PDRG1_HUMAN
ID PDRG1_HUMAN Reviewed; 133 AA.
AC Q9NUG6; B2R511; Q96GP3; Q9BUW8;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=p53 and DNA damage-regulated protein 1;
GN Name=PDRG1; Synonyms=C20orf126, PDRG;
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], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14562055; DOI=10.1038/sj.onc.1207010;
RA Luo X., Huang Y., Sheikh M.S.;
RT "Cloning and characterization of a novel gene PDRG that is differentially
RT regulated by p53 and ultraviolet radiation.";
RL Oncogene 22:7247-7257(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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=Brain, and Muscle;
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].
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 [7]
RP IDENTIFICATION IN THE PAQOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=31738558; DOI=10.1021/acs.jproteome.9b00599;
RA Cloutier P., Poitras C., Faubert D., Bouchard A., Blanchette M.,
RA Gauthier M.S., Coulombe B.;
RT "Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subunit of the
RT PAQosome.";
RL J. Proteome Res. 19:18-27(2020).
CC -!- FUNCTION: May play a role in chaperone-mediated protein folding.
CC {ECO:0000305}.
CC -!- SUBUNIT: Component of the PAQosome complex which is responsible for the
CC biogenesis of several protein complexes and which consists of R2TP
CC complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members
CC PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and
CC DNAAF10/WDR92. {ECO:0000269|PubMed:31738558}.
CC -!- INTERACTION:
CC Q9NUG6; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-307050, EBI-742887;
CC Q9NUG6; Q9UHV9: PFDN2; NbExp=2; IntAct=EBI-307050, EBI-359873;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in normal testis and
CC exhibits reduced but detectable expression in other organs.
CC {ECO:0000269|PubMed:14562055}.
CC -!- INDUCTION: By UV irradiation and repressed by p53/TP53.
CC {ECO:0000269|PubMed:14562055}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY286301; AAP45329.1; -; mRNA.
DR EMBL; AK312021; BAG34958.1; -; mRNA.
DR EMBL; AL031658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76399.1; -; Genomic_DNA.
DR EMBL; BC001856; AAH01856.2; -; mRNA.
DR EMBL; BC009334; AAH09334.1; -; mRNA.
DR CCDS; CCDS13194.1; -.
DR RefSeq; NP_110442.1; NM_030815.2.
DR AlphaFoldDB; Q9NUG6; -.
DR SMR; Q9NUG6; -.
DR BioGRID; 123533; 115.
DR ComplexPortal; CPX-6144; URI1 prefoldin co-chaperone complex.
DR CORUM; Q9NUG6; -.
DR DIP; DIP-27568N; -.
DR IntAct; Q9NUG6; 30.
DR MINT; Q9NUG6; -.
DR STRING; 9606.ENSP00000202017; -.
DR GlyGen; Q9NUG6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NUG6; -.
DR PhosphoSitePlus; Q9NUG6; -.
DR BioMuta; PDRG1; -.
DR DMDM; 24211602; -.
DR EPD; Q9NUG6; -.
DR jPOST; Q9NUG6; -.
DR MassIVE; Q9NUG6; -.
DR MaxQB; Q9NUG6; -.
DR PaxDb; Q9NUG6; -.
DR PeptideAtlas; Q9NUG6; -.
DR PRIDE; Q9NUG6; -.
DR ProteomicsDB; 82671; -.
DR TopDownProteomics; Q9NUG6; -.
DR Antibodypedia; 25293; 210 antibodies from 26 providers.
DR DNASU; 81572; -.
DR Ensembl; ENST00000202017.6; ENSP00000202017.4; ENSG00000088356.6.
DR GeneID; 81572; -.
DR KEGG; hsa:81572; -.
DR MANE-Select; ENST00000202017.6; ENSP00000202017.4; NM_030815.3; NP_110442.1.
DR UCSC; uc002wxd.4; human.
DR CTD; 81572; -.
DR DisGeNET; 81572; -.
DR GeneCards; PDRG1; -.
DR HGNC; HGNC:16119; PDRG1.
DR HPA; ENSG00000088356; Tissue enhanced (parathyroid).
DR MIM; 610789; gene.
DR neXtProt; NX_Q9NUG6; -.
DR OpenTargets; ENSG00000088356; -.
DR PharmGKB; PA25667; -.
DR VEuPathDB; HostDB:ENSG00000088356; -.
DR eggNOG; ENOG502S6V9; Eukaryota.
DR GeneTree; ENSGT00390000013253; -.
DR HOGENOM; CLU_132161_0_0_1; -.
DR InParanoid; Q9NUG6; -.
DR OMA; RQKCREA; -.
DR OrthoDB; 1630799at2759; -.
DR PhylomeDB; Q9NUG6; -.
DR TreeFam; TF329240; -.
DR PathwayCommons; Q9NUG6; -.
DR SignaLink; Q9NUG6; -.
DR BioGRID-ORCS; 81572; 741 hits in 1073 CRISPR screens.
DR GenomeRNAi; 81572; -.
DR Pharos; Q9NUG6; Tbio.
DR PRO; PR:Q9NUG6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NUG6; protein.
DR Bgee; ENSG00000088356; Expressed in pancreatic ductal cell and 185 other tissues.
DR ExpressionAtlas; Q9NUG6; baseline and differential.
DR Genevisible; Q9NUG6; HS.
DR GO; GO:0101031; C:chaperone complex; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IPI:ComplexPortal.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR InterPro; IPR030482; PDRG1.
DR InterPro; IPR002777; PFD_beta-like.
DR PANTHER; PTHR21162; PTHR21162; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..133
FT /note="p53 and DNA damage-regulated protein 1"
FT /id="PRO_0000058277"
SQ SEQUENCE 133 AA; 15511 MW; 13D3293D9724B46A CRC64;
MLSPEAERVL RYLVEVEELA EEVLADKRQI VDLDTKRNQN REGLRALQKD LSLSEDVMVC
FGNMFIKMPH PETKEMIEKD QDHLDKEIEK LRKQLKVKVN RLFEAQGKPE LKGFNLNPLN
QDELKALKVI LKG