RPRD2_HUMAN
ID RPRD2_HUMAN Reviewed; 1461 AA.
AC Q5VT52; A8K6N8; B3KPT1; B4E2Q6; O75048; Q5VT51; Q5VT53; Q6MZL4; Q86XD2;
AC Q9P0D7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Regulation of nuclear pre-mRNA domain-containing protein 2;
GN Name=RPRD2; Synonyms=KIAA0460; ORFNames=HSPC099;
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] (ISOFORMS 1 AND 5).
RC TISSUE=Placenta, and Trachea;
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 2).
RC TISSUE=Salivary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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] (ISOFORM 3).
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167 (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RA Zhang Q.H., Ye M., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L., Fan H.Y.,
RA Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.;
RT "Human partial CDS cloned from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-1461 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [8]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; THR-723 AND SER-1099,
RP AND 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614; SER-758 AND SER-762, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-479; SER-485;
RP THR-517; SER-593; SER-614; THR-723; SER-758; SER-900; SER-909; SER-928 AND
RP SER-1099, 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 [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-374; SER-473; SER-476;
RP THR-482; SER-485; SER-593; THR-598; SER-614; SER-665; THR-732; SER-826;
RP SER-909 AND SER-1099, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-374; SER-473; THR-482;
RP THR-517; SER-593; SER-614; THR-723; SER-928 AND SER-1099, AND
RP IDENTIFICATION BY 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 [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-356; THR-358; SER-374 AND
RP SER-593, AND 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 [18]
RP IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-358; SER-374;
RP SER-485; THR-517; SER-614; SER-663; SER-665; SER-716; THR-723; SER-758;
RP THR-763; SER-769; SER-817; SER-909; SER-965; SER-976 AND SER-1099, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-564 AND THR-723, 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 [22]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1366; ARG-1424 AND ARG-1430, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [23]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 19-149.
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 -!- SUBUNIT: Associates with the RNA polymerase II complex.
CC {ECO:0000269|PubMed:22231121}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5VT52-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VT52-2; Sequence=VSP_019546;
CC Name=3;
CC IsoId=Q5VT52-3; Sequence=VSP_019547;
CC Name=4;
CC IsoId=Q5VT52-4; Sequence=VSP_035574, VSP_035575;
CC Name=5;
CC IsoId=Q5VT52-5; Sequence=VSP_019547, VSP_053733, VSP_053734;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28922.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH45623.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK056707; BAG51793.1; -; mRNA.
DR EMBL; AK291703; BAF84392.1; -; mRNA.
DR EMBL; AK304380; BAG65218.1; -; mRNA.
DR EMBL; BX641025; CAE46016.1; -; mRNA.
DR EMBL; AL356356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL611942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX284695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53552.1; -; Genomic_DNA.
DR EMBL; BC045623; AAH45623.2; ALT_INIT; mRNA.
DR EMBL; AF161362; AAF28922.1; ALT_INIT; mRNA.
DR EMBL; AB007929; BAA32305.2; -; mRNA.
DR CCDS; CCDS44216.1; -. [Q5VT52-1]
DR CCDS; CCDS72907.1; -. [Q5VT52-3]
DR PIR; T00074; T00074.
DR RefSeq; NP_001284602.1; NM_001297673.1. [Q5VT52-5]
DR RefSeq; NP_001284603.1; NM_001297674.1. [Q5VT52-3]
DR RefSeq; NP_056018.2; NM_015203.4. [Q5VT52-1]
DR PDB; 4FLB; X-ray; 1.80 A; A=19-149.
DR PDBsum; 4FLB; -.
DR AlphaFoldDB; Q5VT52; -.
DR SMR; Q5VT52; -.
DR BioGRID; 116852; 118.
DR DIP; DIP-31155N; -.
DR IntAct; Q5VT52; 34.
DR MINT; Q5VT52; -.
DR STRING; 9606.ENSP00000358064; -.
DR GlyConnect; 2891; 1 O-Linked glycan (2 sites).
DR GlyGen; Q5VT52; 39 sites, 2 O-linked glycans (39 sites).
DR iPTMnet; Q5VT52; -.
DR MetOSite; Q5VT52; -.
