MYC_RAT
ID MYC_RAT Reviewed; 439 AA.
AC P09416; Q6B500;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Myc proto-oncogene protein;
DE AltName: Full=Proto-oncogene c-Myc;
DE AltName: Full=Transcription factor p64;
GN Name=Myc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3306601; DOI=10.1093/nar/15.16.6419;
RA Hayashi K., Makino R., Kawamura H., Arisawa A., Yoneda K.;
RT "Characterization of rat c-myc and adjacent regions.";
RL Nucleic Acids Res. 15:6419-6436(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ACI/SegHsd, and Brown Norway/SsNHsd; TISSUE=Spleen;
RA Shull J.D., Buckles L.K.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 BIOTECHNOLOGY.
RX PubMed=20352099; DOI=10.1371/journal.pone.0009838;
RA Chang M.Y., Kim D., Kim C.H., Kang H.C., Yang E., Moon J.I., Ko S.,
RA Park J., Park K.S., Lee K.A., Hwang D.Y., Chung Y., Lanza R., Kim K.S.;
RT "Direct reprogramming of rat neural precursor cells and fibroblasts into
RT pluripotent stem cells.";
RL PLoS ONE 5:E9838-E9838(2010).
RN [5]
RP FUNCTION IN TRANSCRIPTIONAL ACTIVATION, AND INTERACTION WITH ABI1.
RX PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
RA Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
RA Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
RT "Abelson interacting protein 1 (Abi-1) is essential for dendrite
RT morphogenesis and synapse formation.";
RL EMBO J. 26:1397-1409(2007).
CC -!- FUNCTION: Transcription factor that binds DNA in a non-specific manner,
CC yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'.
CC Activates the transcription of growth-related genes (PubMed:17304222).
CC Binds to the VEGFA promoter, promoting VEGFA production and subsequent
CC sprouting angiogenesis (By similarity). Regulator of somatic
CC reprogramming, controls self-renewal of embryonic stem cells. Functions
CC with TAF6L to activate target gene expression through RNA polymerase II
CC pause release (By similarity). Positively regulates transcription of
CC HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate
CC kinase PKM by binding repressively to sequences flanking PKM exon 9,
CC inhibiting exon 9 inclusion and resulting in exon 10 inclusion and
CC production of the PKM M2 isoform (By similarity).
CC {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108,
CC ECO:0000269|PubMed:17304222}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX (By similarity). Interacts
CC with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and
CC KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7.
CC Interacts with PIM2. Interacts with RIOX1 (By similarity). The
CC heterodimer MYC:MAX interacts with ABI1; the interaction may enhance
CC MYC:MAX transcriptional activity (PubMed:17304222). Interacts with
CC TRIM6 (By similarity). Interacts with NPM1; the binary complex is
CC recruited to the promoter of MYC target genes and enhances their
CC transcription (By similarity). Interacts with CIP2A; leading to the
CC stabilization of MYC (By similarity). {ECO:0000250|UniProtKB:P01106,
CC ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:17304222}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P01106}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P01106}.
CC -!- PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-
CC 329 by PIM2 leads to the stabilization of MYC (By similarity).
CC Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence.
CC Phosphorylated at Ser-62 by DYRK2; this primes the protein for
CC subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-
CC 58 and Ser-62 by GSK3 is required for ubiquitination and degradation by
CC the proteasome. Dephosphorylation at Ser-62 by protein phosphatase 2A
CC (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced
CC by AMBRA1 (By similarity). {ECO:0000250|UniProtKB:P01106,
CC ECO:0000250|UniProtKB:P01108}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at
CC Thr-58 and Ser-62, leading to its degradation by the proteasome.
CC Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in
CC the nucleolus, both interacting with of FBXW7, leading to its
CC deubiquitination and preventing degradation. Also polyubiquitinated by
CC the DCX(TRPC4AP) complex. Ubiquitinated by TRIM6 in a phosphorylation-
CC independent manner. {ECO:0000250|UniProtKB:P01106,
CC ECO:0000250|UniProtKB:P01108}.
CC -!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four
CC Yamanaka factors. When combined, these factors are sufficient to
CC reprogram differentiated cells to an embryonic-like state designated
CC iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology
CC and growth properties of ES cells and express ES cell marker genes.
CC {ECO:0000269|PubMed:20352099}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH91699.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y00396; CAA68459.2; -; Genomic_DNA.
DR EMBL; AY679729; AAT92511.1; -; mRNA.
DR EMBL; AY679730; AAT92512.1; -; mRNA.
DR EMBL; BC091699; AAH91699.2; ALT_INIT; mRNA.
DR PIR; A26801; TVRTMC.
DR RefSeq; NP_036735.2; NM_012603.2.
DR PDB; 7LQT; NMR; -; A=13-30.
DR PDBsum; 7LQT; -.
DR AlphaFoldDB; P09416; -.
DR SMR; P09416; -.
DR BioGRID; 246723; 4.
DR CORUM; P09416; -.
DR DIP; DIP-28140N; -.
DR IntAct; P09416; 3.
DR MINT; P09416; -.
DR STRING; 10116.ENSRNOP00000006188; -.
DR ChEMBL; CHEMBL4105894; -.
DR GlyGen; P09416; 1 site.
DR iPTMnet; P09416; -.
DR PhosphoSitePlus; P09416; -.
