RMP_HUMAN
ID RMP_HUMAN Reviewed; 535 AA.
AC O94763; A8K805; H7BY42; Q8TC23; Q9UNU3;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Unconventional prefoldin RPB5 interactor 1;
DE AltName: Full=Protein NNX3;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 19;
DE AltName: Full=RNA polymerase II subunit 5-mediating protein;
DE Short=RPB5-mediating protein;
GN Name=URI1; Synonyms=C19orf2, NNX3, PPP1R19, RMP, URI;
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] (ISOFORM 2), PHOSPHORYLATION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9878255; DOI=10.1006/geno.1998.5609;
RA Van Leuven F., Torrekens S., Moechars D., Hilliker C., Buellens M.,
RA Bollen M., Delabie J.;
RT "Molecular cloning of a gene on chromosome 19q12 coding for a novel
RT intracellular protein: analysis of expression in human and mouse tissues
RT and in human tumor cells, particularly Reed-Sternberg cells in Hodgkin
RT disease.";
RL Genomics 54:511-520(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH POLR2E, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Hepatoma;
RX PubMed=9819440; DOI=10.1128/mcb.18.12.7546;
RA Dorjsuren D., Lin Y., Wei W., Yamashita T., Nomura T., Hayashi N.,
RA Murakami S.;
RT "RMP, a novel RNA polymerase II subunit 5-interacting protein, counteracts
RT transactivation by hepatitis B virus X protein.";
RL Mol. Cell. Biol. 18:7546-7555(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 FUNCTION IN TRANSCRIPTIONAL REGULATION, AND INTERACTION WITH GTF2F1 AND
RP GTF2F2.
RX PubMed=12737519; DOI=10.1038/sj.cr.7290155;
RA Wei W., Gu J.X., Zhu C.Q., Sun F.Y., Dorjsuren D., Lin Y., Murakami S.;
RT "Interaction with general transcription factor IIF (TFIIF) is required for
RT the suppression of activated transcription by RPB5-mediating protein
RT (RMP).";
RL Cell Res. 13:111-120(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH PFDN2; PFDN4; POLR2E; RUVBL2; RUVBL1 AND
RP STAP1.
RX PubMed=14615539; DOI=10.1126/science.1088401;
RA Gstaiger M., Luke B., Hess D., Oakeley E.J., Wirbelauer C., Blondel M.,
RA Vigneron M., Peter M., Krek W.;
RT "Control of nutrient-sensitive transcription programs by the unconventional
RT prefoldin URI.";
RL Science 302:1208-1212(2003).
RN [8]
RP FUNCTION, INTERACTION WITH DMAP1, AND SUBCELLULAR LOCATION.
RX PubMed=15367675; DOI=10.1128/mcb.24.19.8556-8566.2004;
RA Delgermaa L., Hayashi N., Dorjsuren D., Nomura T., Thuy le T.T.,
RA Murakami S.;
RT "Subcellular localization of RPB5-mediating protein and its putative
RT functional partner.";
RL Mol. Cell. Biol. 24:8556-8566(2004).
RN [9]
RP FUNCTION IN DEPHOSPHORYLATION OF PPP1CC, PHOSPHORYLATION AT SER-372 BY
RP RPS6KB1, MUTAGENESIS OF SER-372, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010;
RA Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,
RA Aebersold R., Hess D., Krek W.;
RT "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
RT activates a negative feedback program that counters S6K1 survival
RT signaling.";
RL Mol. Cell 28:28-40(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, 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 [11]
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 [12]
RP FUNCTION, INTERACTION WITH PPP1CC, PHOSPHORYLATION AT SER-372, MUTAGENESIS
RP OF SER-372, AND TISSUE SPECIFICITY.
RX PubMed=21397856; DOI=10.1016/j.ccr.2011.01.019;
RA Theurillat J.P., Metzler S.C., Henzi N., Djouder N., Helbling M.,
RA Zimmermann A.K., Jacob F., Soltermann A., Caduff R.,
RA Heinzelmann-Schwarz V., Moch H., Krek W.;
RT "URI is an oncogene amplified in ovarian cancer cells and is required for
RT their survival.";
RL Cancer Cell 19:317-332(2011).
RN [13]
RP FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH UXT,
RP PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=21730289; DOI=10.1128/mcb.05429-11;
RA Mita P., Savas J.N., Djouder N., Yates J.R. III, Ha S., Ruoff R.,
RA Schafler E.D., Nwachukwu J.C., Tanese N., Cowan N.J., Zavadil J.,
RA Garabedian M.J., Logan S.K.;
RT "Regulation of androgen receptor-mediated transcription by RPB5 binding
RT protein URI/RMP.";
RL Mol. Cell. Biol. 31:3639-3652(2011).