DR PhosphoSitePlus; Q5VT52; -.
DR BioMuta; RPRD2; -.
DR DMDM; 74746888; -.
DR EPD; Q5VT52; -.
DR jPOST; Q5VT52; -.
DR MassIVE; Q5VT52; -.
DR MaxQB; Q5VT52; -.
DR PaxDb; Q5VT52; -.
DR PeptideAtlas; Q5VT52; -.
DR PRIDE; Q5VT52; -.
DR ProteomicsDB; 5845; -.
DR ProteomicsDB; 65302; -. [Q5VT52-1]
DR ProteomicsDB; 65303; -. [Q5VT52-2]
DR ProteomicsDB; 65304; -. [Q5VT52-3]
DR ProteomicsDB; 65305; -. [Q5VT52-4]
DR Antibodypedia; 10548; 64 antibodies from 17 providers.
DR DNASU; 23248; -.
DR Ensembl; ENST00000369067.7; ENSP00000358063.3; ENSG00000163125.16. [Q5VT52-4]
DR Ensembl; ENST00000369068.5; ENSP00000358064.4; ENSG00000163125.16. [Q5VT52-1]
DR Ensembl; ENST00000401000.8; ENSP00000383785.4; ENSG00000163125.16. [Q5VT52-3]
DR GeneID; 23248; -.
DR KEGG; hsa:23248; -.
DR MANE-Select; ENST00000369068.5; ENSP00000358064.4; NM_015203.5; NP_056018.2.
DR UCSC; uc001eup.5; human. [Q5VT52-1]
DR CTD; 23248; -.
DR DisGeNET; 23248; -.
DR GeneCards; RPRD2; -.
DR HGNC; HGNC:29039; RPRD2.
DR HPA; ENSG00000163125; Low tissue specificity.
DR MIM; 614695; gene.
DR neXtProt; NX_Q5VT52; -.
DR OpenTargets; ENSG00000163125; -.
DR PharmGKB; PA162402062; -.
DR VEuPathDB; HostDB:ENSG00000163125; -.
DR eggNOG; KOG2669; Eukaryota.
DR GeneTree; ENSGT00950000183094; -.
DR HOGENOM; CLU_144992_0_0_1; -.
DR InParanoid; Q5VT52; -.
DR OMA; NYSHRAQ; -.
DR OrthoDB; 1091009at2759; -.
DR PhylomeDB; Q5VT52; -.
DR TreeFam; TF320926; -.
DR PathwayCommons; Q5VT52; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q5VT52; -.
DR BioGRID-ORCS; 23248; 71 hits in 1091 CRISPR screens.
DR ChiTaRS; RPRD2; human.
DR GeneWiki; KIAA0460; -.
DR GenomeRNAi; 23248; -.
DR Pharos; Q5VT52; Tdark.
DR PRO; PR:Q5VT52; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VT52; protein.
DR Bgee; ENSG00000163125; Expressed in buccal mucosa cell and 217 other tissues.
