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PRP6_MOUSE
ID   PRP6_MOUSE              Reviewed;         941 AA.
AC   Q91YR7; Q3ULJ7; Q542P0; Q8CIK9; Q8R3M8; Q99JN1; Q9CSZ0;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Pre-mRNA-processing factor 6;
DE   AltName: Full=PRP6 homolog;
DE   AltName: Full=U5 snRNP-associated 102 kDa protein;
DE            Short=U5-102 kDa protein;
GN   Name=Prpf6;
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=Embryo, and Embryonic head;
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 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-275 AND SER-279, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Lung, Spleen, 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: Involved in pre-mRNA splicing as component of the U4/U6-U5
CC       tri-snRNP complex, one of the building blocks of the spliceosome.
CC       Enhances dihydrotestosterone-induced transactivation activity of AR, as
CC       well as dexamethasone-induced transactivation activity of NR3C1, but
CC       does not affect estrogen-induced transactivation.
CC       {ECO:0000250|UniProtKB:O94906}.
CC   -!- SUBUNIT: Identified in the spliceosome B complex. Identified in the
CC       spliceosome C complex. Associates with the U5 snRNP particle. Component
CC       of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs
CC       and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A,
CC       SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, LSm
CC       proteins LSm2-8 and Sm proteins. Interacts with ARAF1. Interacts with
CC       AR and NR3C1, but not ESR1, independently of the presence of hormones.
CC       Interacts with USH1G. {ECO:0000250|UniProtKB:O94906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:O94906}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:O94906}. Note=Localized in splicing speckles.
CC       {ECO:0000250|UniProtKB:O94906}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91YR7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91YR7-2; Sequence=VSP_002063, VSP_002064;
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DR   EMBL; BC005801; AAH05801.1; -; mRNA.
DR   EMBL; BC014869; AAH14869.1; -; mRNA.
DR   EMBL; BC023691; AAH23691.2; -; mRNA.
DR   EMBL; BC025030; AAH25030.1; -; mRNA.
DR   EMBL; AK011639; BAB27751.1; -; mRNA.
DR   EMBL; AK145461; BAE26451.1; -; mRNA.
DR   EMBL; AK081998; BAC38390.1; -; mRNA.
DR   EMBL; AL844529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466626; EDL07438.1; -; Genomic_DNA.
DR   CCDS; CCDS38381.1; -. [Q91YR7-1]
DR   RefSeq; NP_598462.1; NM_133701.2. [Q91YR7-1]
DR   PDB; 6QX9; EM; 3.28 A; 5J=18-655.
DR   PDBsum; 6QX9; -.
DR   AlphaFoldDB; Q91YR7; -.
DR   SMR; Q91YR7; -.
DR   BioGRID; 213097; 7.
DR   IntAct; Q91YR7; 4.
DR   MINT; Q91YR7; -.
DR   STRING; 10090.ENSMUSP00000002529; -.
DR   iPTMnet; Q91YR7; -.
DR   PhosphoSitePlus; Q91YR7; -.
DR   EPD; Q91YR7; -.
DR   jPOST; Q91YR7; -.
DR   MaxQB; Q91YR7; -.
DR   PaxDb; Q91YR7; -.
DR   PeptideAtlas; Q91YR7; -.
DR   PRIDE; Q91YR7; -.
DR   ProteomicsDB; 291793; -. [Q91YR7-1]
DR   ProteomicsDB; 291794; -. [Q91YR7-2]
DR   Antibodypedia; 15475; 220 antibodies from 30 providers.
DR   DNASU; 68879; -.
DR   Ensembl; ENSMUST00000002529; ENSMUSP00000002529; ENSMUSG00000002455. [Q91YR7-1]
DR   Ensembl; ENSMUST00000136481; ENSMUSP00000121340; ENSMUSG00000002455. [Q91YR7-1]
DR   GeneID; 68879; -.
DR   KEGG; mmu:68879; -.
DR   UCSC; uc008omy.1; mouse. [Q91YR7-2]
DR   UCSC; uc008omz.1; mouse. [Q91YR7-1]
DR   CTD; 24148; -.
DR   MGI; MGI:1922946; Prpf6.
DR   VEuPathDB; HostDB:ENSMUSG00000002455; -.
DR   eggNOG; KOG0495; Eukaryota.
DR   GeneTree; ENSGT00550000075016; -.
DR   HOGENOM; CLU_007010_0_0_1; -.
DR   InParanoid; Q91YR7; -.
DR   OMA; DGWAWYY; -.
DR   OrthoDB; 335779at2759; -.
DR   PhylomeDB; Q91YR7; -.
