RPR1B_MOUSE
ID RPR1B_MOUSE Reviewed; 326 AA.
AC Q9CSU0; A2ACF2; A2ACF4; A2ACF5; A2ACF6; Q1WDE6; Q3U8H1; Q3UGH1; Q3USX3;
AC Q6GTJ6;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Regulation of nuclear pre-mRNA domain-containing protein 1B;
DE AltName: Full=Cell cycle-related and expression-elevated protein in tumor;
GN Name=Rprd1b; Synonyms=Crept;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ;
RX PubMed=22264791; DOI=10.1016/j.ccr.2011.12.016;
RA Lu D., Wu Y., Wang Y., Ren F., Wang D., Su F., Zhang Y., Yang X., Jin G.,
RA Hao X., He D., Zhai Y., Irwin D.M., Hu J., Sung J.J., Yu J., Jia B.,
RA Chang Z.;
RT "CREPT accelerates tumorigenesis by regulating the transcription of cell-
RT cycle-related genes.";
RL Cancer Cell 21:92-104(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow macrophage, Corpora quadrigemina, Embryo, and
RC Melanocyte;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Liver, Mammary gland, and Retina;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION BY
RP 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-134 AND SER-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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).
CC -!- FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat
CC domain (CTD) of the largest RNA polymerase II subunit POLR2A, and
CC participates in dephosphorylation of the CTD by RPAP2. Transcriptional
CC regulator which enhances expression of CCND1. Promotes binding of RNA
CC polymerase II to the CCDN1 promoter and to the termination region
CC before the poly-A site but decreases its binding after the poly-A site.
CC Prevents RNA polymerase II from reading through the 3' end termination
CC site and may allow it to be recruited back to the promoter through
CC promotion of the formation of a chromatin loop. Also enhances the
CC transcription of a number of other cell cycle-related genes including
CC CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A.
CC Promotes cell proliferation. {ECO:0000250|UniProtKB:Q9NQG5}.
CC -!- SUBUNIT: Homodimer. May form a heterodimer with RPRD1A. Associates with
CC RPAP2. Associates with the RNA polymerase II complex.
CC {ECO:0000250|UniProtKB:Q9NQG5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQG5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CSU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CSU0-2; Sequence=VSP_018618, VSP_018619;
CC Name=3;
CC IsoId=Q9CSU0-3; Sequence=VSP_035576, VSP_035577;
CC -!- TISSUE SPECIFICITY: Widely expressed in the adult with highest levels
CC in liver, colon, prostate and uterus and lowest levels in heart and
CC kidney. Not detected in rectum. {ECO:0000269|PubMed:22264791}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during early embryonic
CC development (at protein level). Low levels detected in the adult.
CC {ECO:0000269|PubMed:22264791}.
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family. {ECO:0000305}.
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DR EMBL; DQ372939; ABD34792.1; -; mRNA.
DR EMBL; AK011979; BAB27954.3; -; mRNA.
DR EMBL; AK139995; BAE24207.1; -; mRNA.
DR EMBL; AK147718; BAE28092.1; -; mRNA.
DR EMBL; AK147930; BAE28237.1; -; mRNA.
DR EMBL; AK152125; BAE30966.1; -; mRNA.
DR EMBL; AK152220; BAE31047.1; -; mRNA.
DR EMBL; AL669824; CAM23181.1; -; Genomic_DNA.
DR EMBL; AL669824; CAM23182.1; -; Genomic_DNA.
DR EMBL; AL669824; CAM23183.1; -; Genomic_DNA.
DR EMBL; AL669824; CAM23184.1; -; Genomic_DNA.
DR EMBL; AL669824; CAM23185.1; -; Genomic_DNA.
DR EMBL; BC028819; AAH28819.3; -; mRNA.
DR EMBL; BC042447; AAH42447.1; -; mRNA.
DR EMBL; BC054350; AAH54350.1; -; mRNA.
DR CCDS; CCDS71176.1; -. [Q9CSU0-2]
DR CCDS; CCDS71177.1; -. [Q9CSU0-1]
DR RefSeq; NP_001278063.1; NM_001291134.1. [Q9CSU0-1]
DR RefSeq; NP_001278064.1; NM_001291135.1. [Q9CSU0-2]
DR RefSeq; NP_001278065.1; NM_001291136.1.
DR RefSeq; NP_081710.1; NM_027434.3.
DR AlphaFoldDB; Q9CSU0; -.
DR SMR; Q9CSU0; -.
DR BioGRID; 214076; 49.
DR IntAct; Q9CSU0; 34.
DR STRING; 10090.ENSMUSP00000029180; -.
