RPAP1_MOUSE
ID RPAP1_MOUSE Reviewed; 1409 AA.
AC Q80TE0; A2AQ24; Q148U0; Q148U1; Q3TJ48; Q3TLZ5; Q3TTA6; Q80UT8; Q91VM0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=RNA polymerase II-associated protein 1;
GN Name=Rpap1; Synonyms=Kiaa1403;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, Placenta, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=129/Sv X 129SvCp, C57BL/6J, and FVB/N;
RC TISSUE=Embryonic stem cell, and 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen, and
RC 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 Required for interaction of the RNA polymerase II complex with
CC acetylated histone H3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of an RNA polymerase II complex that contains POLR2A,
CC POLR2B, POLR2C, POLR2D, POLR2E, POLR2F, POLR2G, POLR2H, POLR2I, POLR2J,
CC POLR2K, POLR2L, RPAP1, FCP1 plus the general transcription factors
CC TFIIB and TFIIF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80TE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TE0-2; Sequence=VSP_024682, VSP_024683;
CC -!- SIMILARITY: Belongs to the RPAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65787.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122505; BAC65787.1; ALT_INIT; mRNA.
DR EMBL; AK161487; BAE36419.1; -; mRNA.
DR EMBL; AK166232; BAE38647.1; -; mRNA.
DR EMBL; AK167589; BAE39647.1; -; mRNA.
DR EMBL; AL844536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012218; AAH12218.1; -; mRNA.
DR EMBL; BC051680; AAH51680.1; -; mRNA.
DR EMBL; BC117973; AAI17974.1; -; mRNA.
DR EMBL; BC117974; AAI17975.1; -; mRNA.
DR CCDS; CCDS16610.1; -. [Q80TE0-1]
DR RefSeq; NP_001157173.1; NM_001163701.1. [Q80TE0-1]
DR RefSeq; NP_796268.3; NM_177294.5. [Q80TE0-1]
DR RefSeq; XP_006500184.1; XM_006500121.3. [Q80TE0-1]
DR RefSeq; XP_011238061.1; XM_011239759.2. [Q80TE0-1]
DR AlphaFoldDB; Q80TE0; -.
DR SMR; Q80TE0; -.
DR BioGRID; 213120; 10.
DR IntAct; Q80TE0; 1.
DR STRING; 10090.ENSMUSP00000097127; -.
DR iPTMnet; Q80TE0; -.
DR PhosphoSitePlus; Q80TE0; -.
DR EPD; Q80TE0; -.
DR MaxQB; Q80TE0; -.
DR PaxDb; Q80TE0; -.
DR PeptideAtlas; Q80TE0; -.
DR PRIDE; Q80TE0; -.
DR ProteomicsDB; 300514; -. [Q80TE0-1]
DR ProteomicsDB; 300515; -. [Q80TE0-2]
DR Antibodypedia; 42079; 129 antibodies from 25 providers.
DR DNASU; 68925; -.
DR Ensembl; ENSMUST00000048493; ENSMUSP00000037275; ENSMUSG00000034032. [Q80TE0-1]
DR Ensembl; ENSMUST00000099529; ENSMUSP00000097127; ENSMUSG00000034032. [Q80TE0-1]
DR Ensembl; ENSMUST00000110793; ENSMUSP00000106420; ENSMUSG00000034032. [Q80TE0-1]
DR GeneID; 68925; -.
DR KEGG; mmu:68925; -.
DR UCSC; uc008luk.2; mouse. [Q80TE0-1]
DR UCSC; uc008lun.2; mouse. [Q80TE0-2]
DR CTD; 26015; -.
DR MGI; MGI:1916175; Rpap1.
DR VEuPathDB; HostDB:ENSMUSG00000034032; -.
DR eggNOG; KOG1894; Eukaryota.
DR eggNOG; KOG4732; Eukaryota.
DR GeneTree; ENSGT00390000007594; -.
DR HOGENOM; CLU_005296_1_0_1; -.
DR InParanoid; Q80TE0; -.
DR OMA; RMDKAPK; -.
DR OrthoDB; 25908at2759; -.
DR PhylomeDB; Q80TE0; -.
DR TreeFam; TF324391; -.
DR BioGRID-ORCS; 68925; 22 hits in 71 CRISPR screens.
DR ChiTaRS; Rpap1; mouse.
DR PRO; PR:Q80TE0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80TE0; protein.
DR Bgee; ENSMUSG00000034032; Expressed in rostral migratory stream and 261 other tissues.
DR ExpressionAtlas; Q80TE0; baseline and differential.
DR Genevisible; Q80TE0; MM.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030880; C:RNA polymerase complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013929; RNA_pol_II_AP1_C.
DR InterPro; IPR013930; RNA_pol_II_AP1_N.
DR InterPro; IPR039913; RPAP1/Rba50.
DR PANTHER; PTHR21483; PTHR21483; 1.
DR Pfam; PF08620; RPAP1_C; 1.