RN [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372; THR-373 AND SER-442, 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 [17]
RP INTERACTION WITH TSC1; TSC2; PRPF8 AND EFTUD2.
RX PubMed=28561026; DOI=10.1038/ncomms15615;
RA Cloutier P., Poitras C., Durand M., Hekmat O., Fiola-Masson E.,
RA Bouchard A., Faubert D., Chabot B., Coulombe B.;
RT "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2
RT to regulate assembly of U5 small nuclear ribonucleoprotein.";
RL Nat. Commun. 8:15615-15615(2017).
RN [18]
RP IDENTIFICATION IN THE PAQOSOME COMPLEX.
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: Involved in gene transcription regulation. Acts as a
CC transcriptional repressor in concert with the corepressor UXT to
CC regulate androgen receptor (AR) transcription. May act as a tumor
CC suppressor to repress AR-mediated gene transcription and to inhibit
CC anchorage-independent growth in prostate cancer cells. Required for
CC cell survival in ovarian cancer cells. Together with UXT, associates
CC with chromatin to the NKX3-1 promoter region. Antagonizes
CC transcriptional modulation via hepatitis B virus X protein.
CC -!- FUNCTION: Plays a central role in maintaining S6K1 signaling and BAD
CC phosphorylation under normal growth conditions thereby protecting cells
CC from potential deleterious effects of sustained S6K1 signaling. The
CC URI1-PPP1CC complex acts as a central component of a negative feedback
CC mechanism that counteracts excessive S6K1 survival signaling to BAD in
CC response to growth factors. Mediates inhibition of PPP1CC phosphatase
CC activity in mitochondria. Coordinates the regulation of nutrient-
CC sensitive gene expression availability in a mTOR-dependent manner.
CC Seems to be a scaffolding protein able to assemble a prefoldin-like
CC complex that contains PFDs and proteins with roles in transcription and
CC ubiquitination.
CC -!- SUBUNIT: Homodimer. Component of the PAQosome complex which is
CC responsible for the biogenesis of several protein complexes and which
CC consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI
CC complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF,
CC POLR2E and DNAAF10/WDR92 (PubMed:31738558). Interacts with POLR2E/RPB5,
CC RUVBL2 AND RUVBL1 (PubMed:14615539, PubMed:9819440). Interacts with
CC PFDN2, PFDN4 and STAP1; the interactions are phosphorylation-dependent
CC and occur in a growth-dependent manner in the mitochondrion
CC (PubMed:14615539). Interacts with UXT (PubMed:21730289). Interacts with
CC PPP1CC; the interaction is phosphorylation-dependent and occurs in a
CC growth factor-dependent manner (PubMed:21397856). Interacts (via the
CC middle C-terminal region) with GTF2F1 and GTF2F2 (PubMed:12737519).
CC Interacts with DMAP1 (PubMed:15367675). Interacts with TSC1 and TSC2
CC (PubMed:28561026). Interacts with PRPF8 and EFTUD2 in a ZNHIT2-
CC dependent manner (PubMed:28561026). {ECO:0000269|PubMed:12737519,
CC ECO:0000269|PubMed:14615539, ECO:0000269|PubMed:15367675,
CC ECO:0000269|PubMed:21397856, ECO:0000269|PubMed:21730289,
CC ECO:0000269|PubMed:28561026, ECO:0000269|PubMed:31738558,
CC ECO:0000269|PubMed:9819440}.
CC -!- INTERACTION:
CC O94763; P35269: GTF2F1; NbExp=3; IntAct=EBI-357067, EBI-457886;
CC O94763; P13984: GTF2F2; NbExp=4; IntAct=EBI-357067, EBI-1030560;
CC O94763; O15294: OGT; NbExp=10; IntAct=EBI-357067, EBI-539828;
CC O94763; Q9UHV9: PFDN2; NbExp=2; IntAct=EBI-357067, EBI-359873;
CC O94763; P19388: POLR2E; NbExp=3; IntAct=EBI-357067, EBI-395189;
CC O94763; P36873: PPP1CC; NbExp=17; IntAct=EBI-357067, EBI-356283;
CC O94763; Q9H6T3: RPAP3; NbExp=2; IntAct=EBI-357067, EBI-356928;
CC O94763; P30561: Ahr; Xeno; NbExp=2; IntAct=EBI-357067, EBI-78863;
CC O94763; P19785: Esr1; Xeno; NbExp=2; IntAct=EBI-357067, EBI-346765;
CC O94763-1; O15294: OGT; NbExp=3; IntAct=EBI-12590720, EBI-539828;
CC O94763-1; P36873: PPP1CC; NbExp=8; IntAct=EBI-12590720, EBI-356283;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion. Cell
CC projection, dendrite {ECO:0000250}. Note=Colocalizes with PFDN2, PFDN4,
CC PPP1CC, RPS6KB1 and STAP1 at mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O94763-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94763-2; Sequence=VSP_032773;
CC Name=3;
CC IsoId=O94763-3; Sequence=VSP_042259;
CC Name=4;
CC IsoId=O94763-4; Sequence=VSP_044769, VSP_044770;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in ovarian cancers (at
CC protein level). Expressed strongly in skeletal muscle. Expressed weakly
CC in brain, heart, pancreas and in prostate epithelial cells.
