ID MEF2A_MOUSE Reviewed; 498 AA. AC Q60929; Q3V155; Q4VA09; Q6P8Q3; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 191. DE RecName: Full=Myocyte-specific enhancer factor 2A; GN Name=Mef2a; 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), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC TISSUE=Cerebellum; RX PubMed=9013788; DOI=10.1016/s0169-328x(96)00135-0; RA Lin X., Shah S., Bulleit R.F.; RT "The expression of MEF2 genes is implicated in CNS neuronal RT differentiation."; RL Brain Res. Mol. Brain Res. 42:307-316(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=NMRI; TISSUE=Brain, and Mammary tumor; 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 INTERACTION WITH HDAC7. RX PubMed=11585834; DOI=10.1074/jbc.m107631200; RA Kao H.-Y., Verdel A., Tsai C.-C., Simon C., Juguilon H., Khochbin S.; RT "Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7."; RL J. Biol. Chem. 276:47496-47507(2001). RN [5] RP TISSUE SPECIFICITY OF ISOFORMS. RX PubMed=15834131; DOI=10.1074/jbc.m502491200; RA Zhu B., Ramachandran B., Gulick T.; RT "Alternative pre-mRNA splicing governs expression of a conserved acidic RT transactivation domain in myocyte enhancer factor 2 factors of striated RT muscle and brain."; RL J. Biol. Chem. 280:28749-28760(2005). RN [6] RP INTERACTION WITH NLK, AND PHOSPHORYLATION AT THR-310. RX PubMed=17785444; DOI=10.1128/mcb.01481-07; RA Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T., RA Shibuya H.; RT "Nemo-like kinase-myocyte enhancer factor 2A signaling regulates anterior RT formation in Xenopus development."; RL Mol. Cell. Biol. 27:7623-7630(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND THR-108 (ISOFORM 3), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-108; SER-233 AND RP THR-413, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND THR-108 RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and RC 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-247, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Transcriptional activator which binds specifically to the CC MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific CC genes. Also involved in the activation of numerous growth factor- and CC stress-induced genes. Mediates cellular functions not only in skeletal CC and cardiac muscle development, but also in neuronal differentiation CC and survival. Plays diverse roles in the control of cell growth, CC survival and apoptosis via p38 MAPK signaling in muscle-specific and/or CC growth factor-related transcription. In cerebellar granule neurons, CC phosphorylated and sumoylated MEF2A represses transcription of NUR77 CC promoting synaptic differentiation. Associates with chromatin to the CC ZNF16 promoter (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Binds DNA as a homo- or heterodimer. Dimerizes with MEF2D. CC Interacts with HDAC7. Interacts with PIAS1; the interaction enhances CC sumoylation. Interacts with HDAC4, HDAC9 and SLC2A4RG. Interacts (via CC the N-terminal) with MAPK7; the interaction results in the CC phosphorylation and transcriptional activity of MEF2A (By similarity). CC {ECO:0000250}. CC -!- INTERACTION: CC Q60929; P12979: Myog; NbExp=2; IntAct=EBI-2639094, EBI-7132875; CC Q60929; P70257-2: Nfix; NbExp=2; IntAct=EBI-2639094, EBI-2639084; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q60929-1; Sequence=Displayed; CC Name=2; CC IsoId=Q60929-2; Sequence=VSP_026031; CC Name=3; CC IsoId=Q60929-3; Sequence=VSP_026060, VSP_026031; CC -!