ID JUNB_HUMAN Reviewed; 347 AA. AC P17275; Q96GH3; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 27-MAR-2024, entry version 229. DE RecName: Full=Transcription factor JunB {ECO:0000305}; DE AltName: Full=Transcription factor AP-1 subunit JunB {ECO:0000305}; GN Name=JUNB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2513129; DOI=10.1016/0092-8674(89)90755-1; RA Schuette J., Viallet J., Nau M., Segal S., Fedorko J., Minna J.; RT "jun-B inhibits and c-fos stimulates the transforming and trans-activating RT activities of c-jun."; RL Cell 59:987-997(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2112242; DOI=10.1093/nar/18.10.3047; RA Nomura N., Ide M., Sasamoto S., Matsui M., Date T., Ishizaki R.; RT "Isolation of human cDNA clones of jun-related genes, jun-B and jun-D."; RL Nucleic Acids Res. 18:3047-3048(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Placenta; RX PubMed=8530030; DOI=10.1006/geno.1995.1135; RA Phinney D.G., Tseng S.W., Ryder K.; RT "Complex genetic organization of junB: multiple blocks of flanking RT evolutionarily conserved sequence at the murine and human junB loci."; RL Genomics 28:228-234(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-230. RG NIEHS SNPs program; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 [6] RP INTERACTION WITH ITCH, AND UBIQUITINATION. RX PubMed=16387660; DOI=10.1016/j.molcel.2005.11.014; RA Yang C., Zhou W., Jeon M.S., Demydenko D., Harada Y., Zhou H., Liu Y.C.; RT "Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated RT tyrosine phosphorylation."; RL Mol. Cell 21:135-141(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102; THR-104 AND SER-117, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; THR-255 AND SER-259, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-117; SER-251 AND RP THR-255, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255 AND SER-259, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; THR-255 AND SER-259, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-33 AND LYS-240, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-36 AND LYS-240, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-33; LYS-36; LYS-81; RP LYS-141; LYS-240 AND LYS-343, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- FUNCTION: Transcription factor involved in regulating gene activity CC following the primary growth factor response. Binds to the DNA sequence CC 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the FOS family to CC form an AP-1 transcription complex, thereby enhancing its DNA binding CC activity to an AP-1 consensus sequence and its transcriptional activity CC (By similarity). {ECO:0000250|UniProtKB:P09450}. CC -!- SUBUNIT: Binds DNA as a homodimer or as a heterodimer with another CC member of the Jun/Fos family. Component of an AP-1 transcription factor CC complex composed of JUN-FOS heterodimers composed of JUN-FOS CC heterodimers (By similarity). As part of the AP-1 transcription factor CC complex, forms heterodimers with FOSB, thereby binding to the AP-1 CC consensus sequence and stimulating transcription (By similarity). CC Interacts with ITCH (via its WW domains). CC {ECO:0000250|UniProtKB:P09450, ECO:0000269|PubMed:16387660}. CC -!