CC {ECO:0000269|PubMed:21397856, ECO:0000269|PubMed:21730289,
CC ECO:0000269|PubMed:9819440, ECO:0000269|PubMed:9878255}.
CC -!- PTM: Phosphorylated. Phosphorylation occurs essentially on serine
CC residues. Phosphorylation occurs in response to androgen treatment in
CC prostate cancer cells in a mTOR-dependent manner. Phosphorylated;
CC hyperhosphorylated in mitochondria in a mTORC-dependent signaling
CC pathway. Phosphorylated at Ser-372 by RPS6KB1 in a growth factor- and
CC rapamycin-dependent manner. S6K1-mediated mitochondrial phosphorylation
CC at Ser-372 disrupts the URI1-PPP1CC complex in the mitochondrion,
CC relieves PPP1CC phosphatase inhibition activity and hence engages a
CC negative feedback diminishing RPS6KB1 kinase activity, preventing
CC sustained S6K1-dependent signaling. {ECO:0000269|PubMed:17936702,
CC ECO:0000269|PubMed:21397856, ECO:0000269|PubMed:21730289,
CC ECO:0000269|PubMed:9878255}.
CC -!- SIMILARITY: Belongs to the RNA polymerase II subunit 5-mediating
CC protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26184.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF091095; AAD08679.1; -; mRNA.
DR EMBL; AB006572; BAA34781.1; -; mRNA.
DR EMBL; AK292170; BAF84859.1; -; mRNA.
DR EMBL; AC008507; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC026184; AAH26184.2; ALT_INIT; mRNA.
DR CCDS; CCDS12420.1; -. [O94763-1]
DR CCDS; CCDS58658.1; -. [O94763-4]
DR RefSeq; NP_001239570.1; NM_001252641.1. [O94763-4]
DR RefSeq; NP_003787.2; NM_003796.3. [O94763-1]
DR AlphaFoldDB; O94763; -.
DR SMR; O94763; -.
DR BioGRID; 114264; 139.
DR ComplexPortal; CPX-6144; URI1 prefoldin co-chaperone complex.
DR CORUM; O94763; -.
DR IntAct; O94763; 65.
DR MINT; O94763; -.
DR STRING; 9606.ENSP00000376097; -.
DR GlyGen; O94763; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94763; -.
DR MetOSite; O94763; -.
DR PhosphoSitePlus; O94763; -.
DR SwissPalm; O94763; -.
DR BioMuta; URI1; -.
DR EPD; O94763; -.
DR jPOST; O94763; -.
DR MassIVE; O94763; -.
DR MaxQB; O94763; -.
DR PaxDb; O94763; -.
DR PeptideAtlas; O94763; -.
DR PRIDE; O94763; -.
DR ProteomicsDB; 43496; -.
DR ProteomicsDB; 50428; -. [O94763-1]
DR ProteomicsDB; 50429; -. [O94763-2]
DR ProteomicsDB; 50430; -. [O94763-3]
DR Antibodypedia; 28848; 230 antibodies from 32 providers.
DR DNASU; 8725; -.
DR Ensembl; ENST00000360605.8; ENSP00000353817.4; ENSG00000105176.18. [O94763-4]
DR Ensembl; ENST00000392271.6; ENSP00000376097.2; ENSG00000105176.18. [O94763-1]
DR GeneID; 8725; -.
DR KEGG; hsa:8725; -.
DR MANE-Select; ENST00000392271.6; ENSP00000376097.2; NM_003796.3; NP_003787.2.
DR UCSC; uc002nsq.4; human. [O94763-1]
DR CTD; 8725; -.
DR DisGeNET; 8725; -.
DR GeneCards; URI1; -.
DR HGNC; HGNC:13236; URI1.
DR HPA; ENSG00000105176; Low tissue specificity.
DR MIM; 603494; gene.
DR neXtProt; NX_O94763; -.
DR OpenTargets; ENSG00000105176; -.
