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Protein

Four and a half LIM domains protein 2

Gene

FHL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C4-typeSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. androgen receptor binding Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. transcription coactivator activity Source: UniProtKB
  4. transcription factor binding Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. atrial cardiac muscle cell development Source: Ensembl
  3. cellular lipid metabolic process Source: Reactome
  4. heart trabecula formation Source: Ensembl
  5. negative regulation of apoptotic process Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. osteoblast differentiation Source: Ensembl
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. response to hormone Source: BHF-UCL
  10. small molecule metabolic process Source: Reactome
  11. transcription, DNA-templated Source: UniProtKB-KW
  12. ventricular cardiac muscle cell development Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Four and a half LIM domains protein 2
Short name:
FHL-2
Alternative name(s):
LIM domain protein DRAL
Skeletal muscle LIM-protein 3
Short name:
SLIM-3
Gene namesi
Name:FHL2
Synonyms:DRAL, SLIM3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3703. FHL2.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. focal adhesion Source: UniProtKB
  3. M band Source: Ensembl
  4. nucleoplasm Source: HPA
  5. nucleus Source: HPA
  6. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA164.

Polymorphism and mutation databases

BioMutaiFHL2.
DMDMi116241364.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279Four and a half LIM domains protein 2PRO_0000075737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei238 – 2381Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ14192.
PRIDEiQ14192.

2D gel databases

UCD-2DPAGEQ14192.

PTM databases

PhosphoSiteiQ14192.

Expressioni

Tissue specificityi

Expressed in skeletal muscle and heart.1 Publication

Gene expression databases

BgeeiQ14192.
CleanExiHS_FHL2.
ExpressionAtlasiQ14192. baseline and differential.
GenevestigatoriQ14192.

Organism-specific databases

HPAiCAB008368.
HPA005922.
HPA006028.

Interactioni

Subunit structurei

Interacts with ZNF638 and TTN/titin. Interacts with E4F1. Interacts with GRB7. Interacts with SIRT1 and FOXO1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-701903,EBI-701903
ARHGAP9Q9BRR93EBI-701903,EBI-750254
ATF3P188473EBI-701903,EBI-712767
BANPQ8N9N53EBI-701903,EBI-744695
BLZF1Q9H2G93EBI-701903,EBI-2548012
BRCA1P383986EBI-701903,EBI-349905
C9orf138A8K8803EBI-701903,EBI-10174528
CCDC92Q53HC05EBI-701903,EBI-719994
CSN2W5RWE13EBI-701903,EBI-10330381
DCP1AQ9NPI63EBI-701903,EBI-374238
DTX2Q4ZH493EBI-701903,EBI-10192429
DTX2Q86UW93EBI-701903,EBI-740376
FAM129AQ9BZQ83EBI-701903,EBI-6916466
FOXO1Q127788EBI-701903,EBI-1108782
GLYR1Q49A263EBI-701903,EBI-2804292
GNG12Q9UBI64EBI-701903,EBI-358636
INCA1Q0VD863EBI-701903,EBI-6509505
JUPP149233EBI-701903,EBI-702484
KANK2Q63ZY33EBI-701903,EBI-2556193
KIAA1217Q5T5P2-63EBI-701903,EBI-10188326
NRF1Q166563EBI-701903,EBI-2547810
RAI2Q9Y5P33EBI-701903,EBI-746228
RELQ048643EBI-701903,EBI-307352
RFX3P483804EBI-701903,EBI-742557
SIGLEC6O436993EBI-701903,EBI-2814604
SIRT1Q96EB62EBI-701903,EBI-1802965
SP2Q020863EBI-701903,EBI-8651703
SPHK1Q9NYA17EBI-701903,EBI-985303
ZFP64Q9NPA53EBI-701903,EBI-711679
ZFP64Q9NTW73EBI-701903,EBI-745730
ZMYM4Q5VZL53EBI-701903,EBI-2514659
ZNF131P52739-23EBI-701903,EBI-10213055
ZNF408Q9H9D43EBI-701903,EBI-347633
ZNF417Q8TAU33EBI-701903,EBI-740727

Protein-protein interaction databases

BioGridi108565. 114 interactions.
DIPiDIP-5980N.
IntActiQ14192. 87 interactions.
MINTiMINT-120725.
STRINGi9606.ENSP00000322909.

