PRC2C_HUMAN
ID PRC2C_HUMAN Reviewed; 2896 AA.
AC Q9Y520; Q05DM8; Q49A39; Q6PD54; Q9H2N2; Q9HA05; Q9NSM8; Q9NXL3; Q9UF29;
AC Q9UPQ6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein PRRC2C;
DE AltName: Full=BAT2 domain-containing protein 1;
DE AltName: Full=HBV X-transactivated gene 2 protein;
DE AltName: Full=HBV XAg-transactivated protein 2;
DE AltName: Full=HLA-B-associated transcript 2-like 2;
DE AltName: Full=Proline-rich and coiled-coil-containing protein 2C;
GN Name=PRRC2C {ECO:0000312|HGNC:HGNC:24903};
GN Synonyms=BAT2D1, BAT2L2, KIAA1096, XTP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Liu Y., Cheng J., Lu Y., Wang G., Mu J., Li K., Zhang L.;
RT "Cloning and identification of human gene 2 transactivated by hepatitis B
RT virus X antigen.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Rhodes S., Huckle E.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-577 (ISOFORM 7).
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-571 (ISOFORM 7), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-561 (ISOFORM 2).
RC TISSUE=Brain, Placenta, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 17-27; 106-119; 375-387; 451-461; 639-665; 795-804;
RP 834-859; 1317-1324; 1516-1526; 1996-2007; 2101-2110; 2130-2148; 2629-2637
RP AND 2662-2679, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 931-2896 (ISOFORM 5), AND VARIANT
RP CYS-1624.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [8]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1454-2896 (ISOFORM 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2393-2896 (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2029-2862 (ISOFORM 4).
RC TISSUE=Colon mucosa, and Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=12443540; DOI=10.1089/104454902760599681;
RA Huang W.C., Taylor S., Nguyen T.B., Tomaszewski J.E., Libertino J.A.,
RA Malkowicz S.B., McGarvey T.W.;
RT "KIAA1096, a gene on chromosome 1q, is amplified and overexpressed in
RT bladder cancer.";
RL DNA Cell Biol. 21:707-715(2002).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500; SER-779; SER-878;
RP SER-2105 AND THR-2673, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2105; THR-2682 AND SER-2686,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2143 AND THR-2673, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-191; SER-779;
RP SER-878; SER-2013; SER-2143 AND THR-2673, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-878, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-392, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779; SER-801; THR-1965;
RP SER-2013; SER-2105 AND THR-2673, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1246; SER-1248; SER-1263;
RP THR-1265; THR-1267; SER-2013; SER-2105 AND SER-2694, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-395; SER-500;
RP SER-779; SER-785; SER-867; SER-878; SER-920; SER-1242; SER-1246; SER-1248;
RP SER-1249; SER-1263; THR-1265; THR-1267; SER-1544; THR-1965; SER-2105;
RP SER-2143; SER-2260 AND THR-2673, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND THR-1267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-242; ARG-255; ARG-266; ARG-279
RP AND ARG-281, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1133, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1133, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29395067; DOI=10.1016/j.molcel.2017.12.020;
RA Youn J.Y., Dunham W.H., Hong S.J., Knight J.D.R., Bashkurov M., Chen G.I.,
RA Bagci H., Rathod B., MacLeod G., Eng S.W.M., Angers S., Morris Q.,
RA Fabian M., Cote J.F., Gingras A.C.;
RT "High-Density Proximity Mapping Reveals the Subcellular Organization of
RT mRNA-Associated Granules and Bodies.";
RL Mol. Cell 69:517.e11-532.e11(2018).
RN [28]
RP VARIANT [LARGE SCALE ANALYSIS] THR-906, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Required for efficient formation of stress granules.
