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Q13642

- FHL1_HUMAN

UniProt

Q13642 - FHL1_HUMAN

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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

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. 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
Complete GO annotation...

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. focal adhesion Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: BHF-UCL
Complete GO annotation...

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

BgeeiQ13642.
ExpressionAtlasiQ13642. baseline and differential.
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. 30 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 1-223.
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.
GeneTreeiENSGT00760000118910.
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) [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

        10         20         30         40         50
MAEKFDCHYC RDPLQGKKYV QKDGHHCCLK CFDKFCANTC VECRKPIGAD
60 70 80 90 100
SKEVHYKNRF WHDTCFRCAK CLHPLANETF VAKDNKILCN KCTTREDSPK
110 120 130 140 150
CKGCFKAIVA GDQNVEYKGT VWHKDCFTCS NCKQVIGTGS FFPKGEDFYC
160 170 180 190 200
VTCHETKFAK HCVKCNKAIT SGGITYQDQP WHADCFVCVT CSKKLAGQRF
210 220 230 240 250
TAVEDQYYCV DCYKNFVAKK CAGCKNPITG KRTVSRVSHP VSKARKPPVC
260 270 280 290 300
HGKRLPLTLF PSANLRGRHP GGERTCPSWV VVLYRKNRSL AAPRGPGLVK
310 320
APVWWPMKDN PGTTTASTAK NAP
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]
CCDS76036.1. [Q13642-3]
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]
ENST00000618438; ENSP00000477609; ENSG00000022267. [Q13642-3]
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 ]
CCDS76036.1. [Q13642-3 ]
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 1-223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108564. 30 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 ]
ENST00000618438 ; ENSP00000477609 ; ENSG00000022267 . [Q13642-3 ]
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.
GeneTreei ENSGT00760000118910.
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

Bgeei Q13642.
ExpressionAtlasi Q13642. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 149 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

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