Structurei

Secondary structure

1
279
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103Combined sources
Beta strandi20 – 223Combined sources
Beta strandi25 – 273Combined sources
Helixi29 – 368Combined sources
Turni41 – 433Combined sources
Beta strandi45 – 473Combined sources
Beta strandi53 – 564Combined sources
Beta strandi59 – 624Combined sources
Turni63 – 653Combined sources
Turni69 – 713Combined sources
Beta strandi76 – 783Combined sources
Helixi90 – 978Combined sources
Beta strandi101 – 1044Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi120 – 1234Combined sources
Turni124 – 1274Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi138 – 1447Combined sources
Beta strandi147 – 1504Combined sources
Helixi151 – 1577Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi171 – 18212Combined sources
Turni183 – 1853Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi201 – 2088Combined sources
Helixi210 – 2167Combined sources
Turni222 – 2254Combined sources
Beta strandi231 – 2333Combined sources
Turni246 – 2483Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi267 – 2715Combined sources
Helixi273 – 2775Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4KNMR-A101-159[»]
1X4LNMR-A221-279[»]
2D8ZNMR-A162-218[»]
2MIUNMR-A1-98[»]
SMRiQ14192. Positions 1-159, 162-218, 225-279.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14192.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 9253LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini101 – 15353LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 21251LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST
Domaini221 – 27555LIM zinc-binding 4PROSITE-ProRule annotationAdd
BLAST

Domaini

The third LIM zinc-binding mediates interaction with E4F1.

Sequence similaritiesi

Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C4-typeSequence AnalysisAdd
BLAST

Keywords - Domaini

LIM domain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG314122.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000231075.
HOVERGENiHBG074526.
InParanoidiQ14192.
KOiK14380.
OrthoDBiEOG7P8P7M.
PhylomeDBiQ14192.
TreeFamiTF321684.

Family and domain databases

Gene3Di2.10.110.10. 5 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14192-1) [UniParc]FASTAAdd to basket

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
MTERFDCHHC NESLFGKKYI LREESPYCVV CFETLFANTC EECGKPIGCD
60 70 80 90 100
CKDLSYKDRH WHEACFHCSQ CRNSLVDKPF AAKEDQLLCT DCYSNEYSSK
110 120 130 140 150
CQECKKTIMP GTRKMEYKGS SWHETCFICH RCQQPIGTKS FIPKDNQNFC
160 170 180 190 200
VPCYEKQHAM QCVQCKKPIT TGGVTYREQP WHKECFVCTA CRKQLSGQRF
210 220 230 240 250
TARDDFAYCL NCFCDLYAKK CAGCTNPISG LGGTKYISFE ERQWHNDCFN
260 270
CKKCSLSLVG RGFLTERDDI LCPDCGKDI
Length:279
Mass (Da):32,193
Last modified:October 17, 2006 - v3
Checksum:iE94E3A7F6601F9F3
GO
Isoform 2 (identifier: Q14192-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-151: DLSYKDRHWH...IPKDNQNFCV → VPARWSTRAA...SQLAMTLPTA
     152-279: Missing.

Show »
Length:151
Mass (Da):15,890
Checksum:i72F31D2DB830DB20
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671K → M.3 Publications
Corresponds to variant rs1127588 [ dbSNP | Ensembl ].
VAR_067455

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei53 – 15199DLSYK…QNFCV → VPARWSTRAAAGMRPASSAT AASSQLEPRVSSPKTIRISV CPAMRNNMPCSAFSAKSPSP REGSLTGSSPGTRSASCAPP AGSSCLGSASQLAMTLPTA in isoform 2. 1 PublicationVSP_056999Add
BLAST
Alternative sequencei152 – 279128Missing in isoform 2. 1 PublicationVSP_057000Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42176 mRNA. Translation: AAA85333.1.
U29332 mRNA. Translation: AAC52073.1.
AB038794 Genomic DNA. Translation: BAA92253.1.
AB158503 mRNA. Translation: BAD69710.1.
DQ307067 mRNA. Translation: ABC25549.1.
AC012360 Genomic DNA. No translation available.
AC068273 Genomic DNA. No translation available.
AC108058 Genomic DNA. No translation available.
BC014397 mRNA. Translation: AAH14397.1.
U60117 mRNA. Translation: AAC50794.1.
CCDSiCCDS2070.1. [Q14192-1]
PIRiJC6565.
RefSeqiNP_001034581.1. NM_001039492.2. [Q14192-1]
NP_001441.4. NM_001450.3. [Q14192-1]
NP_963849.1. NM_201555.1. [Q14192-1]
NP_963851.2. NM_201557.3. [Q14192-1]
XP_005263963.1. XM_005263906.1. [Q14192-1]
UniGeneiHs.443687.

Genome annotation databases

EnsembliENST00000322142; ENSP00000322909; ENSG00000115641. [Q14192-1]
ENST00000358129; ENSP00000350846; ENSG00000115641. [Q14192-2]
ENST00000393352; ENSP00000377020; ENSG00000115641. [Q14192-1]
ENST00000393353; ENSP00000377021; ENSG00000115641. [Q14192-1]
ENST00000408995; ENSP00000386633; ENSG00000115641. [Q14192-1]
ENST00000409807; ENSP00000386665; ENSG00000115641. [Q14192-1]
GeneIDi2274.
KEGGihsa:2274.
UCSCiuc002tct.3. human. [Q14192-1]

