ID GPS2_MOUSE Reviewed; 327 AA. AC Q921N8; DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 136. DE RecName: Full=G protein pathway suppressor 2 {ECO:0000303|PubMed:22424771}; DE Short=GPS-2 {ECO:0000303|PubMed:22424771}; GN Name=Gps2 {ECO:0000303|PubMed:22424771, ECO:0000312|MGI:MGI:1891751}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; 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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RFX4. RX PubMed=18218630; DOI=10.1074/jbc.m708209200; RA Zhang D., Harry G.J., Blackshear P.J., Zeldin D.C.; RT "G-protein pathway suppressor 2 (GPS2) interacts with the regulatory factor RT X4 variant 3 (RFX4_v3) and functions as a transcriptional co-activator."; RL J. Biol. Chem. 283:8580-8590(2008). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2N; TRAF1; TRAF2 RP AND TRAF6. RX PubMed=22424771; DOI=10.1016/j.molcel.2012.01.025; RA Cardamone M.D., Krones A., Tanasa B., Taylor H., Ricci L., Ohgi K.A., RA Glass C.K., Rosenfeld M.G., Perissi V.; RT "A protective strategy against hyperinflammatory responses requiring the RT nontranscriptional actions of GPS2."; RL Mol. Cell 46:91-104(2012). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22666460; DOI=10.1371/journal.pone.0038130; RA Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A., Pastan I.; RT "ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA regulate RT adipogenesis in 3T3-L1 cells."; RL PLoS ONE 7:E38130-E38130(2012). RN [7] RP FUNCTION. RX PubMed=24953653; DOI=10.1016/j.celrep.2014.05.041; RA Cardamone M.D., Tanasa B., Chan M., Cederquist C.T., Andricovich J., RA Rosenfeld M.G., Perissi V.; RT "GPS2/KDM4A pioneering activity regulates promoter-specific recruitment of RT PPARgamma."; RL Cell Rep. 8:163-176(2014). RN [8] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-312 AND ARG-323, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [9] RP FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION IN THE N-COR COMPLEX, AND RP INTERACTION WITH PPARG. RX PubMed=25519902; DOI=10.1074/jbc.m114.598797; RA Guo C., Li Y., Gow C.H., Wong M., Zha J., Yan C., Liu H., Wang Y., RA Burris T.P., Zhang J.; RT "The optimal corepressor function of nuclear receptor corepressor (NCoR) RT for peroxisome proliferator-activated receptor gamma requires G protein RT pathway suppressor 2."; RL J. Biol. Chem. 290:3666-3679(2015). RN [10] RP SUBCELLULAR LOCATION, INTERACTION WITH TBL1X, METHYLATION AT ARG-312 AND RP ARG-323, SUMOYLATION AT LYS-45 AND LYS-71, UBIQUITINATION, AND MUTAGENESIS RP OF LYS-45; 52-LYS-LYS-53; LYS-71; LYS-254; LYS-300; ARG-312; ARG-323 AND RP LYS-327. RX PubMed=26070566; DOI=10.1074/jbc.m115.637660; RA Huang J., Cardamone M.D., Johnson H.E., Neault M., Chan M., Floyd Z.E., RA Mallette F.A., Perissi V.; RT "Exchange factor TBL1 and arginine methyltransferase PRMT6 cooperate in RT protecting G protein pathway suppressor 2 (GPS2) from proteasomal RT degradation."; RL J. Biol. Chem. 290:19044-19054(2015). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=27270589; DOI=10.1038/nm.4114; RA Fan R., Toubal A., Goni S., Drareni K., Huang Z., Alzaid F., Ballaire R., RA Ancel P., Liang N., Damdimopoulos A., Hainault I., Soprani A., RA Aron-Wisnewsky J., Foufelle F., Lawrence T., Gautier J.F., Venteclef N., RA Treuter E.; RT "Loss of the co-repressor GPS2 sensitizes macrophage activation upon RT metabolic stress induced by obesity and type 2 diabetes."; RL Nat. Med. 22:780-791(2016). RN [12] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=28039360; DOI=10.1074/jbc.m116.755132; RA Lentucci C., Belkina