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Protein

Four and a half LIM domains protein 1

Gene

FHL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Zinc fingeri7 – 31C4-typeSequence analysisAdd BLAST25

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • animal organ morphogenesis Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • muscle organ development Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  • negative regulation of G2/M transition of mitotic cell cycle Source: UniProtKB
  • positive regulation of potassium ion transport Source: BHF-UCL
  • regulation of membrane depolarization Source: BHF-UCL
  • 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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000022267-MONOMER.
SIGNORiQ13642.

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
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3702. FHL1.

Subcellular locationi

Isoform 2 :

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
  • focal adhesion Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Emery-Dreifuss muscular dystrophy 6, X-linked (EDMD6)1 Publication
The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry.
Disease descriptionA form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.
See also OMIM:300696
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075357209C → R in EDMD6. 1 PublicationCorresponds to variant rs122459149dbSNPEnsembl.1
Natural variantiVAR_075358276C → Y in EDMD6; drastically reduced protein levels in muscle. 1 Publication1
Scapuloperoneal myopathy, X-linked dominant (SPM)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300695
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042603122W → S in SPM. 1 PublicationCorresponds to variant rs122458140dbSNPEnsembl.1
Natural variantiVAR_076566154H → P in SPM. 1 Publication1
Myopathy, X-linked, with postural muscle atrophy (XMPMA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300696
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042604128T → TI in XMPMA. 1 Publication1
Natural variantiVAR_042605224C → W in XMPMA. 2 PublicationsCorresponds to variant rs122458141dbSNPEnsembl.1
Natural variantiVAR_075359280V → M in XMPMA. 1 PublicationCorresponds to variant rs267606811dbSNPEnsembl.1
Isoform 1 (identifier: Q13642-1)
Natural varianti246H → Y in XMPMA, unknown pathological significance. 1 Publication1
Reducing body myopathy, X-linked 1A, severe, with infantile or early childhood onset (RBMX1A)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300717
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075350101C → F in RBMX1A; unknown pathological significance. 1 Publication1
Natural variantiVAR_075353123H → L in RBMX1A. 1 PublicationCorresponds to variant rs267606812dbSNPEnsembl.1
Natural variantiVAR_075354123H → Q in RBMX1A. 1 PublicationCorresponds to variant rs267606813dbSNPEnsembl.1
Natural variantiVAR_045999123H → Y in RBMX1A; the mutant protein initiates aggregation of the FHL1 protein causing reducing bodies formation; dominant-negative effect. 2 PublicationsCorresponds to variant rs122458142dbSNPEnsembl.1
Natural variantiVAR_046000132C → F in RBMX1A; the mutant protein initiates aggregation of the FHL1 protein causing reducing bodies formation; dominant-negative effect. 2 PublicationsCorresponds to variant rs122458143dbSNPEnsembl.1
Natural variantiVAR_075356150C → Y in RBMX1A; unknown pathological significance. 1 PublicationCorresponds to variant rs122459146dbSNPEnsembl.1
Reducing body myopathy, X-linked 1B, with late childhood or adult onset (RBMX1B)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300718
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075351102 – 104Missing in RBMX1B; unknown pathological significance. 1 Publication3
Natural variantiVAR_075352104C → R in RBMX1B; unknown pathological significance. 1 PublicationCorresponds to variant rs122459147dbSNPEnsembl.1
Natural variantiVAR_075355150C → S in RBMX1B. 1 Publication1
Natural variantiVAR_046001153C → R in RBMX1B. 2 PublicationsCorresponds to variant rs122458144dbSNPEnsembl.1
Natural variantiVAR_046002153C → Y in RBMX1B. 2 PublicationsCorresponds to variant rs122458145dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Emery-Dreifuss muscular dystrophy

Organism-specific databases

DisGeNETi2273.
MalaCardsiFHL1.
MIMi300695. phenotype.
300696. phenotype.
300717. phenotype.
300718. phenotype.
OpenTargetsiENSG00000022267.
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.

Polymorphism and mutation databases

BioMutaiFHL1.
DMDMi59800384.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000757352 – 323Four and a half LIM domains protein 1Add BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4N6-acetyllysineBy similarity1
Cross-linki86Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ13642.
PaxDbiQ13642.
PeptideAtlasiQ13642.
PRIDEiQ13642.
TopDownProteomicsiQ13642-1. [Q13642-1]

PTM databases

iPTMnetiQ13642.
PhosphoSitePlusiQ13642.

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

BgeeiENSG00000022267.
ExpressionAtlasiQ13642. baseline and differential.
GenevisibleiQ13642. HS.

Organism-specific databases

HPAiCAB020817.
HPA001040.
HPA001391.