DR Genevisible; Q5VT52; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; IDA:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
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 3D-structure; Acetylation; Alternative splicing; Methylation;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052"
FT CHAIN 2..1461
FT /note="Regulation of nuclear pre-mRNA domain-containing
FT protein 2"
FT /id="PRO_0000244355"
FT DOMAIN 19..149
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT REGION 311..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1279
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25489052"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 517
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 598
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 723
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NXI6"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 763
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NXI6"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1366
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1424
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1430
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019546"
FT VAR_SEQ 146..171
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019547"
FT VAR_SEQ 147..152
FT /note="TTFKTQ -> KCLFLS (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_035574"
FT VAR_SEQ 153..1461
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_035575"
FT VAR_SEQ 932..960
FT /note="SKNDSFFTPDSNHNSLSQSTTGHLSLPQK -> KHPCRSHGSPTHVRRGESP
FT GLHHFHHVDD (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053733"
FT VAR_SEQ 961..1461
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053734"
FT VARIANT 351
FT /note="M -> V (in dbSNP:rs41273537)"
FT /id="VAR_061700"
FT CONFLICT 167
FT /note="W -> C (in Ref. 6; AAF28922)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="T -> A (in Ref. 1; BAG51793)"
FT /evidence="ECO:0000305"
FT CONFLICT 1297
FT /note="P -> L (in Ref. 1; BAG51793)"
FT /evidence="ECO:0000305"
FT CONFLICT 1385
FT /note="G -> R (in Ref. 1; BAG51793)"
FT /evidence="ECO:0000305"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:4FLB"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:4FLB"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4FLB"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:4FLB"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:4FLB"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:4FLB"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:4FLB"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:4FLB"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:4FLB"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:4FLB"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:4FLB"
SQ SEQUENCE 1461 AA; 156020 MW; E08CAF3148F89F67 CRC64;
MAAGGGGGSS KASSSSASSA GALESSLDRK FQSVTNTMES IQGLSSWCIE NKKHHSTIVY
HWMKWLRRSA YPHRLNLFYL ANDVIQNCKR KNAIIFRESF ADVLPEAAAL VKDPSVSKSV
ERIFKIWEDR NVYPEEMIVA LREALSTTFK TQKQLKENLN KQPNKQWKKS QTSTNPKAAL
KSKIVAEFRS QALIEELLLY KRSEDQIELK EKQLSTMRVD VCSTETLKCL KDKTGGKKFS
KEFEEASSKL EEFVNGLDKQ VKNGPSLTEA LENAGIFYEA QYKEVKVVAN AYKTFANRVN
NLKKKLDQLK STLPDPEESP VPSPSMDAPS PTGSESPFQG MGGEESQSPT MESEKSATPE
PVTDNRDVED MELSDVEDDG SKIIVEDRKE KPAEKSAVST SVPTKPTENI SKASSCTPVP
VTMTATPPLP KPVNTSLSPS PALALPNLAN VDLAKISSIL SSLTSVMKNT GVSPASRPSP
GTPTSPSNLT SGLKTPAPAT TTSHNPLANI LSKVEITPES ILSALSKTQT QSAPALQGLS
SLLQSVTGNP VPASEAASQS TSASPANTTV STIKGRNLPS SAQPFIPKSF NYSPNSSTSE
VSSTSASKAS IGQSPGLPST TFKLPSNSLG FTATHNTSPA APPTEVTICQ SSEVSKPKLE
SESTSPSLEM KIHNFLKGNP GFSGLNLNIP ILSSLGSSAP SESHPSDFQR GPTSTSIDNI
DGTPVRDERS GTPTQDEMMD KPTSSSVDTM SLLSKIISPG SSTPSSTRSP PPGRDESYPR
ELSNSVSTYR PFGLGSESPY KQPSDGMERP SSLMDSSQEK FYPDTSFQED EDYRDFEYSG
PPPSAMMNLE KKPAKSILKS SKLSDTTEYQ PILSSYSHRA QEFGVKSAFP PSVRALLDSS
ENCDRLSSSP GLFGAFSVRG NEPGSDRSPS PSKNDSFFTP DSNHNSLSQS TTGHLSLPQK
QYPDSPHPVP HRSLFSPQNT LAAPTGHPPT SGVEKVLAST ISTTSTIEFK NMLKNASRKP
SDDKHFGQAP SKGTPSDGVS LSNLTQPSLT ATDQQQQEEH YRIETRVSSS CLDLPDSTEE
KGAPIETLGY HSASNRRMSG EPIQTVESIR VPGKGNRGHG REASRVGWFD LSTSGSSFDN
GPSSASELAS LGGGGSGGLT GFKTAPYKER APQFQESVGS FRSNSFNSTF EHHLPPSPLE
HGTPFQREPV GPSSAPPVPP KDHGGIFSRD APTHLPSVDL SNPFTKEAAL AHAAPPPPPG
EHSGIPFPTP PPPPPPGEHS SSGGSGVPFS TPPPPPPPVD HSGVVPFPAP PLAEHGVAGA
VAVFPKDHSS LLQGTLAEHF GVLPGPRDHG GPTQRDLNGP GLSRVRESLT LPSHSLEHLG
PPHGGGGGGG SNSSSGPPLG PSHRDTISRS GIILRSPRPD FRPREPFLSR DPFHSLKRPR
PPFARGPPFF APKRPFFPPR Y