Polymorphism and mutation databases

BioMutaiFHL2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42176 mRNA. Translation: AAA85333.1.
U29332 mRNA. Translation: AAC52073.1.
AB038794 Genomic DNA. Translation: BAA92253.1.
AB158503 mRNA. Translation: BAD69710.1.
DQ307067 mRNA. Translation: ABC25549.1.
AC012360 Genomic DNA. No translation available.
AC068273 Genomic DNA. No translation available.
AC108058 Genomic DNA. No translation available.
BC014397 mRNA. Translation: AAH14397.1.
U60117 mRNA. Translation: AAC50794.1.
CCDSiCCDS2070.1. [Q14192-1]
PIRiJC6565.
RefSeqiNP_001034581.1. NM_001039492.2. [Q14192-1]
NP_001441.4. NM_001450.3. [Q14192-1]
NP_963849.1. NM_201555.1. [Q14192-1]
NP_963851.2. NM_201557.3. [Q14192-1]
XP_005263963.1. XM_005263906.1. [Q14192-1]
UniGeneiHs.443687.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4KNMR-A101-159[»]
1X4LNMR-A221-279[»]
2D8ZNMR-A162-218[»]
2MIUNMR-A1-98[»]
SMRiQ14192. Positions 1-159, 162-218, 225-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108565. 114 interactions.
DIPiDIP-5980N.
IntActiQ14192. 87 interactions.
MINTiMINT-120725.
STRINGi9606.ENSP00000322909.

PTM databases

PhosphoSiteiQ14192.

Polymorphism and mutation databases

BioMutaiFHL2.
DMDMi116241364.

2D gel databases

UCD-2DPAGEQ14192.

Proteomic databases

PaxDbiQ14192.
PRIDEiQ14192.

Protocols and materials databases

DNASUi2274.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322142; ENSP00000322909; ENSG00000115641. [Q14192-1]
ENST00000358129; ENSP00000350846; ENSG00000115641. [Q14192-2]
ENST00000393352; ENSP00000377020; ENSG00000115641. [Q14192-1]
ENST00000393353; ENSP00000377021; ENSG00000115641. [Q14192-1]
ENST00000408995; ENSP00000386633; ENSG00000115641. [Q14192-1]
ENST00000409807; ENSP00000386665; ENSG00000115641. [Q14192-1]
GeneIDi2274.
KEGGihsa:2274.
UCSCiuc002tct.3. human. [Q14192-1]

Organism-specific databases

CTDi2274.
GeneCardsiGC02M105974.
HGNCiHGNC:3703. FHL2.
HPAiCAB008368.
HPA005922.
HPA006028.
MIMi602633. gene.
neXtProtiNX_Q14192.
Orphaneti154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA164.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG314122.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000231075.
HOVERGENiHBG074526.
InParanoidiQ14192.
KOiK14380.
OrthoDBiEOG7P8P7M.
PhylomeDBiQ14192.
TreeFamiTF321684.

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.

Miscellaneous databases

ChiTaRSiFHL2. human.
EvolutionaryTraceiQ14192.
GeneWikiiFHL2.
GenomeRNAii2274.
NextBioi9247.
PROiQ14192.
SOURCEiSearch...

Gene expression databases

BgeeiQ14192.
CleanExiHS_FHL2.
ExpressionAtlasiQ14192. baseline and differential.
GenevestigatoriQ14192.

Family and domain databases

Gene3Di2.10.110.10. 5 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-167.
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Leukocyte.
  4. "FHL3 negatively regulates human high-affinity IgE receptor beta-chain gene expression by acting as a transcriptional co-repressor of MZF-1."
    Takahashi K., Matsumoto C., Ra C.
    Biochem. J. 386:191-200(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  5. "The FHL2 LIM-domain protein is implicated in hematopoiesis and leukemogenesis."
    Qian Z., Mao L., Fernald A., Yu H., Luo R., Anastasi J., Le Beau M.M.
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-167.
    Tissue: Bone marrow.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Placenta.
  8. "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] OF 127-279 (ISOFORM 1), VARIANT MET-167.
    Tissue: Heart muscle.
  9. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ZNF638.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TTN.
  11. "Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation."
    Yang Y., Hou H., Haller E.M., Nicosia S.V., Bai W.
    EMBO J. 24:1021-1032(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SIRT1 AND FOXO1.
  12. Cited for: FUNCTION, INTERACTION WITH E4F1, SUBCELLULAR LOCATION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "The cell migration protein Grb7 associates with transcriptional regulator FHL2 in a Grb7 phosphorylation-dependent manner."
    Siamakpour-Reihani S., Argiros H.J., Wilmeth L.J., Haas L.L., Peterson T.A., Johnson D.L., Shuster C.B., Lyons B.A.
    J. Mol. Recognit. 22:9-17(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GRB7.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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.

Entry informationi

Entry nameiFHL2_HUMAN
AccessioniPrimary (citable) accession number: Q14192
Secondary accession number(s): Q13229
, Q13644, Q2I5I4, Q5TM15, Q9P294
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: April 29, 2015
This is version 148 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.