- TISSUE SPECIFICITY: Widely expressed though mainly restricted to CC skeletal and cardiac muscle, brain, neurons and lymphocytes. CC Differentially expressed depending on if isoforms contain the beta CC domain or not, with the total expression of the beta domain-lacking CC isoforms vastly exceding that of the beta domain-containing isoforms. CC Isoforms containing the beta domain are expressed primarily in skeletal CC and cardiac muscle and in brain. Also present in lung and testis. CC Splicing to include the beta domain is induced in differentiating CC myocytes. Isoforms lacking the beta domain are expressed less CC abundantly in skeletal muscle, brain and lymphocytes, and are uniquely CC found in ovary, liver, spleen and kidney. In embryos, the beta domain- CC containing and beta domain-lacking isoforms are equally expressed. Also CC expressed cerebellar granule neurons and other regions of the CNS. CC Highest levels in the olfactory bulb, cortex, hippocampus, thalamus and CC cerebellum. {ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:9013788}. CC -!- DEVELOPMENTAL STAGE: In the developing cerebellum, increasing levels CC after birth. The majority of this increase occurs around postnataL day CC 9 reaching a peak at postnatal day 15-18 which is maintained in adults. CC {ECO:0000269|PubMed:9013788}. CC -!- DOMAIN: The beta domain, missing in a number of isoforms, is required CC for enhancement of transcriptional activity. {ECO:0000250}. CC -!- PTM: Constitutive phosphorylation on Ser-406 promotes Lys-401 CC sumoylation thus preventing acetylation at this site. Dephosphorylation CC on Ser-406 by PPP3CA upon neuron depolarization promotes a switch from CC sumoylation to acetylation on residue Lys-403 leading to inhibition of CC dendrite claw differentiation. Phosphorylation on Thr-312 and Thr-319 CC are the main sites involved in p38 MAPK signaling and activate CC transcription. Phosphorylated on these sites by MAPK14/p38alpha and CC MAPK11/p38beta, but not by MAPK13/p38delta nor by MAPK12/p38gamma. CC Phosphorylation on Ser-408 by CDK5 induced by neurotoxicity inhibits CC MEF2A transcriptional activation leading to apoptosis of cortical CC neurons. Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced CC by EGF (By similarity). Isoform 3 is phosphorylated on Ser-98 and Thr- CC 108. {ECO:0000250, ECO:0000269|PubMed:17785444}. CC -!- PTM: Sumoylation on Lys-401 is enhanced by PIAS1 and represses CC transcriptional activity. Phosphorylation on Ser-406 is required for CC sumoylation. Has no effect on nuclear location nor on DNA binding. CC Sumoylated with SUMO1 and, to a lesser extent with SUMO2 and SUMO3. CC PIASx facilitates sumoylation in postsynaptic dendrites in the CC cerebellar cortex and promotes their morphogenesis (By similarity). CC {ECO:0000250}. CC -!- PTM: Acetylation on Lys-401 activates transcriptional activity. CC Acetylated by p300 on several sites in diffentiating myocytes. CC Acetylation on Lys-4 increases DNA binding and transactivation. CC Hyperacetylation by p300 leads to enhanced cardiac myocyte growth and CC heart failure (By similarity). {ECO:0000250}. CC -!- PTM: Proteolytically cleaved in cerebellar granule neurons on several CC sites by caspase 3 and caspase 7 following neurotoxicity. CC Preferentially cleaves the CDK5-mediated hyperphosphorylated form which CC leads to neuron apoptosis and transcriptional inactivation (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MEF2 family. {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; U30823; AAA74030.1; -; mRNA. DR EMBL; AK132678; BAE21297.1; -; mRNA. DR EMBL; BC061128; AAH61128.1; -; mRNA. DR EMBL; BC096598; AAH96598.1; -; mRNA. DR CCDS; CCDS39981.1; -. [Q60929-1] DR CCDS; CCDS71979.1; -. [Q60929-3] DR CCDS; CCDS71980.1; -. [Q60929-2] DR RefSeq; NP_001028885.1; NM_001033713.2. [Q60929-1] DR RefSeq; NP_001278120.1; NM_001291191.1. [Q60929-3] DR RefSeq; NP_001278121.1; NM_001291192.1. [Q60929-3] DR RefSeq; NP_001278124.1; NM_001291195.1. [Q60929-2] DR RefSeq; NP_001278125.1; NM_001291196.1. DR RefSeq; XP_006540749.1; XM_006540686.3. DR RefSeq; XP_011249116.1; XM_011250814.2. DR RefSeq; XP_017177500.1; XM_017322011.1. DR