system development. In the heart, FHL1expression was observed strongly in developing outflow tract, and to a lesser extent in myocardium. FHL3 displays low and ubiquitous expression during mouse development. Cardiac ventricular expression of FHL1, but not FHL2 or FHL3, was upregulated in two mouse models of cardiac hypertrophic and dilated cardiomyopathy. Taken together, these data indicate the potential importance of this FHL family in the development and maintenance of the cardiovascular system and striated muscle, and suggest that FHL1 may play a role in the development of heart disease. PMID: [10906474] 

4. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

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Function
May have an involvement in muscle development orhypertrophy. Isoform 2 binds to RBP-J and plays a negativeregulatory role in the RBP-J-mediated transcription in mammaliansystems. 
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Subcellular Location
Isoform 2: Nucleus. 
Tissue Specificity
Isoform 1 seems to be most abundant in eachtissue and isoform 2 much less abundant. Isoform 1 is highlyexpressed in skeletal muscle and lung, and to a lesser extent inheart, brain and kidney. Isoform 2 was found in brain, lung kidneyand genital organs. 
Gene Ontology
GO IDGO termEvidence
GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell.
GO:0005634 C:nucleus IEA:UniProtKB-SubCell.
GO:0008270 F:zinc ion binding IEA:InterPro.
GO:0030154 P:cell differentiation IEA:UniProtKB-KW.
GO:0007275 P:multicellular organismal development IEA:UniProtKB-KW.
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Interpro
IPR001781;    Znf_LIM.
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Pfam
PF00412;    LIM;    4.
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SMART
SM00132;    LIM;    4.
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PROSITE
PS00478;    LIM_DOMAIN_1;    4.
PS50023;    LIM_DOMAIN_2;    4.
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PRINTS
Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    280       Four and a half LIM domains protein 1.
                             /FTId=PRO_0000075736.
DOMAIN       40     92       LIM zinc-binding 1.
DOMAIN      101    153       LIM zinc-binding 2.
DOMAIN      162    212       LIM zinc-binding 3.
DOMAIN      221    276       LIM zinc-binding 4.
ZN_FING       7     31       C4-type (Potential).
VAR_SEQ     168    194       AITSGGITYQDQPWHAECFVCVTCSKK -> GLVKAPVWWP
                             MKDNPGTTTASTAKNAP (in isoform 2).
                             /FTId=VSP_003120.
VAR_SEQ     195    280       Missing (in isoform 2).
                             /FTId=VSP_003121.
CONFLICT     98     98       S -> F (in Ref. 1; AAC02727).
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Nucleotide Sequence
Length: 2377 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 280 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
Gene Symbol Ref Databases
Akap12MINT 
CBX4MINT 
RING1MINT 
RBPJMINT 
Other Protein-Protein interaction resources
String database  
View Microarray data
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