ID FHL2_HUMAN Reviewed; 279 AA. AC Q14192; Q13229; Q13644; Q2I5I4; Q5TM15; Q9P294; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 28-FEB-2018, entry version 175. DE RecName: Full=Four and a half LIM domains protein 2; DE Short=FHL-2; DE AltName: Full=LIM domain protein DRAL; DE AltName: Full=Skeletal muscle LIM-protein 3; DE Short=SLIM-3; GN Name=FHL2; Synonyms=DRAL, SLIM3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Skeletal muscle; RX PubMed=9150430; DOI=10.1089/dna.1997.16.433; RA Genini M., Schwalbe P., Scholl F.A., Remppis A., Mattei M.-G., RA Schaefer B.W.; RT "Subtractive cloning and characterization of DRAL, a novel LIM-domain RT protein down-regulated in rhabdomyosarcoma."; RL DNA Cell Biol. 16:433-442(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-167. RC TISSUE=Heart; RX PubMed=9573400; DOI=10.1016/S0378-1119(97)00644-6; RA Chan K.K., Tsui S.K.W., Lee S.M.Y., Luk S.C.W., Liew C.C., Fung K.P., RA Waye M.M.Y., Lee C.Y.; RT "Molecular cloning and characterization of FHL2, a novel LIM domain RT protein preferentially expressed in human heart."; RL Gene 210:345-350(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Leukocyte; RX PubMed=11001931; DOI=10.1093/oxfordjournals.hmg.a018919; RA Tanahashi H., Tabira T.; RT "Alzheimer's disease-associated presenilin 2 interacts with DRAL, an RT LIM-domain protein."; RL Hum. Mol. Genet. 9:2281-2289(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=15453830; DOI=10.1042/BJ20040775; RA Takahashi K., Matsumoto C., Ra C.; RT "FHL3 negatively regulates human high-affinity IgE receptor beta-chain RT gene expression by acting as a transcriptional co-repressor of MZF- RT 1."; RL Biochem. J. 386:191-200(2005). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-167. RC TISSUE=Bone marrow; RA Qian Z., Mao L., Fernald A., Yu H., Luo R., Anastasi J., Le Beau M.M.; RT "The FHL2 LIM-domain protein is implicated in hematopoiesis and RT leukemogenesis."; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 127-279 (ISOFORM 1), AND VARIANT RP MET-167. RC TISSUE=Heart muscle; RX PubMed=8753811; DOI=10.1006/bbrc.1996.1222; RA Morgan M.J., Madgwick A.J.A.; RT "Slim defines a novel family of LIM-proteins expressed in skeletal RT muscle."; RL Biochem. Biophys. Res. Commun. 225:632-638(1996). RN [9] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ZNF638. RX PubMed=11813260; DOI=10.1002/jcb.10041.abs; RA Ng E.K.O., Chan K.K., Wong C.H., Tsui S.K.W., Ngai S.M., Lee S.M.Y., RA Kotaka M., Lee C.Y., Waye M.M.Y., Fung K.P.; RT "Interaction of the heart-specific LIM domain protein, FHL2, with DNA- RT binding nuclear protein, hNP220."; RL J. Cell. Biochem. 84:556-566(2002). RN [10] RP INTERACTION WITH TTN. RX PubMed=12432079; DOI=10.1242/jcs.00181; RA Lange S., Auerbach D., McLoughlin P., Perriard E., Schafer B.W., RA Perriard J.