AlphaFoldDB; Q60929; -. DR SMR; Q60929; -. DR BioGRID; 201381; 3. DR IntAct; Q60929; 4. DR MINT; Q60929; -. DR STRING; 10090.ENSMUSP00000117496; -. DR iPTMnet; Q60929; -. DR PhosphoSitePlus; Q60929; -. DR EPD; Q60929; -. DR jPOST; Q60929; -. DR MaxQB; Q60929; -. DR PaxDb; 10090-ENSMUSP00000117496; -. DR PeptideAtlas; Q60929; -. DR ProteomicsDB; 295991; -. [Q60929-1] DR ProteomicsDB; 295992; -. [Q60929-2] DR ProteomicsDB; 295993; -. [Q60929-3] DR Pumba; Q60929; -. DR Antibodypedia; 3854; 1171 antibodies from 44 providers. DR Ensembl; ENSMUST00000032776.15; ENSMUSP00000032776.9; ENSMUSG00000030557.18. [Q60929-3] DR Ensembl; ENSMUST00000076325.12; ENSMUSP00000075664.6; ENSMUSG00000030557.18. [Q60929-3] DR Ensembl; ENSMUST00000107476.8; ENSMUSP00000103100.2; ENSMUSG00000030557.18. [Q60929-2] DR Ensembl; ENSMUST00000135493.8; ENSMUSP00000138566.2; ENSMUSG00000030557.18. [Q60929-1] DR Ensembl; ENSMUST00000156690.8; ENSMUSP00000117496.2; ENSMUSG00000030557.18. [Q60929-1] DR GeneID; 17258; -. DR KEGG; mmu:17258; -. DR UCSC; uc009hie.3; mouse. [Q60929-3] DR UCSC; uc009hif.3; mouse. [Q60929-1] DR UCSC; uc009hig.3; mouse. [Q60929-2] DR AGR; MGI:99532; -. DR CTD; 4205; -. DR MGI; MGI:99532; Mef2a. DR VEuPathDB; HostDB:ENSMUSG00000030557; -. DR eggNOG; KOG0014; Eukaryota. DR GeneTree; ENSGT00940000156205; -. DR HOGENOM; CLU_022902_4_0_1; -. DR InParanoid; Q60929; -. DR OMA; MNTQRIS; -. DR OrthoDB; 448298at2759; -. DR PhylomeDB; Q60929; -. DR TreeFam; TF314067; -. DR Reactome; R-MMU-525793; Myogenesis. DR BioGRID-ORCS; 17258; 4 hits in 79 CRISPR screens. DR ChiTaRS; Mef2a; mouse. DR PRO; PR:Q60929; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q60929; Protein. DR Bgee; ENSMUSG00000030557; Expressed in medial dorsal nucleus of thalamus and 272 other cell types or tissues. DR ExpressionAtlas; Q60929; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB. DR GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:0046332; F:SMAD binding; ISS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0061337; P:cardiac conduction; IMP:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB. DR GO; GO:0048813; P:dendrite morphogenesis; ISO:MGI. DR GO; GO:0006351; P:DNA-templated transcription; ISO:MGI. DR GO; GO:0070375; P:ERK5 cascade; ISS:UniProtKB. DR GO; GO:0007507; P:heart development; IBA:GO_Central. DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB. DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:UniProtKB. DR GO; GO:0048311; P:mitochondrion distribution; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI. DR GO; GO:0046326; P:positive regulation of glucose import; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0055005; P:ventricular cardiac myofibril assembly; IMP:UniProtKB. DR CDD; cd00265; MADS_MEF2_like; 1. DR Gene3D; 3.40.1810.10; Transcription factor, MADS-box; 1. DR InterPro; IPR022102; HJURP_C. DR InterPro; IPR033896; MADS_MEF2-like. DR InterPro; IPR002100; TF_MADSbox. DR InterPro; IPR036879; TF_MADSbox_sf. DR PANTHER; PTHR48019:SF109; MYOCYTE-SPECIFIC ENHANCER FACTOR 2A; 1. DR PANTHER; PTHR48019; SERUM RESPONSE FACTOR HOMOLOG; 1. DR Pfam; PF12347; HJURP_C; 1. DR Pfam; PF00319; SRF-TF; 1. DR PRINTS; PR00404; MADSDOMAIN. DR SMART; SM00432; MADS; 1. DR SUPFAM; SSF55455; SRF-like; 1. DR PROSITE; PS00350; MADS_BOX_1; 1. DR PROSITE; PS50066; MADS_BOX_2; 1. DR Genevisible; Q60929; MM. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; Apoptosis; KW Developmental protein; Differentiation; DNA-binding; Isopeptide bond; KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..498 FT /note="Myocyte-specific enhancer factor 2A" FT /id="PRO_0000199429" FT DOMAIN 3..57 FT /note="MADS-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251" FT DNA_BIND 58..86 FT /note="Mef2-type" FT /evidence="ECO:0000255" FT REGION 172..