Full text data of RPRD1B
RPRD1B
(C20orf77, CREPT)
[Confidence: low (only semi-automatic identification from reviews)]
Regulation of nuclear pre-mRNA domain-containing protein 1B (Cell cycle-related and expression-elevated protein in tumor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Regulation of nuclear pre-mRNA domain-containing protein 1B (Cell cycle-related and expression-elevated protein in tumor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NQG5
ID RPR1B_HUMAN Reviewed; 326 AA.
AC Q9NQG5; Q1WDE7; Q6PKF4;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 93.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RNA POLYMERASE
RP II, 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.,
RA Jin G., Hao X., He D., Zhai Y., Irwin D.M., Hu J., Sung J.J., Yu J.,
RA Jia B., Chang Z.;
RT "CREPT accelerates tumorigenesis by regulating the transcription of
RT cell-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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX, AND FUNCTION.
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
RT regions by CTD interaction domain-containing proteins RPRD1A and
RT RPRD1B.";
RL Transcription 2:237-242(2011).
CC -!- FUNCTION: Interacts with phosphorylated C-terminal heptapeptide
CC repeat domain (CTD) of the largest RNA polymerase II subunit
CC POLR2A, and participates in dephosphorylation of the CTD.
CC Transcriptional regulator which enhances expression of CCND1.
CC Promotes binding of RNA polymerase II to the CCDN1 promoter and to
CC the termination region before the poly-A site but decreases its
CC binding after the poly-A site. Prevents RNA polymerase II from
CC reading through the 3' end termination site and may allow it to be
CC recruited back to the promoter through promotion of the formation
CC of a chromatin loop. Also enhances the transcription of a number
CC of other cell cycle-related genes including CDK2, CDK4, CDK6 and
CC cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell
CC proliferation.
CC -!- SUBUNIT: Associates with the RNA polymerase II complex.
CC -!- INTERACTION:
CC P24928:POLR2A; NbExp=5; IntAct=EBI-747925, EBI-295301;
CC -!- SUBCELLULAR LOCATION: Nucleus.
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
CC tumors than in adjacent non-tumor tissue (at protein level).
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family.
CC -!- SIMILARITY: Contains 1 CID domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01696.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR EMBL; DQ372938; ABD34791.1; -; mRNA.
DR EMBL; AK312468; BAG35375.1; -; mRNA.
DR EMBL; AL109823; CAC01532.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76045.1; -; Genomic_DNA.
DR EMBL; BC001696; AAH01696.1; ALT_SEQ; mRNA.
DR EMBL; BC033629; AAH33629.1; -; mRNA.
DR RefSeq; NP_067038.1; NM_021215.3.
DR UniGene; Hs.278839; -.
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 PDBsum; 4FLA; -.
DR PDBsum; 4FU3; -.
DR PDBsum; 4HFG; -.
DR ProteinModelPortal; Q9NQG5; -.
DR SMR; Q9NQG5; 2-129, 175-301.
DR IntAct; Q9NQG5; 2.
DR MINT; MINT-1475221; -.
DR STRING; 9606.ENSP00000362532; -.
DR PhosphoSite; Q9NQG5; -.
DR DMDM; 23813907; -.
DR PaxDb; Q9NQG5; -.
DR PeptideAtlas; Q9NQG5; -.
DR PRIDE; Q9NQG5; -.
DR DNASU; 58490; -.
DR Ensembl; ENST00000373433; ENSP00000362532; ENSG00000101413.
DR GeneID; 58490; -.
DR KEGG; hsa:58490; -.
DR UCSC; uc002xho.4; human.
DR CTD; 58490; -.
DR GeneCards; GC20P036662; -.
DR H-InvDB; HIX0015799; -.
DR HGNC; HGNC:16209; RPRD1B.
DR MIM; 614694; gene.
DR neXtProt; NX_Q9NQG5; -.
DR PharmGKB; PA162402043; -.
DR eggNOG; NOG291577; -.
DR HOGENOM; HOG000007456; -.
DR HOVERGEN; HBG051177; -.
DR InParanoid; Q9NQG5; -.
DR KO; K15559; -.
DR OMA; ATQANSK; -.
DR OrthoDB; EOG7V1FRR; -.
DR PhylomeDB; Q9NQG5; -.
DR ChiTaRS; RPRD1B; human.
DR GenomeRNAi; 58490; -.
DR NextBio; 64964; -.
DR PRO; PR:Q9NQG5; -.
DR ArrayExpress; Q9NQG5; -.
DR Bgee; Q9NQG5; -.
DR CleanEx; HS_RPRD1B; -.
DR Genevestigator; Q9NQG5; -.
