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PWP1_MOUSE
ID   PWP1_MOUSE              Reviewed;         501 AA.
AC   Q99LL5; Q9D6T6;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Periodic tryptophan protein 1 homolog;
GN   Name=Pwp1;
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=Cerebellum, 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=Czech II, and 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-49, AND IDENTIFICATION BY
RP   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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-58 AND SER-493, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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: Chromatin-associated factor that regulates transcription (By
CC       similarity). Regulates Pol I-mediated rRNA biogenesis and, probably,
CC       Pol III-mediated transcription (By similarity). Regulates the
CC       epigenetic status of rDNA (By similarity).
CC       {ECO:0000250|UniProtKB:Q13610}.
CC   -!- SUBUNIT: Associates with the RNA polymerase (Pol I) complex. Interacts
CC       with POLR1E. {ECO:0000250|UniProtKB:Q13610}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13610}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:Q13610}. Chromosome
CC       {ECO:0000250|UniProtKB:Q13610}. Note=Associates with chromatin regions
CC       of rDNA. {ECO:0000250|UniProtKB:Q13610}.
CC   -!- SIMILARITY: Belongs to the WD repeat PWP1 family. {ECO:0000305}.
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DR   EMBL; AK009972; BAB26622.1; -; mRNA.
DR   EMBL; AK082158; BAC38427.1; -; mRNA.
DR   EMBL; BC003199; AAH03199.1; -; mRNA.
DR   EMBL; BC023137; AAH23137.1; -; mRNA.
DR   CCDS; CCDS24092.1; -.
DR   RefSeq; NP_598754.2; NM_133993.3.
DR   AlphaFoldDB; Q99LL5; -.
DR   SMR; Q99LL5; -.
DR   BioGRID; 222026; 27.
DR   IntAct; Q99LL5; 4.
DR   STRING; 10090.ENSMUSP00000001836; -.
DR   iPTMnet; Q99LL5; -.
DR   PhosphoSitePlus; Q99LL5; -.
DR   EPD; Q99LL5; -.
DR   jPOST; Q99LL5; -.
DR   MaxQB; Q99LL5; -.
DR   PaxDb; Q99LL5; -.
DR   PeptideAtlas; Q99LL5; -.
DR   PRIDE; Q99LL5; -.
DR   ProteomicsDB; 302036; -.
DR   Antibodypedia; 18254; 87 antibodies from 25 providers.
DR   DNASU; 103136; -.
DR   Ensembl; ENSMUST00000001836; ENSMUSP00000001836; ENSMUSG00000001785.
DR   GeneID; 103136; -.
DR   KEGG; mmu:103136; -.
DR   UCSC; uc007gnc.2; mouse.
DR   CTD; 11137; -.
DR   MGI; MGI:1914735; Pwp1.
DR   VEuPathDB; HostDB:ENSMUSG00000001785; -.
DR   eggNOG; KOG0270; Eukaryota.
DR   GeneTree; ENSGT00390000017324; -.
DR   HOGENOM; CLU_023867_1_1_1; -.
DR   InParanoid; Q99LL5; -.
DR   OMA; CFVPRGV; -.
DR   OrthoDB; 737539at2759; -.
DR   PhylomeDB; Q99LL5; -.
DR   TreeFam; TF314868; -.
DR   BioGRID-ORCS; 103136; 27 hits in 72 CRISPR screens.
DR   ChiTaRS; Pwp1; mouse.
DR   PRO; PR:Q99LL5; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q99LL5; protein.
DR   Bgee; ENSMUSG00000001785; Expressed in primitive streak and 258 other tissues.
DR   ExpressionAtlas; Q99LL5; baseline and differential.
DR   Genevisible; Q99LL5; MM.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:1990889; F:H4K20me3 modified histone binding; IDA:MGI.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IMP:MGI.
DR   GO; GO:0033140; P:negative regulation of peptidyl-serine phosphorylation of STAT protein; IMP:MGI.
DR   GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:MGI.
DR   GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR044285; PWP1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR14091; PTHR14091; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ribosome biogenesis; Transcription; Transcription regulation; WD repeat.
FT   CHAIN           1..501
FT                   /note="Periodic tryptophan protein 1 homolog"
FT                   /id="PRO_0000051172"
FT   REPEAT          185..229
FT                   /note="WD 1"
FT   REPEAT          253..293
FT                   /note="WD 2"
FT   REPEAT          296..336
FT                   /note="WD 3"
FT   REPEAT          382..422
FT                   /note="WD 4"
FT   REPEAT          427..467
FT                   /note="WD 5"
FT   REGION          38..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..107
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13610"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         85
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13610"
FT   MOD_RES         484
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13610"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        247
FT                   /note="K -> R (in Ref. 1; BAB26622)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  55587 MW;  704A050633F0C2B1 CRC64;
     MNRSRQVTCV AWVRRGVAKE TPDKVELSKE EVNRLIAEAK GKLQEEGGSE EEEAGNPSED
     GMQSGPTQAP PRESLEDGDP QDDRTLDDDE LAGYDLDNYD EEDNPDAETI GESLLGLTVY
     GSNDQDPYVT LKDTEQYEHE DFLIKPTDNL IVCGRAEQEQ CNLEVHVYNQ EEESFYVHHD
     ILLSAYPLSV EWLNFDPSPD ASTGNYIAVG NMTPVIEVWD LDIVDSLEPV FTLGSKLSKK
     KKKKGKKSSS AEGHTDAVLD LSWNKTVRNV LASASADSTV VLWDLSVGKS VARLTAHTDK
     VQTLQFHPFE AQTLISGSYD KSVALYDCRD PSQNHRQWRF SGQIERVTWN HFSPCHFLAS
     TDDGFVYNLD ARSDKPIFTL NAHNDEISGL DLSSQIKGCL VTASADKFVK IWDILGDRPS
     LIHSRDMKMG VLFCSSCCPD LPFVYAFGGQ KEGLRVWDIS TVSSVNEAFG RRERLVIGGT
     KGLSVSGPCG SRSPQQTPME S
 
 
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