CC {ECO:0000269|PubMed:29395067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000305|PubMed:29395067}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q9Y520-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y520-2; Sequence=VSP_035244;
CC Name=3;
CC IsoId=Q9Y520-3; Sequence=VSP_035247, VSP_035248;
CC Name=4;
CC IsoId=Q9Y520-4; Sequence=VSP_035249;
CC Name=5;
CC IsoId=Q9Y520-5; Sequence=VSP_035245;
CC Name=6;
CC IsoId=Q9Y520-6; Sequence=VSP_035246, VSP_035249;
CC Name=7;
CC IsoId=Q9Y520-7; Sequence=VSP_035250;
CC -!- TISSUE SPECIFICITY: Overexpressed in bladder cancer.
CC {ECO:0000269|PubMed:12443540}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06090.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH45713.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH58930.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA90997.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF488829; AAO49478.1; -; mRNA.
DR EMBL; AL096857; CAB51071.1; -; mRNA.
DR EMBL; AL021579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF253978; AAG44627.1; -; mRNA.
DR EMBL; BC006090; AAH06090.1; ALT_SEQ; mRNA.
DR EMBL; BC045713; AAH45713.1; ALT_SEQ; mRNA.
DR EMBL; BC058930; AAH58930.1; ALT_SEQ; mRNA.
DR EMBL; AB029019; BAA83048.2; -; mRNA.
DR EMBL; AL133635; CAB63759.1; -; mRNA.
DR EMBL; AL162004; CAB82345.1; -; mRNA.
DR EMBL; AK000190; BAA90997.1; ALT_SEQ; mRNA.
DR EMBL; AK022492; BAB14056.1; -; mRNA.
DR CCDS; CCDS1296.2; -. [Q9Y520-4]
DR PIR; T43454; T43454.
DR PIR; T47182; T47182.
DR RefSeq; NP_055987.2; NM_015172.3. [Q9Y520-4]
DR RefSeq; XP_005245074.1; XM_005245017.2. [Q9Y520-7]
DR RefSeq; XP_006711301.1; XM_006711238.3. [Q9Y520-1]
DR SMR; Q9Y520; -.
DR BioGRID; 116822; 165.
DR DIP; DIP-47285N; -.
DR IntAct; Q9Y520; 56.
DR MINT; Q9Y520; -.
DR STRING; 9606.ENSP00000343629; -.
DR GlyConnect; 2856; 1 O-Linked glycan (2 sites).
DR GlyGen; Q9Y520; 68 sites, 2 O-linked glycans (68 sites).
DR iPTMnet; Q9Y520; -.
DR MetOSite; Q9Y520; -.
DR PhosphoSitePlus; Q9Y520; -.
DR BioMuta; PRRC2C; -.
DR DMDM; 341942262; -.
DR EPD; Q9Y520; -.
DR jPOST; Q9Y520; -.
DR MassIVE; Q9Y520; -.
DR MaxQB; Q9Y520; -.
DR PaxDb; Q9Y520; -.
DR PeptideAtlas; Q9Y520; -.
DR PRIDE; Q9Y520; -.
DR ProteomicsDB; 86273; -. [Q9Y520-1]
DR ProteomicsDB; 86274; -. [Q9Y520-2]
DR ProteomicsDB; 86275; -. [Q9Y520-3]
DR ProteomicsDB; 86276; -. [Q9Y520-4]
DR ProteomicsDB; 86277; -. [Q9Y520-5]
DR ProteomicsDB; 86278; -. [Q9Y520-6]
DR ProteomicsDB; 86279; -. [Q9Y520-7]
DR Antibodypedia; 20552; 32 antibodies from 10 providers.
DR DNASU; 23215; -.
DR Ensembl; ENST00000338920.8; ENSP00000343629.4; ENSG00000117523.18. [Q9Y520-4]
DR Ensembl; ENST00000426496.6; ENSP00000410219.3; ENSG00000117523.18. [Q9Y520-4]
DR Ensembl; ENST00000647382.2; ENSP00000495867.2; ENSG00000117523.18. [Q9Y520-7]
DR GeneID; 23215; -.
DR KEGG; hsa:23215; -.
DR MANE-Select; ENST00000647382.2; ENSP00000495867.2; NM_001387844.1; NP_001374773.1. [Q9Y520-7]
DR UCSC; uc010pmg.3; human. [Q9Y520-1]
DR CTD; 23215; -.
