RPR1B_HUMAN
ID RPR1B_HUMAN Reviewed; 326 AA.
AC Q9NQG5; Q1WDE7; Q6PKF4;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
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=C20orf77, CREPT;
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], FUNCTION, INTERACTION WITH RNA POLYMERASE II,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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].
RC TISSUE=Hippocampus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma;
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 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [10]
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 [11]
RP IDENTIFICATION BY 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 [12]
RP IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22231121; DOI=10.4161/trns.2.5.17803;
RA Ni Z., Olsen J.B., Guo X., Zhong G., Ruan E.D., Marcon E., Young P.,
RA Guo H., Li J., Moffat J., Emili A., Greenblatt J.F.;
RT "Control of the RNA polymerase II phosphorylation state in promoter regions
RT by CTD interaction domain-containing proteins RPRD1A and RPRD1B.";
RL Transcription 2:237-242(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-134 AND TYR-161, 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 [16] {ECO:0007744|PDB:4FU3, ECO:0007744|PDB:4HFG}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-135.
RG Structural genomics consortium (SGC);
RT "CID of human RPRD1B.";
RL Submitted (JUN-2012) to the PDB data bank.
RN [17] {ECO:0007744|PDB:4NAD}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 177-326, FUNCTION, AND
RP INTERACTION WITH POLR2A.
RX PubMed=24399136; DOI=10.1007/s11427-013-4589-7;
RA Mei K., Jin Z., Ren F., Wang Y., Chang Z., Wang X.;
RT "Structural basis for the recognition of RNA polymerase II C-terminal
RT domain by CREPT and p15RS.";
RL Sci. China Life Sci. 57:97-106(2014).
RN [18] {ECO:0007744|PDB:4FLA, ECO:0007744|PDB:4Q94, ECO:0007744|PDB:4Q96}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-135, MUTAGENESIS OF ARG-114,
RP FUNCTION, AND SUBUNIT.
RX PubMed=24997600; DOI=10.1038/nsmb.2853;
RA Ni Z., Xu C., Guo X., Hunter G.O., Kuznetsova O.V., Tempel W., Marcon E.,
RA Zhong G., Guo H., Kuo W.H., Li J., Young P., Olsen J.B., Wan C.,
RA Loppnau P., El Bakkouri M., Senisterra G.A., He H., Huang H., Sidhu S.S.,
RA Emili A., Murphy S., Mosley A.L., Arrowsmith C.H., Min J., Greenblatt J.F.;
RT "RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds
RT for Ser5 dephosphorylation.";
RL Nat. Struct. Mol. Biol. 21:686-695(2014).
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:0000269|PubMed:22231121,
CC ECO:0000269|PubMed:22264791, ECO:0000269|PubMed:24399136,
CC ECO:0000269|PubMed:24997600}.
CC -!- SUBUNIT: Homodimer (PubMed:24997600). May form a heterodimer with
CC RPRD1A (PubMed:24997600). Associates with RPAP2 (PubMed:24997600).
CC Associates with the RNA polymerase II complex (PubMed:22231121,
CC PubMed:24399136, PubMed:24997600). {ECO:0000269|PubMed:22231121,
CC ECO:0000269|PubMed:24399136, ECO:0000269|PubMed:24997600}.
