JUN_RAT
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 03-AUG-2022, entry version 192.
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 DSIPI; this
CC interaction inhibits the binding of active AP1 to its target DNA.
CC Interacts with HIVEP3. Component of the SMAD3/SMAD4/JUN/FOS/complex
CC which forms at the AP1 promoter site. The SMAD3/SMAD4 heterodimer acts
CC synergistically with the JUN/FOS heterodimer to activate transcription
CC in response to TGF-beta. Interacts (via its basic DNA binding and
CC leucine zipper domains) with SMAD3 (via an N-terminal domain); the
CC interaction is required for TGF-beta-mediated transactivation of the
CC SMAD3/SMAD4/JUN/FOS/complex (By similarity). Component of an AP-1
CC transcription factor complex (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). Binds to HIPK3 (By similarity). Interacts with
CC methylated RNF187 (PubMed:20852630). Interacts (when phosphorylated)
CC with FBXW7 (By similarity). Interacts with PRR7 (PubMed:27458189).
CC Found in a complex with PRR7 and FBXW7 (By similarity). Interacts with
CC PRR7 and FBXW7; the interaction inhibits ubiquitination-mediated JUN
CC degradation promoting its phosphorylation and transcriptional activity
CC (By similarity). Interacts with RBM39 (By similarity). Interacts with
CC PAGE4 (By similarity). {ECO:0000250|UniProtKB:P05412,
CC ECO:0000250|UniProtKB:P05627, ECO:0000269|PubMed:20852630,
CC ECO:0000269|PubMed:27458189, 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).
CC {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}.
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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 IntAct; P17325; 3.
DR MINT; P17325; -.
DR STRING; 10116.ENSRNOP00000011732; -.
DR BindingDB; P17325; -.
DR ChEMBL; CHEMBL3341579; -.
DR iPTMnet; P17325; -.
DR PhosphoSitePlus; P17325; -.
DR PaxDb; P17325; -.
DR Ensembl; ENSRNOT00000011731; ENSRNOP00000011732; ENSRNOG00000026293.
DR GeneID; 24516; -.
DR KEGG; rno:24516; -.
DR UCSC; RGD:2943; rat.
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; 1090460at2759; -.
DR PhylomeDB; P17325; -.
DR TreeFam; TF323952; -.
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 PRO; PR:P17325; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000026293; Expressed in lung and 20 other tissues.
DR Genevisible; P17325; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO: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:0007568; P:aging; IEP:RGD.
DR GO; GO:0001525; P:angiogenesis; IMP:RGD.
DR GO; GO:0031103; P:axon regeneration; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0072740; P:cellular response to anisomycin; ISO:RGD.
DR GO; GO:0071276; P:cellular response to cadmium ion; 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:0051365; P:cellular response to potassium ion starvation; IMP:RGD.
DR GO; GO:1990646; P:cellular response to prolactin; IEP:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0061029; P:eyelid development in camera-type eye; 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:0043922; P:negative regulation by host of viral transcription; 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:0043392; P:negative regulation of DNA binding; 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:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; 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: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:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
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:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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:0042542; P:response to hydrogen peroxide; 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:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IDA: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:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR015558; C_Jun/v-Jun.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462:SF8; PTHR11462:SF8; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF03957; Jun; 1.
DR PRINTS; PR00043; LEUZIPPRJUN.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 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 203..217
FT /note="Pro residues"
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
