ID JUN_RAT Reviewed; 334 AA. AC P17325; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 02-SEP-2026, entry version 211. DE RecName: Full=Transcription factor Jun {ECO:0000305}; DE AltName: Full=Activator protein 1; DE Short=AP1; DE AltName: Full=Proto-oncogene c-Jun; DE AltName: Full=Transcription factor AP-1 subunit Jun {ECO:0000305}; DE AltName: Full=V-jun avian sarcoma virus 17 oncogene homolog; GN Name=Jun; Synonyms=Rjg-9; 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 [MRNA]. RC TISSUE=Liver; RX PubMed=2507134; RA Sakai M., Okuda A., Hatayama I., Sato K., Nishi S., Muramatsu M.; RT "Structure and expression of the rat c-jun messenger RNA: tissue RT distribution and increase during chemical hepatocarcinogenesis."; RL Cancer Res. 49:5633-5637(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Fischer; RX PubMed=2113275; DOI=10.1093/nar/18.11.3400; RA Kitabayashi I., Saka F., Gachelin G., Yokoyama K.; RT "Nucleotide sequence of rat c-jun protooncogene."; RL Nucleic Acids Res. 18:3400-3400(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Fischer; RX PubMed=1310930; DOI=10.1002/j.1460-2075.1992.tb05039.x; RA Kitabayashi I., Kawakami Z., Chiu R., Ozawa K., Matsuoka T., Toyoshima S., RA Umesono K., Evans R.M., Gachelin G., Yokoyama K.; RT "Transcriptional regulation of the c-jun gene by retinoic acid and E1A RT during differentiation of F9 cells."; RL EMBO J. 11:167-175(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [5] RP INTERACTION WITH BATF3. RX PubMed=9154808; DOI=10.1128/mcb.17.6.3094; RA Aronheim A., Zandi E., Hennemann H., Elledge S.J., Karin M.; RT "Isolation of an AP-1 repressor by a novel method for detecting protein- RT protein interactions."; RL Mol. Cell. Biol. 17:3094-3102(1997). RN [6] RP INTERACTION WITH RNF187. RX PubMed=20852630; DOI=10.1038/ncb2098; RA Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J., Behrens A.; RT "Identification of a co-activator that links growth factor signalling to c- RT Jun/AP-1 activation."; RL Nat. Cell Biol. 12:963-972(2010). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [8] RP INTERACTION WITH PRR7, AND UBIQUITINATION. RX PubMed=27458189; DOI=10.15252/embj.201593070; RA Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S., RA Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.; RT "Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and regulates RT NMDA-mediated excitotoxicity."; RL EMBO J. 35:1923-1934(2016). CC -!- FUNCTION: Transcription factor that recognizes and binds to the AP-1 CC consensus motif 5'-TGA[GC]TCA-3' (By similarity). Heterodimerizes with CC proteins of the FOS family to form an AP-1 transcription complex, CC thereby enhancing its DNA binding activity to the AP-1 consensus CC sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity CC (By similarity). Together with FOSB, plays a role in activation-induced CC cell death of T cells by binding to the AP-1 promoter site of CC FASLG/CD95L, and inducing its transcription in response to activation CC of the TCR/CD3 signaling pathway (By similarity). Promotes activity of CC NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic CC gene expression upon cAMP signaling pathway stimulation. Involved in CC activated KRAS-mediated transcriptional activation of USP28. Binds to CC the USP28 promoter (By similarity). {ECO:0000250|UniProtKB:P05412, CC ECO:0000250|UniProtKB:P05627}. CC -!- SUBUNIT: Heterodimer with either BATF3 or ATF7 (PubMed:9154808). CC Heterodimer with FOS (By similarity). Heterodimer with FOSB (By CC similarity). Component of an AP-1 transcription factor complex composed CC of JUN-FOS heterodimers (By similarity). As part of the AP-1 CC transcription factor complex, forms heterodimers with FOSB, thereby CC binding to the AP-1 consensus sequence and stimulating transcription CC (By similarity). Interacts with FOS and FOSB (By similarity). The CC ATF7/JUN heterodimer is essential for ATF7 transactivation activity. CC Interacts with MYBBP1A, SP1, SPIB and TCF20. Interacts with COPS5; CC indirectly leading to its phosphorylation. Interacts with TSC22D3 (via CC N-terminus); this interaction inhibits the binding of active AP1 to its CC target DNA. Interacts with HIVEP3. Component of the CC SMAD3/SMAD4/JUN/FOS/complex which forms at the AP1 promoter site. The CC SMAD3/SMAD4 heterodimer acts synergistically with the JUN/FOS CC heterodimer to activate transcription in response to TGF-beta. CC Interacts (via its basic DNA binding and leucine zipper domains) with CC SMAD3 (via an N-terminal domain); the interaction is required for TGF- CC beta-mediated transactivation of the SMAD3/SMAD4/JUN/FOS/complex (By CC similarity). Binds to HIPK3 (By similarity). Interacts with methylated CC RNF187 (PubMed:20852630). Interacts (when phosphorylated) with FBXW7 CC (By similarity). Interacts with PRR7 (PubMed:27458189). Found in a CC complex with PRR7 and FBXW7 (By similarity). Interacts with PRR7 and CC FBXW7; the interaction inhibits ubiquitination-mediated JUN degradation CC promoting its phosphorylation and transcriptional activity (By CC similarity). Interacts with RBM39 (By similarity). Interacts with PAGE4 CC (By similarity). Interacts with ARK2N and CSNK2B; the interaction with CC ARK2N is mediated by CSNK2B (By similarity). CC {ECO:0000250|UniProtKB:P05412, ECO:0000250|UniProtKB:P05627, CC ECO:0000269|PubMed:20852630, ECO:0000269|PubMed:27458189, CC ECO:0000269|PubMed:9154808}. CC -!