CC -!- INTERACTION:
CC Q9NQG5; Q9NQY0: BIN3; NbExp=3; IntAct=EBI-747925, EBI-2653038;
CC Q9NQG5; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-747925, EBI-979174;
CC Q9NQG5; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-747925, EBI-742054;
CC Q9NQG5; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-747925, EBI-740641;
CC Q9NQG5; P09017: HOXC4; NbExp=3; IntAct=EBI-747925, EBI-3923226;
CC Q9NQG5; P61970: NUTF2; NbExp=3; IntAct=EBI-747925, EBI-591778;
CC Q9NQG5; O15212: PFDN6; NbExp=3; IntAct=EBI-747925, EBI-356973;
CC Q9NQG5; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-747925, EBI-11532361;
CC Q9NQG5; P24928: POLR2A; NbExp=10; IntAct=EBI-747925, EBI-295301;
CC Q9NQG5; P20618: PSMB1; NbExp=3; IntAct=EBI-747925, EBI-372273;
CC Q9NQG5; Q86WH2: RASSF3; NbExp=3; IntAct=EBI-747925, EBI-2845202;
CC Q9NQG5; Q8IXW5: RPAP2; NbExp=4; IntAct=EBI-747925, EBI-395878;
CC Q9NQG5; Q96P16: RPRD1A; NbExp=4; IntAct=EBI-747925, EBI-1053506;
CC Q9NQG5; Q96P16-1: RPRD1A; NbExp=4; IntAct=EBI-747925, EBI-16112633;
CC Q9NQG5; Q96P16-3: RPRD1A; NbExp=3; IntAct=EBI-747925, EBI-12840198;
CC Q9NQG5; Q9NQG5: RPRD1B; NbExp=8; IntAct=EBI-747925, EBI-747925;
CC Q9NQG5; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-747925, EBI-742688;
CC Q9NQG5; Q9H5V9: STEEP1; NbExp=3; IntAct=EBI-747925, EBI-1053419;
CC Q9NQG5; O14787-2: TNPO2; NbExp=3; IntAct=EBI-747925, EBI-12076664;
CC Q9NQG5; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-747925, EBI-10180829;
CC Q9NQG5; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-747925, EBI-12227803;
CC Q9NQG5; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-747925, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22231121,
CC ECO:0000269|PubMed:22264791}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in a range of tumor
CC tissues including colon, lung, liver, breast, prostate, stomach,
CC uterine endometrium and cervical cancers with higher levels in tumors
CC than in adjacent non-tumor tissue (at protein level).
CC {ECO:0000269|PubMed:22264791}.
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01696.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; DQ372938; ABD34791.1; -; mRNA.
DR EMBL; AK312468; BAG35375.1; -; mRNA.
DR EMBL; AL109823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76045.1; -; Genomic_DNA.
DR EMBL; BC001696; AAH01696.1; ALT_SEQ; mRNA.
DR EMBL; BC033629; AAH33629.1; -; mRNA.
DR CCDS; CCDS13301.1; -.
DR RefSeq; NP_067038.1; NM_021215.3.
DR PDB; 4FLA; X-ray; 2.20 A; A/B/C/D=172-305.
DR PDB; 4FU3; X-ray; 1.90 A; A/B=2-135.
DR PDB; 4HFG; X-ray; 2.00 A; A/B=2-135.
DR PDB; 4NAD; X-ray; 2.80 A; A/B=177-326.
DR PDB; 4Q94; X-ray; 1.85 A; A/B=2-135.
DR PDB; 4Q96; X-ray; 1.85 A; A/B/D/E=2-135.
DR PDBsum; 4FLA; -.
DR PDBsum; 4FU3; -.
DR PDBsum; 4HFG; -.
DR PDBsum; 4NAD; -.
DR PDBsum; 4Q94; -.
DR PDBsum; 4Q96; -.
DR AlphaFoldDB; Q9NQG5; -.
DR SMR; Q9NQG5; -.
DR BioGRID; 121820; 192.
DR DIP; DIP-61537N; -.
DR IntAct; Q9NQG5; 65.
DR MINT; Q9NQG5; -.
DR STRING; 9606.ENSP00000362532; -.
DR GlyGen; Q9NQG5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQG5; -.
DR MetOSite; Q9NQG5; -.
DR PhosphoSitePlus; Q9NQG5; -.
DR BioMuta; RPRD1B; -.
DR DMDM; 23813907; -.
DR EPD; Q9NQG5; -.
DR jPOST; Q9NQG5; -.
DR MassIVE; Q9NQG5; -.
DR MaxQB; Q9NQG5; -.
DR PaxDb; Q9NQG5; -.
DR PeptideAtlas; Q9NQG5; -.
DR PRIDE; Q9NQG5; -.