DR DisGeNET; 23215; -.
DR GeneCards; PRRC2C; -.
DR HGNC; HGNC:24903; PRRC2C.
DR HPA; ENSG00000117523; Low tissue specificity.
DR MIM; 617373; gene.
DR neXtProt; NX_Q9Y520; -.
DR OpenTargets; ENSG00000117523; -.
DR PharmGKB; PA165750415; -.
DR VEuPathDB; HostDB:ENSG00000117523; -.
DR eggNOG; KOG4817; Eukaryota.
DR GeneTree; ENSGT00950000183161; -.
DR InParanoid; Q9Y520; -.
DR OMA; SWIQGGS; -.
DR TreeFam; TF328738; -.
DR PathwayCommons; Q9Y520; -.
DR SignaLink; Q9Y520; -.
DR BioGRID-ORCS; 23215; 54 hits in 1084 CRISPR screens.
DR ChiTaRS; PRRC2C; human.
DR GenomeRNAi; 23215; -.
DR Pharos; Q9Y520; Tbio.
DR PRO; PR:Q9Y520; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y520; protein.
DR Bgee; ENSG00000117523; Expressed in epithelium of nasopharynx and 206 other tissues.
DR ExpressionAtlas; Q9Y520; baseline and differential.
DR Genevisible; Q9Y520; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:0034063; P:stress granule assembly; IMP: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;
KW Direct protein sequencing; Isopeptide bond; Methylation; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..2896
FT /note="Protein PRRC2C"
FT /id="PRO_0000349239"
FT REGION 28..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1670..1785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2005..2164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2218..2238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2257..2290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2317..2341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2668..2701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2824..2896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1020..1046
FT /evidence="ECO:0000255"
FT COILED 1682..1717
FT /evidence="ECO:0000255"
FT COMPBIAS 85..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..720
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1929
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1930..1989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2022..2069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2077..2091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2104..2136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2143..2164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2264..2290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2677..2701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 242
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3TLH4"
FT MOD_RES 242
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 255
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 266
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 279
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 281
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TLH4"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1267
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1965
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1983
