Four and a half LIM domains protein 2

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Reviewed, UniProtKB/Swiss-Prot Q14192 (FHL2_HUMAN)

Last modified February 9, 2010. Version 94. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Four and a half LIM domains protein 2
      Short name=FHL-2
Alternative name(s):
    Skeletal muscle LIM-protein 3
      Short name=SLIM-3
    LIM domain protein DRAL

Gene names

Name:	FHL2
Synonyms:	DRAL, SLIM3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Ref.8
Subunit structure	Interacts with ZNF638 and TTN/titin. Interacts with E4F1. Ref.8 Ref.6 Ref.7
Subcellular location	Cytoplasm. Nucleus Ref.8 Ref.6.
Tissue specificity	Expressed in skeletal muscle and heart. Ref.6
Domain	The third LIM zinc-binding mediates interaction with E4F1.
Sequence similarities	Contains 4 LIM zinc-binding domains.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	LIM domain Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	androgen receptor signaling pathway Non-traceable author statement. Source: UniProtKB positive regulation of transcription, DNA-dependent Non-traceable author statement. Source: UniProtKB response to hormone stimulus Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoskeleton Inferred from direct assay. Source: HPA focal adhesion Inferred from direct assay. Source: HPA nucleus Ref.1 Inferred from direct assay. Source: HPA
Molecular function	androgen receptor binding Non-traceable author statement. Source: UniProtKB identical protein binding Inferred from physical interaction. Source: IntAct transcription coactivator activity Non-traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-701903,EBI-701903
ATF3	P18847	1	EBI-701903,EBI-712767
SPHK1	Q9NYA1	4	EBI-701903,EBI-985303
SPHK2	Q9NRA0	1	EBI-701903,EBI-985324
ZNF408	Q9H9D4	1	EBI-701903,EBI-347633

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 279

279

Four and a half LIM domains protein 2

PRO_0000075737

Regions

Domain

40 – 92

LIM zinc-binding 1

Domain

101 – 153

LIM zinc-binding 2

Domain

162 – 212

LIM zinc-binding 3

Domain

221 – 275

LIM zinc-binding 4

Zinc finger

7 – 31

C4-type Potential

Amino acid modifications

Modified residue

238

Phosphoserine Ref.9

Experimental info

Sequence conflict

167

K → M in AAC52073. Ref.2

Sequence conflict

167

K → M in AAC50794. Ref.5

Secondary structure

279

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q14192-1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: E94E3A7F6601F9F3
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FASTA

279

32,193

        10         20         30         40         50         60 
MTERFDCHHC NESLFGKKYI LREESPYCVV CFETLFANTC EECGKPIGCD CKDLSYKDRH 

        70         80         90        100        110        120 
WHEACFHCSQ CRNSLVDKPF AAKEDQLLCT DCYSNEYSSK CQECKKTIMP GTRKMEYKGS 

       130        140        150        160        170        180 
SWHETCFICH RCQQPIGTKS FIPKDNQNFC VPCYEKQHAM QCVQCKKPIT TGGVTYREQP 

       190        200        210        220        230        240 
WHKECFVCTA CRKQLSGQRF TARDDFAYCL NCFCDLYAKK CAGCTNPISG LGGTKYISFE 

