TR150_MOUSE
ID TR150_MOUSE Reviewed; 951 AA.
AC Q569Z6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Thyroid hormone receptor-associated protein 3;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 150 kDa component;
DE Short=Trap150;
GN Name=Thrap3; Synonyms=Trap150;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-315; SER-320;
RP SER-379; SER-924 AND SER-935, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-679, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-572; SER-679;
RP SER-924 AND SER-935, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-248; SER-253;
RP SER-572 AND SER-679, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-238; SER-243;
RP SER-248; SER-253; SER-315; SER-320; THR-324; TYR-328; SER-379; SER-572;
RP SER-679; THR-870; SER-924 AND SER-935, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-346; LYS-452; LYS-468; LYS-476;
RP LYS-524 AND LYS-555, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP FUNCTION, INTERACTION WITH HELZ2 AND PPARG, AND SUBCELLULAR LOCATION.
RX PubMed=23525231; DOI=10.1210/me.2012-1332;
RA Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S.,
RA Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K.,
RA Okada S., Yamada M., Mori M.;
RT "THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
RT differentiation.";
RL Mol. Endocrinol. 27:769-780(2013).
RN [10]
RP FUNCTION, INTERACTION WITH CLOCK AND ARNTL, AND INDUCTION.
RX PubMed=24043798; DOI=10.1073/pnas.1305980110;
RA Lande-Diner L., Boyault C., Kim J.Y., Weitz C.J.;
RT "A positive feedback loop links circadian clock factor CLOCK-BMAL1 to the
RT basic transcriptional machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:16021-16026(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-101; ARG-108 AND ARG-841, 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).
CC -!- FUNCTION: Involved in pre-mRNA splicing. Remains associated with
CC spliced mRNA after splicing which probably involves interactions with
CC the exon junction complex (EJC). Can trigger mRNA decay which seems to
CC be independent of nonsense-mediated decay involving premature stop
CC codons (PTC) recognition. May be involved in nuclear mRNA decay.
CC Involved in regulation of signal-induced alternative splicing. During
CC splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ
CC from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-
CC D1/CCND1 mRNA stability probably by acting as component of the SNARP
CC complex which associates with both the 3'end of the CCND1 gene and its
CC mRNA. Involved in response to DNA damage. Is excluced from DNA damage
CC sites in a manner that parallels transcription inhibition; the function
CC may involve the SNARP complex. Initially thought to play a role in
CC transcriptional coactivation through its association with the TRAP
CC complex; however, it is not regarded as a stable Mediator complex
CC subunit. Cooperatively with HELZ2, enhances the transcriptional
CC activation mediated by PPARG, maybe through the stabilization of the
CC PPARG binding to DNA in presence of ligand. May play a role in the
CC terminal stage of adipocyte differentiation. Plays a role in the
CC positive regulation of the circadian clock. Acts as a coactivator of
CC the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional
CC activator activity and binding to circadian target genes
CC (PubMed:24043798). {ECO:0000269|PubMed:23525231,
CC ECO:0000269|PubMed:24043798}.
CC -!- SUBUNIT: Associated with the large multiprotein complex TRAP (Mediator
CC complex-like). Interacts with SFPQ; the interaction is dependent on
CC SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to an
CC ESS1 exonic splicing silencer element-containing RNA. Interacts with
CC NXF1. Component of the SNARP complex which consists at least of SNIP1,
CC SNW1, THRAP3, BCLAF1 and PNN. Associated with spliced mRNP complexes.
CC Interacts with HELZ2 and PPARG. Interacts with CLOCK and ARNTL/BMAL1
CC (By similarity). Component of a MACOM-like complex, named WTAP complex,
CC composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y2W1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23525231}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q9Y2W1}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9Y2W1}.
CC -!- INDUCTION: Expressed in a circadian manner in the liver with a peak at
CC approximately circadian time (CT) 8 hours (at protein level).
CC {ECO:0000269|PubMed:24043798}.
CC -!- SIMILARITY: Belongs to the BCLAF1/THRAP3 family. {ECO:0000305}.
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DR EMBL; BC092239; AAH92239.1; -; mRNA.
DR CCDS; CCDS18645.1; -.
DR RefSeq; NP_666265.3; NM_146153.3.
DR RefSeq; XP_006503104.1; XM_006503041.3.
DR RefSeq; XP_011238805.1; XM_011240503.2.
DR AlphaFoldDB; Q569Z6; -.
DR BioGRID; 231014; 15.
DR CORUM; Q569Z6; -.
DR IntAct; Q569Z6; 16.
DR MINT; Q569Z6; -.
DR STRING; 10090.ENSMUSP00000079722; -.
DR iPTMnet; Q569Z6; -.
DR PhosphoSitePlus; Q569Z6; -.
DR SwissPalm; Q569Z6; -.
DR EPD; Q569Z6; -.
DR jPOST; Q569Z6; -.
DR MaxQB; Q569Z6; -.
DR PaxDb; Q569Z6; -.
DR PeptideAtlas; Q569Z6; -.
DR PRIDE; Q569Z6; -.
DR ProteomicsDB; 258836; -.
DR DNASU; 230753; -.
DR Ensembl; ENSMUST00000080919; ENSMUSP00000079722; ENSMUSG00000043962.
DR GeneID; 230753; -.
DR KEGG; mmu:230753; -.
DR UCSC; uc008usv.1; mouse.
DR CTD; 9967; -.
DR MGI; MGI:2442637; Thrap3.
DR VEuPathDB; HostDB:ENSMUSG00000043962; -.
DR eggNOG; ENOG502QR38; Eukaryota.
DR GeneTree; ENSGT00950000183163; -.
DR HOGENOM; CLU_014485_1_0_1; -.
DR InParanoid; Q569Z6; -.
DR OMA; SHSYKVE; -.
DR OrthoDB; 380969at2759; -.
DR PhylomeDB; Q569Z6; -.
DR TreeFam; TF335939; -.
DR BioGRID-ORCS; 230753; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Thrap3; mouse.
DR PRO; PR:Q569Z6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q569Z6; protein.
DR Bgee; ENSMUSG00000043962; Expressed in embryonic post-anal tail and 256 other tissues.
DR ExpressionAtlas; Q569Z6; baseline and differential.
DR Genevisible; Q569Z6; MM.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IC:MGI.
DR InterPro; IPR026667; THRAP3.
DR InterPro; IPR029199; THRAP3_BCLAF1.
DR PANTHER; PTHR15268; PTHR15268; 1.
DR PANTHER; PTHR15268:SF16; PTHR15268:SF16; 1.
DR Pfam; PF15440; THRAP3_BCLAF1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ATP-binding; Biological rhythms; Isopeptide bond;
KW Methylation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CHAIN 2..951
FT /note="Thyroid hormone receptor-associated protein 3"
FT /id="PRO_0000235980"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..190
FT /note="Required for mRNA splicing activation"
FT /evidence="ECO:0000250"
FT REGION 117..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..951
FT /note="Required for mRNA decay activity"
FT /evidence="ECO:0000250"
FT REGION 660..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..49
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..139
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 549..556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 17
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 66
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 101
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 108
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 221
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 328
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 346
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 452
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 468
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 476
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 516
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 524
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 555
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 808
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT MOD_RES 841
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M7V8"
FT MOD_RES 870
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 333
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 386
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 398
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 448
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 448
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 468
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 524
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 599
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 694
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 702
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 706
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 708
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 753
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 756
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 872
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
FT CROSSLNK 875
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2W1"
SQ SEQUENCE 951 AA; 108178 MW; 40DF483027363B4E CRC64;
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSVSRS RKRRLSSRSR SRSYSPAHNR
ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP
RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RSSSNHSRVE SSKRKSTKEK
KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDIKGSESS KPWPDATTYG AGSASRASVS
DLSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSNA SQMGSSMSGG AGYQSGAHQG
QFDHGSGSLS PSKKSPVGKS PPATGSAYGS SQKEESAASG GAAYSKRYLE EQKTENGKDK
EQKQTNADKE KLKEKGGFSD ADVKMKSDPF APKTDSEKPF RGSQSPKRYK LRDDFEKKMA
DFHKEELDEH DKDKSKGRKE PEFDDEPKFM SKVIAGASKN QEEEKSGKWE SLHTGKEKQR
KAEEMEDEPF TERSRKEERG GSKRSESGHR GFVPEKNFRV TAYKAVQEKS SSPPPRKTSE
SRDKLGSKGD FSSGKSSFSI TREAQVNVRM DSFDEDLARP SGLLAQERKL CRDLVHSNKK
EQEFRSIFQH IQSAQSQRSP SELFAQHIVT IVHHVKEHHF GSSGMTLHER FTKYLKRGNE
QEAAKNKKSP EIHRRIDISP STFRKHGLTH EELKSPREPG YKAEGKYKDD PVDLRLDIER
RKKHKERDLK RGKSRESVDS RDSSHSRERS TEKTEKTHKG SKKQKKHRRA RDRSRSSSSS
SQSSHSYKAE EYPEEAEERE ESTSGFDKSR LGTKDFVGPN ERGGRARGTF QFRARGRGWG
RGNYSGNNNN NSNNDFQKRS REEEWDPEYT PKSKKYYLHD DREGEGSDKW MGRGRGRGAF
PRGRGRFMFR KSSTSPKWAH DKFSGEEGEI EDDESGTENR EEKDSLQPSA E
