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Q13642 (FHL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FHL1
Synonyms:SLIM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have an involvement in muscle development or hypertrophy.

Subcellular location

Isoform 1: Cytoplasm.

Isoform 3: Cytoplasm. Nucleus.

Isoform 2: Nucleus. Cytoplasmcytosol. Note: Predominantly nuclear in myoblasts but is cytosolic in differentiated myotubes. Ref.5 Ref.6 Ref.7

Tissue specificity

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. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Developmental stage

Elevated levels during postnatal muscle growth. Ref.13

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

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.

Sequence similarities

Contains 3 LIM zinc-binding domains.

Sequence caution

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

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

Ontologies

Keywords
   Biological processDifferentiation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainLIM domain
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionDevelopmental protein
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

muscle organ development

Non-traceable author statement Ref.13. Source: UniProtKB

negative regulation of G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 21702045. Source: UniProtKB

negative regulation of G2/M transition of mitotic cell cycle

Inferred from direct assay PubMed 21702045. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay PubMed 21702045. Source: UniProtKB

organ morphogenesis

Non-traceable author statement Ref.13. Source: UniProtKB

positive regulation of potassium ion transport

Inferred from direct assay PubMed 18281375. Source: BHF-UCL

regulation of membrane depolarization

Inferred from direct assay PubMed 18281375. Source: BHF-UCL

regulation of potassium ion transmembrane transporter activity

Inferred from direct assay PubMed 18281375. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 21702045. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 21702045. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 18281375. Source: BHF-UCL

   Molecular_functionion channel binding

Inferred from physical interaction PubMed 18281375. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NRIP1P485526EBI-912547,EBI-746484
PPP2CBP627143EBI-8477209,EBI-1044367

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q13642-2)

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.
Isoform 1 (identifier: Q13642-1)

Also known as: FHL1; FHL1A; SLIM1;

The sequence of this isoform differs from the canonical sequence as follows:
     231-323: KRTVSRVSHP...TTASTAKNAP → FGKGSSVVAY...VYCPDCAKKL
Isoform 3 (identifier: Q13642-3)

Also known as: FHL1C;

The sequence of this isoform differs from the canonical sequence as follows:
     168-296: Missing.
Isoform 4 (identifier: Q13642-4)

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.
Isoform 5 (identifier: Q13642-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 323322Four and a half LIM domains protein 1
PRO_0000075735

Regions

Domain40 – 9253LIM zinc-binding 1
Domain101 – 15353LIM zinc-binding 2
Domain162 – 21251LIM zinc-binding 3
Zinc finger7 – 3125C4-type Potential

Amino acid modifications

Modified residue41N6-acetyllysine By similarity

Natural variations

Alternative sequence11M → MTFYVASLALELIWMLSSPA GPSSYKVGTM in isoform 4.
VSP_043162
Alternative sequence11M → MASHRHSGPSSYKVGTM in isoform 5.
VSP_043404
Alternative sequence168 – 296129Missing in isoform 3.
VSP_010693
Alternative sequence231 – 32393KRTVS…AKNAP → FGKGSSVVAYEGQSWHDYCF HCKKCSVNLANKRFVFHQEQ VYCPDCAKKL in isoform 1, isoform 4 and isoform 5.
VSP_010694
Natural variant1221W → S in SPM. Ref.19
VAR_042603
Natural variant1231H → 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. Ref.20
VAR_045999
Natural variant1281T → TI in XMPMA. Ref.18
VAR_042604
Natural variant1321C → 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. Ref.20
VAR_046000
Natural variant1531C → R in RBM; X-linked childhood-onset. Ref.20
VAR_046001
Natural variant1531C → Y in RBM; X-linked childhood-onset. Ref.20
VAR_046002
Natural variant2241C → W in XMPMA. Ref.18
VAR_042605

Experimental info

Sequence conflict731H → Q in AAC52021. Ref.1
Sequence conflict81 – 9111VAKDNKILCNK → CGQGQQRSCAQ in AAD21579. Ref.4
Sequence conflict981S → F Ref.1
Sequence conflict981S → F Ref.4
Sequence conflict1581F → L Ref.1
Sequence conflict1581F → L Ref.13
Sequence conflict2391H → R in AAC72390. Ref.5

Secondary structure

................................................. 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (FHL1B) (SLIMMER) [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 50FD17F7B2606823

FASTA32336,263
        10         20         30         40         50         60 
MAEKFDCHYC RDPLQGKKYV QKDGHHCCLK CFDKFCANTC VECRKPIGAD SKEVHYKNRF 

        70         80         90        100        110        120 
WHDTCFRCAK CLHPLANETF VAKDNKILCN KCTTREDSPK CKGCFKAIVA GDQNVEYKGT 