A.C., Cederquist C.T., Chan M., Johnson H.E., RA Prasad S., Lopacinski A., Nikolajczyk B.S., Monti S., Snyder-Cappione J., RA Tanasa B., Cardamone M.D., Perissi V.; RT "Inhibition of Ubc13-mediated ubiquitination by GPS2 regulates multiple RT stages of B Cell development."; RL J. Biol. Chem. 292:2754-2772(2017). RN [13] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=28123943; DOI=10.1016/j.molmet.2016.10.007; RA Cederquist C.T., Lentucci C., Martinez-Calejman C., Hayashi V., Orofino J., RA Guertin D., Fried S.K., Lee M.J., Cardamone M.D., Perissi V.; RT "Systemic insulin sensitivity is regulated by GPS2 inhibition of AKT RT ubiquitination and activation in adipose tissue."; RL Mol. Metab. 6:125-137(2017). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-45 AND LYS-71, AND RP MUTAGENESIS OF LYS-45 AND LYS-71. RX PubMed=29499132; DOI=10.1016/j.molcel.2018.01.037; RA Cardamone M.D., Tanasa B., Cederquist C.T., Huang J., Mahdaviani K., Li W., RA Rosenfeld M.G., Liesa M., Perissi V.; RT "Mitochondrial retrograde signaling in mammals is mediated by the RT transcriptional cofactor GPS2 via direct mitochondria-to-nucleus RT translocation."; RL Mol. Cell 69:757-772(2018). CC -!- FUNCTION: Key regulator of inflammation, lipid metabolism and CC mitochondrion homeostasis that acts by inhibiting the activity of the CC ubiquitin-conjugating enzyme UBE2N/Ubc13, thereby inhibiting 'Lys-63'- CC linked ubiquitination (PubMed:22424771, PubMed:24953653, CC PubMed:28039360, PubMed:28123943, PubMed:29499132). In the nucleus, can CC both acts as a corepressor and coactivator of transcription, depending CC on the context (PubMed:18218630, PubMed:24953653, PubMed:25519902, CC PubMed:27270589, PubMed:28039360). Acts as a transcription coactivator CC in adipocytes by promoting the recruitment of PPARG to promoters: acts CC by inhibiting the activity of the ubiquitin-conjugating enzyme CC UBE2N/Ubc13, leading to stabilization of KDM4A and subsequent histone CC H3 'Lys-9' (H3K9) demethylation (PubMed:22666460, PubMed:24953653). CC Promotes cholesterol efflux by acting as a transcription coactivator CC (By similarity). Acts as a regulator of B-cell development by CC inhibiting UBE2N/Ubc13, thereby restricting the activation of Toll-like CC receptors (TLRs) and B-cell antigen receptors (BCRs) signaling pathways CC (PubMed:28039360). Acts as a key mediator of mitochondrial stress CC response: in response to mitochondrial depolarization, relocates from CC the mitochondria to the nucleus following desumoylation and CC specifically promotes expression of nuclear-encoded mitochondrial genes CC (PubMed:29499132). Promotes transcription of nuclear-encoded CC mitochondrial genes by inhibiting UBE2N/Ubc13 (PubMed:29499132). Can CC also act as a corepressor as part of the N-Cor repressor complex by CC repressing active PPARG (PubMed:25519902). Plays an anti-inflammatory CC role in macrophages and is required for insulin sensitivity by acting CC as a corepressor (PubMed:27270589). Plays an anti-inflammatory role CC during the hepatic acute phase response by interacting with sumoylated CC NR1H2 and NR5A2 proteins, thereby preventing N-Cor corepressor complex CC dissociation (By similarity). In the cytosol, also plays a non- CC transcriptional role by regulating insulin signaling and pro- CC inflammatory pathways (PubMed:22424771, PubMed:28123943). In the CC cytoplasm, acts as a negative regulator of inflammation by inhibiting CC the pro-inflammatory TNF-alpha pathway; acts by repressing UBE2N/Ubc13 CC activity (PubMed:22424771). In the cytoplasm of adipocytes, restricts CC