DR GO; GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IDA:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR006903; RNA_pol_II-bd.
DR Pfam; PF04818; CTD_bind; 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; Complete proteome; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 326 Regulation of nuclear pre-mRNA domain-
FT containing protein 1B.
FT /FTId=PRO_0000079441.
FT DOMAIN 1 133 CID.
FT MOD_RES 134 134 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT CONFLICT 21 21 Q -> H (in Ref. 5; AAH33629).
FT HELIX 6 15
FT HELIX 19 21
FT HELIX 22 32
FT HELIX 34 36
FT HELIX 37 50
FT TURN 53 55
FT HELIX 56 70
FT TURN 71 73
FT HELIX 76 82
FT HELIX 85 97
FT HELIX 102 113
FT HELIX 119 127
FT HELIX 177 202
FT HELIX 206 208
FT HELIX 211 216
FT HELIX 220 298
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
//
ID RPR1B_HUMAN Reviewed; 326 AA.
AC Q9NQG5; Q1WDE7; Q6PKF4;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 93.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RNA POLYMERASE
RP II, 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.,
RA Jin G., Hao X., He D., Zhai Y., Irwin D.M., Hu J., Sung J.J., Yu J.,
RA Jia B., Chang Z.;
RT "CREPT accelerates tumorigenesis by regulating the transcription of
RT cell-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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX, AND FUNCTION.
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
RT regions by CTD interaction domain-containing proteins RPRD1A and
RT RPRD1B.";
RL Transcription 2:237-242(2011).
CC -!- FUNCTION: Interacts with phosphorylated C-terminal heptapeptide
CC repeat domain (CTD) of the largest RNA polymerase II subunit
CC POLR2A, and participates in dephosphorylation of the CTD.
CC Transcriptional regulator which enhances expression of CCND1.
CC Promotes binding of RNA polymerase II to the CCDN1 promoter and to
CC the termination region before the poly-A site but decreases its
CC binding after the poly-A site. Prevents RNA polymerase II from
CC reading through the 3' end termination site and may allow it to be
CC recruited back to the promoter through promotion of the formation
CC of a chromatin loop. Also enhances the transcription of a number
CC of other cell cycle-related genes including CDK2, CDK4, CDK6 and
CC cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell
CC proliferation.
CC -!- SUBUNIT: Associates with the RNA polymerase II complex.
CC -!- INTERACTION:
CC P24928:POLR2A; NbExp=5; IntAct=EBI-747925, EBI-295301;
CC -!- SUBCELLULAR LOCATION: Nucleus.
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
CC tumors than in adjacent non-tumor tissue (at protein level).
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family.
CC -!- SIMILARITY: Contains 1 CID domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01696.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR EMBL; DQ372938; ABD34791.1; -; mRNA.
DR EMBL; AK312468; BAG35375.1; -; mRNA.
DR EMBL; AL109823; CAC01532.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76045.1; -; Genomic_DNA.
DR EMBL; BC001696; AAH01696.1; ALT_SEQ; mRNA.
DR EMBL; BC033629; AAH33629.1; -; mRNA.
DR RefSeq; NP_067038.1; NM_021215.3.
DR UniGene; Hs.278839; -.
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 PDBsum; 4FLA; -.
DR PDBsum; 4FU3; -.
DR PDBsum; 4HFG; -.
DR ProteinModelPortal; Q9NQG5; -.
DR SMR; Q9NQG5; 2-129, 175-301.
DR IntAct; Q9NQG5; 2.
DR MINT; MINT-1475221; -.
DR STRING; 9606.ENSP00000362532; -.
DR PhosphoSite; Q9NQG5; -.
DR DMDM; 23813907; -.
DR PaxDb; Q9NQG5; -.
DR PeptideAtlas; Q9NQG5; -.
DR PRIDE; Q9NQG5; -.
DR DNASU; 58490; -.
DR Ensembl; ENST00000373433; ENSP00000362532; ENSG00000101413.
DR GeneID; 58490; -.
DR KEGG; hsa:58490; -.
DR UCSC; uc002xho.4; human.
DR CTD; 58490; -.
DR GeneCards; GC20P036662; -.
DR H-InvDB; HIX0015799; -.
DR HGNC; HGNC:16209; RPRD1B.
DR MIM; 614694; gene.
DR neXtProt; NX_Q9NQG5; -.
DR PharmGKB; PA162402043; -.
DR eggNOG; NOG291577; -.
DR HOGENOM; HOG000007456; -.
DR HOVERGEN; HBG051177; -.
DR InParanoid; Q9NQG5; -.
DR KO; K15559; -.