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 240..268 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 264..281 FT /note="Required for interaction with MAPKs" FT /evidence="ECO:0000250" FT REGION 287..294 FT /note="Beta domain" FT /evidence="ECO:0000250" FT REGION 388..498 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..220 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 388..403 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..439 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 441..457 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 174..175 FT /note="Cleavage" FT /evidence="ECO:0000305" FT SITE 211..212 FT /note="Cleavage" FT /evidence="ECO:0000305" FT SITE 457..458 FT /note="Cleavage" FT /evidence="ECO:0000305" FT MOD_RES 59 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000250" FT MOD_RES 98 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 108 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 233 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 247 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 253 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q02078" FT MOD_RES 310 FT /note="Phosphothreonine; by MAPK7" FT /evidence="ECO:0000250|UniProtKB:Q02078" FT MOD_RES 310 FT /note="Phosphothreonine; by NLK" FT /evidence="ECO:0000269|PubMed:17785444" FT MOD_RES 317 FT /note="Phosphothreonine; by MAPK7" FT /evidence="ECO:0000250|UniProtKB:Q02078" FT MOD_RES 353 FT /note="Phosphoserine; by MAPK7" FT /evidence="ECO:0000250|UniProtKB:Q02078" FT MOD_RES 401 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q2MJT0" FT MOD_RES 406 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q02078" FT MOD_RES 413 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 444 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q02078" FT CROSSLNK 401 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250" FT VAR_SEQ 87..130 FT /note="TLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGP -> ALNK FT KEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIA (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_026060" FT VAR_SEQ 287..294 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_026031" FT CONFLICT 98 FT /note="S -> N (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 116 FT /note="S -> I (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 133 FT /note="L -> F (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 151 FT /note="A -> P (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 154 FT /note="Y -> D (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 174..175 FT /note="DS -> ET (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="G -> S (in Ref. 2; BAE21297)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="V -> A (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 367 FT /note="Q -> E (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 373..374 FT /note="AA -> TT (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 419..423 FT /note="QQQQQ -> HHHHH (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT CONFLICT 478 FT /note="P -> A (in Ref. 1; AAA74030)" FT /evidence="ECO:0000305" FT MOD_RES Q60929-3:98 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES Q60929-3:108 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" SQ SEQUENCE 498 AA; 53579 MW; FE291C3E3E0A5E70 CRC64; MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCESPD ADDYFEHSPL SEDRFSKLNE DSDFIFKRGP PGLPPQNFSM SVTVPVTSPN ALSYTNPGSS LVSPSLAASS TLADSSMLSP PPATLHRNVS PGAPQRPPST GSASGMLSTT DLTVPNGAGN SPVGNGFVNS RASPNLIGNT GANSLGKVMP TKSPPPPGGG SLGMNSRKPD LRVVIPPSSK GMMPPLSEEE ELELNAQRIS SSQATQPLAT PVVSVTTPSL PPQGLVYSAM PTAYNTDYSL TSADLSALQG FTSPGMLSLG QASAWQQHHL GQAALSSLVA GGQLSQGSNL SINTNQNINI KSEPISPPRD RMTPSGFQQQ QQQPQQQPPP QPPQPQPRQE MGRSPVDSLS SSSSSYDGSD REDPRGDFHS PIVLGRPPNT EDRESPSVKR MRMDTWVT //