- INTERACTION: CC P17275; P15336: ATF2; NbExp=3; IntAct=EBI-748062, EBI-1170906; CC P17275; P18847: ATF3; NbExp=6; IntAct=EBI-748062, EBI-712767; CC P17275; P18848: ATF4; NbExp=3; IntAct=EBI-748062, EBI-492498; CC P17275; P17544: ATF7; NbExp=2; IntAct=EBI-748062, EBI-765623; CC P17275; Q16520: BATF; NbExp=32; IntAct=EBI-748062, EBI-749503; CC P17275; Q8N1L9: BATF2; NbExp=5; IntAct=EBI-748062, EBI-742695; CC P17275; Q9NR55: BATF3; NbExp=6; IntAct=EBI-748062, EBI-10312707; CC P17275; P28329-3: CHAT; NbExp=3; IntAct=EBI-748062, EBI-25837549; CC P17275; P35638: DDIT3; NbExp=2; IntAct=EBI-748062, EBI-742651; CC P17275; P22607: FGFR3; NbExp=3; IntAct=EBI-748062, EBI-348399; CC P17275; P01100: FOS; NbExp=13; IntAct=EBI-748062, EBI-852851; CC P17275; Q6FG41: FOS; NbExp=4; IntAct=EBI-748062, EBI-10198738; CC P17275; P53539: FOSB; NbExp=6; IntAct=EBI-748062, EBI-2806743; CC P17275; P15407: FOSL1; NbExp=9; IntAct=EBI-748062, EBI-744510; CC P17275; P15408: FOSL2; NbExp=8; IntAct=EBI-748062, EBI-3893419; CC P17275; Q8WYK2: JDP2; NbExp=3; IntAct=EBI-748062, EBI-1248415; CC P17275; P56279: TCL1A; NbExp=2; IntAct=EBI-748062, EBI-749995; CC P17275; Q86XI8: ZSWIM9; NbExp=2; IntAct=EBI-748062, EBI-2682158; CC P17275; P0C746: HBZ; Xeno; NbExp=2; IntAct=EBI-748062, EBI-10890294; CC P17275; Q9DGW5: MDV005; Xeno; NbExp=2; IntAct=EBI-748062, EBI-10889526; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- INDUCTION: By growth factors. CC -!- PTM: Ubiquitinated by ITCH, leading to its degradation. CC {ECO:0000269|PubMed:16387660}. CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/178/JUNB"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/junb/"; 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; M29039; AAA59198.1; -; Genomic_DNA. DR EMBL; X51345; CAA35738.1; -; mRNA. DR EMBL; U20734; AAA74915.1; -; Genomic_DNA. DR EMBL; AY751746; AAU43800.1; -; Genomic_DNA. DR EMBL; BC004250; AAH04250.1; -; mRNA. DR EMBL; BC009465; AAH09465.1; -; mRNA. DR EMBL; BC009466; AAH09466.1; -; mRNA. DR CCDS; CCDS12280.1; -. DR PIR; S10183; TVHUJB. DR RefSeq; NP_002220.1; NM_002229.2. DR AlphaFoldDB; P17275; -. DR SMR; P17275; -. DR BioGRID; 109929; 125. DR ComplexPortal; CPX-6421; bZIP transcription factor complex, ATF2-JUNB. DR ComplexPortal; CPX-6476; bZIP transcription factor complex, ATF3-JUNB. DR ComplexPortal; CPX-6563; bZIP transcription factor complex, ATF4-JUNB. DR ComplexPortal; CPX-6787; bZIP transcription factor complex, ATF7-JUNB. DR ComplexPortal; CPX-7003; bZIP transcription factor complex, BATF-JUNB. DR ComplexPortal; CPX-7061; bZIP transcription factor complex, BATF2-JUNB. DR ComplexPortal; CPX-7101; bZIP transcription factor complex, BATF3-JUNB. DR DIP; DIP-1052N; -. DR IntAct; P17275; 66. DR MINT; P17275; -. DR STRING; 9606.ENSP00000303315; -. DR GlyCosmos; P17275; 21 sites, 2 glycans. DR GlyGen; P17275; 22 sites, 2 O-linked glycans (22 sites). DR iPTMnet; P17275; -. DR PhosphoSitePlus; P17275; -. DR BioMuta; JUNB; -. DR DMDM; 135304; -. DR EPD; P17275; -. DR jPOST; P17275; -. DR MassIVE; P17275; -. DR PaxDb; 9606-ENSP00000303315; -. DR PeptideAtlas; P17275; -. DR ProteomicsDB; 53465; -. DR Pumba; P17275; -. DR Antibodypedia; 3847; 1015 antibodies from 45 providers. DR DNASU; 3726; -. DR Ensembl; ENST00000302754.6; ENSP00000303315.4; ENSG00000171223.6. DR GeneID; 3726; -. DR KEGG; hsa:3726; -. DR MANE-Select; ENST00000302754.6; ENSP00000303315.4; NM_002229.3; NP_002220.1. DR AGR; HGNC:6205; -. DR CTD; 3726; -. DR DisGeNET; 3726; -. DR GeneCards; JUNB; -. DR HGNC; HGNC:6205; JUNB. DR HPA; ENSG00000171223; Low tissue specificity. DR MIM; 165161; gene. DR neXtProt; NX_P17275; -. DR OpenTargets; ENSG00000171223; -. DR PharmGKB; PA30007; -. DR VEuPathDB; HostDB:ENSG00000171223; -. DR eggNOG; KOG0837; Eukaryota. DR GeneTree; ENSGT00940000161195; -. DR HOGENOM; CLU_057007_0_0_1; -. DR InParanoid; P17275; -. DR OMA; HFQHAAR; -. DR OrthoDB; 4493275at2759; -. DR PhylomeDB; P17275; -. DR PathwayCommons; P17275; -. DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-9031628; NGF-stimulated transcription. DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer. DR