PRC2B_HUMAN
ID PRC2B_HUMAN Reviewed; 2229 AA.
AC Q5JSZ5; O60270; Q5JSZ7; Q66VZ2; Q68CR0; Q96EI9; Q9H683;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein PRRC2B;
DE AltName: Full=HLA-B-associated transcript 2-like 1;
DE AltName: Full=Proline-rich coiled-coil protein 2B;
GN Name=PRRC2B; Synonyms=BAT2L, BAT2L1, KIAA0515;
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 [LARGE SCALE MRNA] (ISOFORM 3).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Zhou G., Shen C., Li H., Ke R., Zhong G., Lin L., Yang S.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-2229 (ISOFORM 5).
RC TISSUE=Colon carcinoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1560-2229.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-1754, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-168, AND
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776 (ISOFORM 1), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-168; SER-226;
RP SER-416; THR-736; SER-740; SER-745; SER-1132; SER-1231; SER-1470 AND
RP SER-1843, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776 (ISOFORM 1),
RP AND IDENTIFICATION BY MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-388, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-168; SER-388;
RP SER-740; SER-745 AND SER-1507, 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 [16]
RP IDENTIFICATION BY MASS 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).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; THR-228; SER-388;
RP SER-416; SER-480; SER-556; SER-613; SER-740; SER-745 AND SER-765, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [19]
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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-963, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-251; LYS-734 AND LYS-963, AND
RP IDENTIFICATION BY MASS 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).
CC -!- INTERACTION:
CC Q5JSZ5; P54253: ATXN1; NbExp=5; IntAct=EBI-744891, EBI-930964;
CC Q5JSZ5; Q96KQ7: EHMT2; NbExp=2; IntAct=EBI-744891, EBI-744366;
CC Q5JSZ5; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-744891, EBI-3957603;
CC Q5JSZ5-5; P54253: ATXN1; NbExp=6; IntAct=EBI-21531669, EBI-930964;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=5;
CC IsoId=Q5JSZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JSZ5-2; Sequence=VSP_022760;
CC Name=3;
CC IsoId=Q5JSZ5-3; Sequence=VSP_022760, VSP_022761;
CC Name=4;
CC IsoId=Q5JSZ5-4; Sequence=VSP_022760, VSP_022762;
CC Name=1;
CC IsoId=Q5JSZ5-5; Sequence=VSP_039905;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH18678.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK026162; BAB15380.1; -; mRNA.
DR EMBL; AY700780; AAU10087.1; -; mRNA.
DR EMBL; AL358781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012289; AAH12289.1; -; mRNA.
DR EMBL; CR749818; CAH18678.1; ALT_SEQ; mRNA.
DR EMBL; AB011087; BAA25441.1; -; mRNA.
DR CCDS; CCDS48044.1; -. [Q5JSZ5-1]
DR PIR; T00083; T00083.
DR RefSeq; NP_037450.2; NM_013318.3. [Q5JSZ5-1]
DR AlphaFoldDB; Q5JSZ5; -.
DR BioGRID; 124226; 233.
DR IntAct; Q5JSZ5; 65.
DR MINT; Q5JSZ5; -.
DR STRING; 9606.ENSP00000349856; -.
DR GlyGen; Q5JSZ5; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; Q5JSZ5; -.
DR MetOSite; Q5JSZ5; -.
DR PhosphoSitePlus; Q5JSZ5; -.
DR BioMuta; PRRC2B; -.
DR DMDM; 308153415; -.
DR EPD; Q5JSZ5; -.
DR jPOST; Q5JSZ5; -.
DR MassIVE; Q5JSZ5; -.
DR MaxQB; Q5JSZ5; -.
DR PaxDb; Q5JSZ5; -.
DR PeptideAtlas; Q5JSZ5; -.
DR PRIDE; Q5JSZ5; -.
DR ProteomicsDB; 63178; -. [Q5JSZ5-1]
DR ProteomicsDB; 63179; -. [Q5JSZ5-2]
DR ProteomicsDB; 63180; -. [Q5JSZ5-3]
DR ProteomicsDB; 63181; -. [Q5JSZ5-4]
DR ProteomicsDB; 63182; -. [Q5JSZ5-5]
DR DNASU; 84726; -.
DR Ensembl; ENST00000682501.1; ENSP00000508073.1; ENSG00000288701.1. [Q5JSZ5-5]
DR Ensembl; ENST00000683519.1; ENSP00000508048.1; ENSG00000288701.1. [Q5JSZ5-1]
DR Ensembl; ENST00000684596.1; ENSP00000508005.1; ENSG00000288701.1. [Q5JSZ5-1]
DR GeneID; 84726; -.
