EYA1_MOUSE
ID EYA1_MOUSE Reviewed; 591 AA.
AC P97767; G5E864; O08818;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Eyes absent homolog 1;
DE EC=3.1.3.16 {ECO:0000269|PubMed:14628052};
DE EC=3.1.3.48 {ECO:0000269|PubMed:14628052};
GN Name=Eya1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=9006082; DOI=10.1242/dev.124.1.219;
RA Xu P.-X., Woo I., Her H., Beier D.R., Maas R.L.;
RT "Mouse Eya homologues of the Drosophila eyes absent gene require Pax6 for
RT expression in lens and nasal placode.";
RL Development 124:219-231(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC STRAIN=CB/20;
RX PubMed=9020840; DOI=10.1038/ng0297-157;
RA Abdelhak S., Kalatzis V., Heilig R., Compain S., Samson D., Vincent C.,
RA Weil D., Cruaud C., Sahly I., Leibovici M., Bitner-Glindzicz M.,
RA Francis M., Lacombe D., Vigneron J., Charachon R., Boven K., Bedbeder P.,
RA van Regemorter N., Weissenbach J., Petit C.;
RT "A human homologue of the Drosophila eyes absent gene underlies branchio-
RT oto-renal (BOR) syndrome and identifies a novel gene family.";
RL Nat. Genet. 15:157-164(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-321, AND DISEASE.
RC STRAIN=129/SvJ;
RX PubMed=10072433; DOI=10.1093/hmg/8.4.645;
RA Johnson K.R., Cook S.A., Erway L.C., Matthews A.N., Sanford L.P.,
RA Paradies N.E., Friedman R.A.;
RT "Inner ear and kidney anomalies caused by IAP insertion in an intron of the
RT Eya1 gene in a mouse model of BOR syndrome.";
RL Hum. Mol. Genet. 8:645-653(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 431-549.
RC TISSUE=Embryo;
RX PubMed=9887327; DOI=10.1093/hmg/8.1.11;
RA Borsani G., DeGrandi A., Ballabio A., Bulfone A., Bernard L., Banfi S.,
RA Gattuso C., Mariani M., Dixon M., Donnai D., Metcalfe K., Winter R.,
RA Robertson M., Axton R., Brown A., van Heyningen V., Hanson I.;
RT "EYA4, a novel vertebrate gene related to Drosophila eyes absent.";
RL Hum. Mol. Genet. 8:11-23(1999).
RN [7]
RP FUNCTION, INTERACTION WITH SIX2; SIX4 AND SIX5, AND SUBCELLULAR LOCATION.
RX PubMed=10490620; DOI=10.1128/mcb.19.10.6815;
RA Ohto H., Kamada S., Tago K., Tominaga S., Ozaki H., Sato S., Kawakami K.;
RT "Cooperation of six and eya in activation of their target genes through
RT nuclear translocation of Eya.";
RL Mol. Cell. Biol. 19:6815-6824(1999).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=10471511; DOI=10.1038/12722;
RA Xu P.X., Adams J., Peters H., Brown M.C., Heaney S., Maas R.;
RT "Eya1-deficient mice lack ears and kidneys and show abnormal apoptosis of
RT organ primordia.";
RL Nat. Genet. 23:113-117(1999).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14628042; DOI=10.1038/nature02083;
RA Li X., Oghi K.A., Zhang J., Krones A., Bush K.T., Glass C.K., Nigam S.K.,
RA Aggarwal A.K., Maas R., Rose D.W., Rosenfeld M.G.;
RT "Eya protein phosphatase activity regulates Six1-Dach-Eya transcriptional
RT effects in mammalian organogenesis.";
RL Nature 426:247-254(2003).
RN [10]
RP ERRATUM OF PUBMED:14628042.
RA Li X., Oghi K.A., Zhang J., Krones A., Bush K.T., Glass C.K., Nigam S.K.,
RA Aggarwal A.K., Maas R., Rose D.W., Rosenfeld M.G.;
RL Nature 427:265-265(2004).
RN [11]
RP CATALYTIC ACTIVITY.
RX PubMed=14628052; DOI=10.1038/nature02093;
RA Rayapureddi J.P., Kattamuri C., Steinmetz B.D., Frankfort B.J.,
RA Ostrin E.J., Mardon G., Hegde R.S.;
RT "Eyes absent represents a class of protein tyrosine phosphatases.";
RL Nature 426:295-298(2003).
RN [12]
RP INTERACTION WITH SIX3.
RX PubMed=16024294; DOI=10.1016/j.modgep.2005.04.010;
RA Purcell P., Oliver G., Mardon G., Donner A.L., Maas R.L.;
RT "Pax6-dependence of Six3, Eya1 and Dach1 expression during lens and nasal
RT placode induction.";
RL Gene Expr. Patterns 6:110-118(2005).
RN [13]
RP SUMOYLATION, AND MUTAGENESIS OF LYS-43 AND LYS-459.
RX PubMed=16990542; DOI=10.1126/science.1128406;
RA Alkuraya F.S., Saadi I., Lund J.J., Turbe-Doan A., Morton C.C., Maas R.L.;
RT "SUMO1 haploinsufficiency leads to cleft lip and palate.";
RL Science 313:1751-1751(2006).
RN [14]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17098221; DOI=10.1016/j.ydbio.2006.08.059;
RA Grifone R., Demignon J., Giordani J., Niro C., Souil E., Bertin F.,
RA Laclef C., Xu P.X., Maire P.;
RT "Eya1 and Eya2 proteins are required for hypaxial somitic myogenesis in the
RT mouse embryo.";
RL Dev. Biol. 302:602-616(2007).
RN [15]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP H2AX.
RX PubMed=19234442; DOI=10.1038/nature07849;
RA Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.;
RT "Tyrosine dephosphorylation of H2AX modulates apoptosis and survival
RT decisions.";
RL Nature 458:591-596(2009).
CC -!- FUNCTION: Functions both as protein phosphatase and as transcriptional
CC coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5
CC (PubMed:10490620). Tyrosine phosphatase that dephosphorylates 'Tyr-142'
CC of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the
CC recruitment of DNA repair complexes containing MDC1. 'Tyr-142'
CC phosphorylation of histone H2AX plays a central role in DNA repair and
CC acts as a mark that distinguishes between apoptotic and repair
CC responses to genotoxic stress (PubMed:19234442). Its function as
CC histone phosphatase may contribute to its function in transcription
CC regulation during organogenesis (PubMed:14628042). Has also phosphatase
CC activity with proteins phosphorylated on Ser and Thr residues (in
CC vitro). Required for normal embryonic development of the craniofacial
CC and trunk skeleton, kidneys and ears (PubMed:10471511). Together with
CC SIX1, it plays an important role in hypaxial muscle development; in
CC this it is functionally redundant with EYA2 (PubMed:17098221).
CC {ECO:0000269|PubMed:10471511, ECO:0000269|PubMed:10490620,
CC ECO:0000269|PubMed:14628042, ECO:0000269|PubMed:17098221,
CC ECO:0000269|PubMed:19234442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:14628052};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:14628052};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:14628052};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O00167};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:O00167};
CC -!- SUBUNIT: Probably interacts with SIX2, SIX4 and SIX5. Interacts with
CC H2AX in response to DNA damage. Interacts with SIX3; promotes EYA1
CC translocation to the nucleus. {ECO:0000269|PubMed:10490620,
CC ECO:0000269|PubMed:16024294, ECO:0000269|PubMed:19234442}.
CC -!- INTERACTION:
CC P97767; Q9WUB0: Rbck1; NbExp=2; IntAct=EBI-1368503, EBI-6141072;
CC P97767; Q91WA6: Sharpin; NbExp=4; IntAct=EBI-1368503, EBI-646097;
CC P97767; Q62231: Six1; NbExp=3; IntAct=EBI-1368503, EBI-1368483;
CC P97767; Q62232: Six2; NbExp=3; IntAct=EBI-1368503, EBI-1368736;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10490620}. Nucleus
CC {ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:19234442}.
CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
CC {ECO:0000250|UniProtKB:Q99502}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97767-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97767-2; Sequence=VSP_001487, VSP_001488;
CC -!- TISSUE SPECIFICITY: Extensively expressed in cranial placodes,
CC branchial arches, CNS and developing eye and nose.
CC {ECO:0000269|PubMed:9006082}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:16990542}.
CC -!- DISEASE: Note=A spontaneous mutation leading to decreased Eya1
CC expression gives rise to the Eya1-bor phenotype. It is characterized by
CC circling behavior and deafness, due to gross morphological
CC abnormalities of the inner ear, and dysmorphic or missing kidneys. This
CC autosomal recessive trait resembles human branchio-oto-renal (BOR)
CC syndrome. {ECO:0000269|PubMed:10072433}.
CC -!- DISRUPTION PHENOTYPE: Complete perinatal lethality in homozygotes, due
CC to severe craniofacial and skeletal defects, combined with an absence
CC of thymus, kidneys, parotid glands and ears. Mice present multiple
CC skeletal defects in skull, neck, rib and pelvic girdle, but no major
CC defects in muscle development. Otic anomalies involve the inner, middle
CC and outer ears, with malformed auricles and eardrums, malformations of
CC the incus, malleus, and stapes, while the tympanic cavity never formed.
CC Likewise, mice display an absence of inner ear structures.
CC Heterozygotes present milder symptoms with low penetrance, including
CC renal defects, similar to human BOR (branchio-oto-renal) syndrome.
CC Increased apoptosis and loss of renal tubules seen in the developing
CC kidney with increased immunostaining for 'Ser-139' phosphorylated H2AX.
CC Mice lacking both Six1 and Eya1 show defects in kidney development,
CC complete absence of hypaxial muscle, severe reduction in epaxial muscle
CC and a 5-10-fold by volume smaller pituarity than the wild-type gland.
CC Mice lacking both Eya1 and Eya2 display complete embryonic lethality,
CC due to severe defects in muscle development, including the absence of a
CC diaphragm and of ventral hypaxial muscles of the trunk and the complete
CC absence of muscles in forelimbs and hindlimbs, similar to the phenotype
CC of mice lacking both Six1 and Six4. While Six1 is normally expressed in
CC these mice, it does not active transcription from cognate promoter
CC elements, and does not activate transcription of Pax3.
CC {ECO:0000269|PubMed:10471511, ECO:0000269|PubMed:14628042,
CC ECO:0000269|PubMed:17098221, ECO:0000269|PubMed:19234442}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB48017.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U61110; AAB48017.1; ALT_FRAME; mRNA.
DR EMBL; Y10263; CAA71312.1; -; Genomic_DNA.
DR EMBL; AC119875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466536; EDL14327.1; -; Genomic_DNA.
DR EMBL; AF097544; AAD19355.1; -; Genomic_DNA.
DR EMBL; AJ007995; CAA07818.1; -; mRNA.
DR CCDS; CCDS78545.1; -. [P97767-1]
DR RefSeq; NP_001297388.1; NM_001310459.1. [P97767-1]
DR RefSeq; XP_017170837.1; XM_017315348.1. [P97767-1]
DR AlphaFoldDB; P97767; -.
DR SMR; P97767; -.
DR BioGRID; 199559; 16.
DR CORUM; P97767; -.
DR IntAct; P97767; 5.
DR STRING; 10090.ENSMUSP00000079493; -.
DR iPTMnet; P97767; -.
DR PhosphoSitePlus; P97767; -.
DR MaxQB; P97767; -.
DR PaxDb; P97767; -.
DR PRIDE; P97767; -.
DR ProteomicsDB; 275954; -. [P97767-1]
DR ProteomicsDB; 275955; -. [P97767-2]
DR Antibodypedia; 25098; 234 antibodies from 31 providers.
DR DNASU; 14048; -.
DR Ensembl; ENSMUST00000027066; ENSMUSP00000027066; ENSMUSG00000025932. [P97767-1]
DR Ensembl; ENSMUST00000190337; ENSMUSP00000141112; ENSMUSG00000025932. [P97767-1]
DR GeneID; 14048; -.
DR KEGG; mmu:14048; -.
DR UCSC; uc007aiw.1; mouse. [P97767-1]
DR CTD; 2138; -.
DR MGI; MGI:109344; Eya1.
DR VEuPathDB; HostDB:ENSMUSG00000025932; -.
DR eggNOG; KOG3107; Eukaryota.
DR GeneTree; ENSGT00950000182978; -.
DR InParanoid; P97767; -.
DR OMA; FTAGMQQ; -.
DR OrthoDB; 1030296at2759; -.
DR PhylomeDB; P97767; -.
DR TreeFam; TF319337; -.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR SABIO-RK; P97767; -.
DR BioGRID-ORCS; 14048; 2 hits in 98 CRISPR screens.
DR ChiTaRS; Eya1; mouse.
DR PRO; PR:P97767; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P97767; protein.
DR Bgee; ENSMUSG00000025932; Expressed in epithelium of cochlear duct and 245 other tissues.
DR ExpressionAtlas; P97767; baseline and differential.
DR Genevisible; P97767; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IDA:UniProtKB.
DR GO; GO:0140793; F:histone tyrosine phosphatase activity (H2-Y142 specific); ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0048856; P:anatomical structure development; IGI:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0035909; P:aorta morphogenesis; IMP:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0007501; P:mesodermal cell fate specification; IDA:UniProtKB.
DR GO; GO:0001656; P:metanephros development; IMP:MGI.
DR GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0048665; P:neuron fate specification; IGI:MGI.
DR GO; GO:0071599; P:otic vesicle development; IGI:MGI.
DR GO; GO:0071600; P:otic vesicle morphogenesis; IMP:MGI.
DR GO; GO:0042473; P:outer ear morphogenesis; IMP:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:InterPro.
DR GO; GO:0060037; P:pharyngeal system development; IMP:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0072513; P:positive regulation of secondary heart field cardioblast proliferation; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0048752; P:semicircular canal morphogenesis; IMP:MGI.
DR GO; GO:0014706; P:striated muscle tissue development; IGI:MGI.
DR GO; GO:0001657; P:ureteric bud development; IGI:MGI.
DR CDD; cd02601; HAD_Eya; 1.
DR Gene3D; 3.40.50.12350; -; 1.
DR InterPro; IPR006545; EYA_dom.
DR InterPro; IPR042577; EYA_dom_metazoan.
DR InterPro; IPR038102; EYA_dom_sf.
DR InterPro; IPR028472; EYA_fam.
DR InterPro; IPR028471; Eyes_absent_h1.
DR PANTHER; PTHR10190; PTHR10190; 1.
DR PANTHER; PTHR10190:SF11; PTHR10190:SF11; 1.
DR TIGRFAMs; TIGR01658; EYA-cons_domain; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromatin regulator; Cytoplasm;
KW Developmental protein; DNA damage; DNA repair; Hydrolase; Magnesium;
KW Metal-binding; Nucleus; Protein phosphatase; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..591
FT /note="Eyes absent homolog 1"
FT /id="PRO_0000218644"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT ACT_SITE 329
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 555
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT VAR_SEQ 1..41
FT /note="MEMQDLTSPHSRLSGSSESPSGPKLDSSHINSTSMTPNGTE -> MLLFPQV
FT A (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001487"
FT VAR_SEQ 140..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001488"
FT MUTAGEN 43
FT /note="K->R: Markedly reduced sumoylation; when associated
FT with R-459."
FT /evidence="ECO:0000269|PubMed:16990542"
FT MUTAGEN 459
FT /note="K->R: Markedly reduced sumoylation; when associated
FT with R-43."
FT /evidence="ECO:0000269|PubMed:16990542"
FT CONFLICT 117
FT /note="M -> V (in Ref. 2; CAA71312)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="L -> F (in Ref. 2; CAA71312)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..325
FT /note="FI -> LL (in Ref. 1; AAB48017)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="T -> R (in Ref. 1; AAB48017)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="N -> K (in Ref. 1; AAB48017)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="I -> S (in Ref. 1; AAB48017)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="S -> G (in Ref. 2; CAA71312)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="R -> G (in Ref. 2; CAA71312)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="V -> L (in Ref. 2; CAA71312)"
FT /evidence="ECO:0000305"
FT CONFLICT 551..552
FT /note="VV -> LL (in Ref. 1; AAB48017)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="E -> K (in Ref. 2; CAA71312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 64324 MW; D31F71852FBDC76C CRC64;
MEMQDLTSPH SRLSGSSESP SGPKLDSSHI NSTSMTPNGT EVKTEPMSSS EIASTAADGS
LDSFSGSALG SSSFSPRPAH PFSPPQIYPS KSYPHILPTP SSQTMAAYGQ TQFTTGMQQA
TAYATYPQPG QPYGISSYGA LWAGIKTESG LSQSQSPGQT GFLSYGTSFG TPQPGQAPYS
YQMQGSSFTT SSGLYSGNNS LTNSSGFNSS QQDYPSYPGF GQGQYAQYYN SSPYPAHYMT
SSNTSPTTPS TNATYQLQEP PSGVTSQAVT DPTAEYSTIH SPSTPIKETD SERLRRGSDG
KSRGRGRRNN NPSPPPDSDL ERVFIWDLDE TIIVFHSLLT GSYANRYGRD PPTSVSLGLR
MEEMIFNLAD THLFFNDLEE CDQVHIDDVS SDDNGQDLST YNFGTDGFPA AATSANLCLA
TGVRGGVDWM RKLAFRYRRV KEIYNTYKNN VGGLLGPAKR EAWLQLRAEI EALTDSWLTL
ALKALSLIHS RTNCVNILVT TTQLIPALAK VLLYGLGIVF PIENIYSATK IGKESCFERI
IQRFGRKVVY VVIGDGVEEE QGAKKHAMPF WRVSSHSDLM ALHHALELEY L