Interactioni

Binary interactionsi

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

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108564. 34 interactors.
IntActiQ13642. 29 interactors.
STRINGi9606.ENSP00000071281.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 43Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi53 – 56Combined sources4
Beta strandi59 – 62Combined sources4
Turni63 – 65Combined sources3
Beta strandi69 – 71Combined sources3
Beta strandi81 – 83Combined sources3
Beta strandi86 – 88Combined sources3
Helixi90 – 93Combined sources4
Beta strandi102 – 104Combined sources3
Beta strandi110 – 112Combined sources3
Beta strandi114 – 116Combined sources3
Beta strandi121 – 123Combined sources3
Turni124 – 126Combined sources3
Beta strandi130 – 132Combined sources3
Beta strandi141 – 144Combined sources4
Beta strandi147 – 150Combined sources4
Helixi151 – 157Combined sources7
Beta strandi163 – 165Combined sources3
Beta strandi174 – 176Combined sources3
Beta strandi179 – 181Combined sources3
Turni183 – 186Combined sources4
Turni189 – 191Combined sources3
Beta strandi200 – 202Combined sources3
Beta strandi207 – 209Combined sources3
Helixi210 – 217Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ13642.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 92LIM zinc-binding 1PROSITE-ProRule annotationAdd BLAST53
Domaini101 – 153LIM zinc-binding 2PROSITE-ProRule annotationAdd BLAST53
Domaini162 – 212LIM zinc-binding 3PROSITE-ProRule annotationAdd BLAST51

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri7 – 31C4-typeSequence analysisAdd BLAST25

Keywords - Domaini

LIM domain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410INGD. Eukaryota.
ENOG410YDMU. LUCA.
GeneTreeiENSGT00760000118910.
HOVERGENiHBG074526.
InParanoidiQ13642.
KOiK14365.
OMAiEDQFYCV.
OrthoDBiEOG091G07C5.
PhylomeDBiQ13642.
TreeFamiTF318571.

Family and domain databases

Gene3Di2.10.110.10. 4 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. AlignAdd to basket

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73H → Q in AAC52021 (PubMed:8753811).Curated1
Sequence conflicti81 – 91VAKDNKILCNK → CGQGQQRSCAQ in AAD21579 (PubMed:10352231).CuratedAdd BLAST11
Sequence conflicti98S → F (PubMed:8753811).Curated1
Sequence conflicti98S → F (PubMed:10352231).Curated1
Sequence conflicti158F → L (PubMed:8753811).Curated1
Sequence conflicti158F → L (PubMed:7626119).Curated1
Sequence conflicti239H → R in AAC72390 (PubMed:10524257).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075350101C → F in RBMX1A; unknown pathological significance. 1 Publication1
Natural variantiVAR_075351102 – 104Missing in RBMX1B; unknown pathological significance. 1 Publication3
Natural variantiVAR_075352104C → R in RBMX1B; unknown pathological significance. 1 PublicationCorresponds to variant rs122459147dbSNPEnsembl.1
Natural variantiVAR_042603122W → S in SPM. 1 PublicationCorresponds to variant rs122458140dbSNPEnsembl.1
Natural variantiVAR_075353123H → L in RBMX1A. 1 PublicationCorresponds to variant rs267606812dbSNPEnsembl.1
Natural variantiVAR_075354123H → Q in RBMX1A. 1 PublicationCorresponds to variant rs267606813dbSNPEnsembl.1
Natural variantiVAR_045999123H → Y in RBMX1A; the mutant protein initiates aggregation of the FHL1 protein causing reducing bodies formation; dominant-negative effect. 2 PublicationsCorresponds to variant rs122458142dbSNPEnsembl.1
Natural variantiVAR_042604128T → TI in XMPMA. 1 Publication1
Natural variantiVAR_046000132C → F in RBMX1A; the mutant protein initiates aggregation of the FHL1 protein causing reducing bodies formation; dominant-negative effect. 2 PublicationsCorresponds to variant rs122458143dbSNPEnsembl.1
Natural variantiVAR_075355150C → S in RBMX1B. 1 Publication1
Natural variantiVAR_075356150C → Y in RBMX1A; unknown pathological significance. 1 PublicationCorresponds to variant rs122459146dbSNPEnsembl.1
Natural variantiVAR_046001153C → R in RBMX1B. 2 PublicationsCorresponds to variant rs122458144dbSNPEnsembl.1
Natural variantiVAR_046002153C → Y in RBMX1B. 2 PublicationsCorresponds to variant rs122458145dbSNPEnsembl.1
Natural variantiVAR_076566154H → P in SPM. 1 Publication1
Natural variantiVAR_075357209C → R in EDMD6. 1 PublicationCorresponds to variant rs122459149dbSNPEnsembl.1
Natural variantiVAR_042605224C → W in XMPMA. 2 PublicationsCorresponds to variant rs122458141dbSNPEnsembl.1
Natural variantiVAR_075358276C → Y in EDMD6; drastically reduced protein levels in muscle. 1 Publication1
Natural variantiVAR_075359280V → M in XMPMA. 1 PublicationCorresponds to variant rs267606811dbSNPEnsembl.1
Isoform 1 (identifier: Q13642-1)
Natural varianti246H → Y in XMPMA, unknown pathological significance. 1 Publication1
Natural varianti275D → N.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0431621M → MTFYVASLALELIWMLSSPA GPSSYKVGTM in isoform 4. 1 Publication1
Alternative sequenceiVSP_0434041M → MASHRHSGPSSYKVGTM in isoform 5. 1 Publication1
Alternative sequenceiVSP_010693168 – 296Missing in isoform 3. 1 PublicationAdd BLAST129
Alternative sequenceiVSP_010694231 – 323KRTVS…AKNAP → FGKGSSVVAYEGQSWHDYCF HCKKCSVNLANKRFVFHQEQ VYCPDCAKKL in isoform 1, isoform 4 and isoform 5. 6 PublicationsAdd BLAST93

