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PUM3_MOUSE
ID   PUM3_MOUSE              Reviewed;         647 AA.
AC   Q8BKS9; Q6A0E6; Q8BU15;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Pumilio homolog 3 {ECO:0000305};
GN   Name=Pum3 {ECO:0000312|MGI:MGI:106253};
GN   Synonyms=D19Bwg1357e {ECO:0000312|MGI:MGI:106253},
GN   Kiaa0020 {ECO:0000312|MGI:MGI:106253};
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, and NOD;
RC   TISSUE=Embryo, Embryonic spinal ganglion, and Thymus;
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] OF 152-647.
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=19319195; DOI=10.1371/journal.pone.0004980;
RA   Kuo M.W., Wang S.H., Chang J.C., Chang C.H., Huang L.J., Lin H.H., Yu A.L.,
RA   Li W.H., Yu J.;
RT   "A novel puf-A gene predicted from evolutionary analysis is involved in the
RT   development of eyes and primordial germ-cells.";
RL   PLoS ONE 4:E4980-E4980(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas, and Spleen;
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).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the
CC       degradation of PARP1 by CASP3 following genotoxic stress. Binds to
CC       double-stranded RNA or DNA without sequence specificity. Involved in
CC       development of the eye and of primordial germ cells.
CC       {ECO:0000250|UniProtKB:Q15397, ECO:0000250|UniProtKB:X1WGX5}.
CC   -!- SUBUNIT: Interacts with PARP1 (via catalytic domain).
CC       {ECO:0000250|UniProtKB:Q15397}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q15397}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q15397}. Chromosome
CC       {ECO:0000250|UniProtKB:Q15397}. Note=Localizes predominantly in the
CC       nucleolus with minor punctate signals in the nucleoplasm.
CC       {ECO:0000250|UniProtKB:Q15397}.
CC   -!- TISSUE SPECIFICITY: In the adult eye, expressed primarily in retinal
CC       ganglion cells and, to a lesser extent, in the pigmented cells.
CC       {ECO:0000269|PubMed:19319195}.
CC   -!- DOMAIN: A 90 degree bend between Pumilio repeats 3 and 4 gives rise to
CC       a L-shaped protein. {ECO:0000250|UniProtKB:Q15397}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC34427.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC40135.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAE24873.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK050829; BAC34427.1; ALT_INIT; mRNA.
DR   EMBL; AK088081; BAC40135.1; ALT_FRAME; mRNA.
DR   EMBL; AK141893; BAE24873.1; ALT_INIT; mRNA.
DR   EMBL; AK172872; BAD32150.1; -; mRNA.
DR   RefSeq; NP_803425.1; NM_177474.5.
DR   RefSeq; XP_006527246.1; XM_006527183.3.
DR   AlphaFoldDB; Q8BKS9; -.
DR   SMR; Q8BKS9; -.
DR   BioGRID; 206863; 4.
DR   STRING; 10090.ENSMUSP00000075573; -.
DR   iPTMnet; Q8BKS9; -.
DR   PhosphoSitePlus; Q8BKS9; -.
DR   EPD; Q8BKS9; -.
DR   MaxQB; Q8BKS9; -.
DR   PaxDb; Q8BKS9; -.
DR   PeptideAtlas; Q8BKS9; -.
DR   PRIDE; Q8BKS9; -.
DR   ProteomicsDB; 301926; -.
DR   DNASU; 52874; -.
DR   GeneID; 52874; -.
DR   KEGG; mmu:52874; -.
DR   UCSC; uc008hby.1; mouse.
DR   CTD; 9933; -.
DR   MGI; MGI:106253; Pum3.
DR   eggNOG; KOG2050; Eukaryota.
DR   InParanoid; Q8BKS9; -.
DR   OMA; WILDDVY; -.
DR   OrthoDB; 845051at2759; -.
DR   PhylomeDB; Q8BKS9; -.
DR   TreeFam; TF312954; -.
DR   BioGRID-ORCS; 52874; 4 hits in 40 CRISPR screens.
DR   ChiTaRS; Pum3; mouse.
DR   PRO; PR:Q8BKS9; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8BKS9; protein.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0010835; P:regulation of protein ADP-ribosylation; ISS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012959; CPL_dom.
DR   InterPro; IPR033133; PUM-HD.
DR   InterPro; IPR040059; PUM3.
DR   InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR   PANTHER; PTHR13389; PTHR13389; 1.
DR   Pfam; PF08144; CPL; 1.
DR   SMART; SM00025; Pumilio; 6.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   PROSITE; PS50302; PUM; 6.
DR   PROSITE; PS50303; PUM_HD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; DNA-binding; Nucleus; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..647
FT                   /note="Pumilio homolog 3"
FT                   /id="PRO_0000075930"
FT   DOMAIN          142..509
FT                   /note="PUM-HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT   REPEAT          176..211
FT                   /note="Pumilio 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          212..247
FT                   /note="Pumilio 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          248..276
FT                   /note="Pumilio 3"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          288..324
FT                   /note="Pumilio 4"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          325..360
FT                   /note="Pumilio 5"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          361..396
FT                   /note="Pumilio 6"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          397..434
FT                   /note="Pumilio 7"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          435..503
FT                   /note="Pumilio 8"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          504..550
FT                   /note="Pumilio 9"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          551..595
FT                   /note="Pumilio 10"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REPEAT          596..635
FT                   /note="Pumilio 11"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   REGION          1..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           105..117
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q15397"
FT   COMPBIAS        10..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         33
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   647 AA;  72800 MW;  193533640A3AFE50 CRC64;
     MEVKGKKKFT GKSPQTSQGK NKFHKNSESS SSKTFPRKAV KEGGPKVTSK NFEKGATKPG
     KKGVKQFKNK PQGGKGPKDK FQKANKFSKK RKFQPDGESD ESGAKKPKWD DFKKKKKELK
     QSRQLSDKTN YDIVVRAKHI WESLRRKDCD KEKRVKLMSD LQKLIQGKIK TIAFAHDSTR
     VIQCFIQYGN EEQRKQAFQE LQGDLVELSK AKYSRNIVKK FLMYGSKPQV AEIIRSFKGH
     VRKMLRHSEA SAIVEYAYND KAILEQRNML TEELYGNTFQ LYKSADHPTL DKVLELQPAK
     LELIMDEMKQ ILTPMAQKEA VIKHSLVHKV FLDFFTYAPP KPRSELIEAI REAVVYLAHT
     HDGARVAMHC LWHGTPKDRK VIVKTMKTYV EKVANGQYSH LVLLAAFDCI DDTKLVKQII
     ISEIISSLPS IVNDKYGRKV LLYLMSPRDP AHTVPELIEL LQKGDGNAHS KKDTAIRRRE
     LLESISPALL SYLQGHTQEV VLDKSACVLV SDMLGSATGD VQPAMDAIAS LAAAELHPGG
     KDGELHVAEH PAGHLVLKWL LEQDKKMKES GKEGCFAKTL VERVGMKNLK SWASINRGAI
     ILSSLLQSCD QEVVNKVKGG LKPLIPTLEK NKSSSRGIQT LLEKLTA
 
 
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