GPS2_MOUSE
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 03-AUG-2022, entry version 128.
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}.
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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.ENSMUSP00000054072; -.
DR iPTMnet; Q921N8; -.
DR PhosphoSitePlus; Q921N8; -.
DR EPD; Q921N8; -.
DR MaxQB; Q921N8; -.
DR PaxDb; Q921N8; -.
DR PeptideAtlas; Q921N8; -.
DR PRIDE; Q921N8; -.
DR ProteomicsDB; 271073; -.
DR Antibodypedia; 11906; 222 antibodies from 26 providers.
DR DNASU; 56310; -.
DR Ensembl; ENSMUST00000057884; ENSMUSP00000054072; ENSMUSG00000023170.
DR Ensembl; ENSMUST00000072581; ENSMUSP00000072389; ENSMUSG00000023170.
DR Ensembl; ENSMUST00000116358; ENSMUSP00000112062; ENSMUSG00000023170.
DR GeneID; 56310; -.
DR KEGG; mmu:56310; -.
DR UCSC; uc007jsp.1; mouse.
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; QIEHANQ; -.
DR OrthoDB; 1206280at2759; -.
DR PhylomeDB; Q921N8; -.
DR TreeFam; TF329067; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR BioGRID-ORCS; 56310; 12 hits in 75 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 225 other 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 InterPro; IPR026094; GPS2.
DR PANTHER; PTHR22654; PTHR22654; 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 A-
FT 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 A-
FT 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
