ID ZN593_MOUSE Reviewed; 134 AA. AC Q9DB42; Q3UZX2; Q99J54; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 2. DT 27-MAR-2024, entry version 157. DE RecName: Full=Zinc finger protein 593; DE AltName: Full=Zinc finger protein T86; GN Name=Znf593; Synonyms=Zfp593; 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 Pituitary; 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 MRNA]. RC 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver, Lung, 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-60S ribosomal particles maturation by CC promoting the nuclear export of the 60S ribosome. Negatively modulates CC the DNA binding activity of Oct-2 and therefore its transcriptional CC regulatory activity. {ECO:0000250|UniProtKB:O00488}. CC -!- SUBUNIT: Associates with pre-60S ribosomal particles. CC {ECO:0000250|UniProtKB:O00488}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000250|UniProtKB:O00488}. Cytoplasm CC {ECO:0000250|UniProtKB:Q08004}. Note=Shuttles between the nucleus and CC the cytoplasm. {ECO:0000250|UniProtKB:Q08004}. CC -!- DOMAIN: The protein is largely disordered, with the exception of the CC zinc finger domain. {ECO:0000250|UniProtKB:O00488}. CC -!- SIMILARITY: Belongs to the ZNF593/BUD20 C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH03465.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB23902.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK005247; BAB23902.1; ALT_INIT; mRNA. DR EMBL; AK133585; BAE21733.1; -; mRNA. DR EMBL; AL627314; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003465; AAH03465.1; ALT_INIT; mRNA. DR CCDS; CCDS51325.1; -. DR RefSeq; NP_077177.2; NM_024215.2. DR AlphaFoldDB; Q9DB42; -. DR SMR; Q9DB42; -. DR BioGRID; 212620; 3. DR IntAct; Q9DB42; 2. DR STRING; 10090.ENSMUSP00000030644; -. DR iPTMnet; Q9DB42; -. DR PhosphoSitePlus; Q9DB42; -. DR SwissPalm; Q9DB42; -. DR EPD; Q9DB42; -. DR jPOST; Q9DB42; -. DR MaxQB; Q9DB42; -. DR PaxDb; 10090-ENSMUSP00000030644; -. DR PeptideAtlas; Q9DB42; -. DR ProteomicsDB; 299591; -. DR Pumba; Q9DB42; -. DR Antibodypedia; 30564; 77 antibodies from 19 providers. DR DNASU; 68040; -. DR Ensembl; ENSMUST00000030644.8; ENSMUSP00000030644.8; ENSMUSG00000028840.11. DR GeneID; 68040; -. DR KEGG; mmu:68040; -. DR UCSC; uc008vej.1; mouse. DR AGR; MGI:1915290; -. DR CTD; 68040; -. DR MGI; MGI:1915290; Zfp593. DR VEuPathDB; HostDB:ENSMUSG00000028840; -. DR eggNOG; KOG3408; Eukaryota. DR GeneTree; ENSGT00390000004173; -. DR HOGENOM; CLU_117291_1_2_1; -. DR InParanoid; Q9DB42; -. DR OMA; MKDHFRS; -. DR OrthoDB; 230013at2759; -. DR PhylomeDB; Q9DB42; -. DR TreeFam; TF315114; -. DR BioGRID-ORCS; 68040; 7 hits in 77 CRISPR screens. DR PRO; PR:Q9DB42; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q9DB42; Protein. DR Bgee; ENSMUSG00000028840; Expressed in paneth cell and 228 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; ISS:ParkinsonsUK-UCL. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:ParkinsonsUK-UCL. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:1990275; F:preribosome binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2. DR InterPro; IPR022755; Znf_C2H2_jaz. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR46095; ZINC FINGER PROTEIN 593; 1. DR PANTHER; PTHR46095:SF1; ZINC FINGER PROTEIN 593; 1. DR Pfam; PF12171; zf-C2H2_jaz; 1. DR SMART; SM00451; ZnF_U1; 1. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. DR Genevisible; Q9DB42; MM. PE 1: Evidence at protein level; KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; KW Ribosome biogenesis; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..134 FT /note="Zinc finger protein 593" FT /id="PRO_0000047685" FT ZN_FING 61..85 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 85..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..51 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 47 FT /note="P -> R (in Ref. 3; AAH03465)" FT /evidence="ECO:0000305" SQ SEQUENCE 134 AA; 15147 MW; 62D0A3C01FD3FB70 CRC64; MGRSRRTGAH RAHSLARQMK AKKRRPDLDE IHRELRPQGL PRPKPEPDAE PDPDLPGGGL HRCLACARYF IDSANLKTHF RSKDHKKRLK QLSVEPYSQE EAERAAGMGS YVQPQRLGVP TEVSTDIPEM DTST //