DR ProteomicsDB; 82148; -.
DR ABCD; Q9NQG5; 1 sequenced antibody.
DR Antibodypedia; 26806; 218 antibodies from 26 providers.
DR DNASU; 58490; -.
DR Ensembl; ENST00000373433.9; ENSP00000362532.4; ENSG00000101413.12.
DR GeneID; 58490; -.
DR KEGG; hsa:58490; -.
DR MANE-Select; ENST00000373433.9; ENSP00000362532.4; NM_021215.4; NP_067038.1.
DR UCSC; uc002xho.5; human.
DR CTD; 58490; -.
DR DisGeNET; 58490; -.
DR GeneCards; RPRD1B; -.
DR HGNC; HGNC:16209; RPRD1B.
DR HPA; ENSG00000101413; Tissue enhanced (liver).
DR MIM; 614694; gene.
DR neXtProt; NX_Q9NQG5; -.
DR OpenTargets; ENSG00000101413; -.
DR PharmGKB; PA162402043; -.
DR VEuPathDB; HostDB:ENSG00000101413; -.
DR eggNOG; KOG2669; Eukaryota.
DR GeneTree; ENSGT00950000183094; -.
DR HOGENOM; CLU_055523_1_0_1; -.
DR InParanoid; Q9NQG5; -.
DR OMA; KTWQREL; -.
DR OrthoDB; 1091009at2759; -.
DR PhylomeDB; Q9NQG5; -.
DR TreeFam; TF320926; -.
DR PathwayCommons; Q9NQG5; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q9NQG5; -.
DR SIGNOR; Q9NQG5; -.
DR BioGRID-ORCS; 58490; 317 hits in 1097 CRISPR screens.
DR ChiTaRS; RPRD1B; human.
DR GenomeRNAi; 58490; -.
DR Pharos; Q9NQG5; Tbio.
DR PRO; PR:Q9NQG5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NQG5; protein.
DR Bgee; ENSG00000101413; Expressed in ileal mucosa and 173 other tissues.
DR ExpressionAtlas; Q9NQG5; baseline and differential.
DR Genevisible; Q9NQG5; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IMP:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; IDA: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 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..326
FT /note="Regulation of nuclear pre-mRNA domain-containing
FT protein 1B"
FT /id="PRO_0000079441"
FT DOMAIN 2..133
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT REGION 127..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 161
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96P16"
FT MUTAGEN 114
FT /note="R->A: Complete loss of binding to POLR2A CTD in
FT vivo."
FT /evidence="ECO:0000269|PubMed:24997600"
FT CONFLICT 21
FT /note="Q -> H (in Ref. 5; AAH33629)"
FT /evidence="ECO:0000305"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:4Q94"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:4Q94"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4Q94"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:4Q94"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4Q94"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:4Q94"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4Q94"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:4Q94"
FT HELIX 85..113
FT /evidence="ECO:0007829|PDB:4Q94"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:4Q94"
FT HELIX 177..202
FT /evidence="ECO:0007829|PDB:4FLA"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:4FLA"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:4FLA"
FT HELIX 220..298
FT /evidence="ECO:0007829|PDB:4FLA"
SQ SEQUENCE 326 AA; 36900 MW; 9057EEF6F3D18215 CRC64;
MSSFSESALE KKLSELSNSQ QSVQTLSLWL IHHRKHAGPI VSVWHRELRK AKSNRKLTFL
YLANDVIQNS KRKGPEFTRE FESVLVDAFS HVAREADEGC KKPLERLLNI WQERSVYGGE
FIQQLKLSME DSKSPPPKAT EEKKSLKRTF QQIQEEEDDD YPGSYSPQDP SAGPLLTEEL
IKALQDLENA ASGDATVRQK IASLPQEVQD VSLLEKITDK EAAERLSKTV DEACLLLAEY
NGRLAAELED RRQLARMLVE YTQNQKDVLS EKEKKLEEYK QKLARVTQVR KELKSHIQSL
PDLSLLPNVT GGLAPLPSAG DLFSTD
