LIMD1_HUMAN
ID LIMD1_HUMAN Reviewed; 676 AA.
AC Q9UGP4; Q17RQ1; Q9BQQ9; Q9NQ47;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=LIM domain-containing protein 1;
GN Name=LIMD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10647888; DOI=10.1007/s004399900188;
RA Kiss H., Kedra D., Yang Y., Kost-Alimova M., Kiss C., O'Brien K.P.,
RA Fransson I., Klein G., Imreh S., Dumanski J.P.;
RT "A novel gene containing LIM domains (LIMD1) is located within the common
RT eliminated region 1 (C3CER1) in 3p21.3.";
RL Hum. Genet. 105:552-559(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11352561; DOI=10.1006/geno.2000.6498;
RA Kiss H., Kedra D., Kiss C., Kost-Alimova M., Yang Y., Klein G., Imreh S.,
RA Dumanski J.P.;
RT "The LZTFL1 gene is a part of a transcriptional map covering 250 kb within
RT the common eliminated region 1 (C3CER1) in 3p21.3.";
RL Genomics 73:10-19(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-277, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [5]
RP FUNCTION, INTERACTION WITH RB1, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15542589; DOI=10.1073/pnas.0407123101;
RA Sharp T.V., Munoz F., Bourboulia D., Presneau N., Darai E., Wang H.-W.,
RA Cannon M., Butcher D.N., Nicholson A.G., Klein G., Imreh S., Boshoff C.;
RT "LIM domains-containing protein 1 (LIMD1), a tumor suppressor encoded at
RT chromosome 3p21.3, binds pRB and represses E2F-driven transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16531-16536(2004).
RN [6]
RP INTERACTION WITH SQSTM1.
RX PubMed=15870274; DOI=10.1128/mcb.25.10.4010-4022.2005;
RA Feng Y., Longmore G.D.;
RT "The LIM protein Ajuba influences interleukin-1-induced NF-kappaB
RT activation by affecting the assembly and activity of the protein kinase
RT Czeta/p62/TRAF6 signaling complex.";
RL Mol. Cell. Biol. 25:4010-4022(2005).
RN [7]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=18439753; DOI=10.1016/j.canlet.2008.03.015;
RA Huggins C.J., Andrulis I.L.;
RT "Cell cycle regulated phosphorylation of LIMD1 in cell lines and expression
RT in human breast cancers.";
RL Cancer Lett. 267:55-66(2008).
RN [8]
RP INTERACTION WITH SNAI1.
RX PubMed=18331720; DOI=10.1016/j.devcel.2008.01.005;
RA Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L.,
RA Longmore G.D.;
RT "Ajuba LIM proteins are snail/slug corepressors required for neural crest
RT development in Xenopus.";
RL Dev. Cell 14:424-436(2008).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18712738; DOI=10.1002/ijc.23851;
RA Spendlove I., Al-Attar A., Watherstone O., Webb T.M., Ellis I.O.,
RA Longmore G.D., Sharp T.V.;
RT "Differential subcellular localisation of the tumour suppressor protein
RT LIMD1 in breast cancer correlates with patient survival.";
RL Int. J. Cancer 123:2247-2253(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-421 AND SER-424, AND
RP IDENTIFICATION 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LATS1 AND LATS2.
RX PubMed=20303269; DOI=10.1016/j.cub.2010.02.035;
RA Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B.,
RA Longmore G.D.;
RT "Ajuba LIM proteins are negative regulators of the Hippo signaling
RT pathway.";
RL Curr. Biol. 20:657-662(2010).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4E; AGO1; AGO2;
RP DCP2 AND DDX6.
RX PubMed=20616046; DOI=10.1073/pnas.0914987107;
RA James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M.,
RA Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J.,
RA Longmore G.D., Bushell M., Sharp T.V.;
RT "LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-
RT mediated gene silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; SER-277 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [17]
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., Buerckstuemmer T.,
RA 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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP FUNCTION, INTERACTION WITH EGLN1/PHD2; EGLN2/PHD1; EGLN3/PHD3 AND VHL, AND
RP IDENTIFICATION IN A COMPLEX WITH CUL2; EGLN1/PHD2; VHL AND ELOB.
RX PubMed=22286099; DOI=10.1038/ncb2424;
RA Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C., Feng Y.,
RA Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J., Ingvarsson S.,
RA Ratcliffe P.J., Longmore G.D., Sharp T.V.;
RT "The LIMD1 protein bridges an association between the prolyl hydroxylases
RT and VHL to repress HIF-1 activity.";
RL Nat. Cell Biol. 14:201-208(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-277, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Adapter or scaffold protein which participates in the
CC assembly of numerous protein complexes and is involved in several
CC cellular processes such as cell fate determination, cytoskeletal
CC organization, repression of gene transcription, cell-cell adhesion,
CC cell differentiation, proliferation and migration. Positively regulates
CC microRNA (miRNA)-mediated gene silencing and is essential for P-body
CC formation and integrity. Acts as a hypoxic regulator by bridging an
CC association between the prolyl hydroxylases and VHL enabling efficient
CC degradation of HIF1A. Acts as a transcriptional corepressor for
CC SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription.