-C., Ehler E.; RT "Subcellular targeting of metabolic enzymes to titin in heart muscle RT may be mediated by DRAL/FHL-2."; RL J. Cell Sci. 115:4925-4936(2002). RN [11] RP FUNCTION, AND INTERACTION WITH SIRT1 AND FOXO1. RX PubMed=15692560; DOI=10.1038/sj.emboj.7600570; RA Yang Y., Hou H., Haller E.M., Nicosia S.V., Bai W.; RT "Suppression of FOXO1 activity by FHL2 through SIRT1-mediated RT deacetylation."; RL EMBO J. 24:1021-1032(2005). RN [12] RP FUNCTION, INTERACTION WITH E4F1, AND SUBCELLULAR LOCATION. RX PubMed=16652157; DOI=10.1038/sj.onc.1209567; RA Paul C., Lacroix M., Iankova I., Julien E., Schaefer B.W., RA Labalette C., Wei Y., Le Cam A., Le Cam L., Sardet C.; RT "The LIM-only protein FHL2 is a negative regulator of E4F1."; RL Oncogene 25:5475-5484(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP FUNCTION, AND INTERACTION WITH GRB7. RX PubMed=18853468; DOI=10.1002/jmr.916; RA Siamakpour-Reihani S., Argiros H.J., Wilmeth L.J., Haas L.L., RA Peterson T.A., Johnson D.L., Shuster C.B., Lyons B.A.; RT "The cell migration protein Grb7 associates with transcriptional RT regulator FHL2 in a Grb7 phosphorylation-dependent manner."; RL J. Mol. Recognit. 22:9-17(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-167 AND LYS-220, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [17] RP STRUCTURE BY NMR OF 98-279. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of LIM domains in LIM-protein 3."; RL Submitted (JUN-2006) to the PDB data bank. CC -!- FUNCTION: May function as a molecular transmitter linking various CC signaling pathways to transcriptional regulation. Negatively CC regulates the transcriptional repressor E4F1 and may function in CC cell growth. Inhibits the transcriptional activity of FOXO1 and CC its apoptotic function by enhancing the interaction of FOXO1 with CC SIRT1 and FOXO1 deacetylation. {ECO:0000269|PubMed:15692560, CC ECO:0000269|PubMed:16652157, ECO:0000269|PubMed:18853468}. CC -!- SUBUNIT: Interacts with ZNF638 and TTN/titin. Interacts with E4F1. CC Interacts with GRB7. Interacts with SIRT1 and FOXO1. CC {ECO:0000269|PubMed:11813260, ECO:0000269|PubMed:12432079, CC ECO:0000269|PubMed:15692560, ECO:0000269|PubMed:16652157, CC ECO:0000269|PubMed:18853468}. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-701903, EBI-701903; CC Q9BRR9:ARHGAP9; NbExp=3; IntAct=EBI-701903, EBI-750254; CC P18847:ATF3; NbExp=3; IntAct=EBI-701903, EBI-712767; CC A0A0S2Z5G4:BANP; NbExp=3; IntAct=EBI-701903, EBI-16429704; CC B4DE54:BANP; NbExp=4; IntAct=EBI-701903, EBI-16429313; CC Q8N9N5:BANP; NbExp=3; IntAct=EBI-701903, EBI-744695; CC Q8N9N5-2:BANP; NbExp=5; IntAct=EBI-701903, EBI-11524452; CC Q8N9N5-7:BANP; NbExp=3; IntAct=EBI-701903, EBI-16429296; CC Q9H2G9:BLZF1; NbExp=5; IntAct=EBI-701903, EBI-2548012; CC P38398:BRCA1; NbExp=6; IntAct=EBI-701903, EBI-349905; CC Q53HC0:CCDC92; NbExp=9; IntAct=EBI-701903, EBI-719994; CC W5RWE1:CSN2; NbExp=3; IntAct=EBI-701903, EBI-10330381; CC Q9NPI6:DCP1A; NbExp=5; IntAct=EBI-701903, EBI-374238; CC Q86UW9:DTX2; NbExp=6; IntAct=EBI-701903, EBI-740376; CC Q9BZQ8:FAM129A; NbExp=5; IntAct=EBI-701903, EBI-6916466; CC Q12778:FOXO1; NbExp=8; IntAct=EBI-701903, EBI-1108782; CC Q49A26:GLYR1; NbExp=3; IntAct=EBI-701903, EBI-2804292; CC Q9UKD1:GMEB2; NbExp=4; IntAct=EBI-701903, EBI-948296; CC