DR KEGG; hsa:84726; -.
DR MANE-Select; ENST00000683519.1; ENSP00000508048.1; NM_013318.4; NP_037450.2.
DR UCSC; uc004cam.2; human. [Q5JSZ5-1]
DR CTD; 84726; -.
DR GeneCards; PRRC2B; -.
DR HGNC; HGNC:28121; PRRC2B.
DR MIM; 619544; gene.
DR neXtProt; NX_Q5JSZ5; -.
DR PharmGKB; PA165585468; -.
DR VEuPathDB; HostDB:ENSG00000130723; -.
DR eggNOG; KOG4817; Eukaryota.
DR GeneTree; ENSGT00950000183161; -.
DR HOGENOM; CLU_001247_0_0_1; -.
DR InParanoid; Q5JSZ5; -.
DR OMA; NQRDCHS; -.
DR PhylomeDB; Q5JSZ5; -.
DR TreeFam; TF328738; -.
DR PathwayCommons; Q5JSZ5; -.
DR SignaLink; Q5JSZ5; -.
DR BioGRID-ORCS; 84726; 18 hits in 1060 CRISPR screens.
DR ChiTaRS; PRRC2B; human.
DR GeneWiki; KIAA0515; -.
DR GenomeRNAi; 84726; -.
DR Pharos; Q5JSZ5; Tdark.
DR PRO; PR:Q5JSZ5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5JSZ5; protein.
DR ExpressionAtlas; Q5JSZ5; differential.
DR Genevisible; Q5JSZ5; HS.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
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 Alternative splicing; Coiled coil; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..2229
FT /note="Protein PRRC2B"
FT /id="PRO_0000274481"
FT REGION 49..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1650..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1790..1809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1861..1890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2086..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2138..2229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 495..553
FT /evidence="ECO:0000255"
FT COILED 1563..1587
FT /evidence="ECO:0000255"
FT COMPBIAS 87..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2088..2102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2146..2184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPM1"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 736
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 734
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 963
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..1903
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_022760"
FT VAR_SEQ 775..1468
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_039905"
FT VAR_SEQ 2075
FT /note="Q -> QQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022761"
FT VAR_SEQ 2159..2229
FT /note="PSSASPSGKPSGSAVNMGSVQGHYVQQAKQRVDEKPSLGAVKLQEAPSAASQ
FT MKRTGAIKPRAVKVEESKA -> QNNEWMRNPAWEP (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_022762"
FT VARIANT 417
FT /note="M -> V (in dbSNP:rs34553878)"
FT /id="VAR_057735"
FT VARIANT 1630
FT /note="S -> T (in dbSNP:rs10736851)"
FT /id="VAR_030289"
FT VARIANT 1675
FT /note="L -> P (in dbSNP:rs10751478)"
FT /id="VAR_030290"
FT CONFLICT 936
FT /note="T -> S (in Ref. 5; CAH18678)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="P -> L (in Ref. 5; CAH18678)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044
FT /note="M -> T (in Ref. 5; CAH18678)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="A -> V (in Ref. 5; CAH18678)"