CC Negatively regulates the Hippo signaling pathway and antagonizes
CC phosphorylation of YAP1. Inhibits E2F-mediated transcription, and
CC suppresses the expression of the majority of genes with E2F1-responsive
CC elements. Regulates osteoblast development, function, differentiation
CC and stress osteoclastogenesis. Enhances the ability of TRAF6 to
CC activate adapter protein complex 1 (AP-1) and negatively regulates the
CC canonical Wnt receptor signaling pathway in osteoblasts. May act as a
CC tumor suppressor by inhibiting cell proliferation.
CC {ECO:0000269|PubMed:15542589, ECO:0000269|PubMed:20303269,
CC ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:21834987,
CC ECO:0000269|PubMed:22286099}.
CC -!- SUBUNIT: Interacts (via LIM domains) with TRAF6. Found in a complex
CC with TRAF6, PRKCZ and SQSTM1. Interacts (via LIM domains) SNAI2/SLUG
CC (via SNAG domain) and SCRT1 (via SNAG domain) (By similarity).
CC Interacts with SQSTM1 and RB1. Found in a complex composed of LIMD1,
CC VHL, EGLN1/PHD2, ELOB and CUL2. Interacts with EIF4E, AGO1, AGO2, DCP2,
CC DDX6, LATS1, LATS2, EGLN1/PHD2, EGLN2/PHD1 and EGLN3/PHD3. Interacts
CC (via LIM zinc-binding 2) with isoform 1 and isoform 3 of VHL. Interacts
CC (via LIM domains) with SNAI1 (via SNAG domain). {ECO:0000250,
CC ECO:0000269|PubMed:15542589, ECO:0000269|PubMed:15870274,
CC ECO:0000269|PubMed:18331720, ECO:0000269|PubMed:20303269,
CC ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:22286099}.
CC -!- INTERACTION:
CC Q9UGP4; Q9UL18: AGO1; NbExp=3; IntAct=EBI-2652871, EBI-527363;
CC Q9UGP4; Q9UKV8: AGO2; NbExp=11; IntAct=EBI-2652871, EBI-528269;
CC Q9UGP4; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-2652871, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body. Cell
CC junction, adherens junction. Cell junction, focal adhesion.
CC Note=Shuttles between cytoplasm and nucleus but is localized
CC predominantly to the cytoplasm. Found in the nucleus but not nucleoli.
CC Colocalizes with VCL in the focal adhesions. Down-regulation and/or
CC elimination of its expression from the nucleus of neoplastic cells
CC correlates strongly with poor patient prognosis and aggressive forms of
CC breast carcinoma. Conversely, strong nuclear localization correlates
CC with low-tumor grade and better patient prognosis.
CC -!- TISSUE SPECIFICITY: Expressed in normal and breast cancer tissues (at
CC protein level). Ubiquitous. {ECO:0000269|PubMed:10647888,
CC ECO:0000269|PubMed:18712738}.
CC -!- INDUCTION: Down-regulated in lung cancer.
CC {ECO:0000269|PubMed:15542589}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:18439753}.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LIMD1ID41158ch3p21.html";
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DR EMBL; AJ132408; CAB63652.1; -; mRNA.
DR EMBL; AJ312686; CAC35917.1; -; Genomic_DNA.
DR EMBL; AJ297357; CAB95944.1; -; Genomic_DNA.
DR EMBL; BC117236; AAI17237.1; -; mRNA.
DR EMBL; BC117238; AAI17239.1; -; mRNA.
DR CCDS; CCDS2729.1; -.
DR RefSeq; NP_055055.1; NM_014240.2.
DR AlphaFoldDB; Q9UGP4; -.
DR BioGRID; 114475; 99.
DR IntAct; Q9UGP4; 48.
DR MINT; Q9UGP4; -.
DR STRING; 9606.ENSP00000273317; -.
DR GlyGen; Q9UGP4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UGP4; -.
DR PhosphoSitePlus; Q9UGP4; -.
DR BioMuta; LIMD1; -.
DR DMDM; 47605932; -.
DR EPD; Q9UGP4; -.
DR jPOST; Q9UGP4; -.
DR MassIVE; Q9UGP4; -.
DR MaxQB; Q9UGP4; -.
DR PaxDb; Q9UGP4; -.
DR PeptideAtlas; Q9UGP4; -.
DR PRIDE; Q9UGP4; -.
DR ProteomicsDB; 84252; -.
DR Antibodypedia; 29569; 217 antibodies from 26 providers.
DR DNASU; 8994; -.
DR Ensembl; ENST00000273317.5; ENSP00000273317.4; ENSG00000144791.10.
DR GeneID; 8994; -.
DR KEGG; hsa:8994; -.
DR MANE-Select; ENST00000273317.5; ENSP00000273317.4; NM_014240.3; NP_055055.1.
DR UCSC; uc003coq.4; human.
DR CTD; 8994; -.
DR DisGeNET; 8994; -.
DR GeneCards; LIMD1; -.
DR HGNC; HGNC:6612; LIMD1.
DR HPA; ENSG00000144791; Low tissue specificity.
DR MIM; 604543; gene.
DR neXtProt; NX_Q9UGP4; -.
DR OpenTargets; ENSG00000144791; -.
DR PharmGKB; PA30385; -.
DR VEuPathDB; HostDB:ENSG00000144791; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000159019; -.
DR HOGENOM; CLU_001357_11_1_1; -.
DR InParanoid; Q9UGP4; -.
DR OMA; SKLTMDG; -.
DR OrthoDB; 326249at2759; -.
DR PhylomeDB; Q9UGP4; -.
DR TreeFam; TF320310; -.
DR PathwayCommons; Q9UGP4; -.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR SignaLink; Q9UGP4; -.
DR BioGRID-ORCS; 8994; 10 hits in 1087 CRISPR screens.
DR ChiTaRS; LIMD1; human.
DR GeneWiki; LIMD1; -.
DR GenomeRNAi; 8994; -.
DR Pharos; Q9UGP4; Tbio.
DR PRO; PR:Q9UGP4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UGP4; protein.
DR Bgee; ENSG00000144791; Expressed in lower lobe of lung and 186 other tissues.
DR ExpressionAtlas; Q9UGP4; baseline and differential.
DR Genevisible; Q9UGP4; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016442; C:RISC complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IDA:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0002076; P:osteoblast development; ISS:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR InterPro; IPR028734; LIMD1.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24219:SF3; PTHR24219:SF3; 1.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Cell junction; Cytoplasm; LIM domain; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Tumor suppressor; Zinc.
FT CHAIN 1..676
FT /note="LIM domain-containing protein 1"
FT /id="PRO_0000075801"
FT DOMAIN 470..531
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 535..595
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 595..664
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 54..134
FT /note="Mediates nuclear export"
FT REGION 104..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..260
FT /note="Interaction with EGLN1/PHD2"
FT REGION 189..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..442
FT /note="Interaction with RB1"
FT /evidence="ECO:0000269|PubMed:15542589"
FT REGION 472..676
FT /note="Necessary for nuclear localization"
FT COMPBIAS 229..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B5DEH0"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B5DEH0"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VARIANT 36
FT /note="G -> D (in dbSNP:rs2578662)"
FT /id="VAR_050147"
FT VARIANT 415
FT /note="G -> R (in dbSNP:rs3733113)"
FT /id="VAR_021993"
SQ SEQUENCE 676 AA; 72190 MW; 085DF06F047B49E6 CRC64;
MDKYDDLGLE ASKFIEDLNM YEASKDGLFR VDKGAGNNPE FEETRRVFAT KMAKIHLQQQ
QQQLLQEETL PRGSRGPVNG GGRLGPQARW EVVGSKLTVD GAAKPPLAAS TGAPGAVTTL
AAGQPPYPPQ EQRSRPYLHG TRHGSQDCGS RESLATSEMS AFHQPGPCED PSCLTHGDYY
DNLSLASPKW GDKPGVSPSI GLSVGSGWPS SPGSDPPLPK PCGDHPLNHR QLSLSSSRSS
EGSLGGQNSG IGGRSSEKPT GLWSTASSQR VSPGLPSPNL ENGAPAVGPV QPRTPSVSAP
LALSCPRQGG LPRSNSGLGG EVSGVMSKPN VDPQPWFQDG PKSYLSSSAP SSSPAGLDGS
QQGAVPGLGP KPGCTDLGTG PKLSPTSLVH PVMSTLPELS CKEGPLGWSS DGSLGSVLLD
SPSSPRVRLP CQPLVPGPEL RPSAAELKLE ALTQRLEREM DAHPKADYFG ACVKCSKGVF
GAGQACQAMG NLYHDTCFTC AACSRKLRGK AFYFVNGKVF CEEDFLYSGF QQSADRCFLC
GHLIMDMILQ ALGKSYHPGC FRCVICNECL DGVPFTVDSE NKIYCVRDYH KVLAPKCAAC
GLPILPPEGS DETIRVVSMD RDYHVECYHC EDCGLELNDE DGHRCYPLED HLFCHSCHVK
RLEKRPSSTA LHQHHF