DR   TreeFam; TF105743; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR   BioGRID-ORCS; 68879; 26 hits in 76 CRISPR screens.
DR   ChiTaRS; Prpf6; mouse.
DR   PRO; PR:Q91YR7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q91YR7; protein.
DR   Bgee; ENSMUSG00000002455; Expressed in floor plate of midbrain and 270 other tissues.
DR   ExpressionAtlas; Q91YR7; baseline and differential.
DR   Genevisible; Q91YR7; MM.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:MGI.
DR   GO; GO:0005682; C:U5 snRNP; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006403; P:RNA localization; ISO:MGI.
DR   GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISO:MGI.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR010491; PRP1_N.
DR   InterPro; IPR027108; Prp6/Prp1/STA1.
DR   InterPro; IPR045075; Syf1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR11246; PTHR11246; 1.
DR   PANTHER; PTHR11246:SF1; PTHR11246:SF1; 1.
DR   Pfam; PF06424; PRP1_N; 1.
DR   SMART; SM00386; HAT; 13.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Spliceosome.
FT   CHAIN           1..941
FT                   /note="Pre-mRNA-processing factor 6"
FT                   /id="PRO_0000205760"
FT   REPEAT          384..416
FT                   /note="HAT 1"
FT   REPEAT          418..444
FT                   /note="HAT 2"
FT   REPEAT          445..476
FT                   /note="HAT 3"
FT   REPEAT          554..586
FT                   /note="HAT 4"
FT   REPEAT          588..620
FT                   /note="HAT 5"
FT   REPEAT          622..654
FT                   /note="HAT 6"
FT   REPEAT          689..721
FT                   /note="HAT 7"
FT   REPEAT          723..755
FT                   /note="HAT 8"
FT   REPEAT          855..887
FT                   /note="HAT 9"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94906"
FT   MOD_RES         180
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O94906"
FT   MOD_RES         266
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O94906"
FT   MOD_RES         275
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         550..570
FT                   /note="CVAHNALECARAIYAYALQVF -> VSFLACFPACSLDRNSGPINL (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002063"
FT   VAR_SEQ         571..941
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002064"
FT   CONFLICT        232
FT                   /note="T -> A (in Ref. 1; BAE26451)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        390
FT                   /note="K -> R (in Ref. 1; BAE26451)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   941 AA;  106722 MW;  A08C3AC49AE1B9E9 CRC64;
     MNKKKKPFLG MPAPLGYVPG LGRGATGFTT RSDIGPARDA NDPVDDRHAP PGKRTVGDQM
     KKNQAADDDD EDLNDTNYDE FNGYAGSLFS SGPYEKDDEE ADAIYAALDK RMDERRKERR
     EQREKEEIEK YRMERPKIQQ QFSDLKRKLA EVTEEEWLSI PEVGDARNKR QRNPRYEKLT
     PVPDSFFAKH LQTGENHTSV DPRQTQFGGL NTPYPGGLNT PYPGGMTPGL MTPGTGELDM
     RKIGQARNTL MDMRLSQVSD SVSGQTVVDP KGYLTDLNSM IPTHGGDIND IKKARLLLKS
     VRETNPHHPP AWIASARLEE VTGKLQVARN LIMKGTEMCP KSEDVWLEAA RLQPGDTAKA
     VVAQAVRHLP QSVRIYIRAA ELETDIRAKK RVLRKALEHV PNSVRLWKAA VELEEPEDAR
     IMLSRAVECC PTSVELWLAL ARLETYENAR KVLNKARENI PTDRHIWITA AKLEEANGNT
     QMVEKIIDRA ITSLRANGVE INREQWIQDA EECDRAGSVA TCQAVMRAVI GIGIEEEDRK
     HTWMEDADSC VAHNALECAR AIYAYALQVF PSKKSVWLRA AYFEKNHGTR ESLEALLQRA
     VAHCPKAEVL WLMGAKSKWL AGDVPAARSI LALAFQANPN SEEIWLAAVK LESENNEYER
     ARRLLAKARS SAPTARVFMK SVKLEWVLGN ISAAQELCEE ALRHYEDFPK LWMMKGQIEE
     QGELMEKARE AYNQGLKKCP HSTPLWLLLS RLEEKIGQLT RARAILEKSR LKNPKNPGLW
     LESVRLEYRA GLKNIANTLM AKALQECPNS GILWSEAVFL EARPQRKTKS VDALKKCEHD
     PHVLLAVAKL FWSERKITKA REWFHRTVKI DSDLGDAWAF FYKFELQHGT EEQQEEVRKR
     CENAEPRHGE LWCAVSKDIT NWQRKIGEIL VLVAARIKNT F
 
 
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