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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
 
 
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