Q13642 (FHL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	FHL1
Synonyms:	SLIM1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Cytoplasm › cytosol. 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	X-linked dominant scapuloperoneal myopathy (SPM) [MIM:300695]: Scapuloperoneal syndrome (SPS) was initially described more than 120 years ago by Jules Broussard as 'une forme hereditaire d'atrophie musculaire progressive' beginning in the lower legs and affecting the shoulder region earlier and more severely than distal arm. The etiology of this condition remains unclear. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 X-linked myopathy with postural muscle atrophy (XMPMA) [MIM:300696]: Myopathies are inherited muscle disorders characterized by weakness and atrophy of voluntary skeletal muscle, and several types of myopathy also show involvement of cardiac muscle. XMPMA is a distinct form of adult-onset X-linked recessive myopathy with several features in common with other myopathies, but the presentation of a pseudoathletic phenotype, scapuloperoneal weakness, and bent spine is unique and might render the clinical phenotype distinguishable from other myopathies. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 X-linked severe early-onset reducing body myopathy (RBM) [MIM:300717]: Rare muscle disorder causing progressive muscular weakness and characteristic intracytoplasmic inclusions in myofibers. Clinical presentations of RBM have ranged from early-onset fatal to childhood onset to adult onset cases. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 X-linked childhood-onset reducing body myopathy (CO-RBM) [MIM:300718]: This disorder is allelic to severe early-onset reducing body myopathy (RBM). 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 process	Differentiation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Cardiomyopathy Disease mutation
Domain	LIM domain Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Developmental protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell 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_component	cytoplasm 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_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NRIP1	P48552	6	EBI-912547,EBI-746484

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.14

Chain

2 – 323

322

Four and a half LIM domains protein 1

PRO_0000075735

Regions

Domain

40 – 92

53

LIM zinc-binding 1

Domain

101 – 153

53

LIM zinc-binding 2

Domain

162 – 212

51

LIM zinc-binding 3

Zinc finger

7 – 31

25

C4-type Potential

Natural variations

Alternative sequence

1

1

M → MTFYVASLALELIWMLSSPA GPSSYKVGTM in isoform 4.

VSP_043162

Alternative sequence

1

1

M → MASHRHSGPSSYKVGTM in isoform 5.

VSP_043404

Alternative sequence

168 – 296

129

Missing in isoform 3.

VSP_010693

Alternative sequence

231 – 323

93

KRTVS…AKNAP → FGKGSSVVAYEGQSWHDYCF HCKKCSVNLANKRFVFHQEQ VYCPDCAKKL in isoform 1, isoform 4 and isoform 5.

VSP_010694

Natural variant

122

1

W → S in SPM. Ref.19

VAR_042603

Natural variant

123

1

H → 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 variant

128

1

T → TI in XMPMA. Ref.18

VAR_042604

Natural variant

132

1

C → 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 variant

153

1

C → R in RBM; X-linked childhood-onset. Ref.20

VAR_046001

Natural variant

153

1

C → Y in RBM; X-linked childhood-onset. Ref.20

VAR_046002

Natural variant

224

1

C → W in XMPMA. Ref.18

VAR_042605

Experimental info

Sequence conflict

73

1

H → Q in AAC52021. Ref.1

Sequence conflict

81 – 91

11

VAKDNKILCNK → CGQGQQRSCAQ in AAD21579. Ref.4

Sequence conflict

98

1

S → F Ref.1

Sequence conflict

98

1

S → F Ref.4

Sequence conflict

158

1

F → L Ref.1

Sequence conflict

158

1

F → L Ref.13

Sequence conflict

239

1

H → R in AAC72390. Ref.5

Secondary structure

1

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323

Helix Strand Turn

Details...

