PRC2B_MOUSE
ID PRC2B_MOUSE Reviewed; 1486 AA.
AC Q7TPM1; A2AN31; Q8C755;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, 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 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 SER-222; SER-387 AND SER-415, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, and Spleen;
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).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TPM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TPM1-2; Sequence=VSP_022764, VSP_022765;
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DR EMBL; AK052511; BAC35022.1; -; mRNA.
DR EMBL; AL808027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055116; AAH55116.1; -; mRNA.
DR CCDS; CCDS15907.1; -. [Q7TPM1-1]
DR RefSeq; NP_001153106.1; NM_001159634.1.
DR RefSeq; NP_766249.2; NM_172661.3. [Q7TPM1-1]
DR AlphaFoldDB; Q7TPM1; -.
DR BioGRID; 230675; 13.
DR IntAct; Q7TPM1; 5.
DR MINT; Q7TPM1; -.
DR STRING; 10090.ENSMUSP00000035734; -.
DR iPTMnet; Q7TPM1; -.
DR PhosphoSitePlus; Q7TPM1; -.
DR EPD; Q7TPM1; -.
DR jPOST; Q7TPM1; -.
DR MaxQB; Q7TPM1; -.
DR PaxDb; Q7TPM1; -.
DR PeptideAtlas; Q7TPM1; -.
DR PRIDE; Q7TPM1; -.
DR ProteomicsDB; 291859; -. [Q7TPM1-1]
DR ProteomicsDB; 291860; -. [Q7TPM1-2]
DR DNASU; 227723; -.
DR Ensembl; ENSMUST00000036691; ENSMUSP00000035734; ENSMUSG00000039262. [Q7TPM1-1]
DR GeneID; 227723; -.
DR KEGG; mmu:227723; -.
DR UCSC; uc008jem.2; mouse. [Q7TPM1-1]
DR CTD; 84726; -.
DR MGI; MGI:1923304; Prrc2b.
DR VEuPathDB; HostDB:ENSMUSG00000039262; -.
DR eggNOG; KOG4817; Eukaryota.
DR GeneTree; ENSGT00950000183161; -.
DR HOGENOM; CLU_001247_0_0_1; -.
DR InParanoid; Q7TPM1; -.
DR OrthoDB; 17901at2759; -.
DR TreeFam; TF328738; -.
DR BioGRID-ORCS; 227723; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Prrc2b; mouse.
DR PRO; PR:Q7TPM1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q7TPM1; protein.
DR Bgee; ENSMUSG00000039262; Expressed in superior cervical ganglion and 234 other tissues.
DR ExpressionAtlas; Q7TPM1; baseline and differential.
DR Genevisible; Q7TPM1; MM.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR InterPro; IPR009738; BAT2_N.
DR InterPro; IPR033184; PRRC2.
DR PANTHER; PTHR14038; PTHR14038; 2.
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..1486
FT /note="Protein PRRC2B"
FT /id="PRO_0000274482"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 494..544
FT /evidence="ECO:0000255"
FT COILED 880..904
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 753
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT CROSSLNK 751
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5JSZ5"
FT VAR_SEQ 1..766
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022764"
FT VAR_SEQ 1475..1486
FT /note="QSEWMKNPAWEP -> PSSASPSGKPSGSAVNMGSVQGHYVQQAKRVDEKPG
FT LGTVKLQEASSATSQMKRTGAIKPRAVKVEGSKA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022765"
FT CONFLICT 1342
FT /note="P -> S (in Ref. 1; BAC35022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1486 AA; 160913 MW; 53BF3D0BD583D731 CRC64;
MSDRLGQITQ GKDGKSKYST LSLFDKYKGR SVGAVRSSVI PRHGLQSLGK VATARRMPPP
ANLPSLKSEN KGNDPNIVIV PKDGTGWANK QDQQDPKSSS VTASQPPESQ PQPGLQKSVS
NLQKPTQSIS QENTNSVPGG PKSWAQLSGK PVGHEGGLRG SSRLLSFSPE EFPTLKAAGG
QDKAGKEKGA LDLSYGPGPS LRPQNVTSWR EGGGRNIISA ASLSASPTEL GSRNASGADG
APSLACTSDS KEPSLRPAQP SRRGASQFMG HGYQPPTYHD MLPAFMCSPQ SSENQTTVER
SSFPLPQLRL EPRVPFRQFQ MNDQDGKERP GVARPVRPLR QLVERAPRPT IINAENLKGL
DDLDTDADDG WAGLHEEVDY SEKLKFSDDE DEEDVVKDGR SKWNNWDPRR QRALSLSSAD
STDAKRTQEE GKDWSGTAGG SRVIRKVPEP QPPSRKLHSW ASGPDYQKPT MGSMFRQHSA
EDKEDKPPPR QKFIQSEMSE AVERARKRRE EEERRAREER LAACAAKLKQ LDQKCRQAQK
ANETPKPVEK EVPRSPGIEK VSPPENGPVV RKGSPEFPVQ EAPTMFLEET PATSPTVAQS
NSSSSSSSSS SIEEEVRESG SPAQEFSKYQ KSLPPRFQRQ QQQQQQQQQQ QQQQEQLYKM
QHWQPVYPPP SHPQRTFYPH HPQMLGFDPR WMMMPSYMDP RITPTRTPVD FYPSALHPSG
LMKPMMPQES LSGTGCRSED QNCVPSLQER KVTALDPAPV WSPEGYMALQ NKGYSLPHPK
SADTLAMGMH VRSPDEALPG GLGSHSPYAL ERTTHASSDG PETPSKKSER EVSLPTQRAS
EQEEARKQFD LGYGNALIDN CASSPGEENE ASSVVGEGFI EVLTKKQRRL LEEERRKKEQ
AAQVPVKGRG LSSRIPPRFA KKQNGLCLEQ DVTVPGSSLG TEIWENSSQA LPVQGAASDS
WRTAVTAFSS TEPGTSEQGF KSSQGDSGVD LSAESRESSA TSSQRSSPYG TLKPEEISGP
GLAESKADSH KDQAQKQAEH KDSEQGSAQS KEHRPGPIGN ERSLKNRKGS EGAERLPGAV
VPPVNGVEIH VDSVLPVPPI EFGVSPKDSD FSLPPGSVSG PVGNPVAKLQ DVLASNAGLT
QSIPILRRDH HMQRAIGLSP MSFPTADLTL KMESARKAWE NSPSLPEQSS PGGAGSGIQP
PSSVGASNGV NYSSFGGVSM PPMPVASVAP SASIPGSHLP PLYLDGHVFA SQPRLVPQTI
PQQQSYQQAA TAQQIPISLH TSLQAQAQLG LRGGLPVSQS QEIFSSLQPF RSQVYMHPSL
SPPSTMILSG GTALKPPYSA FPGIQPLEMV KPQSGSPYQP MSGNQALVYE GQLGQAAGLG
TSQMLDSQLP QLTMPLPRYG SGQQPLILPQ SIQLPPGQSL SVGAPRRVPP PGSQPPVLNT
SRESAPMELK GFHFADSKQN VPTGGSAPSP QAYRQSEWMK NPAWEP