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006724744.2. [Q13642-2]
XP_006724808.1. XM_006724745.3. [Q13642-2]
XP_006724809.1. XM_006724746.2. [Q13642-2]
XP_006724810.1. XM_006724747.2. [Q13642-1]
XP_016884846.1. XM_017029357.1. [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]
ENST00000628568; ENSP00000486782; ENSG00000022267. [Q13642-1]
ENST00000629039; ENSP00000486439; ENSG00000022267. [Q13642-1]
ENST00000630084; ENSP00000485897; ENSG00000022267. [Q13642-1]
GeneIDi2273.
KEGGihsa:2273.
UCSCiuc004ezl.3. human. [Q13642-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006724744.2. [Q13642-2]
XP_006724808.1. XM_006724745.3. [Q13642-2]
XP_006724809.1. XM_006724746.2. [Q13642-2]
XP_006724810.1. XM_006724747.2. [Q13642-1]
XP_016884846.1. XM_017029357.1. [Q13642-1]
UniGeneiHs.435369.

3D structure databases

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

Protein-protein interaction databases

BioGridi108564. 34 interactors.
IntActiQ13642. 29 interactors.
STRINGi9606.ENSP00000071281.

PTM databases

iPTMnetiQ13642.
PhosphoSitePlusiQ13642.

Polymorphism and mutation databases

BioMutaiFHL1.
DMDMi59800384.

Proteomic databases

EPDiQ13642.
PaxDbiQ13642.
PeptideAtlasiQ13642.
PRIDEiQ13642.
TopDownProteomicsiQ13642-1. [Q13642-1]

Protocols and materials databases

DNASUi2273.
Structural Biology KnowledgebaseSearch...

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]
ENST00000628568; ENSP00000486782; ENSG00000022267. [Q13642-1]
ENST00000629039; ENSP00000486439; ENSG00000022267. [Q13642-1]
ENST00000630084; ENSP00000485897; ENSG00000022267. [Q13642-1]
GeneIDi2273.
KEGGihsa:2273.
UCSCiuc004ezl.3. human. [Q13642-2]

Organism-specific databases

CTDi2273.
DisGeNETi2273.
GeneCardsiFHL1.
GeneReviewsiFHL1.
HGNCiHGNC:3702. FHL1.
HPAiCAB020817.
HPA001040.
HPA001391.
MalaCardsiFHL1.
MIMi300163. gene.
300695. phenotype.
300696. phenotype.
300717. phenotype.
300718. phenotype.
neXtProtiNX_Q13642.
OpenTargetsiENSG00000022267.
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.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INGD. Eukaryota.
ENOG410YDMU. LUCA.
GeneTreeiENSGT00760000118910.
HOVERGENiHBG074526.
InParanoidiQ13642.
KOiK14365.
OMAiEDQFYCV.
OrthoDBiEOG091G07C5.
PhylomeDBiQ13642.
TreeFamiTF318571.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000022267-MONOMER.
SIGNORiQ13642.

Miscellaneous databases

ChiTaRSiFHL1. human.
EvolutionaryTraceiQ13642.
GeneWikiiFHL1.
GenomeRNAii2273.
PROiQ13642.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000022267.
ExpressionAtlasiQ13642. baseline and differential.
GenevisibleiQ13642. HS.

Family and domain databases

Gene3Di2.10.110.10. 4 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 170 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.