Beta strand

41 – 43

3

Beta strand

49 – 51

3

Beta strand

53 – 56

4

Beta strand

59 – 62

4

Turn

63 – 65

3

Beta strand

69 – 71

3

Beta strand

81 – 83

3

Beta strand

86 – 88

3

Helix

90 – 93

4

Beta strand

102 – 104

3

Beta strand

110 – 112

3

Beta strand

114 – 116

3

Beta strand

121 – 123

3

Turn

124 – 126

3

Beta strand

130 – 132

3

Beta strand

141 – 144

4

Beta strand

147 – 150

4

Helix

151 – 157

7

Beta strand

163 – 165

3

Beta strand

174 – 176

3

Beta strand

179 – 181

3

Turn

183 – 186

4

Turn

189 – 191

3

Beta strand

200 – 202

3

Beta strand

207 – 209

3

Helix

210 – 216

7

Beta strand

222 – 224

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (FHL1B) (SLIMMER) [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 50FD17F7B2606823	FASTA	323	36,263
	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
	Isoform 1 (FHL1) (FHL1A) (SLIM1) [UniParc]. Checksum: 2FC873D70E62834D	FASTA	280	31,895
	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 FGKGSSVVAY 250 260 270 280 EGQSWHDYCF HCKKCSVNLA NKRFVFHQEQ VYCPDCAKKL
	Isoform 3 (FHL1C) [UniParc]. Checksum: 2DBD610944FFE5EC	FASTA	194	22,017
	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 HCVKCNKGLV KAPVWWPMKD 190 NPGTTTASTA KNAP
	Isoform 4 [UniParc]. Checksum: 70D165A814166097	FASTA	309	34,997
	10 20 30 40 50 60 MTFYVASLAL ELIWMLSSPA GPSSYKVGTM AEKFDCHYCR DPLQGKKYVQ KDGHHCCLKC 70 80 90 100 110 120 FDKFCANTCV ECRKPIGADS KEVHYKNRFW HDTCFRCAKC LHPLANETFV AKDNKILCNK 130 140 150 160 170 180 CTTREDSPKC KGCFKAIVAG DQNVEYKGTV WHKDCFTCSN CKQVIGTGSF FPKGEDFYCV 190 200 210 220 230 240 TCHETKFAKH CVKCNKAITS GGITYQDQPW HADCFVCVTC SKKLAGQRFT AVEDQYYCVD 250 260 270 280 290 300 CYKNFVAKKC AGCKNPITGF GKGSSVVAYE GQSWHDYCFH CKKCSVNLAN KRFVFHQEQV YCPDCAKKL
	Isoform 5 [UniParc]. Checksum: 24EAD21C9DEF4DAD	FASTA	296	33,579
	10 20 30 40 50 60 MASHRHSGPS SYKVGTMAEK FDCHYCRDPL QGKKYVQKDG HHCCLKCFDK FCANTCVECR 70 80 90 100 110 120 KPIGADSKEV HYKNRFWHDT CFRCAKCLHP LANETFVAKD NKILCNKCTT REDSPKCKGC 130 140 150 160 170 180 FKAIVAGDQN VEYKGTVWHK DCFTCSNCKQ VIGTGSFFPK GEDFYCVTCH ETKFAKHCVK 190 200 210 220 230 240 CNKAITSGGI TYQDQPWHAD CFVCVTCSKK LAGQRFTAVE DQYYCVDCYK NFVAKKCAGC 250 260 270 280 290 KNPITGFGKG SSVVAYEGQS WHDYCFHCKK CSVNLANKRF VFHQEQVYCP DCAKKL

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. , 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.

IPI

IPI00014398.
IPI00029028.
IPI00055606.
IPI00647207.
IPI00930706.

PIR

G01884.
G02741. JC4893.

RefSeq

NP_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.

UniGene

Hs.435369.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X63	NMR	-	A	91-158	[»]
2CUP	NMR	-	A	40-126	[»]
2CUR	NMR	-	A	162-216	[»]
2EGQ	NMR	-	A	211-280	[»]

ProteinModelPortal

Q13642.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13642. 19 interactions.

Polymorphism databases

DMDM

59800384.

Proteomic databases

PaxDb

Q13642.

PRIDE

Q13642.

Protocols and materials databases

DNASU

2273.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000345434; ENSP00000071281; ENSG00000022267.
ENST00000370683; ENSP00000359717; ENSG00000022267.
ENST00000370690; ENSP00000359724; ENSG00000022267.
ENST00000394153; ENSP00000377709; ENSG00000022267.
ENST00000394155; ENSP00000377710; ENSG00000022267.
ENST00000535737; ENSP00000444815; ENSG00000022267.
ENST00000539015; ENSP00000437673; ENSG00000022267.
ENST00000543669; ENSP00000443333; ENSG00000022267.

GeneID

2273.

KEGG

hsa:2273.

UCSC

uc004ezo.3. human.
uc004ezq.2. human.

Organism-specific databases

CTD

2273.

GeneCards

GC0XP135229.

HGNC

HGNC:3702. FHL1.

HPA

CAB020817.
HPA001040.
HPA001391.

MIM

300163. gene.
300695. phenotype.
300696. phenotype.
300717. phenotype.
300718. phenotype.

neXtProt

NX_Q13642.

Orphanet

97239. Reducing body myopathy.
85146. Scapuloperoneal amyotrophy.
98863. X-linked Emery-Dreifuss muscular dystrophy.
178461. X-linked myopathy with postural muscle atrophy.

PharmGKB

PA28141.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG314122.

HOVERGEN

HBG074526.

InParanoid

Q13642.

KO

K14365.

OrthoDB

EOG4GQQ56.

PhylomeDB

Q13642.

Gene expression databases

ArrayExpress

Q13642.

Bgee

Q13642.

Genevestigator

Q13642.

GermOnline

ENSG00000022267. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 3 hits.

InterPro

IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 3 hits.
[Graphical view]

SMART

SM00132. LIM. 3 hits.
[Graphical view]

PROSITE

PS00478. LIM_DOMAIN_1. 3 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FHL1. human.

EvolutionaryTrace

Q13642.

GenomeRNAi

2273.

NextBio

9243.

SOURCE

Search...

Entry information

Entry name

FHL1_HUMAN

Accession

Primary (citable) accession number: Q13642
Secondary accession number(s): B7Z5T4 , 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:	May 1, 2013
This is version 133 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.