       130        140        150        160        170        180 
VWHKDCFTCS NCKQVIGTGS FFPKGEDFYC VTCHETKFAK HCVKCNKAIT SGGITYQDQP 

       190        200        210        220        230        240 
WHADCFVCVT CSKKLAGQRF TAVEDQYYCV DCYKNFVAKK CAGCKNPITG KRTVSRVSHP 

       250        260        270        280        290        300 
VSKARKPPVC HGKRLPLTLF PSANLRGRHP GGERTCPSWV VVLYRKNRSL AAPRGPGLVK 

       310        320 
APVWWPMKDN PGTTTASTAK NAP 

« Hide

Isoform 1 (FHL1) (FHL1A) (SLIM1) [UniParc].

Checksum: 2FC873D70E62834D
Show »

FASTA28031,895
Isoform 3 (FHL1C) [UniParc].

Checksum: 2DBD610944FFE5EC
Show »

FASTA19422,017
Isoform 4 [UniParc].

Checksum: 70D165A814166097
Show »

FASTA30934,997
Isoform 5 [UniParc].

Checksum: 24EAD21C9DEF4DAD
Show »

FASTA29633,579

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The developmental regulation of a novel muscle LIM-protein."
Morgan M.J., Madgwick A.J.A., Charleston B., Pell J.M., Loughna P.T.
Biochem. Biophys. Res. Commun. 212:840-846(1995) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy."
Schessl J., Zou Y., McGrath M.J., Cowling B.S., Maiti B., Chin S.S., Sewry C., Battini R., Hu Y., Cottle D.L., Rosenblatt M., Spruce L., Ganguly A., Kirschner J., Judkins A.R., Golden J.A., Goebel H.-H., Muntoni F. expand/collapse author list , Flanigan K.M., Mitchell C.A., Boennemann C.G.
J. Clin. Invest. 118:904-912(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RBM TYR-123; PHE-132; TYR-153 AND ARG-153.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRG01884.
G02741. JC4893.
RefSeqNP_001153171.1. NM_001159699.1.
NP_001153172.1. NM_001159700.1.
NP_001153173.1. NM_001159701.1.
NP_001153174.1. NM_001159702.2.
NP_001153175.1. NM_001159703.1.
NP_001153176.1. NM_001159704.1.
NP_001161291.1. NM_001167819.1.
NP_001440.2. NM_001449.4.
UniGeneHs.435369.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X63NMR-A91-158[»]
2CUPNMR-A40-126[»]
2CURNMR-A162-216[»]
2EGQNMR-A211-280[»]
ProteinModelPortalQ13642.
SMRQ13642. Positions 2-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108564. 30 interactions.
IntActQ13642. 27 interactions.

Polymorphism databases

DMDM59800384.

Proteomic databases

PaxDbQ13642.
PRIDEQ13642.

Protocols and materials databases

DNASU2273.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345434; 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]
GeneID2273.
KEGGhsa:2273.
UCSCuc004ezl.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

CTD2273.
GeneCardsGC0XP135229.
HGNCHGNC:3702. FHL1.
HPACAB020817.
HPA001040.
HPA001391.
MIM300163. gene.
300695. phenotype.
300696. phenotype.
300717. phenotype.
300718. phenotype.
neXtProtNX_Q13642.
Orphanet155. Familial isolated hypertrophic cardiomyopathy.
97239. Reducing body myopathy.
85146. Scapuloperoneal amyotrophy.
98863. X-linked Emery-Dreifuss muscular dystrophy.
178461. X-linked myopathy with postural muscle atrophy.
PharmGKBPA28141.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314122.
HOVERGENHBG074526.
InParanoidQ13642.
KOK14365.
OMAFHEEQVY.
OrthoDBEOG7P8P7M.
PhylomeDBQ13642.
TreeFamTF318571.

Gene expression databases

ArrayExpressQ13642.
BgeeQ13642.
GenevestigatorQ13642.

Family and domain databases

Gene3D2.10.110.10. 3 hits.
InterProIPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 3 hits.
[Graphical view]
SMARTSM00132. LIM. 3 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 3 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFHL1. human.
EvolutionaryTraceQ13642.
GeneWikiFHL1.
GenomeRNAi2273.
NextBio9243.
PROQ13642.
SOURCESearch...

Entry information

Entry nameFHL1_HUMAN
AccessionPrimary (citable) accession number: Q13642
Secondary accession number(s): B7Z5T4 expand/collapse secondary AC list , B7Z793, O95212, Q13230, Q13645, Q5JXI7, Q5M7Y6, Q6IB30, Q9NZ40, Q9UKZ8, Q9Y630
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM