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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}.
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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
 
 
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