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TLH4"
FT MOD_RES 2013
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 2105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 2260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2673
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2682
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 2686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 2694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2814
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TLH4"
FT MOD_RES 2823
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3TLH4"
FT MOD_RES 2823
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3TLH4"
FT CROSSLNK 1133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035244"
FT VAR_SEQ 37
FT /note="T -> TVA (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_035250"
FT VAR_SEQ 1759..1805
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10470851"
FT /id="VSP_035245"
FT VAR_SEQ 2185..2249
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_035246"
FT VAR_SEQ 2687..2700
FT /note="PFRATSTSPNSQSS -> SGLLLQVRTASPAK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.2"
FT /id="VSP_035247"
FT VAR_SEQ 2701..2896
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.2"
FT /id="VSP_035248"
FT VAR_SEQ 2732..2810
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_035249"
FT VARIANT 235
FT /note="A -> T (in dbSNP:rs10913157)"
FT /id="VAR_046290"
FT VARIANT 343
FT /note="N -> K (in dbSNP:rs36013361)"
FT /id="VAR_046291"
FT VARIANT 468
FT /note="E -> G (in dbSNP:rs704839)"
FT /id="VAR_046292"
FT VARIANT 906
FT /note="A -> T (in dbSNP:rs760644)"
FT /evidence="ECO:0007744|PubMed:21269460"
FT /id="VAR_046293"
FT VARIANT 959
FT /note="P -> S (in dbSNP:rs34269512)"
FT /id="VAR_046294"
FT VARIANT 1624
FT /note="S -> C (in dbSNP:rs235468)"
FT /evidence="ECO:0000269|PubMed:10470851"
FT /id="VAR_046295"
FT VARIANT 1771
FT /note="P -> S (in dbSNP:rs1687056)"
FT /id="VAR_046296"
FT VARIANT 1868
FT /note="L -> R (in dbSNP:rs3820169)"
FT /id="VAR_046297"
FT VARIANT 1885
FT /note="A -> T (in dbSNP:rs12025905)"
FT /id="VAR_046298"
FT VARIANT 1924
FT /note="P -> R (in dbSNP:rs183523)"
FT /id="VAR_046299"
FT VARIANT 2717
FT /note="T -> A (in dbSNP:rs2421847)"
FT /id="VAR_059584"
FT CONFLICT 454..456
FT /note="EIS -> GIY (in Ref. 5; AAH45713)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="Q -> P (in Ref. 5; AAH45713)"
FT /evidence="ECO:0000305"
FT CONFLICT 1940
FT /note="V -> A (in Ref. 9; CAB82345)"
FT /evidence="ECO:0000305"
FT CONFLICT 2443
FT /note="A -> V (in Ref. 10; BAB14056)"
FT /evidence="ECO:0000305"
FT CONFLICT 2539
FT /note="I -> V (in Ref. 10; BAA90997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2896 AA; 316911 MW; F0E037C36F04CDF9 CRC64;
MSEKSGQSTK AKDGKKYATL SLFNTYKGKS LETQKTTARH GLQSLGKVGI SRRMPPPANL
PSLKAENKGN DPNVNIVPKD GTGWASKQEQ HEEEKTPEVP PAQPKPGVAA PPEVAPAPKS
WASNKQGGQG DGIQVNSQFQ QEFPSLQAAG DQEKKEKETN DDNYGPGPSL RPPNVACWRD
