JUNB_HUMAN
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 03-AUG-2022, entry version 220.
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="http://atlasgeneticsoncology.org/Genes/JUNBID178.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/junb/";
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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; 115.
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; 65.
DR MINT; P17275; -.
DR STRING; 9606.ENSP00000303315; -.
DR GlyGen; P17275; 21 sites, 2 O-linked glycans (21 sites).
DR iPTMnet; P17275; -.
DR PhosphoSitePlus; P17275; -.
DR BioMuta; JUNB; -.
DR DMDM; 135304; -.
DR EPD; P17275; -.
DR jPOST; P17275; -.
DR MassIVE; P17275; -.
DR PaxDb; P17275; -.
DR PeptideAtlas; P17275; -.
DR PRIDE; P17275; -.
DR ProteomicsDB; 53465; -.
DR Antibodypedia; 3847; 925 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 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; PTPAHYL; -.
DR OrthoDB; 1090460at2759; -.
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; 121 hits in 1112 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 199 other tissues.
DR ExpressionAtlas; P17275; baseline and differential.
DR Genevisible; P17275; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC: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; IC: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; IC: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 InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR029822; JunB.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462:SF37; PTHR11462:SF37; 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; 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
