PRC2C_MOUSE
ID PRC2C_MOUSE Reviewed; 2846 AA.
AC Q3TLH4; E9QKG5; Q05CS4; Q05DM5; Q3TKF3; Q3UXU5; Q4FZE4; Q66K03; Q6P3F4;
AC Q80TK3; Q80YR0; Q8BMJ4; Q8C1K7; Q8CGH3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein PRRC2C;
DE AltName: Full=BAT2 domain-containing protein 1;
DE AltName: Full=HLA-B-associated transcript 2-like 2;
DE AltName: Full=Proline-rich and coiled-coil-containing protein 2C;
GN Name=Prrc2c; Synonyms=Bat2d, Bat2d1, Bat2l2, Kiaa1096;
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 MRNA] OF 1-1105 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, Mammary gland, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-591 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1285-1687, AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 2540-2811 (ISOFORM 5).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Embryo, Jaw, Limb, Lung, Mammary tumor, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 906-2074.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2625, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-853 AND THR-2625,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2625, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-904; THR-1238;
RP SER-1935; SER-1938 AND THR-2625, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-243; ARG-280; ARG-282; ARG-2766
RP AND ARG-2775, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Required for efficient formation of stress granules.
CC {ECO:0000250|UniProtKB:Q9Y520}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9Y520}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TLH4-1; Sequence=Displayed;
CC Name=5;
CC IsoId=Q3TLH4-5; Sequence=VSP_035255;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06723.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH21412.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH37745.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH80672.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH99612.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC25414.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC65723.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE22468.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AC118643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK013732; BAC25414.1; ALT_FRAME; mRNA.
DR EMBL; AK030766; BAC27127.1; -; mRNA.
DR EMBL; AK135245; BAE22468.1; ALT_SEQ; mRNA.
DR EMBL; AK166509; BAE38818.1; -; mRNA.
DR EMBL; AK167018; BAE39192.1; -; mRNA.
DR EMBL; BC006723; AAH06723.1; ALT_SEQ; mRNA.
DR EMBL; BC021412; AAH21412.1; ALT_SEQ; mRNA.
DR EMBL; BC037745; AAH37745.1; ALT_SEQ; mRNA.
DR EMBL; BC050871; AAH50871.1; -; mRNA.
DR EMBL; BC064009; AAH64009.1; -; mRNA.
DR EMBL; BC080672; AAH80672.1; ALT_SEQ; mRNA.
DR EMBL; BC099612; AAH99612.1; ALT_SEQ; mRNA.
DR EMBL; AK122441; BAC65723.1; ALT_FRAME; Transcribed_RNA.
DR CCDS; CCDS35749.1; -. [Q3TLH4-1]
DR RefSeq; NP_001074759.1; NM_001081290.1. [Q3TLH4-1]
DR RefSeq; XP_011237086.1; XM_011238784.2. [Q3TLH4-5]
DR SMR; Q3TLH4; -.
DR BioGRID; 230531; 24.
DR IntAct; Q3TLH4; 6.
DR MINT; Q3TLH4; -.
DR STRING; 10090.ENSMUSP00000138433; -.
DR iPTMnet; Q3TLH4; -.
DR PhosphoSitePlus; Q3TLH4; -.
DR SwissPalm; Q3TLH4; -.
DR EPD; Q3TLH4; -.
DR jPOST; Q3TLH4; -.
DR MaxQB; Q3TLH4; -.
DR PaxDb; Q3TLH4; -.
DR PeptideAtlas; Q3TLH4; -.
DR PRIDE; Q3TLH4; -.
DR ProteomicsDB; 289396; -. [Q3TLH4-1]
DR ProteomicsDB; 289397; -. [Q3TLH4-5]
DR Antibodypedia; 20552; 32 antibodies from 10 providers.
DR Ensembl; ENSMUST00000182660; ENSMUSP00000138433; ENSMUSG00000040225. [Q3TLH4-1]
DR GeneID; 226562; -.
DR KEGG; mmu:226562; -.
DR UCSC; uc007dgr.1; mouse. [Q3TLH4-1]
DR CTD; 23215; -.
DR MGI; MGI:1913754; Prrc2c.
DR VEuPathDB; HostDB:ENSMUSG00000040225; -.
DR eggNOG; KOG4817; Eukaryota.
DR GeneTree; ENSGT00950000183161; -.
DR HOGENOM; CLU_000586_0_0_1; -.
DR InParanoid; Q3TLH4; -.
DR OMA; TDDNYGP; -.
DR OrthoDB; 17901at2759; -.
DR PhylomeDB; Q3TLH4; -.
DR BioGRID-ORCS; 226562; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Prrc2c; mouse.