GGKAAGSPSS SDQDEKLPGQ DESTAGTSEQ NDILKVVEKR IACGPPQAKL NGQQAALASQ
YRAMMPPYMF QQYPRMTYPP LHGPMRFPPS LSETNKGLRG RGPPPSWASE PERPSILSAS
ELKELDKFDN LDAEADEGWA GAQMEVDYTE QLNFSDDDEQ GSNSPKENNS EDQGSKASEN
NENKKETDEV SNTKSSSQIP AQPSVAKVPY GKGPSFNQER GTSSHLPPPP KLLAQQHPPP
DRQAVPGRPG PFPSKQQVAD EDEIWKQRRR QQSEISAAVE RARKRREEEE RRMEEQRKAA
CAEKLKRLDE KLGILEKQPS PEEIRERERE KEREREKELE KEQEQEREKE REKDRERQQE
KEKELEKEQE KQREMEKERK QEKEKELERQ KEKEKELQKM KEQEKECELE KEREKLEEKI
EPREPNLEPM VEKQESENSC NKEEEPVFTR QDSNRSEKEA TPVVHETEPE SGSQPRPAVL
SGYFKQFQKS LPPRFQRQQE QMKQQQWQQQ QQQGVLPQTV PSQPSSSTVP PPPHRPLYQP
MQPHPQHLAS MGFDPRWLMM QSYMDPRMMS GRPAMDIPPI HPGMIPPKPL MRRDQMEGSP
NSSESFEHIA RSARDHAISL SEPRMLWGSD PYPHAEPQQA TTPKATEEPE DVRSEAALDQ
EQITAAYSVE HNQLEAHPKA DFIRESSEAQ VQKFLSRSVE DVRPHHTDAN NQSACFEAPD
QKTLSAPQEE RISAVESQPS RKRSVSHGSN HTQKPDEQRS EPSAGIPKVT SRCIDSKEPI
ERPEEKPKKE GFIRSSEGPK PEKVYKSKSE TRWGPRPSSN RREEVNDRPV RRSGPIKKPV
LRDMKEEREQ RKEKEGEKAE KVTEKVVVKP EKTEKKDLPP PPPPPQPPAP IQPQSVPPPI
QPEAEKFPST ETATLAQKPS QDTEKPLEPV STVQVEPAVK TVNQQTMAAP VVKEEKQPEK
VISKDLVIER PRPDSRPAVK KESTLPPRTY WKEARERDWF PDQGYRGRGR GEYYSRGRSY
RGSYGGRGRG GRGHTRDYPQ YRDNKPRAEH IPSGPLRQRE ESETRSESSD FEVVPKRRRQ
RGSETDTDSE IHESASDKDS LSKGKLPKRE ERPENKKPVK PHSSFKPDNH VRIDNRLLEK
PYVRDDDKAK PGFLPKGEPT RRGRGGTFRR GGRDPGGRPS RPSTLRRPAY RDNQWNPRQS
EVPKPEDGEP PRRHEQFIPI AADKRPPKFE RKFDPARERP RRQRPTRPPR QDKPPRFRRL
REREAASKSN EVVAVPTNGT VNNVAQEPVN TLGDISGNKT PDLSNQNSSD QANEEWETAS
ESSDFNERRE RDEKKNADLN AQTVVKVGEN VLPPKREIAK RSFSSQRPVD RQNRRGNNGP
PKSGRNFSGP RNERRSGPPS KSGKRGPFDD QPAGTTGVDL INGSSAHHQE GVPNGTGQKN
SKDSTGKKRE DPKPGPKKPK EKVDALSQFD LNNYASVVII DDHPEVTVIE DPQSNLNDDG
FTEVVSKKQQ KRLQDEERRK KEEQVIQVWN KKNANEKGRS QTSKLPPRFA KKQATGIQQA
QSSASVPPLA SAPLPPSTSA SVPASTSAPL PATLTPVPAS TSAPVPASTL APVLASTSAP
VPASPLAPVS ASASVSASVP ASTSAAAITS SSAPASAPAP TPILASVSTP ASVTILASAS
IPILASALAS TSAPTPAPAA SSPAAPVITA PTIPASAPTA SVPLAPASAS APAPAPTPVS
APNPAPPAPA QTQAQTHKPV QNPLQTTSQS SKQPPPSIRL PSAQTPNGTD YVASGKSIQT
PQSHGTLTAE LWDNKVAPPA VLNDISKKLG PISPPQPPSV SAWNKPLTSF GSAPSSEGAK
NGQESGLEIG TDTIQFGAPA SNGNENEVVP VLSEKSADKI PEPKEQRQKQ PRAGPIKAQK
LPDLSPVENK EHKPGPIGKE RSLKNRKVKD AQQVEPEGQE KPSPATVRST DPVTTKETKA
VSEMSTEIGT MISVSSAEYG TNAKESVTDY TTPSSSLPNT VATNNTKMED TLVNNVPLPN
TLPLPKRETI QQSSSLTSVP PTTFSLTFKM ESARKAWENS PNVREKGSPV TSTAPPIATG
VSSSASGPST ANYNSFSSAS MPQIPVASVT PTASLSGAGT YTTSSLSTKS TTTSDPPNIC
KVKPQQLQTS SLPSASHFSQ LSCMPSLIAQ QQQNPQVYVS QSAAAQIPAF YMDTSHLFNT
QHARLAPPSL AQQQGFQPGL SQPTSVQQIP IPIYAPLQGQ HQAQLSLGAG PAVSQAQELF
SSSLQPYRSQ PAFMQSSLSQ PSVVLSGTAI HNFPTVQHQE LAKAQSGLAF QQTSNTQPIP
ILYEHQLGQA SGLGGSQLID THLLQARANL TQASNLYSGQ VQQPGQTNFY NTAQSPSALQ
QVTVPLPASQ LSLPNFGSTG QPLIALPQTL QPPLQHTTPQ AQAQSLSRPA QVSQPFRGLI
PAGTQHSMIA TTGKMSEMEL KAFGSGIDIK PGTPPIAGRS TTPTSSPFRA TSTSPNSQSS
KMNSIVYQKQ FQSAPATVRM TQPFPTQFAP QILSQPNLVP PLVRAPHTNT FPAPVQRPPM
ALASQMPPPL TTGLMSHARL PHVARGPCGS LSGVRGNQAQ AALKAEQDMK AKQRAEVLQS
TQRFFSEQQQ SKQIGGGKAQ KVDSDSSKPP ETLTDPPGVC QEKVEEKPPP APSIATKPVR
TGPIKPQAIK TEETKS
