RPAP3_HUMAN
ID RPAP3_HUMAN Reviewed; 665 AA.
AC Q9H6T3; B4DRW9; Q6PHR5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=RNA polymerase II-associated protein 3;
GN Name=RPAP3;
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 3).
RC TISSUE=Tongue;
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 GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Blood;
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 [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP RNA POLYMERASE II COMPLEX.
RX PubMed=17643375; DOI=10.1016/j.molcel.2007.06.027;
RA Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C.,
RA Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B.,
RA Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.;
RT "Systematic analysis of the protein interaction network for the human
RT transcription machinery reveals the identity of the 7SK capping enzyme.";
RL Mol. Cell 27:262-274(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-116; SER-119; SER-121
RP AND SER-481, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
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 [8]
RP INTERACTION WITH PIH1D1.
RX PubMed=21078300; DOI=10.1016/j.bbrc.2010.11.031;
RA Inoue M., Saeki M., Egusa H., Niwa H., Kamisaki Y.;
RT "PIH1D1, a subunit of R2TP complex, inhibits doxorubicin-induced
RT apoptosis.";
RL Biochem. Biophys. Res. Commun. 403:340-344(2010).
RN [9]
RP IDENTIFICATION IN THE R2TP COMPLEX.
RX PubMed=20864032; DOI=10.1016/j.molcel.2010.08.037;
RA Horejsi Z., Takai H., Adelman C.A., Collis S.J., Flynn H., Maslen S.,
RA Skehel J.M., de Lange T., Boulton S.J.;
RT "CK2 phospho-dependent binding of R2TP complex to TEL2 is essential for
RT mTOR and SMG1 stability.";
RL Mol. Cell 39:839-850(2010).
RN [10]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-119 AND SER-121, AND
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [18]
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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
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: Forms an interface between the RNA polymerase II enzyme and
CC chaperone/scaffolding protein, suggesting that it is required to
CC connect RNA polymerase II to regulators of protein complex formation.
CC {ECO:0000269|PubMed:17643375}.
CC -!- SUBUNIT: Tightly associated with the RNA polymerase II complex
CC (PubMed:17643375). Component of the R2TP complex composed at least of
CC RUVBL1, RUVBL2, RPAP3 and PIHD1 (PubMed:20864032). Component of the
CC PAQosome complex which is responsible for the biogenesis of several
CC protein complexes and which consists of R2TP complex members RUVBL1,
CC RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT
CC and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92 (PubMed:31738558).
CC Interacts with PIH1D1 (PubMed:21078300). Interacts with TSC1 and TSC2
CC (PubMed:28561026). Interacts with PRPF8 and EFTUD2 in a ZNHIT2-
CC dependent manner (PubMed:28561026). {ECO:0000269|PubMed:17643375,
CC ECO:0000269|PubMed:20864032, ECO:0000269|PubMed:21078300,
CC ECO:0000269|PubMed:28561026, ECO:0000269|PubMed:31738558}.
CC -!- INTERACTION:
CC Q9H6T3; Q96MX6: DNAAF10; NbExp=5; IntAct=EBI-356928, EBI-2434101;
CC Q9H6T3; P07900: HSP90AA1; NbExp=6; IntAct=EBI-356928, EBI-296047;
CC Q9H6T3; Q9UHV9: PFDN2; NbExp=2; IntAct=EBI-356928, EBI-359873;
CC Q9H6T3; P54274: TERF1; NbExp=2; IntAct=EBI-356928, EBI-710997;
CC Q9H6T3; O94763: URI1; NbExp=2; IntAct=EBI-356928, EBI-357067;
CC Q9H6T3; Q9UBK9: UXT; NbExp=2; IntAct=EBI-356928, EBI-357355;
CC Q9H6T3; Q98140: ORF24; Xeno; NbExp=2; IntAct=EBI-356928, EBI-14033488;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H6T3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6T3-2; Sequence=VSP_027957;
CC Name=3;
CC IsoId=Q9H6T3-3; Sequence=VSP_044882;
CC -!- SIMILARITY: Belongs to the RPAP3 family. {ECO:0000305}.
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DR EMBL; AK025561; BAB15170.1; -; mRNA.
DR EMBL; AK299465; BAG61431.1; -; mRNA.
DR EMBL; AC004241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW57938.1; -; Genomic_DNA.
DR EMBL; BC056415; AAH56415.1; -; mRNA.
