RPR1A_MOUSE
ID RPR1A_MOUSE Reviewed; 312 AA.
AC Q8VDS4; Q5DTP5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Regulation of nuclear pre-mRNA domain-containing protein 1A;
DE AltName: Full=Cyclin-dependent kinase inhibitor 2B-related protein;
DE AltName: Full=p15INK4B-related protein;
GN Name=Rprd1a; Synonyms=Kiaa4077, P15rs;
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].
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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. May act as a
CC negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the
CC cell cycle. {ECO:0000250|UniProtKB:Q96P16}.
CC -!- SUBUNIT: May form a heterodimer with RPRD1B. Associates with the RNA
CC polymerase II subunit POLR2A (via CTD phosphorylated at 'Ser-2' and
CC 'Ser-7' of the heptad repeats). {ECO:0000250|UniProtKB:Q96P16}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96P16}.
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90282.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK220475; BAD90282.1; ALT_INIT; mRNA.
DR EMBL; BC021395; AAH21395.1; -; mRNA.
DR EMBL; BC023084; AAH23084.1; -; mRNA.
DR CCDS; CCDS29102.1; -.
DR RefSeq; NP_659110.1; NM_144861.2.
DR RefSeq; XP_006525887.1; XM_006525824.3.
DR RefSeq; XP_006525888.1; XM_006525825.3.
DR AlphaFoldDB; Q8VDS4; -.
DR SMR; Q8VDS4; -.
DR BioGRID; 230378; 4.
DR STRING; 10090.ENSMUSP00000043618; -.
DR iPTMnet; Q8VDS4; -.
DR PhosphoSitePlus; Q8VDS4; -.
DR SwissPalm; Q8VDS4; -.
DR EPD; Q8VDS4; -.
DR MaxQB; Q8VDS4; -.
DR PaxDb; Q8VDS4; -.
DR PeptideAtlas; Q8VDS4; -.
DR PRIDE; Q8VDS4; -.
DR ProteomicsDB; 299947; -.
DR Antibodypedia; 22307; 123 antibodies from 23 providers.
DR DNASU; 225283; -.
DR Ensembl; ENSMUST00000046206; ENSMUSP00000043618; ENSMUSG00000040446.
DR GeneID; 225283; -.
DR KEGG; mmu:225283; -.
DR UCSC; uc008egu.1; mouse.
DR CTD; 55197; -.
DR MGI; MGI:2385066; Rprd1a.
DR VEuPathDB; HostDB:ENSMUSG00000040446; -.
DR eggNOG; KOG2669; Eukaryota.
DR GeneTree; ENSGT00950000183094; -.
DR HOGENOM; CLU_055523_1_0_1; -.
DR InParanoid; Q8VDS4; -.
DR OMA; MAYNDDA; -.
DR OrthoDB; 1091009at2759; -.
DR PhylomeDB; Q8VDS4; -.
DR TreeFam; TF320926; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 225283; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Rprd1a; mouse.
DR PRO; PR:Q8VDS4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8VDS4; protein.
DR Bgee; ENSMUSG00000040446; Expressed in olfactory tubercle and 251 other tissues.
DR Genevisible; Q8VDS4; MM.
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; IBA:GO_Central.
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 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; Coiled coil; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96P16"
FT CHAIN 2..312
FT /note="Regulation of nuclear pre-mRNA domain-containing
FT protein 1A"
FT /id="PRO_0000311345"
FT DOMAIN 2..133
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT COILED 244..286
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P16"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P16"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P16"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P16"
SQ SEQUENCE 312 AA; 35701 MW; D7C90635A8992D27 CRC64;
MSAFSEAALE KKLSELSNSQ QSVQTLSLWL IHHRKHSRPI VTVWERELRK AKPNRKLTFL
YLANDVIQNS KRKGPEFTKD FAPVIVEAFK HVSSETDESC KKHLGRVLSI WEERSVYEND
VLEQLKHALY GDKKARKRTY EQIKVDENEN CSSLGSPSEP PQTLDLVRAL QDLENAASGD
AAVHQRIASL PVEVQEVSLL EKITDKESGE RLSKMVEDAC MLLADYNGRL AAEIDDRKQL
TRMLADFLRC QKEALAEKEH KLEEYKRKLA RVSLVRKELR ARIQSLPDLS RLPNVTGSHM
HLPFAGDIYS ED