RPAP3_MOUSE
ID RPAP3_MOUSE Reviewed; 660 AA.
AC Q9D706;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=RNA polymerase II-associated protein 3;
GN Name=Rpap3; Synonyms=D15Ertd682e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-120 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q9H6T3}.
CC -!- SUBUNIT: Tightly associated with the RNA polymerase II complex (By
CC similarity). Component of the R2TP complex composed at least of RUVBL1,
CC RUVBL2, RPAP3 and PIHD1 (By similarity). Component of the PAQosome
CC complex which is responsible for the biogenesis of several protein
CC complexes and which consists of R2TP complex members RUVBL1, RUVBL2,
CC RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1
CC as well as ASDURF, POLR2E and DNAAF10/WDR92 (By similarity). Interacts
CC with PIH1D1 (By similarity). Interacts with TSC1 and TSC2 (By
CC similarity). Interacts with PRPF8 and EFTUD2 in a ZNHIT2-dependent
CC manner (By similarity). {ECO:0000250|UniProtKB:Q9H6T3}.
CC -!- SIMILARITY: Belongs to the RPAP3 family. {ECO:0000305}.
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DR EMBL; AK009765; BAB26489.1; -; mRNA.
DR EMBL; AK169097; BAE40880.1; -; mRNA.
DR EMBL; BC004046; AAH04046.1; -; mRNA.
DR CCDS; CCDS27782.1; -.
DR RefSeq; NP_082279.1; NM_028003.2.
DR AlphaFoldDB; Q9D706; -.
DR SMR; Q9D706; -.
DR BioGRID; 215031; 21.
DR IntAct; Q9D706; 3.
DR MINT; Q9D706; -.
DR STRING; 10090.ENSMUSP00000023104; -.
DR iPTMnet; Q9D706; -.
DR PhosphoSitePlus; Q9D706; -.
DR EPD; Q9D706; -.
DR jPOST; Q9D706; -.
DR MaxQB; Q9D706; -.
DR PaxDb; Q9D706; -.
DR PeptideAtlas; Q9D706; -.
DR PRIDE; Q9D706; -.
DR ProteomicsDB; 300475; -.
DR Antibodypedia; 25352; 166 antibodies from 29 providers.
DR Ensembl; ENSMUST00000023104; ENSMUSP00000023104; ENSMUSG00000022466.
DR GeneID; 71919; -.
DR KEGG; mmu:71919; -.
DR UCSC; uc007xkv.1; mouse.
DR CTD; 79657; -.
DR MGI; MGI:1277218; Rpap3.
DR VEuPathDB; HostDB:ENSMUSG00000022466; -.
DR eggNOG; KOG4648; Eukaryota.
DR GeneTree; ENSGT00940000156749; -.
DR HOGENOM; CLU_023272_1_0_1; -.
DR InParanoid; Q9D706; -.
DR OMA; GTAQFHV; -.
DR OrthoDB; 1617844at2759; -.
DR PhylomeDB; Q9D706; -.
DR TreeFam; TF106243; -.
DR BioGRID-ORCS; 71919; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Rpap3; mouse.
DR PRO; PR:Q9D706; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D706; protein.
DR Bgee; ENSMUSG00000022466; Expressed in cleaving embryo and 244 other tissues.
DR Genevisible; Q9D706; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0097255; C:R2TP complex; ISO:MGI.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:MGI.
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 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 Acetylation; Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT CHAIN 2..660
FT /note="RNA polymerase II-associated protein 3"
FT /id="PRO_0000302795"
FT REPEAT 8..41
FT /note="TPR 1"
FT REPEAT 134..167
FT /note="TPR 2"
FT REPEAT 169..201
FT /note="TPR 3"
FT REPEAT 202..235
FT /note="TPR 4"
FT REPEAT 284..317
FT /note="TPR 5"
FT REPEAT 319..351
FT /note="TPR 6"
FT REPEAT 352..385
FT /note="TPR 7"
FT REGION 42..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT CROSSLNK 493
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
SQ SEQUENCE 660 AA; 74096 MW; 0D04AAD9F1D479CC CRC64;
MTSASKAVEL QLQVKHNAEE LQDFMRDLEH WEKDMKEKDL ELRRQGGVAE ENLPPIRNGN
FRKKKKKGKA KESSRKTKEE NTKNRIKSYD YDAWAKLDVD RILDELDKED STHDSLSQES
ESDEDGIRVD SQKALVLKEK GNKYFKQGKY DEAIECYTKG MDADPYNPVL PTNRASAYFR
LKKFAVAESD CNLAIALSRT YTKAYARRGA ARFALQKLED ARKDYEKVLE LEPDNFEATN
ELRKINQALT SKENSGPGAA AAAESKPAAG ESKPTGGQQG RQKAIAEKDL GNGFFKEGKY
EQAIECYTRG IAADRTNALL PANRAMAYLK IQRYEEAERD CTQAIVLDGS YSKAFARRGT
ARTFLGKINE AKQDFETVLL LEPGNKQAAT ELSRIKKELI EKGHWDDVFL DSTQRHHVVK
AVDNPPRGSP KALKKVFIEE TGNLIETVDA PDSSATVPES DRATAAVGTG TKKNPSEGVS
LPAGDRPRAK VLKIEAVSDT SAPQAQVGVK QDARQPGSEK ASVRAEQMPG QLAAAGLPPV
PANSFQLESD FRQLRSSPEM LYQYVKNIEP SLYPKLFQKN LDPDVFNQII KILHDFYIER
EKPALIFEVL ERLSQLRRFD MAVMFMSGPE RKLTNVLFNH LEKSDLKEDS VEELKKRYGG