FT /evidence="ECO:0000305"
FT CONFLICT 1933
FT /note="F -> L (in Ref. 2; AAU10087)"
FT /evidence="ECO:0000305"
FT CONFLICT 1985
FT /note="Q -> R (in Ref. 2; AAU10087)"
FT /evidence="ECO:0000305"
FT CONFLICT 2069
FT /note="L -> S (in Ref. 2; AAU10087)"
FT /evidence="ECO:0000305"
FT CONFLICT 2135
FT /note="G -> S (in Ref. 2; AAU10087)"
FT /evidence="ECO:0000305"
FT MOD_RES Q5JSZ5-5:776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648"
SQ SEQUENCE 2229 AA; 242967 MW; 0F5F13DAC0217A6D CRC64;
MSDRLGQITK GKDGKSKYST LSLFDKYKGK SVDAIRSSVI PRHGLQSLGK VAAARRMPPP
ANLPSLKSEN KGNDPNIVIV PKDGTGWANK QDQQDPKSSS ATASQPPESL PQPGLQKSVS
NLQKPTQSIS QENTNSVPGG PKSWAQLNGK PVGHEGGLRG SSRLLSFSPE EFPTLKAAGG
QDKAGKEKGV LDLSYGPGPS LRPQNVTSWR EGGGRHIISA TSLSTSPTEL GSRNSSTGDG
APSSACTSDS KDPSLRPAQP VRKGASQFMG NVYHPPTYHD MLPAFMCSPK SSENQGTVER
GSFPLPQLRL EPRVPFRQFQ MNDQDGKENR LGLSRPLRPL RQLVERAPRP TIINAENLKG
LDDLDADADD GWAGLHEEVD YSEKLKFSDD EEEEEVVKDG RPKWNSWDPR RQRQLSMSSA
DSADAKRTRE EGKDWAEAVG ASRVVRKAPD PQPPPRKLHG WAPGPDYQKS SMGSMFRQQS
IEDKEDKPPP RQKFIQSEMS EAVERARKRR EEEERRAREE RLAACAAKLK QLDQKCKQAR
KAGEARKQAE KEVPWSPSAE KASPQENGPA VHKGSPEFPA QETPTTFPEE APTVSPAVAQ
SNSSEEEARE AGSPAQEFKY QKSLPPRFQR QQQQQQQEQL YKMQHWQPVY PPPSHPQRTF
YPHHPQMLGF DPRWMMMPSY MDPRITPTRT PVDFYPSALH PSGLMKPMMP QESLNGTGCR
SEDQNCVPPL QERKVTPIDS PPVWSPEGYM ALQSKGYPLP HPKSSDTLAM DMRVRNESSF
SASLGRAGGV SAQRDLFEER GEEYLSAFDK KAQADFDSCI SSQRIGQELL FPPQENVQDA
GAPGGHTQNL RCSPLEPDFV PDEKKPECGS WDVSHQPETA DTAHGVERET PREGTAFNIS
SWDKNGSPNK QPSSEPEWTP EPRSSSSQHP EQTGRTRRSG PIKKPVLKAL KVEDKEKELE
KIKQELGEES TRLAKEKEQS PTAEKDEDEE NDASLANSST TTLEDKGPGH ATFGREATKF
EEEEKPDKAW EARPPRESSD VPPMKRNNWI FIDEEQAFGV RGQARGRGRG FREFTFRGRP
AGGNGSGLCG GGVLGARSIY CSSQRSGRGR GLREFARPED CPRAKPRRRV ASETHSEGSE
YEELPKRRRQ RGSENGNEGS LLEREESTLK KGDCRDSWRS NKGCSEDHSG LDAKSRGPRA
FGRALPPRLS NCGYGRRTFV SKESPHWQSK SPGSSWQEYG PSDTCGSRRP TDRDYVPDSY
RHPDAFGGRG FEDSRAEDKR SFFQDEHVAD SENAENRPFR RRRPPRQDKP PRFRRLRQER
ESLGLWGPEE EPHLLAGQWP GRPKLCSGDK SGTVGRRSPE LSYQNSSDHA NEEWETASES
SDFSERRERR EGPGSEPDSQ VDGGLSGASL GEKKELAKRS FSSQRPVVDR QSRKLEPGGF
GEKPVRPGGG DTSPRYESQQ NGTPLKVKRS PDEALPGGLS GCSSGSGHSP YALERAAHAS
ADLPEASSKK AEKEAKLAAP RAGEQGEAMK QFDLNYGSAI IENCGSSPGE ESEVGSMVGE
GFIEVLTKKQ RRLLEEERRK KEQAVQVPVK GRGLSSRIPP RFAKKQNNLC LEQGDVTVPG
SSLGTEIWES SSQALPVQAP ANDSWRKAVT AFSSTETGSA EQGFKSSQGD SGVDLSAESR
ESSATSSQRS SPYGTLKPEE MSGPGLAEPK ADSHKEQAPK PSEQKDSEQG SGQSKEHRPG
PIGNERSLKN RKGSEGAERL QGAVVPPVNG VEIHVDSVLP VPPIEFGVSP KDSDFSLPPG
SASGPTGSPV VKLQDALASN AGLTQSIPIL RRDHHIQRAI GLSPMSFPTA DLTLKMESAR
KAWENSPSLP EQSSPGGAGS GIQPPSSVGA SSGVNYSSFG GVSMPPMPVA SVAPSASMPG
SHLPPLYLDG HVFASQPRLV PQTIPQQQSY QQAAAAQQIP ISLHTSLQAQ AQLGLRGGLP
VSQSQEIFSS LQPFRSQVYM HPSLSPPSTM ILSGGTALKP PYSAFPGMQP LEMVKPQSGS
PYQPMSGNQA LVYEGQLSQA AGLGASQMLD SQLPQLTMPL PRYGSGQQPL ILPQSIQLPP
GQSLSVGAPR RIPPPGSQPP VLNTSREPSQ MEMKGFHFAD SKQNVPSGGP VPSPQTYRPS
SASPSGKPSG SAVNMGSVQG HYVQQAKQRV DEKPSLGAVK LQEAPSAASQ MKRTGAIKPR
AVKVEESKA