the activation of insulin signaling via inhibition of UBE2N/Ubc13- CC mediated ubiquitination of AKT (PubMed:28123943). Able to suppress G- CC protein- and mitogen-activated protein kinase-mediated signal CC transduction (By similarity). {ECO:0000250|UniProtKB:Q13227, CC ECO:0000269|PubMed:18218630, ECO:0000269|PubMed:22424771, CC ECO:0000269|PubMed:22666460, ECO:0000269|PubMed:24953653, CC ECO:0000269|PubMed:25519902, ECO:0000269|PubMed:27270589, CC ECO:0000269|PubMed:28039360, ECO:0000269|PubMed:28123943, CC ECO:0000269|PubMed:29499132}. CC -!- SUBUNIT: Component of the N-Cor repressor complex, at least composed of CC NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2 (PubMed:25519902). CC Interacts (when sumoylated at Lys-71) with TBL1X; leading to protect CC GPS2 from degradation by the proteasome (PubMed:26070566). Interacts CC with UBE2N; leading to inhibit UBE2N/Ubc13 activity (PubMed:22424771). CC Interacts with TRAF1 (PubMed:22424771). Interacts with TRAF2 CC (PubMed:22424771). Interacts with TRAF6 (PubMed:22424771). Interacts CC with PPARG (when in the liganded conformation) (PubMed:25519902). CC Interacts with (sumoylated) NR1H2; interaction with sumoylated NR1H2 CC and NR5A2 onto hepatic acute phase protein promoters prevents N-Cor CC corepressor complex dissociation (By similarity). Interacts with CC (sumoylated) NR5A2; interaction with sumoylated NR1H2 and NR5A2 onto CC hepatic acute phase protein promoters prevents N-Cor corepressor CC complex dissociation (By similarity). Interacts with NR1H3 (By CC similarity). Interacts with RFX4 (PubMed:18218630). Interacts with CC ANKRD26 (By similarity). {ECO:0000250|UniProtKB:Q13227, CC ECO:0000269|PubMed:18218630, ECO:0000269|PubMed:22424771, CC ECO:0000269|PubMed:25519902, ECO:0000269|PubMed:26070566}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18218630, CC ECO:0000269|PubMed:22424771, ECO:0000269|PubMed:22666460, CC ECO:0000269|PubMed:26070566, ECO:0000269|PubMed:29499132}. CC Mitochondrion {ECO:0000269|PubMed:29499132}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:22424771}. Note=Sumoylation regulates the CC subcellular location (PubMed:29499132). Relocates from the mitochondria CC to the nucleus following desumoylation, leading to mediate CC mitochondrial stress response (PubMed:29499132). CC {ECO:0000250|UniProtKB:Q13227, ECO:0000269|PubMed:29499132}. CC -!- PTM: Sumoylation regulates its subcellular location (PubMed:26070566, CC PubMed:29499132). Sumoylation at Lys-45 and Lys-71 regulates the CC shuttling between the cytoplasm and the nucleus (By similarity). CC Sumoylation at Lys-71 is required for interaction with TBL1X CC (PubMed:26070566). Sumoylated at Lys-45 and Lys-71 in mitochondrion CC (PubMed:29499132). Desumoylation by SENP1 leads to relocation from the CC mitochondria to the nucleus (PubMed:29499132). CC {ECO:0000250|UniProtKB:Q13227, ECO:0000269|PubMed:26070566, CC ECO:0000269|PubMed:29499132}. CC -!- PTM: Ubiquitinated at the C-terminus by SIAH2; leading to its CC degradation by the proteasome. Interaction with TBL1X and methylation CC at Arg-323 protect GPS2 against ubiquitination and degradation. CC {ECO:0000269|PubMed:26070566}. CC -!