Q9UBI6:GNG12; NbExp=6; IntAct=EBI-701903, EBI-358636; CC P51610-1:HCFC1; NbExp=5; IntAct=EBI-701903, EBI-396188; CC A0A024R8L2:hCG_1987119; NbExp=4; IntAct=EBI-701903, EBI-14103818; CC Q0VD86:INCA1; NbExp=3; IntAct=EBI-701903, EBI-6509505; CC P14923:JUP; NbExp=5; IntAct=EBI-701903, EBI-702484; CC Q63ZY3:KANK2; NbExp=5; IntAct=EBI-701903, EBI-2556193; CC Q5T5P2-6:KIAA1217; NbExp=3; IntAct=EBI-701903, EBI-10188326; CC P33176:KIF5B; NbExp=4; IntAct=EBI-701903, EBI-355878; CC Q16656:NRF1; NbExp=3; IntAct=EBI-701903, EBI-2547810; CC Q16656-4:NRF1; NbExp=4; IntAct=EBI-701903, EBI-11742836; CC Q96BD5:PHF21A; NbExp=4; IntAct=EBI-701903, EBI-745085; CC P78424:POU6F2; NbExp=4; IntAct=EBI-701903, EBI-12029004; CC Q9Y5P3:RAI2; NbExp=5; IntAct=EBI-701903, EBI-746228; CC Q04864:REL; NbExp=3; IntAct=EBI-701903, EBI-307352; CC P48380:RFX3; NbExp=6; IntAct=EBI-701903, EBI-742557; CC Q8IYX7:SAXO1; NbExp=3; IntAct=EBI-701903, EBI-3957636; CC O43699:SIGLEC6; NbExp=3; IntAct=EBI-701903, EBI-2814604; CC Q96EB6:SIRT1; NbExp=2; IntAct=EBI-701903, EBI-1802965; CC Q02086:SP2; NbExp=3; IntAct=EBI-701903, EBI-8651703; CC Q9NYA1:SPHK1; NbExp=7; IntAct=EBI-701903, EBI-985303; CC Q9ERP3:Trim54 (xeno); NbExp=2; IntAct=EBI-701903, EBI-15626796; CC P25490:YY1; NbExp=4; IntAct=EBI-701903, EBI-765538; CC Q9NPA5:ZFP64; NbExp=3; IntAct=EBI-701903, EBI-711679; CC Q9NTW7:ZFP64; NbExp=3; IntAct=EBI-701903, EBI-745730; CC Q5VZL5:ZMYM4; NbExp=3; IntAct=EBI-701903, EBI-2514659; CC P52739-2:ZNF131; NbExp=5; IntAct=EBI-701903, EBI-10213055; CC Q9H9D4:ZNF408; NbExp=3; IntAct=EBI-701903, EBI-347633; CC Q8TAU3:ZNF417; NbExp=3; IntAct=EBI-701903, EBI-740727; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14192-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14192-2; Sequence=VSP_056999, VSP_057000; CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle and heart. CC {ECO:0000269|PubMed:11813260}. CC -!- DOMAIN: The third LIM zinc-binding mediates interaction with E4F1. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/FHL2ID44092ch2q12.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42176; AAA85333.1; -; mRNA. DR EMBL; U29332; AAC52073.1; -; mRNA. DR EMBL; AB038794; BAA92253.1; -; Genomic_DNA. DR EMBL; AB158503; BAD69710.1; -; mRNA. DR EMBL; DQ307067; ABC25549.1; -; mRNA. DR EMBL; AC012360; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC068273; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108058; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014397; AAH14397.1; -; mRNA. DR EMBL; U60117; AAC50794.1; -; mRNA. DR CCDS; CCDS2070.1; -. [Q14192-1] DR PIR; JC6565; JC6565. DR RefSeq; NP_001034581.1; NM_001039492.2. [Q14192-1] DR RefSeq; NP_001305823.1; NM_001318894.1. [Q14192-1] DR RefSeq; NP_001305824.1; NM_001318895.1. [Q14192-1] DR RefSeq; NP_001305825.1; NM_001318896.1. [Q14192-1] DR RefSeq; NP_001305826.1; NM_001318897.1. DR RefSeq; NP_001441.4; NM_001450.3. [Q14192-1] DR RefSeq; NP_963849.1; NM_201555.1. [Q14192-1] DR RefSeq; NP_963851.2; NM_201557.3. [Q14192-1] DR RefSeq; XP_011509100.1; XM_011510798.2. [Q14192-1] DR