DR Pfam; PF08621; RPAP1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1409
FT /note="RNA polymerase II-associated protein 1"
FT /id="PRO_0000284842"
FT REGION 34..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWH6"
FT VAR_SEQ 1282..1290
FT /note="LPVPLECYT -> VCPTLSRPS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024682"
FT VAR_SEQ 1291..1409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024683"
FT CONFLICT 83
FT /note="H -> R (in Ref. 1; BAC65787 and 4; AAI17974/
FT AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="G -> S (in Ref. 1; BAC65787 and 4; AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="F -> V (in Ref. 1; BAC65787 and 4; AAI17974/
FT AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="K -> E (in Ref. 1; BAC65787 and 4; AAI17974/
FT AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="Q -> R (in Ref. 4; AAI17974)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="E -> T (in Ref. 1; BAC65787 and 4; AAI17974/
FT AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="L -> Q (in Ref. 2; BAE39647)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="I -> V (in Ref. 1; BAC65787 and 4; AAI17974/
FT AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 879
FT /note="N -> T (in Ref. 1; BAC65787, 2; BAE38647 and 4;
FT AAH51680/AAI17974)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="P -> Q (in Ref. 2; BAE39647)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="N -> K (in Ref. 1; BAC65787 and 4; AAH51680/
FT AAI17974/AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 977
FT /note="F -> L (in Ref. 1; BAC65787 and 4; AAH51680/
FT AAI17974/AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="R -> Q (in Ref. 1; BAC65787 and 4; AAH51680/
FT AAI17974/AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 1094
FT /note="C -> R (in Ref. 1; BAC65787 and 4; AAH51680/
FT AAI17974/AAI17975)"
FT /evidence="ECO:0000305"
FT CONFLICT 1183
FT /note="S -> N (in Ref. 2; BAE39647)"
FT /evidence="ECO:0000305"
FT CONFLICT 1263
FT /note="A -> T (in Ref. 2; BAE38647)"
FT /evidence="ECO:0000305"
FT CONFLICT 1305
FT /note="R -> W (in Ref. 4; AAI17974)"
FT /evidence="ECO:0000305"
FT CONFLICT 1311
FT /note="T -> S (in Ref. 1; BAC65787 and 4; AAH12218/
FT AAH51680/AAI17974/AAI17975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1409 AA; 155270 MW; 7E49F6D8A2D31687 CRC64;
MMLSRPKPGE SEVDLLRFQS QFLEAGAAPA VQLVKGSRRH GDAPPDRLPP QDHRDVVMLD
NLPDLPPALL PAPAKRARPS PGHPLPHDED PEERLNRHDQ HITAVLSKIV ERDTSSVTVT
LPVPSGVAFP PVFHRSQERQ VKPAASGKRS IFAQEIAARR VSGNRVTSAE QVVPSLDTPE
GAVPCETPSF RDRSNQLPGR SHGFHRPNLV TGKGLRSKVA EQEVQTIHEE NVARLQAMDP
EEILKEQQQL LAQLDPSLVA FLRSHSQVQE QTGTKATKKQ SPKRPSVLVT KEEPVTSTRT
REPRTGDKLE EKPEATVEDK MEDKLQPRTP ALKLPMTPSK DWLHMDTVEL DKLHWTQDLP
PLRRQQTQER MQARFSLQGE LLAPDVDLPT HLGLHHHGEE AERAGYSLQE LFHLTRSQVS
QQRALALQVL SQIVGRAQAG EFGDRLVGSV LRLLLDAGFL FLLRFSLDDR VDSVIAAAVR
ALRTLLVAPG DEELLDRTFS WYHGASVFPL MPSQDDKEDE DEDEELETEK VKRKTPEEGS
RPPPDLARHD VIKGLLATNL LPRLRYVLEV TCPGPSVILD ILAVLIRLAR HSLESAMRVL
ECPRLMETIV QEFLPTSWSP IGVGPTPSLY KVPCASAMKL LRVLASAGRN IAARLLSGFD
VRSRLCRFIA EAPHDLALPP EEAEILTTEA FRLWAVAASY GQGGDLYREL YPVLLRALQT
LPTELSAHPL QPLAMQRVAA LFTLLTQLTL AASSIPPEPA SGPAESCVPA IPSSVTWTQV
SGLKPLVEPC LKQTLKFLPR PDVWNALGPV PSACLLFLGA YYQAWSRQSH LCPEDWLQDM
ERLLDESLLP LLSQPPLGSL WDSLRDCSPL CNPLSCASNP EALPSLVSLG CAGGCPPLSV
AGSASPFPFL TALLSLINTL VQSHKGLCGQ LSAVLTAPGL QNYFLQCVAP APAPQLTPFS
AWALHHEYHL QYLVLSFAHK AATLQPEPAA STALHHAVAL VLLSRLLPGS EYLAQELLLS
CVFRLEFLPE SASGGPEAAD FSDGLSLGSS GDPQCRRGAL LVQACRDLPS IRSCYLAHCS
PARASLLSSQ ALYCGELLRV SSLLLPVPKE PLLATDWPFQ PLIHLYHRAS DTPSGPPAAD
TVGVAMRVLQ WVLVLESWRP EVLWAVPPAA RLARLMCVYL VDSELFRETP IQRLVAALLA
RLCRPQVLPN LKLDCPLPGL TSFPDLYASF LDHFEAVSFG DHLFGALVLL PLQRRFSVTL
RLALFGEHVG VLRALGLPLT QLPVPLECYT EPAEDSLPLL QLYFRALVTG TLRARWCPIL
YTVAVAHVNS FIFCQDPKSS DEVKTARRSM LQRTWLLTDE GLRQHLLHYK LPNSSLPEGF
ELYSQLPRLR QQCLQTLPTE GLQNGGVKT
