MEF2A_MOUSE
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 03-AUG-2022, entry version 182.
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 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}.
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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. [Q60929-1]
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; Q60929; -.
DR PeptideAtlas; Q60929; -.
DR PRIDE; Q60929; -.
DR ProteomicsDB; 295991; -. [Q60929-1]
DR ProteomicsDB; 295992; -. [Q60929-2]
DR ProteomicsDB; 295993; -. [Q60929-3]
DR Antibodypedia; 3854; 1075 antibodies from 44 providers.
DR Ensembl; ENSMUST00000032776; ENSMUSP00000032776; ENSMUSG00000030557. [Q60929-3]
DR Ensembl; ENSMUST00000076325; ENSMUSP00000075664; ENSMUSG00000030557. [Q60929-3]
DR Ensembl; ENSMUST00000107476; ENSMUSP00000103100; ENSMUSG00000030557. [Q60929-2]
DR Ensembl; ENSMUST00000135493; ENSMUSP00000138566; ENSMUSG00000030557. [Q60929-1]
DR Ensembl; ENSMUST00000156690; ENSMUSP00000117496; ENSMUSG00000030557. [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 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; 729387at2759; -.
DR PhylomeDB; Q60929; -.
DR TreeFam; TF314067; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 17258; 3 hits in 74 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 269 other tissues.
DR ExpressionAtlas; Q60929; baseline and differential.
DR Genevisible; Q60929; MM.
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: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: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:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; ISO: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; -; 1.
DR InterPro; IPR022102; HJURP_C.
DR InterPro; IPR033896; MADS_MEF2-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF12347; HJURP_C; 1.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
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