       250        260        270 
ERQWHNDCFN CKKCSLSLVG RGFLTERDDI LCPDCGKDI

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Subtractive cloning and characterization of DRAL, a novel LIM-domain protein down-regulated in rhabdomyosarcoma." Genini M., Schwalbe P., Scholl F.A., Remppis A., Mattei M.-G., Schaefer B.W. DNA Cell Biol. 16:433-442(1997) [PubMed: 9150430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[2]	"Molecular cloning and characterization of FHL2, a novel LIM domain protein preferentially expressed in human heart." Chan K.K., Tsui S.K.W., Lee S.M.Y., Luk S.C.W., Liew C.C., Fung K.P., Waye M.M.Y., Lee C.Y. Gene 210:345-350(1998) [PubMed: 9573400] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[3]	"Alzheimer's disease-associated presenilin 2 interacts with DRAL, an LIM-domain protein." Tanahashi H., Tabira T. Hum. Mol. Genet. 9:2281-2289(2000) [PubMed: 11001931] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leukocyte.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	"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: 8753811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 127-279. Tissue: Heart muscle.
[6]	"Interaction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220." Ng E.K.O., Chan K.K., Wong C.H., Tsui S.K.W., Ngai S.M., Lee S.M.Y., Kotaka M., Lee C.Y., Waye M.M.Y., Fung K.P. J. Cell. Biochem. 84:556-566(2002) [PubMed: 11813260] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ZNF638.
[7]	"Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2." Lange S., Auerbach D., McLoughlin P., Perriard E., Schafer B.W., Perriard J.-C., Ehler E. J. Cell Sci. 115:4925-4936(2002) [PubMed: 12432079] [Abstract] Cited for: INTERACTION WITH TTN.
[8]	"The LIM-only protein FHL2 is a negative regulator of E4F1." Paul C., Lacroix M., Iankova I., Julien E., Schaefer B.W., Labalette C., Wei Y., Le Cam A., Le Cam L., Sardet C. Oncogene 25:5475-5484(2006) [PubMed: 16652157] [Abstract] Cited for: FUNCTION, INTERACTION WITH E4F1, SUBCELLULAR LOCATION.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, MASS SPECTROMETRY.
[10]	"Solution structure of LIM domains in LIM-protein 3." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 98-279.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42176 mRNA. Translation: AAA85333.1.
U29332 mRNA. Translation: AAC52073.1.
AB038794 Genomic DNA. Translation: BAA92253.1.
BC014397 mRNA. Translation: AAH14397.1.
U60117 mRNA. Translation: AAC50794.1.

IPI

IPI00743342.

PIR

JC6565.

RefSeq

NP_001034581.1.
NP_001441.4.
NP_963849.1.
NP_963851.2.

UniGene

Hs.443687

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X4K	NMR	-	A	98-159	[»]
1X4L	NMR	-	A	221-279	[»]
2D8Z	NMR	-	A	162-218	[»]

SMR

Q14192. Positions 28-94, 38-176, 100-232.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5980N.

IntAct

Q14192. 19 interactions.

STRING

Q14192.

PTM databases

PhosphoSite

Q14192.

Proteomic databases

PRIDE

Q14192.

Genome annotation databases

Ensembl

GeneID

2274.

KEGG

hsa:2274.

UCSC

uc002tcu.1. human.

Organism-specific databases

CTD

2274.

GeneCards

GC02M105343.

H-InvDB

HIX0002345.

HGNC

HGNC:3703. FHL2.

HPA

CAB008368.
HPA005922.
HPA006028.

MIM

602633. gene.

Orphanet

154. Cardiomyopathy, familial dilated.

PharmGKB

PA29267.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11875.

HOVERGEN

Q14192.

InParanoid

Q14192.

OrthoDB

EOG9NW24W.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.

Gene expression databases

ArrayExpress

Q14192.

Bgee

Q14192.

CleanEx

HS_FHL2.

Genevestigator

Q14192.

GermOnline

ENSG00000115641. Homo sapiens.

Family and domain databases

InterPro

IPR001781. Znf_LIM.
[Graphical view]

Gene3D

G3DSA:2.10.110.10. Znf_LIM. 2 hits.

Pfam

PF00412. LIM. 4 hits.
[Graphical view]

SMART

SM00132. LIM. 4 hits.
[Graphical view]

PROSITE

PS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

9247.

SOURCE

Search...

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Entry information

Entry name

FHL2_HUMAN

Accession

Primary (citable) accession number: Q14192
Secondary accession number(s): Q13229, Q13644, Q9P294

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 17, 2006
Last modified:	February 9, 2010
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents