ID DYR1A_MOUSE Reviewed; 763 AA. AC Q61214; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 203. DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 1A; DE EC=2.7.11.23 {ECO:0000250|UniProtKB:Q13627}; DE EC=2.7.12.1 {ECO:0000269|PubMed:20167603}; DE AltName: Full=Dual specificity YAK1-related kinase; DE AltName: Full=MP86; DE AltName: Full=Protein kinase minibrain homolog; DE Short=MNBH; GN Name=Dyrk1a; Synonyms=Dyrk; 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], AND TISSUE SPECIFICITY. RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo; RX PubMed=8975710; DOI=10.1006/geno.1996.0636; RA Song W.J., Sternberg L.R., Kasten-Sportes C., van Keuren M.L., Chung S.H., RA Slack A.C., Miller D.E., Glover T.W., Chiang P.W., Lou L., Kurnit D.W.; RT "Isolation of human and murine homologues of the Drosophila minibrain gene: RT human homologue maps to 21q22.2 in the Down syndrome 'critical region'."; RL Genomics 38:331-339(1996). RN [2] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=9070862; DOI=10.1006/bbrc.1997.6154; RA Song W.J., Chung S.H., Kurnit D.M.; RT "The murine Dyrk protein maps to chromosome 16, localizes to the nucleus, RT and can form multimers."; RL Biochem. Biophys. Res. Commun. 231:640-644(1997). RN [3] RP INTERACTION WITH RAD54L2. RX PubMed=15199138; DOI=10.1128/mcb.24.13.5821-5834.2004; RA Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.; RT "Dyrk1A potentiates steroid hormone-induced transcription via the chromatin RT remodeling factor Arip4."; RL Mol. Cell. Biol. 24:5821-5834(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=18938227; DOI=10.1016/j.neuroscience.2008.09.034; RA Sitz J.H., Baumgaertel K., Haemmerle B., Papadopoulos C., Hekerman P., RA Tejedor F.J., Becker W., Lutz B.; RT "The Down syndrome candidate dual-specificity tyrosine phosphorylation- RT regulated kinase 1A phosphorylates the neurodegeneration-related septin RT 4."; RL Neuroscience 157:596-605(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-748 AND SER-758, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP FUNCTION, INTERACTION WITH SIRT1, AND CATALYTIC ACTIVITY. RX PubMed=20167603; DOI=10.1074/jbc.m110.102574; RA Guo X., Williams J.G., Schug T.T., Li X.; RT "DYRK1A and DYRK3 promote cell survival through phosphorylation and RT activation of SIRT1."; RL J. Biol. Chem. 285:13223-13232(2010). RN [8] RP FUNCTION, AND INTERACTION WITH CRY2. RX PubMed=20123978; DOI=10.1128/mcb.01047-09; RA Kurabayashi N., Hirota T., Sakai M., Sanada K., Fukada Y.; RT "DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism RT directing proteasomal degradation of CRY2 for circadian timekeeping."; RL Mol. Cell. Biol. 30:1757-1768(2010). RN [9] RP TISSUE SPECIFICITY. RX PubMed=22998443; DOI=10.1021/jm301034u; RA Tahtouh T., Elkins J.M., Filippakopoulos P., Soundararajan M., Burgy G., RA Durieu E., Cochet C., Schmid R.S., Lo D.C., Delhommel F., Oberholzer A.E., RA Pearl L.H., Carreaux F., Bazureau J.P., Knapp S., Meijer L.; RT "Selectivity, cocrystal structures, and neuroprotective properties of RT leucettines, a family of protein kinase inhibitors derived from the marine RT sponge alkaloid leucettamine B."; RL J. Med. Chem. 55:9312-9330(2012). CC -!- FUNCTION: Dual-specificity kinase which possesses both serine/threonine CC and tyrosine kinase activities (PubMed:18938227, PubMed:20123978). CC Exhibits a substrate preference for proline at position P+1 and CC arginine at position P-3 (By similarity). Plays an important role in CC double-strand breaks (DSBs) repair following DNA damage (By CC similarity). Mechanistically, phosphorylates RNF169 and increases its CC ability to block accumulation of TP53BP1 at the DSB sites thereby CC promoting homologous recombination repair (HRR) (By similarity). Also CC acts as a positive regulator of transcription by acting as a CTD kinase CC that mediates phosphorylation of the CTD (C-terminal domain) of the CC large subunit of RNA polymerase II (RNAP II) POLR2A (By similarity). CC May play a role in a signaling pathway regulating nuclear functions of CC cell proliferation (By similarity). Modulates alternative splicing by CC phosphorylating the splice factor SRSF6 (By similarity). Has pro- CC survival function and negatively regulates the apoptotic process CC (PubMed:20167603). Promotes cell survival upon genotoxic stress through CC phosphorylation of SIRT1 (PubMed:20167603). This in turn inhibits CC p53/TP53 activity and apoptosis (PubMed:20167603). Phosphorylates CC SEPTIN4, SEPTIN5 and SF3B1 at 'Thr-434' (PubMed:18938227). CC {ECO:0000250|UniProtKB:Q13627, ECO:0000250|UniProtKB:Q63470, CC ECO:0000269|PubMed:18938227, ECO:0000269|PubMed:20123978, CC ECO:0000269|PubMed:20167603}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; CC Evidence={ECO:0000269|PubMed:20167603}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.12.1; Evidence={ECO:0000269|PubMed:20167603}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; CC Evidence={ECO:0000269|PubMed:20167603}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho- CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA- CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, CC ChEBI:CHEBI:456216; EC=2.7.11.23; CC Evidence={ECO:0000250|UniProtKB:Q13627}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10217; CC Evidence={ECO:0000250|UniProtKB:Q13627}; CC -!