- PTM: Methylated at Arg-312 and Arg-323 by PRMT6. Methylation at Arg-323 CC protects from degradation by the proteasome. CC {ECO:0000269|PubMed:26070566}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethality (PubMed:25519902). Embryonic CC fibroblast cells show reduced corepressor function of the N-CoR complex CC for PPARG, leading to constitutive activation of PPARG target genes and CC spontaneous adipogenesis of the cells (PubMed:25519902). Conditional CC knockout mice lacking Gps2 in B-cells show developmental defects at CC multiple stages of B-cell differentiation, caused by of aberrant CC activation of 'Lys-63'-linked ubiquitination events and altered gene CC expression programs downstream of the misregulated signaling pathways CC (PubMed:28039360). Conditional knockout mice lacking Gps2 in CC macrophages show inappropriate corepressor complex function, leading to CC enhancer activation, pro-inflammatory gene expression and CC hypersensitivity toward metabolic-stress signals (PubMed:27270589). CC Conditional knockout mice lacking Gps2 in adipose tissues show obesity CC associated with constitutive insulin signaling, increased lipid CC deposition in the white adipose tissue and improved systemic insulin CC sensitivity (PubMed:28123943). Conditional knockout mice lacking Gps2 CC in adipose tissues display reduced mitochondrial content in brown CC adipose tissue (PubMed:29499132). {ECO:0000269|PubMed:25519902, CC ECO:0000269|PubMed:27270589, ECO:0000269|PubMed:28039360, CC ECO:0000269|PubMed:28123943, ECO:0000269|PubMed:29499132}. 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; AL596185; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466596; EDL12472.1; -; Genomic_DNA. DR EMBL; CH466596; EDL12474.1; -; Genomic_DNA. DR EMBL; BC011317; AAH11317.1; -; mRNA. DR EMBL; BC138879; AAI38880.1; -; mRNA. DR EMBL; BC138880; AAI38881.1; -; mRNA. DR CCDS; CCDS24922.1; -. DR RefSeq; NP_062700.2; NM_019726.3. DR RefSeq; XP_006533850.1; XM_006533787.2. DR AlphaFoldDB; Q921N8; -. DR SMR; Q921N8; -. DR CORUM; Q921N8; -. DR STRING; 10090.ENSMUSP00000072389; -. DR iPTMnet; Q921N8; -. DR PhosphoSitePlus; Q921N8; -. DR EPD; Q921N8; -. DR MaxQB; Q921N8; -. DR PaxDb; 10090-ENSMUSP00000054072; -. DR PeptideAtlas; Q921N8; -. DR ProteomicsDB; 271073; -. DR Pumba; Q921N8; -. DR Antibodypedia; 11906; 248 antibodies from 26 providers. DR DNASU; 56310; -. DR Ensembl; ENSMUST00000057884.6; ENSMUSP00000054072.6; ENSMUSG00000023170.15. DR Ensembl; ENSMUST00000072581.9; ENSMUSP00000072389.3; ENSMUSG00000023170.15. DR Ensembl; ENSMUST00000116358.8; ENSMUSP00000112062.2; ENSMUSG00000023170.15. DR GeneID; 56310; -. DR KEGG; mmu:56310; -. DR UCSC; uc007jsp.1; mouse. DR AGR; MGI:1891751; -. DR CTD; 2874; -. DR MGI; MGI:1891751; Gps2. DR VEuPathDB; HostDB:ENSMUSG00000023170; -. DR eggNOG; ENOG502RFJB; Eukaryota. DR GeneTree; ENSGT00390000004049; -. DR HOGENOM; CLU_081471_0_0_1; -. DR InParanoid; Q921N8; -. DR OMA; INMQGSP; -. DR OrthoDB; 3237195at2759; -. DR PhylomeDB; Q921N8; -. DR TreeFam; TF329067; -. DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux. DR BioGRID-ORCS; 56310; 12 hits in 80 CRISPR screens. DR ChiTaRS; Gps2; mouse. DR PRO; PR:Q921N8; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q921N8; Protein. DR Bgee; ENSMUSG00000023170; Expressed in retinal neural layer and 228 other cell types or tissues. DR ExpressionAtlas; Q921N8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central. DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB. DR GO; GO:0030332; F:cyclin binding; ISO:MGI. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB. DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB. DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB. DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB. DR GO; GO:1900045; P:negative regulation of protein K63-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB. DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0045598; P:regulation of fat cell differentiation; IDA:UniProtKB. DR GO; GO:0019216; P:regulation of lipid metabolic process; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0098780; P:response to mitochondrial depolarisation; IDA:UniProtKB. DR CDD; cd22249; UDM1_RNF168_RNF169-like; 1. DR InterPro; IPR026094; GPS2. DR PANTHER; PTHR22654; G PROTEIN PATHWAY SUPPRESSOR 2; 1. DR PANTHER; PTHR22654:SF2; G PROTEIN PATHWAY SUPPRESSOR 2; 1. DR Pfam; PF15991; G_path_suppress; 1. PE 1: Evidence at protein level; KW Activator; Coiled coil; Cytoplasm; Isopeptide bond; Methylation; KW Mitochondrion; Nucleus; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..327 FT /note="G protein pathway suppressor 2" FT /id="PRO_0000441803" FT REGION 26..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 61..94 FT /note="interaction with SUMO" FT /evidence="ECO:0000250|UniProtKB:Q13227" FT REGION 178..208 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 253..285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 300..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 14..109 FT /evidence="ECO:0000255" FT COMPBIAS 253..273 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..315 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 312 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000269|PubMed:26070566, FT ECO:0007744|PubMed:24129315" FT MOD_RES 323 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000269|PubMed:26070566, FT ECO:0007744|PubMed:24129315" FT MOD_RES 323 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q13227" FT CROSSLNK 45 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:26070566, FT ECO:0000269|PubMed:29499132" FT CROSSLNK 71 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:26070566, FT ECO:0000269|PubMed:29499132" FT MUTAGEN 45 FT /note="K->R: Decreased stability of the protein, probably FT due inability to interact with TBL1X; when associated with FT R-71. Abolishes sumoylation; when associated with R-71." FT /evidence="ECO:0000269|PubMed:29499132" FT MUTAGEN 52..53 FT /note="KK->AA: Does not affect localization to the FT nucleus." FT /evidence="ECO:0000269|PubMed:26070566" FT MUTAGEN 71 FT /note="K->R: Decreased stability of the protein, probably FT due inability to interact with TBL1X; when associated with FT R-45. Abolishes sumoylation; when associated with R-45." FT /evidence="ECO:0000269|PubMed:26070566, FT ECO:0000269|PubMed:29499132" FT MUTAGEN 254 FT /note="K->A: Increased stability due to impaired FT ubiquitination; when associated with A-300 and A-327." FT /evidence="ECO:0000269|PubMed:26070566" FT MUTAGEN 300 FT /note="K->A: Increased stability due to impaired FT ubiquitination; when associated with A-254 and A-327." FT /evidence="ECO:0000269|PubMed:26070566" FT MUTAGEN 312 FT /note="R->A: Abolished methylation; when associated with FT A-323." FT /evidence="ECO:0000269|PubMed:26070566" FT MUTAGEN 323 FT /note="R->A: Promotes ubiquitination and degradation by the FT proteasome. Abolished methylation; when associated with FT A-312." FT /evidence="ECO:0000269|PubMed:26070566" FT MUTAGEN 327 FT /note="K->A: Increased stability due to impaired FT ubiquitination; when associated with A-254 and A-300." FT /evidence="ECO:0000269|PubMed:26070566" SQ SEQUENCE 327 AA; 36738 MW; 3008661CE6579F4B CRC64; MPALLERPKL SNAMARALHR HIMMERERKR QEEEEVDKMM EQKMKEEQER RKKKEMEERM SLEETKEQIL KLQEKLSALQ EEKHQLFLQL KKVLHEEEKR RRKEQSDLTT LTSAAYQQSL TVHTGTHLLS MQGSPGGHNR PGTLMAADRA KQMFGPQVLT TRHYVGSAAA FAGTPEHGQF QGSPGGAYGT AQPPPHYGPT QPAYSPSQQL RAPSAFPAVQ YLSQPQPQPY AVHGHFQPTQ TGFLQPGSTL SLQKQMEHAN QQTSFSDSSS LRPMHPQALH PAPGLLASPQ LPVQIQAAGK SGFATTSQPG PRLPFIQHSQ NPRFYHK //