SignaLink; P17275; -. DR SIGNOR; P17275; -. DR BioGRID-ORCS; 3726; 125 hits in 1188 CRISPR screens. DR ChiTaRS; JUNB; human. DR GeneWiki; JUNB; -. DR GenomeRNAi; 3726; -. DR Pharos; P17275; Tbio. DR PRO; PR:P17275; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P17275; Protein. DR Bgee; ENSG00000171223; Expressed in mucosa of stomach and 201 other cell types or tissues. DR ExpressionAtlas; P17275; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal. DR GO; GO:0035976; C:transcription factor AP-1 complex; IDA:CAFA. DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl. DR GO; GO:0046697; P:decidualization; IEA:Ensembl. DR GO; GO:0060136; P:embryonic process involved in female pregnancy; IEA:Ensembl. DR GO; GO:0140467; P:integrated stress response signaling; NAS:ComplexPortal. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0033687; P:osteoblast proliferation; IEA:Ensembl. DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl. DR GO; GO:0002158; P:osteoclast proliferation; IEA:Ensembl. DR GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:CAFA. DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central. DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:2000319; P:regulation of T-helper 17 cell differentiation; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0001829; P:trophectodermal cell differentiation; IEA:Ensembl. DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl. DR CDD; cd14696; bZIP_Jun; 1. DR Gene3D; 1.20.5.170; -; 1. 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:SF37; TRANSCRIPTION FACTOR JUNB; 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. DR Genevisible; P17275; HS. PE 1: Evidence at protein level; KW Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..347 FT /note="Transcription factor JunB" FT /id="PRO_0000076438" FT DOMAIN 268..331 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 51..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 239..260 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 268..295 FT /note="Basic motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 296..324 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT MOD_RES 102 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 104 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 117 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 240 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09450" FT MOD_RES 251 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT MOD_RES 255 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT CROSSLNK 4 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 33 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 36 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 81 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 141 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 240 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 240 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 343 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 230 FT /note="L -> V (in dbSNP:rs17880705)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_021081" FT CONFLICT 124 FT /note="A -> G (in Ref. 5; AAH09465)" FT /evidence="ECO:0000305" SQ SEQUENCE 347 AA; 35879 MW; DF8CD1CD4409C6BE CRC64; MCTKMEQPFY HDDSYTATGY GRAPGGLSLH DYKLLKPSLA VNLADPYRSL KAPGARGPGP EGGGGGSYFS GQGSDTGASL KLASSELERL IVPNSNGVIT TTPTPPGQYF YPRGGGSGGG AGGAGGGVTE EQEGFADGFV KALDDLHKMN HVTPPNVSLG ATGGPPAGPG GVYAGPEPPP VYTNLSSYSP ASASSGGAGA AVGTGSSYPT TTISYLPHAP PFAGGHPAQL GLGRGASTFK EEPQTVPEAR SRDATPPVSP INMEDQERIK VERKRLRNRL AATKCRKRKL ERIARLEDKV KTLKAENAGL SSTAGLLREQ VAQLKQKVMT HVSNGCQLLL GVKGHAF //