DR CCDS; CCDS53782.1; -. [Q9H6T3-3]
DR CCDS; CCDS53783.1; -. [Q9H6T3-2]
DR CCDS; CCDS8753.1; -. [Q9H6T3-1]
DR RefSeq; NP_001139547.1; NM_001146075.1. [Q9H6T3-2]
DR RefSeq; NP_001139548.1; NM_001146076.1. [Q9H6T3-3]
DR RefSeq; NP_078880.2; NM_024604.2. [Q9H6T3-1]
DR PDB; 4CGV; X-ray; 2.54 A; A/B/C/D=120-255.
DR PDB; 4CGW; X-ray; 3.00 A; A/B=265-381.
DR PDB; 6EZ4; NMR; -; A=535-665.
DR PDB; 6FD7; NMR; -; A=133-255.
DR PDB; 6FDP; NMR; -; A=281-395.
DR PDB; 6FDT; NMR; -; A=281-396.
DR PDB; 6FM8; X-ray; 1.78 A; A=576-625.
DR PDB; 6FO1; EM; 3.57 A; G=1-665.
DR PDB; 6GXZ; X-ray; 2.96 A; A/C=281-445.
DR PDB; 6ZBK; X-ray; 1.49 A; A=133-255.
DR PDBsum; 4CGV; -.
DR PDBsum; 4CGW; -.
DR PDBsum; 6EZ4; -.
DR PDBsum; 6FD7; -.
DR PDBsum; 6FDP; -.
DR PDBsum; 6FDT; -.
DR PDBsum; 6FM8; -.
DR PDBsum; 6FO1; -.
DR PDBsum; 6GXZ; -.
DR PDBsum; 6ZBK; -.
DR AlphaFoldDB; Q9H6T3; -.
DR SMR; Q9H6T3; -.
DR BioGRID; 122783; 155.
DR ComplexPortal; CPX-6143; R2TP core co-chaperone complex.
DR ComplexPortal; CPX-6153; R2T co-chaperone complex. [Q9H6T3-2]
DR DIP; DIP-47508N; -.
DR IntAct; Q9H6T3; 78.
DR MINT; Q9H6T3; -.
DR STRING; 9606.ENSP00000005386; -.
DR GlyGen; Q9H6T3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H6T3; -.
DR MetOSite; Q9H6T3; -.
DR PhosphoSitePlus; Q9H6T3; -.
DR BioMuta; RPAP3; -.
DR DMDM; 158564023; -.
DR EPD; Q9H6T3; -.
DR jPOST; Q9H6T3; -.
DR MassIVE; Q9H6T3; -.
DR MaxQB; Q9H6T3; -.
DR PaxDb; Q9H6T3; -.
DR PeptideAtlas; Q9H6T3; -.
DR PRIDE; Q9H6T3; -.
DR ProteomicsDB; 81032; -. [Q9H6T3-1]
DR ProteomicsDB; 81033; -. [Q9H6T3-2]
DR Antibodypedia; 25352; 166 antibodies from 29 providers.
DR DNASU; 79657; -.
DR Ensembl; ENST00000005386.8; ENSP00000005386.3; ENSG00000005175.10. [Q9H6T3-1]
DR Ensembl; ENST00000380650.4; ENSP00000370024.4; ENSG00000005175.10. [Q9H6T3-2]
DR Ensembl; ENST00000432584.7; ENSP00000401823.3; ENSG00000005175.10. [Q9H6T3-3]
DR GeneID; 79657; -.
DR KEGG; hsa:79657; -.
DR MANE-Select; ENST00000005386.8; ENSP00000005386.3; NM_024604.3; NP_078880.2.
DR UCSC; uc001rpr.4; human. [Q9H6T3-1]
DR CTD; 79657; -.
DR GeneCards; RPAP3; -.
DR HGNC; HGNC:26151; RPAP3.
DR HPA; ENSG00000005175; Low tissue specificity.
DR MIM; 611477; gene.
DR neXtProt; NX_Q9H6T3; -.
DR OpenTargets; ENSG00000005175; -.
DR PharmGKB; PA162401982; -.
DR VEuPathDB; HostDB:ENSG00000005175; -.
DR eggNOG; KOG4648; Eukaryota.
DR GeneTree; ENSGT00940000156749; -.
DR HOGENOM; CLU_023272_1_0_1; -.
DR InParanoid; Q9H6T3; -.
DR OMA; GTAQFHV; -.
DR OrthoDB; 1617844at2759; -.
DR PhylomeDB; Q9H6T3; -.
DR TreeFam; TF106243; -.
DR PathwayCommons; Q9H6T3; -.
DR SignaLink; Q9H6T3; -.