DR PRO; PR:Q3TLH4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3TLH4; protein.
DR Bgee; ENSMUSG00000040225; Expressed in dorsal pancreas and 234 other tissues.
DR ExpressionAtlas; Q3TLH4; baseline and differential.
DR Genevisible; Q3TLH4; MM.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR InterPro; IPR009738; BAT2_N.
DR InterPro; IPR033184; PRRC2.
DR PANTHER; PTHR14038; PTHR14038; 1.
DR Pfam; PF07001; BAT2_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Isopeptide bond;
KW Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..2846
FT /note="Protein PRRC2C"
FT /id="PRO_0000349240"
FT REGION 46..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1960..1996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2025..2108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2209..2249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2269..2293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2617..2655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2778..2846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 995..1026
FT /evidence="ECO:0000255"
FT COILED 1655..1681
FT /evidence="ECO:0000255"
FT COMPBIAS 87..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1872..1893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1894..1908
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..1996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2029..2043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2056..2088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2216..2249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2629..2655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2778..2805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 243
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 256
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 267
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 280
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 282
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 393
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 1238
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 1516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 1917
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 1935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1938
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1965
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 2057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 2095
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 2212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 2625
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2634
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 2638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 2646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT MOD_RES 2766
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2775
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2775
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 1106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y520"
FT VAR_SEQ 2684..2762
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035255"
FT CONFLICT 38..39
FT /note="Missing (in Ref. 2; AAH80672/BAC25414/BAE38818/
FT BAE39192)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="S -> C (in Ref. 2; BAE38818)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="G -> V (in Ref. 2; BAC25414)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="K -> E (in Ref. 2; BAC25414)"
FT /evidence="ECO:0000305"
FT CONFLICT 376..378