UniGene; Hs.443687; -. DR PDB; 1X4K; NMR; -; A=101-159. DR PDB; 1X4L; NMR; -; A=221-279. DR PDB; 2D8Z; NMR; -; A=162-218. DR PDB; 2MIU; NMR; -; A=1-98. DR PDBsum; 1X4K; -. DR PDBsum; 1X4L; -. DR PDBsum; 2D8Z; -. DR PDBsum; 2MIU; -. DR ProteinModelPortal; Q14192; -. DR SMR; Q14192; -. DR BioGrid; 108565; 151. DR CORUM; Q14192; -. DR DIP; DIP-5980N; -. DR IntAct; Q14192; 150. DR MINT; Q14192; -. DR STRING; 9606.ENSP00000322909; -. DR iPTMnet; Q14192; -. DR PhosphoSitePlus; Q14192; -. DR SwissPalm; Q14192; -. DR BioMuta; FHL2; -. DR DMDM; 116241364; -. DR UCD-2DPAGE; Q14192; -. DR EPD; Q14192; -. DR PaxDb; Q14192; -. DR PeptideAtlas; Q14192; -. DR PRIDE; Q14192; -. DR DNASU; 2274; -. DR Ensembl; ENST00000322142; ENSP00000322909; ENSG00000115641. [Q14192-1] DR Ensembl; ENST00000358129; ENSP00000350846; ENSG00000115641. [Q14192-2] DR Ensembl; ENST00000393352; ENSP00000377020; ENSG00000115641. [Q14192-1] DR Ensembl; ENST00000393353; ENSP00000377021; ENSG00000115641. [Q14192-1] DR Ensembl; ENST00000408995; ENSP00000386633; ENSG00000115641. [Q14192-1] DR Ensembl; ENST00000409807; ENSP00000386665; ENSG00000115641. [Q14192-1] DR GeneID; 2274; -. DR KEGG; hsa:2274; -. DR UCSC; uc061mpc.1; human. [Q14192-1] DR CTD; 2274; -. DR DisGeNET; 2274; -. DR EuPathDB; HostDB:ENSG00000115641.18; -. DR GeneCards; FHL2; -. DR HGNC; HGNC:3703; FHL2. DR HPA; CAB008368; -. DR HPA; HPA005922; -. DR HPA; HPA006028; -. DR MalaCards; FHL2; -. DR MIM; 602633; gene. DR neXtProt; NX_Q14192; -. DR OpenTargets; ENSG00000115641; -. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR PharmGKB; PA164; -. DR eggNOG; ENOG410KCU4; Eukaryota. DR eggNOG; ENOG410XRFY; LUCA. DR GeneTree; ENSGT00760000118910; -. DR HOGENOM; HOG000231075; -. DR HOVERGEN; HBG074526; -. DR InParanoid; Q14192; -. DR KO; K14380; -. DR PhylomeDB; Q14192; -. DR TreeFam; TF321684; -. DR Reactome; R-HSA-1989781; PPARA activates gene expression. DR SIGNOR; Q14192; -. DR ChiTaRS; FHL2; human. DR EvolutionaryTrace; Q14192; -. DR GeneWiki; FHL2; -. DR GenomeRNAi; 2274; -. DR PRO; PR:Q14192; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000115641; -. DR CleanEx; HS_FHL2; -. DR ExpressionAtlas; Q14192; baseline and differential. DR Genevisible; Q14192; HS. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0031430; C:M band; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0030018; C:Z disc; IEA:Ensembl. DR GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB. DR GO; GO:0055014; P:atrial cardiac muscle cell development; IEA:Ensembl. DR GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB. DR GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome. DR GO; GO:0009725; P:response to hormone; IMP:BHF-UCL. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl. DR InterPro; IPR037987; FHL2/3/5. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR24205; PTHR24205; 1. DR Pfam; PF00412; LIM; 4. DR SMART; SM00132; LIM; 4. DR PROSITE; PS00478; LIM_DOMAIN_1; 4. DR PROSITE; PS50023; LIM_DOMAIN_2; 4. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Isopeptide bond; LIM domain; Metal-binding; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1 279 Four and a half LIM domains protein 2. FT /FTId=PRO_0000075737. FT DOMAIN 40 92 LIM zinc-binding 1. {ECO:0000255|PROSITE- FT ProRule:PRU00125}. FT DOMAIN 101 153 LIM zinc-binding 2. {ECO:0000255|PROSITE- FT ProRule:PRU00125}. FT DOMAIN 162 212 LIM zinc-binding 3. {ECO:0000255|PROSITE- FT ProRule:PRU00125}. FT DOMAIN 221 275 LIM zinc-binding 4. {ECO:0000255|PROSITE- FT ProRule:PRU00125}. FT ZN_FING 7 31 C4-type. {ECO:0000255}. FT MOD_RES 238 238 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT CROSSLNK 78 78 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 167 167 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 220 220 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT VAR_SEQ 53 151 DLSYKDRHWHEACFHCSQCRNSLVDKPFAAKEDQLLCTDCY FT SNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFICHRCQQ FT PIGTKSFIPKDNQNFCV -> VPARWSTRAAAGMRPASSAT FT AASSQLEPRVSSPKTIRISVCPAMRNNMPCSAFSAKSPSPR FT EGSLTGSSPGTRSASCAPPAGSSCLGSASQLAMTLPTA FT (in isoform 2). FT {ECO:0000303|PubMed:15453830}. FT /FTId=VSP_056999. FT VAR_SEQ 152 279 Missing (in isoform 2). FT {ECO:0000303|PubMed:15453830}. FT /FTId=VSP_057000. FT VARIANT 167 167 K -> M. {ECO:0000269|PubMed:8753811, FT ECO:0000269|PubMed:9573400, FT ECO:0000269|Ref.5}. FT /FTId=VAR_067455. FT TURN 8 10 {ECO:0000244|PDB:2MIU}. FT STRAND 20 22 {ECO:0000244|PDB:2MIU}. FT STRAND 25 27 {ECO:0000244|PDB:2MIU}. FT HELIX 29 36 {ECO:0000244|PDB:2MIU}. FT TURN 41 43 {ECO:0000244|PDB:2MIU}. FT STRAND 45 47 {ECO:0000244|PDB:2MIU}. FT STRAND 53 56 {ECO:0000244|PDB:2MIU}. FT STRAND 59 62 {ECO:0000244|PDB:2MIU}. FT TURN 63 65 {ECO:0000244|PDB:2MIU}. FT TURN 69 71 {ECO:0000244|PDB:2MIU}. FT STRAND 76 78 {ECO:0000244|PDB:2MIU}. FT HELIX 90 97 {ECO:0000244|PDB:2MIU}. FT STRAND 101 104 {ECO:0000244|PDB:1X4K}. FT STRAND 110 112 {ECO:0000244|PDB:1X4K}. FT STRAND 114 117 {ECO:0000244|PDB:1X4K}. FT STRAND 120 123 {ECO:0000244|PDB:1X4K}. FT TURN 124 127 {ECO:0000244|PDB:1X4K}. FT STRAND 130 132 {ECO:0000244|PDB:1X4K}. FT STRAND 138 144 {ECO:0000244|PDB:1X4K}. FT STRAND 147 150 {ECO:0000244|PDB:1X4K}. FT HELIX 151 157 {ECO:0000244|PDB:1X4K}. FT STRAND 163 165 {ECO:0000244|PDB:2D8Z}. FT STRAND 171 182 {ECO:0000244|PDB:2D8Z}. FT TURN 183 185 {ECO:0000244|PDB:2D8Z}. FT STRAND 189 191 {ECO:0000244|PDB:2D8Z}. FT STRAND 201 208 {ECO:0000244|PDB:2D8Z}. FT HELIX 210 216 {ECO:0000244|PDB:2D8Z}. FT TURN 222 225 {ECO:0000244|PDB:1X4L}. FT STRAND 231 233 {ECO:0000244|PDB:1X4L}. FT TURN 246 248 {ECO:0000244|PDB:1X4L}. FT STRAND 252 254 {ECO:0000244|PDB:1X4L}. FT STRAND 267 271 {ECO:0000244|PDB:1X4L}. FT HELIX 273 277 {ECO:0000244|PDB:1X4L}. SQ SEQUENCE 279 AA; 32193 MW; E94E3A7F6601F9F3 CRC64; MTERFDCHHC NESLFGKKYI LREESPYCVV CFETLFANTC EECGKPIGCD CKDLSYKDRH WHEACFHCSQ CRNSLVDKPF AAKEDQLLCT DCYSNEYSSK CQECKKTIMP GTRKMEYKGS SWHETCFICH RCQQPIGTKS FIPKDNQNFC VPCYEKQHAM QCVQCKKPIT TGGVTYREQP WHKECFVCTA CRKQLSGQRF TARDDFAYCL NCFCDLYAKK CAGCTNPISG LGGTKYISFE ERQWHNDCFN CKKCSLSLVG RGFLTERDDI LCPDCGKDI //