- ACTIVITY REGULATION: Inhibited by RANBP9. CC {ECO:0000250|UniProtKB:Q13627}. CC -!- SUBUNIT: Interacts with RANBP9 (By similarity). Interacts with CC RAD54L2/ARIP4 (PubMed:15199138). Interacts with WDR68 (By similarity). CC Interacts with CRY2 (PubMed:20123978). Interacts with SIRT1 CC (PubMed:20167603). {ECO:0000250|UniProtKB:Q13627, CC ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:18938227, CC ECO:0000269|PubMed:20123978, ECO:0000269|PubMed:20167603, CC ECO:0000269|PubMed:9070862}. CC -!- INTERACTION: CC Q61214; Q9ERC8: Dscam; NbExp=2; IntAct=EBI-80344, EBI-1798601; CC Q61214; Q61214: Dyrk1a; NbExp=2; IntAct=EBI-80344, EBI-80344; CC Q61214; Q9JHG6: Rcan1; NbExp=2; IntAct=EBI-80344, EBI-644061; CC Q61214; Q923E4: Sirt1; NbExp=4; IntAct=EBI-80344, EBI-1802585; CC Q61214; P53805-2: RCAN1; Xeno; NbExp=5; IntAct=EBI-80344, EBI-1541912; CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9070862}. CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level) CC (PubMed:22998443). Expressed in a variety of embryonic and adult CC tissues (PubMed:8975710). Expressed abundantly in neurons of the brain, CC spinal cord, and retina in developing embryos (PubMed:8975710). CC Expressed in the entorhinal, temporal and visual cortices and the CC hippocampus of the brain where is colocalizes with SEPTIN4 CC (PubMed:18938227). Expressed and extensively colocalizes with SEPTIN4 CC in apical dendrites of pyramidal cells (PubMed:18938227). Also CC expressed in Purkinje cells in the cerebellum in postnatal day 1 and CC adult mice (PubMed:18938227). {ECO:0000269|PubMed:18938227, CC ECO:0000269|PubMed:22998443, ECO:0000269|PubMed:8975710}. CC -!- DOMAIN: The polyhistidine repeats act as targeting signals to nuclear CC speckles. {ECO:0000250|UniProtKB:Q13627}. CC -!- DOMAIN: The histidine-rich domain (HRD) region is intrinsically CC disordered and promotes the formation of phase-separated liquid CC droplets that enhance its ability to phosphorylate the CTD (C-terminal CC domain) of the large subunit of RNA polymerase II (RNA Pol II). CC {ECO:0000250|UniProtKB:Q13627}. CC -!- PTM: Autophosphorylated on numerous tyrosine residues. Can also CC autophosphorylate on serine and threonine residues (in vitro) (By CC similarity). {ECO:0000250|UniProtKB:Q13627}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MNB/DYRK subfamily. {ECO:0000305}. 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; U58497; AAC52994.1; -; mRNA. DR CCDS; CCDS28350.1; -. DR RefSeq; NP_001106860.1; NM_001113389.1. DR RefSeq; NP_031916.1; NM_007890.2. DR RefSeq; XP_011244396.1; XM_011246094.2. DR RefSeq; XP_011244397.1; XM_011246095.2. DR AlphaFoldDB; Q61214; -. DR SMR; Q61214; -. DR BioGRID; 199347; 30. DR ELM; Q61214; -. DR IntAct; Q61214; 10. DR MINT; Q61214; -. DR STRING; 10090.ENSMUSP00000113660; -. DR BindingDB; Q61214; -. DR ChEMBL; CHEMBL4750; -. DR iPTMnet; Q61214; -. DR PhosphoSitePlus; Q61214; -. DR EPD; Q61214; -. DR jPOST; Q61214; -. DR MaxQB; Q61214; -. DR PaxDb; 10090-ENSMUSP00000113660; -. DR ProteomicsDB; 277654; -. DR Pumba; Q61214; -. DR Antibodypedia; 8587; 457 antibodies from 39 providers. DR DNASU; 13548; -. DR Ensembl; ENSMUST00000023614.5; ENSMUSP00000023614.5; ENSMUSG00000022897.16. DR Ensembl; ENSMUST00000119878.8; ENSMUSP00000113660.2; ENSMUSG00000022897.16. DR GeneID; 13548; -. DR KEGG; mmu:13548; -. DR UCSC; uc008abg.2; mouse. DR AGR; MGI:1330299; -. DR CTD; 1859; -. DR MGI; MGI:1330299; Dyrk1a. DR VEuPathDB; HostDB:ENSMUSG00000022897; -. DR eggNOG; KOG0667; Eukaryota. DR GeneTree; ENSGT00940000157408; -. DR InParanoid; Q61214; -. DR OMA; YNFAEIS; -. DR OrthoDB; 452107at2759; -. DR PhylomeDB; Q61214; -. DR TreeFam; TF314624; -. DR BRENDA; 2.7.12.1; 3474. DR Reactome; R-MMU-1538133; G0 and Early G1. DR BioGRID-ORCS; 13548; 12 hits in 82 CRISPR screens. DR ChiTaRS; Dyrk1a; mouse. DR PRO; PR:Q61214; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q61214; Protein. DR Bgee; ENSMUSG00000022897; Expressed in animal zygote and 270 other cell types or tissues. DR ExpressionAtlas; Q61214; baseline and differential. DR GO; GO:0030424; C:axon; IDA:ARUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL. DR GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL. DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI. DR GO; GO:0003779; F:actin binding; ISO:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI. DR GO; GO:0140857; F:histone H3T45 kinase activity; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:MGI. DR GO; GO:0004672; F:protein kinase activity; ISO:MGI. DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; ISO:MGI. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISS:UniProtKB. DR GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL. DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central. DR GO; GO:0015631; F:tubulin binding; ISO:MGI. DR GO; GO:0034205; P:amyloid-beta formation; ISO:MGI. DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB. DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL. DR GO; GO:0090310; P:negative regulation of DNA methylation-dependent heterochromatin formation; ISO:MGI. DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:ARUK-UCL. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:MGI. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL. DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:ARUK-UCL. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0090312; P:positive regulation of protein deacetylation; IDA:BHF-UCL. DR GO; GO:0033120; P:positive regulation of RNA splicing; ISO:MGI. DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:MGI. DR CDD; cd14226; PKc_DYRK1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR044131; PKc_DYR1A/1B. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1. DR PANTHER; PTHR24058:SF121; DUAL SPECIFICITY TYROSINE-PHOSPHORYLATION-REGULATED KINASE 1A; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q61214; MM. PE 1: Evidence at protein level; KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transcription; KW Transcription regulation; Transferase; Tyrosine-protein kinase. FT CHAIN 1..763 FT /note="Dual specificity tyrosine-phosphorylation-regulated FT kinase 1A" FT /id="PRO_0000085932" FT DOMAIN 159..479 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 33..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 115..136 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 408..442 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 485..540 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 595..625 FT /note="Histidine-rich domain (HRD)" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT REGION 596..679 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 117..134 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 34..61 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 485..528 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 601..624 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 627..679 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 287 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 165..173 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 188 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 238..241 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 111 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 140 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 145 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT MOD_RES 159 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 177 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 219 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q63470" FT MOD_RES 310 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 319 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 321 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 402 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 449 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 529 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13627" FT MOD_RES 538 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 748 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 758 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" SQ SEQUENCE 763 AA; 85494 MW; E117DDD6C5E8C74F CRC64; MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AAQMPHSHQY SDRRQPSISD QQVSALPYSD QIQQPLTNQV MPDIVMLQRR MPQTFRDPAT APLRKLSVDL IKTYKHINEV YYAKKKRRHQ QGQGDDSSHK KERKVYNDGY DDDNYDYIVK NGEKWMDRYE IDSLIGKGSF GQVVKAYDRV EQEWVAIKII KNKKAFLNQA QIEVRLLELM NKHDTEMKYY IVHLKRHFMF RNHLCLVFEM LSYNLYDLLR NTNFRGVSLN LTRKFAQQMC TALLFLATPE LSIIHCDLKP ENILLCNPKR SAIKIVDFGS SCQLGQRIYQ YIQSRFYRSP EVLLGMPYDL AIDMWSLGCI LVEMHTGEPL FSGANEVDQM NKIVEVLGIP PAHILDQAPK ARKFFEKLPD GTWSLKKTKD GKREYKPPGT RKLHNILGVE TGGPGGRRAG ESGHTVADYL KFKDLILRML DYDPKTRIQP YYALQHSFFK KTADEGTNTS NSVSTSPAME QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG HFAAAVQAMD CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH SHHSMTSLSS STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV NLTVYSNPRQ ETGIAGHPTY QFSANTGPAH YMTEGHLAMR QGADREESPM TGVCVQQSPV ASS //