DR PharmGKB; PA134962614; -.
DR VEuPathDB; HostDB:ENSG00000105176; -.
DR eggNOG; KOG3130; Eukaryota.
DR GeneTree; ENSGT00390000002362; -.
DR HOGENOM; CLU_029262_0_0_1; -.
DR InParanoid; O94763; -.
DR OMA; VEKDPMP; -.
DR OrthoDB; 964566at2759; -.
DR PhylomeDB; O94763; -.
DR TreeFam; TF332816; -.
DR PathwayCommons; O94763; -.
DR SignaLink; O94763; -.
DR SIGNOR; O94763; -.
DR BioGRID-ORCS; 8725; 681 hits in 1084 CRISPR screens.
DR ChiTaRS; URI1; human.
DR GeneWiki; C19orf2; -.
DR GenomeRNAi; 8725; -.
DR Pharos; O94763; Tbio.
DR PRO; PR:O94763; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O94763; protein.
DR Bgee; ENSG00000105176; Expressed in adrenal tissue and 204 other tissues.
DR ExpressionAtlas; O94763; baseline and differential.
DR Genevisible; O94763; HS.
DR GO; GO:0101031; C:chaperone complex; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IPI:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0019212; F:phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0001558; P:regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR Pfam; PF02996; Prefoldin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Cytoplasm;
KW Mitochondrion; Nucleus; Oncogene; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..535
FT /note="Unconventional prefoldin RPB5 interactor 1"
FT /id="PRO_0000097365"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..322
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 372
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000269|PubMed:17936702,
FT ECO:0000269|PubMed:21397856, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 373
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9878255"
FT /id="VSP_032773"
FT VAR_SEQ 1..51
FT /note="MEAPTVETPPDPSPPSAPAPALVPLRAPDVARLREEQEKVVTNCQERIQHW
FT -> MRLGNVDFTLGSNVPCVYLVFSVNR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9819440"
FT /id="VSP_042259"
FT VAR_SEQ 1..39
FT /note="MEAPTVETPPDPSPPSAPAPALVPLRAPDVARLREEQEK -> MTTWSSLQG
FT SHVSKRALAYAL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044769"
FT VAR_SEQ 476..535
FT /note="AFSGTVIEKEFVSPSLTPPPAIAHPALPTIPERKEVLLEASEETGKRVSKFK
FT AARLQQKD -> VLRLVGYSRNLAPLNVIL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044770"
FT VARIANT 22
FT /note="L -> P (in dbSNP:rs189187)"
FT /id="VAR_056978"
FT MUTAGEN 372
FT /note="S->A: Does not lead to dissociation of the URI1-
FT PPP1CC complex. Enhances phosphorylation of RPS6KB1 after
FT IGF1 stimulation. Confers a cell survival increase."
FT /evidence="ECO:0000269|PubMed:17936702,
FT ECO:0000269|PubMed:21397856"
FT CONFLICT 7
FT /note="E -> G (in Ref. 3; BAF84859)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="D -> N (in Ref. 5; AAH26184)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="Missing (in Ref. 1; AAD08679, 2; BAA34781, 3;
FT BAF84859 and 5; AAH26184)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="D -> E (in Ref. 3; BAF84859)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="R -> G (in Ref. 2; BAA34781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59832 MW; DBB046A392E3C752 CRC64;
MEAPTVETPP DPSPPSAPAP ALVPLRAPDV ARLREEQEKV VTNCQERIQH WKKVDNDYNA
LRERLSTLPD KLSYNIMVPF GPFAFMPGKL VHTNEVTVLL GDNWFAKCSA KQAVGLVEHR
KEHVRKTIDD LKKVMKNFES RVEFTEDLQK MSDAAGDIVD IREEIKCDFE FKAKHRIAHK
PHSKPKTSDI FEADIANDVK SKDLLADKEL WARLEELERQ EELLGELDSK PDTVIANGED
TTSSEEEKED RNTNVNAMHQ VTDSHTPCHK DVASSEPFSG QVNSQLNCSV NGSSSYHSDD
DDDDDDDDDD DNIDDDDGDN DHEALGVGDN SIPTIYFSHT VEPKRVRINT GKNTTLKFSE
KKEEAKRKRK NSTGSGHSAQ ELPTIRTPAD IYRAFVDVVN GEYVPRKSIL KSRSRENSVC
SDTSESSAAE FDDRRGVLRS ISCEEATCSD TSESILEEEP QENQKKLLPL SVTPEAFSGT
VIEKEFVSPS LTPPPAIAHP ALPTIPERKE VLLEASEETG KRVSKFKAAR LQQKD