DR iPTMnet; Q9CSU0; -.
DR PhosphoSitePlus; Q9CSU0; -.
DR EPD; Q9CSU0; -.
DR jPOST; Q9CSU0; -.
DR MaxQB; Q9CSU0; -.
DR PaxDb; Q9CSU0; -.
DR PeptideAtlas; Q9CSU0; -.
DR PRIDE; Q9CSU0; -.
DR ProteomicsDB; 299929; -. [Q9CSU0-1]
DR ProteomicsDB; 299930; -. [Q9CSU0-2]
DR ProteomicsDB; 299931; -. [Q9CSU0-3]
DR Antibodypedia; 26806; 218 antibodies from 26 providers.
DR Ensembl; ENSMUST00000029180; ENSMUSP00000029180; ENSMUSG00000027651. [Q9CSU0-1]
DR Ensembl; ENSMUST00000109518; ENSMUSP00000105144; ENSMUSG00000027651. [Q9CSU0-2]
DR Ensembl; ENSMUST00000152452; ENSMUSP00000118434; ENSMUSG00000027651. [Q9CSU0-3]
DR GeneID; 70470; -.
DR KEGG; mmu:70470; -.
DR UCSC; uc008npl.2; mouse. [Q9CSU0-1]
DR UCSC; uc008npn.2; mouse. [Q9CSU0-2]
DR CTD; 58490; -.
DR MGI; MGI:1917720; Rprd1b.
DR VEuPathDB; HostDB:ENSMUSG00000027651; -.
DR eggNOG; KOG2669; Eukaryota.
DR GeneTree; ENSGT00950000183094; -.
DR HOGENOM; CLU_055523_0_0_1; -.
DR InParanoid; Q9CSU0; -.
DR OrthoDB; 1091009at2759; -.
DR PhylomeDB; Q9CSU0; -.
DR TreeFam; TF320926; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 70470; 19 hits in 73 CRISPR screens.
DR ChiTaRS; Rprd1b; mouse.
DR PRO; PR:Q9CSU0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CSU0; protein.
DR Bgee; ENSMUSG00000027651; Expressed in metanephric ureteric bud and 260 other tissues.
DR ExpressionAtlas; Q9CSU0; baseline and differential.
DR Genevisible; Q9CSU0; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; ISS:UniProtKB.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR032337; CREPT.
DR InterPro; IPR008942; ENTH_VHS.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF16566; CREPT; 1.
DR SMART; SM00582; RPR; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS51391; CID; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NQG5"
FT CHAIN 2..326
FT /note="Regulation of nuclear pre-mRNA domain-containing
FT protein 1B"
FT /id="PRO_0000079442"
FT DOMAIN 2..133
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT REGION 128..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQG5"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQG5"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 161
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQG5"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P16"
FT VAR_SEQ 220..224
FT /note="KEAAE -> AETEA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_035576"
FT VAR_SEQ 225..326
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_035577"
FT VAR_SEQ 278..294
FT /note="EYKQKLARVTQVRKELK -> RLTQQLQPCSDPQNVSF (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018618"
FT VAR_SEQ 295..326
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018619"
FT CONFLICT 17
FT /note="S -> G (in Ref. 4; BAE30966/BAE31047)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Missing (in Ref. 2; BAB27954/BAE28092/BAE28237, 3;
FT CAM23183/CAM23185 and 4; AAH42447/AAH54350)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..222
FT /note="QEVQDVSLLEKITDKEA -> SGSARRVAARENYRCRN (in Ref. 2;
FT BAE24207)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..326
FT /note="Missing (in Ref. 2; BAE24207)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="S -> P (in Ref. 2; BAB27954)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="P -> S (in Ref. 2; BAE28092/BAE28237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 36884 MW; 904B9792FBBDFA71 CRC64;
MSSFSESALE KKLSELSNSQ QSVQTLSLWL IHHRKHAGPI VSVWHRELRK AKSNRKLTFL
YLANDVIQNS KRKGPEFTRE FESVLVDAFS HVAREADEGC KKPLERLLNI WQERSVYGGE
FIQQLKLSME DSKSPPPKAA EEKKSLKRTF QQIQEEEDDD YPGSYSPQDP SAGPLLTEEL
IKALQDLENA ASGDATVRQK IASLPQEVQD VSLLEKITDK EAAERLSKTV DEACLLLAEY
NGRLAAELED RRQLARMLVE YTQNQKEVLS EKEKKLEEYK QKLARVTQVR KELKSHIQSL
PDLSLLPNVT GGLAPLPSAG DLFSTD