DR PaxDb; P09416; -.
DR GeneID; 24577; -.
DR KEGG; rno:24577; -.
DR UCSC; RGD:3130; rat.
DR CTD; 4609; -.
DR RGD; 3130; Myc.
DR VEuPathDB; HostDB:ENSRNOG00000004500; -.
DR eggNOG; KOG2483; Eukaryota.
DR InParanoid; P09416; -.
DR OrthoDB; 877891at2759; -.
DR PhylomeDB; P09416; -.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR PRO; PR:P09416; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004500; Expressed in spleen and 19 other tissues.
DR ExpressionAtlas; P09416; baseline and differential.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0071943; C:Myc-Max complex; ISO:RGD.
DR GO; GO:0016604; C:nuclear body; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0044195; C:nucleoplasmic reticulum; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0006865; P:amino acid transport; IMP:RGD.
DR GO; GO:0001783; P:B cell apoptotic process; ISO:RGD.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0044337; P:canonical Wnt signaling pathway involved in positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; IMP:RGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
DR GO; GO:1903841; P:cellular response to arsenite(3-); IEP:RGD.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IEP:RGD.
DR GO; GO:0071409; P:cellular response to cycloheximide; IEP:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEP:RGD.
DR GO; GO:1904620; P:cellular response to dimethyl sulfoxide; IEP:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:1990859; P:cellular response to endothelin; IEP:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IEP:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0071378; P:cellular response to growth hormone stimulus; IEP:RGD.
DR GO; GO:0071464; P:cellular response to hydrostatic pressure; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:1990858; P:cellular response to lectin; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR GO; GO:1990646; P:cellular response to prolactin; IEP:RGD.
DR GO; GO:1904586; P:cellular response to putrescine; IEP:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD.
DR GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0051276; P:chromosome organization; ISS:UniProtKB.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISO:RGD.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0045023; P:G0 to G1 transition; IEP:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IMP:RGD.
DR GO; GO:0021854; P:hypothalamus development; IEP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; IEP:RGD.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0046722; P:lactic acid secretion; IMP:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0042474; P:middle ear morphogenesis; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0051782; P:negative regulation of cell division; ISS:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
DR GO; GO:0046325; P:negative regulation of glucose import; IMP:RGD.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0001866; P:NK T cell proliferation; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
DR GO; GO:0030728; P:ovulation; IEP:RGD.
DR GO; GO:0043473; P:pigmentation; ISO:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:RGD.
DR GO; GO:0002904; P:positive regulation of B cell apoptotic process; ISO:RGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:RGD.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IMP:RGD.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; IMP:RGD.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:1905643; P:positive regulation of DNA methylation; ISO:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IMP:RGD.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
DR GO; GO:0090096; P:positive regulation of metanephric cap mesenchymal cell proliferation; ISS:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:RGD.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IMP:RGD.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; ISO:RGD.
DR GO; GO:0032986; P:protein-DNA complex disassembly; ISO:RGD.
DR GO; GO:0006848; P:pyruvate transport; IMP:RGD.
DR GO; GO:0000320; P:re-entry into mitotic cell cycle; IMP:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0010564; P:regulation of cell cycle process; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:RGD.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IMP:RGD.
DR GO; GO:1904672; P:regulation of somatic stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISS:UniProtKB.
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:RGD.
DR GO; GO:0043279; P:response to alkaloid; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:RGD.
DR GO; GO:0019087; P:transformation of host cell by virus; IMP:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR003327; Myc-LZ.
DR InterPro; IPR002418; Tscrpt_reg_Myc.
DR InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF02344; Myc-LZ; 1.
DR Pfam; PF01056; Myc_N; 1.
DR PIRSF; PIRSF001705; Myc_protein; 1.
DR PRINTS; PR00044; LEUZIPPRMYC.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; DNA-binding; Glycoprotein;
KW Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..439
FT /note="Myc proto-oncogene protein"
FT /id="PRO_0000127300"
FT DOMAIN 354..406
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 202..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..434
FT /note="Leucine-zipper"
FT MOTIF 101..109
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT COMPBIAS 202..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 58
FT /note="Phosphothreonine; by GSK3; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 62
FT /note="Phosphoserine; by DYRK2, GSK3 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 144
FT /note="N6-acetyllysine; by PCAF; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 149
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 158
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 275
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 317
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 323
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT MOD_RES 329
FT /note="Phosphoserine; by PIM2; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P01108"
FT MOD_RES 371
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT CARBOHYD 58
FT /note="O-linked (GlcNAc) threonine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:7LQT"
SQ SEQUENCE 439 AA; 48898 MW; 7547DCCECF74554F CRC64;
MPLNVSFANR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW KKFELLPTPP
LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL EMMTELLGGD MVNQSFICDP
DDETFIKNII IQDCMWSGFS AAAKLVSEKL ASYQAARKDS TSLSPARGHS VCSTSSLYLQ
DLTAAASECI DPSVVFPYPL NDSSSPKSCT SSDSTAFSSS SDSLLSSESS PRATPEPLVL
HEETPPTTSS DSEEEQDDEE EIDVVSVEKR QPPAKRSESG SSPSRGHSKP PHSPLVLKRC
HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT EENDKRRTHN
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQADE HKLISEKDLL
RKRREQLKHK LEQLRNSGA