DR BioGRID-ORCS; 79657; 592 hits in 1091 CRISPR screens.
DR ChiTaRS; RPAP3; human.
DR GenomeRNAi; 79657; -.
DR Pharos; Q9H6T3; Tbio.
DR PRO; PR:Q9H6T3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H6T3; protein.
DR Bgee; ENSG00000005175; Expressed in monocyte and 190 other tissues.
DR Genevisible; Q9H6T3; HS.
DR GO; GO:0101031; C:chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0097255; C:R2TP complex; IDA:UniProtKB.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IPI:ComplexPortal.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR025986; RPAP3-like_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13877; RPAP3_C; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13176; TPR_7; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..665
FT /note="RNA polymerase II-associated protein 3"
FT /id="PRO_0000302794"
FT REPEAT 8..41
FT /note="TPR 1"
FT REPEAT 133..166
FT /note="TPR 2"
FT REPEAT 168..200
FT /note="TPR 3"
FT REPEAT 201..234
FT /note="TPR 4"
FT REPEAT 282..315
FT /note="TPR 5"
FT REPEAT 317..349
FT /note="TPR 6"
FT REPEAT 350..383
FT /note="TPR 7"
FT REGION 37..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044882"
FT VAR_SEQ 396..429
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027957"
FT VARIANT 564
FT /note="D -> Y (in dbSNP:rs11168196)"
FT /id="VAR_057354"
FT CONFLICT 484
FT /note="D -> V (in Ref. 1; BAB15170)"
FT /evidence="ECO:0000305"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:6ZBK"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:4CGW"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:4CGW"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:6GXZ"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:6GXZ"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:6GXZ"
FT HELIX 332..345
FT /evidence="ECO:0007829|PDB:6GXZ"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:6GXZ"
FT HELIX 366..379
FT /evidence="ECO:0007829|PDB:6GXZ"
FT HELIX 384..399
FT /evidence="ECO:0007829|PDB:6GXZ"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:6GXZ"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6GXZ"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:6GXZ"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:6GXZ"
FT HELIX 549..559
FT /evidence="ECO:0007829|PDB:6EZ4"
FT HELIX 563..572
FT /evidence="ECO:0007829|PDB:6EZ4"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:6EZ4"
FT HELIX 580..585
FT /evidence="ECO:0007829|PDB:6FM8"
FT HELIX 588..604
FT /evidence="ECO:0007829|PDB:6FM8"
FT HELIX 609..623
FT /evidence="ECO:0007829|PDB:6FM8"
FT HELIX 624..630
FT /evidence="ECO:0007829|PDB:6EZ4"
FT HELIX 633..648
FT /evidence="ECO:0007829|PDB:6EZ4"
FT HELIX 654..664
FT /evidence="ECO:0007829|PDB:6EZ4"
SQ SEQUENCE 665 AA; 75719 MW; 70D5A965E4F1EE35 CRC64;
MTSANKAIEL QLQVKQNAEE LQDFMRDLEN WEKDIKQKDM ELRRQNGVPE ENLPPIRNGN
FRKKKKGKAK ESSKKTREEN TKNRIKSYDY EAWAKLDVDR ILDELDKDDS THESLSQESE
SEEDGIHVDS QKALVLKEKG NKYFKQGKYD EAIDCYTKGM DADPYNPVLP TNRASAYFRL
KKFAVAESDC NLAVALNRSY TKAYSRRGAA RFALQKLEEA KKDYERVLEL EPNNFEATNE
LRKISQALAS KENSYPKEAD IVIKSTEGER KQIEAQQNKQ QAISEKDRGN GFFKEGKYER
AIECYTRGIA ADGANALLPA NRAMAYLKIQ KYEEAEKDCT QAILLDGSYS KAFARRGTAR
TFLGKLNEAK QDFETVLLLE PGNKQAVTEL SKIKKELIEK GHWDDVFLDS TQRQNVVKPI
DNPPHPGSTK PLKKVIIEET GNLIQTIDVP DSTTAAAPEN NPINLANVIA ATGTTSKKNS
SQDDLFPTSD TPRAKVLKIE EVSDTSSLQP QASLKQDVCQ SYSEKMPIEI EQKPAQFATT
VLPPIPANSF QLESDFRQLK SSPDMLYQYL KQIEPSLYPK LFQKNLDPDV FNQIVKILHD
FYIEKEKPLL IFEILQRLSE LKRFDMAVMF MSETEKKIAR ALFNHIDKSG LKDSSVEELK
KRYGG