- INTERACTION: CC P17325; P12841: Fos; NbExp=2; IntAct=EBI-7709365, EBI-8590661; CC P17325; P49185: Mapk8; NbExp=2; IntAct=EBI-7709365, EBI-7456505; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}. CC -!- PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the CC transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by CC DYRK2 at Ser-246; this primes the protein for subsequent CC phosphorylation by GSK3B at Thr-242. Phosphorylated at Thr-242, Ser-246 CC and Ser-252 by GSK3B; phosphorylation reduces its ability to bind DNA. CC Phosphorylated by PLK3 following hypoxia or UV irradiation, leading to CC increase DNA-binding activity (By similarity). Phosphorylated by VRK1 CC (By similarity). {ECO:0000250|UniProtKB:P05412}. CC -!- PTM: Ubiquitinated (PubMed:27458189). Ubiquitination by the SCF(FBXW7) CC is leading to its degradation (By similarity). Ubiquitination takes CC place following phosphorylation, that promotes interaction with FBXW7 CC (By similarity). {ECO:0000250|UniProtKB:P05412, CC ECO:0000269|PubMed:27458189}. CC -!- PTM: Acetylated at Lys-271 by EP300. {ECO:0000250|UniProtKB:P05412}. CC -!- SIMILARITY: Belongs to the bZIP family. Jun 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; X17163; CAA35041.1; -; mRNA. DR EMBL; X17215; CAA35084.1; -; Genomic_DNA. DR EMBL; BC078738; AAH78738.1; -; mRNA. DR PIR; S12742; S12742. DR RefSeq; NP_068607.1; NM_021835.3. DR AlphaFoldDB; P17325; -. DR SMR; P17325; -. DR BioGRID; 246671; 8. DR CORUM; P17325; -. DR DIP; DIP-653N; -. DR FunCoup; P17325; 2361. DR IntAct; P17325; 3. DR MINT; P17325; -. DR STRING; 10116.ENSRNOP00000011732; -. DR BindingDB; P17325; -. DR ChEMBL; CHEMBL3341579; -. DR GlyGen; P17325; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P17325; -. DR PhosphoSitePlus; P17325; -. DR PaxDb; 10116-ENSRNOP00000011732; -. DR Ensembl; ENSRNOT00000011731.5; ENSRNOP00000011732.1; ENSRNOG00000026293.4. DR Ensembl; ENSRNOT00000142314.1; ENSRNOP00000105928.1; ENSRNOG00000026293.4. DR Ensembl; ENSRNOT00055012148; ENSRNOP00055009646; ENSRNOG00055007293. DR Ensembl; ENSRNOT00060024157; ENSRNOP00060019273; ENSRNOG00060014128. DR Ensembl; ENSRNOT00065030925; ENSRNOP00065024633; ENSRNOG00065018436. DR GeneID; 24516; -. DR KEGG; rno:24516; -. DR UCSC; RGD:2943; rat. DR AGR; RGD:2943; -. DR CTD; 3725; -. DR RGD; 2943; Jun. DR eggNOG; KOG0837; Eukaryota. DR GeneTree; ENSGT00940000162061; -. DR HOGENOM; CLU_057007_0_0_1; -. DR InParanoid; P17325; -. DR OMA; HHQHMPA; -. DR OrthoDB; 2187714at2759; -. DR PhylomeDB; P17325; -. DR Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation. DR Reactome; R-RNO-450341; Activation of the AP-1 family of transcription factors. DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression. DR PRO; PR:P17325; -. DR Proteomes; UP000002494; Chromosome 5. DR Bgee; ENSRNOG00000026293; Expressed in lung and 20 other cell types or tissues. DR ExpressionAtlas; P17325; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:RGD. DR GO; GO:0000791; C:euchromatin; ISO:RGD. DR GO; GO:0005654; C:nucleoplasm; ISO:RGD. DR GO; GO:0005634; C:nucleus; IDA:RGD. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0035976; C:transcription factor AP-1 complex; ISO:RGD. DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD. DR GO; GO:0017053; C:transcription repressor complex; ISO:RGD. DR GO; GO:0035497; F:cAMP response element binding; ISO:RGD. DR GO; GO:0003682; F:chromatin binding; ISO:RGD. DR GO; GO:0003677; F:DNA binding; ISO:RGD. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:RGD. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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:0019899; F:enzyme binding; ISO:RGD. DR GO; GO:0140296; F:general transcription initiation factor binding; ISO:RGD. DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD. DR GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0042803; F:protein homodimerization activity; TAS:RGD. DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD. DR GO; GO:0070412; F:R-SMAD binding; ISO:RGD. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD. DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:RGD. DR GO; GO:0001525; P:angiogenesis; IMP:RGD. DR GO; GO:0031103; P:axon regeneration; ISO:RGD. DR GO; GO:0072740; P:cellular response to anisomycin; ISO:RGD. DR GO; GO:0071277; P:cellular response to calcium ion; ISO:RGD. DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD. DR GO; GO:0051365; P:cellular response to potassium ion starvation; IMP:RGD. DR GO; GO:1990646; P:cellular response to prolactin; IEP:RGD. DR GO; GO:0034224; P:cellular response to zinc ion starvation; IEP:RGD. DR GO; GO:0007623; P:circadian rhythm; IEP:RGD. DR GO; GO:0006351; P:DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0061029; P:eyelid development in camera-type eye; ISO:RGD. DR GO; GO:0006955; P:immune response; ISO:RGD. DR GO; GO:0007254; P:JNK cascade; ISO:RGD. DR GO; GO:0035026; P:leading edge cell differentiation; ISO:RGD. DR GO; GO:0007612; P:learning; IMP:RGD. DR GO; GO:0001889; P:liver development; ISO:RGD. DR GO; GO:0051899; P:membrane depolarization; IDA:RGD. DR GO; GO:0001774; P:microglial cell activation; ISO:RGD. DR GO; GO:0030224; P:monocyte differentiation; ISO:RGD. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD. DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD. DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IMP:RGD. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD. DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:2000144; P:positive regulation of DNA-templated transcription initiation; ISO:RGD. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD. DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL. DR GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:RGD. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD. DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD. DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0019046; P:release from viral latency; ISO:RGD. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:RGD. DR GO; GO:0051591; P:response to cAMP; IEP:RGD. DR GO; GO:0034097; P:response to cytokine; IEP:RGD. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD. DR GO; GO:0045471; P:response to ethanol; IEP:RGD. DR GO; GO:1904321; P:response to forskolin; IEP:RGD. DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD. DR GO; GO:0032868; P:response to insulin; IEP:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD. DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD. DR GO; GO:0035994; P:response to muscle stretch; ISO:RGD. DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD. DR GO; GO:0032905; P:transforming growth factor beta1 production; ISO:RGD. DR CDD; cd14696; bZIP_Jun; 1. DR FunFam; 1.20.5.170:FF:000012; Putative transcription factor AP-1; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR050946; AP-1_TF_bZIP. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR InterPro; IPR005643; JNK. DR InterPro; IPR002112; Leuzip_Jun. DR InterPro; IPR008917; TF_DNA-bd_sf. DR PANTHER; PTHR11462; JUN TRANSCRIPTION FACTOR-RELATED; 1. DR PANTHER; PTHR11462:SF8; TRANSCRIPTION FACTOR JUN; 1. DR Pfam; PF00170; bZIP_1; 1. DR Pfam; PF03957; Jun; 1. DR PRINTS; PR00043; LEUZIPPRJUN. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; DNA-binding; Isopeptide bond; Nucleus; KW Phosphoprotein; Proto-oncogene; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..334 FT /note="Transcription factor Jun" FT /id="PRO_0000076432" FT DOMAIN 255..318 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 150..226 FT /note="Interaction with PAGE4" FT /evidence="ECO:0000250|UniProtKB:P05412" FT REGION 184..217 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 255..282 FT /note="Basic motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 283..311 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT COMPBIAS 189..206 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 275 FT /note="Necessary for synergistic transcriptional activity FT with SMAD3" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 8 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 56 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05627" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 63 FT /note="Phosphoserine; by MAPK8 and PLK3" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 73 FT /note="Phosphoserine; by MAPK8 and PLK3" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 89 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 91 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 93 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 242 FT /note="Phosphothreonine; by GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 246 FT /note="Phosphoserine; by DYRK2 and GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 252 FT /note="Phosphoserine; by GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 274 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P05412" FT MOD_RES 289 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000250|UniProtKB:P05412" FT CROSSLNK 35 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P05412" FT CROSSLNK 50 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P05412" FT CROSSLNK 56 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P05412" FT CROSSLNK 70 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P05412" FT CROSSLNK 229 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P05412" SQ SEQUENCE 334 AA; 36001 MW; AFD9DF7D7C791B58 CRC64; MTAKMETTFY DDALNASFLQ SESGAYGYSN PKILKQSMTL NLADPVGNLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVSGA GMVAPAVASV AGAGGGGGYS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GATGLAFPSQ PQQQQQPPQP PHHLPQQIPV QHPRLQALKE EPQTVPEMPG ETPPLSPIDM ESQERIKAER KRMRNRIAAS KCRKRKLERI ARLEEKVKTL KAQNSELAST ANMLREQVAQ LKQKVMNHVN SGCQLMLTQQ LQTF //