FT /note="SSS -> IIF (in Ref. 2; BAC25414)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="A -> T (in Ref. 2; BAE38818)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="E -> K (in Ref. 3; AAH64009)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="E -> G (in Ref. 2; BAE38818)"
FT /evidence="ECO:0000305"
FT CONFLICT 1362
FT /note="E -> G (in Ref. 4; BAC65723)"
FT /evidence="ECO:0000305"
FT CONFLICT 1491
FT /note="K -> M (in Ref. 4; BAC65723)"
FT /evidence="ECO:0000305"
FT CONFLICT 1686
FT /note="N -> K (in Ref. 3; AAH50871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2846 AA; 310892 MW; 2AEFFE844FBC60C8 CRC64;
MSEKSGQSTK AKDGKKYATL SLFNTYKGKS LETQKTTVAA RHGLQSLGKV GISRRMPPPA
NLPSLKAENK GNDPNVNIVP KDGTGWASKQ EQHEEEKAPE VSPAQPKPGV AAPPEVAPAP
KSWASNKQGG QGDGIQVNSQ FQQEFPSLQA AGDQEKKEKE ANDENYGPGP SLRPPNVACW
RDGGKSAGSP SSDQDEKQLG QDESTAITSE QNDILKVVEK RIACGPPQAK LNGQQPALAS
QYRAMMPPYM FQQYPRMAYP PLHGPMRFPP SLSEANKSLR GRGPPPSWAS EPERPSILSA
SELKELDKFD NLDAEADEGW AGAQMEVDYT EQLNFSDDDE QGSTSPKESS SEDQTAKTPE
STENRKEVDE ASSTKSSSQI PAQPPVTKSP YGKGPPFNQE RGPSSHLPPP PKLLAQQHPP
PPDRQIPGRQ GPFPSKPPVP DNDEIWKQRR KQQSEISAAV ERARKRREEE ERRMEEQRKA
ACAEKLKQLD EKLGIIEKQP SPEELRERER EKERERELEK EKERELEKEQ EKQREMERAR
QQEKELEQQR EKEQELQRLR EQEKEGEPKE QEKEEKVEPQ EPVVEPATEN QESENNCKKE
EEPIFTRQDS NRSEKETTQV VQEAEPESGA QPRPGYFKQF QKSLPPRFQR QQEQMKQQQW
QQQQQQQQQG VLPQTVPSQP SNGSVPPPPH RPLYQPMQPH PQHLASMGFD PRWLMMQSYM
DPRMISGRPA MDIPPIHPGM IPPKPLIRRD QMEGSPNSSE SFEHIARSAR DHGISLSEPR
MMWGSDPYHA EPQQAATPKS AEETGDARPE TAMDHEHMTA AYPVEHSQLE THSKTDVARD
STETEEQKFL SRSLEDVKPR HVDTNTQSAC FDVIDQKSLP TSAEERISAL ESQPARKRSV
SHGSNHAQNA EEQRNEPSVS IPKVINRCMD SKETVEKPEE KPRKDGFLRS SEGPKPEKVY
KSKSETRWGP RPSSNRREEG NDRPVRRSGP IKKPVLRDMK EEREQRKEKE GEKLEKVTEK
VVKAEKPEKK DLPLPLPPPA PAQPQPQPLV SPPVQPEPEK PPSTETSTLT QKPSQDEKPL
EPVGSVQVEP VVKTVNQQSV AAPTVKEEKP PEKVINKDVG IERSRPDSRL AVKKDSSLPT
RTYWKEARDR DWFPDQGYRG RGRGEYYSRG RSYRGSYGGR GRGGRGHTRE YPQYRDNKPR
TEHVPSGPLR QREESETRSE SSDFEVVPKR RRQRGSETDT DSEVHESASD KDSVSKGKLP
KREERPENKK PVKPQSSFKP ENHVRIDNRP LEKPYIREED KSKPGFLPKG EPTRRGRGGT
FRRGGRDPGG RPSRPATLRR PAYRDNQWNT RQAEPPKPED GEPPRRHEQF MPIPADKRPP
KFERKFDPAR ERPRRQRPTR PPRQDKPPRF RRLREREAAS KTSEVLVPSN GTANNVVQEP
VNPPADISGN KTPDLSNQNS SDQANEEWET ASESSDFNER RERDEKKNAD KSSQAVVKAG
ESVLPPKREI AKRSFSSQRP GVDRQNRRGN NGPPKSGRNF SGPRNERRNG PPSKGGKRGP
FDDQASGTAG ADPVSGNSAH HQEGVPNGAG QKNSKDAAGK KREDTKPGPK KPKEKVDALS
QFDLNNYASV VIIDDHPEVT VIEDPQSNLN DDGFTEVVSK KQQKRLQDEE RRKKEEQVVQ
VWSKKNIGEK GRSQTSKLPP RFAKKQATGT QQIQAPPSAP VPVSSSAPGL TAPAAAAPAS
TPAPVPILAS ATALVPVSTP APVLTSCPAP VPTSASAPVP ASTSSPVTAS SSSQPSVPAP
TPVLASASTT VSVPILTSAS IPILASALAP ATVSSPTPVV SATAVPSIST PAVPASAPTA
SVPLAPASAA STVPPPASTV QTQTQTQTHK PVQSPLPPSA PSSKQPPPSI RLPSAQTSNG
TDFVAAGKSM PTSQSHGSLT AELWDSKVAA PAVLNDISKK LGPISPPQPP SVSAWNKPLT
SFGSATSSEG TRNGQESGVE IGIDTIQFGA PASNGNENEV VPVLSEKATD KVPEPKEQRQ
KQPRAGPIKA QKLPDLSLVE NKEHKPGPIG KERSLKNRKV KDAQQVEPEG QEKPSPAVVR
STDPETAKET KAVSEMSAEI GAMISVSSAE YGSDAKESVT DYTTPSSSLP NTVATNNAKM
EDTLVNNVPL PNTLPLPKRE TIQQSSSLTS VPPTTFSLTF KMESARKAWE NSPNLREKGS
PVTSTAPPIV SGVSSSASGP STANYSSFSS ASMPQIPVAS VTPTASLSGA GTYTTSSLST
KSTTTSDPPN ICKVKPQQLQ TSSLPSASHF SQLSCMPSLI AQQQQSPQVY VSQSAAAQIP
AFYMDTSHLF NTQHARLAPP SLAQQQGFQP GLSQPTSVQQ IPIPIYAPLQ GQHQAQLSLG
AGPAVSQAQE LFSSSIQPYR SQPAFMQSSL SQPSVVLSGT AIHNFPAVQH QELAKAQSGL
AFQQTSNPQP IPILYDHQLG QASGLGSSQL IDTHLLQARA NLTQASNLYS GQVQQPGQTN
FYNTAQSPSA LQQVTVPLPA SQLSLTNFGS TGQPLIALPQ TLQPQLQHTT PQAQAQSLSR
PAQVSQPFRG LIPAGTQHSM MATTGKMSEM ELKAFGSGID IKPGTPPIGG RSTTPTSSPF
RATSTSPNSQ SSKMNSVVYQ KQFQSAPATV RMAQPFPAQF APQILSQPNL VPPLVRAPHT
NTFPAPVQRP PMALASQMPP PLTTGLMSHA RLPHVARGPC GSLSGVRGNQ AQAALKAEQD
LKAKQRAEVL QSTQRFFSEQ QQNKQIGGKT QRVDSDTSNP ETLSDPPGTC PEKVEEKPPP
APTITTKPVR TGPIKPQAIK TEETKS