DR OMA; ATQANSK; -.
DR OrthoDB; EOG7V1FRR; -.
DR PhylomeDB; Q9NQG5; -.
DR ChiTaRS; RPRD1B; human.
DR GenomeRNAi; 58490; -.
DR NextBio; 64964; -.
DR PRO; PR:Q9NQG5; -.
DR ArrayExpress; Q9NQG5; -.
DR Bgee; Q9NQG5; -.
DR CleanEx; HS_RPRD1B; -.
DR Genevestigator; Q9NQG5; -.
DR GO; GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IDA:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR006903; RNA_pol_II-bd.
DR Pfam; PF04818; CTD_bind; 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; Complete proteome; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 326 Regulation of nuclear pre-mRNA domain-
FT containing protein 1B.
FT /FTId=PRO_0000079441.
FT DOMAIN 1 133 CID.
FT MOD_RES 134 134 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT CONFLICT 21 21 Q -> H (in Ref. 5; AAH33629).
FT HELIX 6 15
FT HELIX 19 21
FT HELIX 22 32
FT HELIX 34 36
FT HELIX 37 50
FT TURN 53 55
FT HELIX 56 70
FT TURN 71 73
FT HELIX 76 82
FT HELIX 85 97
FT HELIX 102 113
FT HELIX 119 127
FT HELIX 177 202
FT HELIX 206 208
FT HELIX 211 216
FT HELIX 220 298
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
//
MIM
614694
*RECORD*
*FIELD* NO
614694
*FIELD* TI
*614694 REGULATION OF NUCLEAR PRE-mRNA DOMAIN-CONTAINING PROTEIN 1B; RPRD1B
;;CELL CYCLE-RELATED AND EXPRESSION-ELEVATED PROTEIN IN TUMOR; CREPT
read more*FIELD* TX
CLONING
Ni et al. (2011) stated that the deduced 326-amino acid RPRD1B protein
contains an N-terminal domain predicted to interact with phosphoserines
in the C-terminal domain of the catalytic subunit of RNA polymerase II
(POLR2A; 180660). Database analysis detected RPRD1B expression in all
adult and fetal tissues and cells examined.
Using RT-PCR and Northern blot analyses, Lu et al. (2012) found that
Crept was highly expressed during the early stages of mouse embryonic
development and that it was expressed in most adult tissues examined.
Immunohistochemical analysis localized CREPT in the nucleus of human
tumor cells.
GENE FUNCTION
Using affinity chromatography and tandem mass spectrometry with HEK293
cells to isolate RNA polymerase II-interacting proteins, Ni et al.
(2011) identified RPRD1A (610347), RPRD1B, and RPRD2 (614695), in
addition to RECQL5 (603781), GRINL1A (606485), and the putative RNA
polymerase II phosphatase RPAP2 (611476). RPRD1A and RPRD1B accompanied
RNA polymerase II from promoter regions to 3-prime UTRs during
transcription in vivo. RPRD1A and RPRD1B coprecipitated with the
C-terminal domain of POLR2A when it was serine phosphorylated, but not
when it was unphosphorylated. Overexpression of RPRD1A or RPRD1B reduced
the amount of serine-phosphorylated POLR2A associated with a target
gene.
Lu et al. (2012) found elevated expression of CREPT in several tumor
tissues compared with paired normal tissues. Overexpression of CREPT in
several human and mouse cell lines increased cell proliferation, colony
formation, and metastasis following injection into nude mice. Knockdown
of CREPT had the opposite effects. CREPT specifically increased
expression of several genes controlling the cell cycle and increased
expression of a cyclin D1 (CCND1; 168461) reporter. Immunoprecipitation
analysis of HEK293 cells revealed that CREPT interacted with RNA
polymerase II. Chromatin immunoprecipitation analysis showed that CREPT
promoted RNA polymerase II binding to both the cyclin D1 promoter and to
a region prior to the poly(A) site. CREPT also promoted loop formation,
suggesting that it may enhance RNA polymerase II recycling from the
terminator to the promoter region during transcription of the cyclin D1
gene.
MAPPING
Hartz (2012) mapped the RPRD1B gene to chromosome 20q11.23 based on an
alignment of the RPRD1B sequence (GenBank GENBANK AL117521) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 6/22/2012.
2. Lu, D.; Wu, Y.; Wang, Y.; Ren, F.; Wang, D.; Su, F.; Zhang, Y.;
Yang, X.; Jin, G.; Hao, X.; He, D.; Zhai, Y.; Irwin, D. M.; Hu, J.;
Sung, J. J. Y.; Yu, J.; Jia, B.; Chang, Z.: CREPT accelerates tumorigenesis
by regulating the transcription of cell-cycle-related genes. Cancer
Cell 21: 92-104, 2012.
3. Ni, Z.; Olsen, J. B.; Guo, X.; Zhong, G.; Ruan, E. D.; Marcon,
E.; Young, P.; Guo, H.; Li, J.; Moffat, J.; Emili, A.; Greenblatt,
J. F.: Control of the RNA polymerase II phosphorylation state in
promoter regions by CTD interaction domain-containing proteins RPRD1A
and RPRD1B. Transcription 2: 237-242, 2011.
*FIELD* CD
Patricia A. Hartz: 6/27/2012
*FIELD* ED
mgross: 06/27/2012
mgross: 6/27/2012
*RECORD*
*FIELD* NO
614694
*FIELD* TI
*614694 REGULATION OF NUCLEAR PRE-mRNA DOMAIN-CONTAINING PROTEIN 1B; RPRD1B
;;CELL CYCLE-RELATED AND EXPRESSION-ELEVATED PROTEIN IN TUMOR; CREPT
read more*FIELD* TX
CLONING
Ni et al. (2011) stated that the deduced 326-amino acid RPRD1B protein
contains an N-terminal domain predicted to interact with phosphoserines
in the C-terminal domain of the catalytic subunit of RNA polymerase II
(POLR2A; 180660). Database analysis detected RPRD1B expression in all
adult and fetal tissues and cells examined.
Using RT-PCR and Northern blot analyses, Lu et al. (2012) found that
Crept was highly expressed during the early stages of mouse embryonic
development and that it was expressed in most adult tissues examined.
Immunohistochemical analysis localized CREPT in the nucleus of human
tumor cells.
GENE FUNCTION
Using affinity chromatography and tandem mass spectrometry with HEK293
cells to isolate RNA polymerase II-interacting proteins, Ni et al.
(2011) identified RPRD1A (610347), RPRD1B, and RPRD2 (614695), in
addition to RECQL5 (603781), GRINL1A (606485), and the putative RNA
polymerase II phosphatase RPAP2 (611476). RPRD1A and RPRD1B accompanied
RNA polymerase II from promoter regions to 3-prime UTRs during
transcription in vivo. RPRD1A and RPRD1B coprecipitated with the
C-terminal domain of POLR2A when it was serine phosphorylated, but not
when it was unphosphorylated. Overexpression of RPRD1A or RPRD1B reduced
the amount of serine-phosphorylated POLR2A associated with a target
gene.
Lu et al. (2012) found elevated expression of CREPT in several tumor
tissues compared with paired normal tissues. Overexpression of CREPT in
several human and mouse cell lines increased cell proliferation, colony
formation, and metastasis following injection into nude mice. Knockdown
of CREPT had the opposite effects. CREPT specifically increased
expression of several genes controlling the cell cycle and increased
expression of a cyclin D1 (CCND1; 168461) reporter. Immunoprecipitation
analysis of HEK293 cells revealed that CREPT interacted with RNA
polymerase II. Chromatin immunoprecipitation analysis showed that CREPT
promoted RNA polymerase II binding to both the cyclin D1 promoter and to
a region prior to the poly(A) site. CREPT also promoted loop formation,
suggesting that it may enhance RNA polymerase II recycling from the
terminator to the promoter region during transcription of the cyclin D1
gene.
MAPPING
Hartz (2012) mapped the RPRD1B gene to chromosome 20q11.23 based on an
alignment of the RPRD1B sequence (GenBank GENBANK AL117521) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 6/22/2012.
2. Lu, D.; Wu, Y.; Wang, Y.; Ren, F.; Wang, D.; Su, F.; Zhang, Y.;
Yang, X.; Jin, G.; Hao, X.; He, D.; Zhai, Y.; Irwin, D. M.; Hu, J.;
Sung, J. J. Y.; Yu, J.; Jia, B.; Chang, Z.: CREPT accelerates tumorigenesis
by regulating the transcription of cell-cycle-related genes. Cancer
Cell 21: 92-104, 2012.
3. Ni, Z.; Olsen, J. B.; Guo, X.; Zhong, G.; Ruan, E. D.; Marcon,
E.; Young, P.; Guo, H.; Li, J.; Moffat, J.; Emili, A.; Greenblatt,
J. F.: Control of the RNA polymerase II phosphorylation state in
promoter regions by CTD interaction domain-containing proteins RPRD1A
and RPRD1B. Transcription 2: 237-242, 2011.
*FIELD* CD
Patricia A. Hartz: 6/27/2012
*FIELD* ED
mgross: 06/27/2012
mgross: 6/27/2012