ZN593_HUMAN
ID ZN593_HUMAN Reviewed; 134 AA.
AC O00488; B2R4S0; Q5T2H7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Zinc finger protein 593;
DE AltName: Full=Zinc finger protein T86;
GN Name=ZNF593; Synonyms=ZT86;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 3-134, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=T-cell lymphoma;
RX PubMed=9115366; DOI=10.1093/nar/25.10.1984;
RA Terunuma A., Shiba K., Noda T.;
RT "A novel genetic system to isolate a dominant negative effector on DNA-
RT binding activity of Oct-2.";
RL Nucleic Acids Res. 25:1984-1990(1997).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP STRUCTURE BY NMR OF 20-134 IN COMPLEX WITH ZINC IONS, AND DOMAIN.
RX PubMed=18287285; DOI=10.1110/ps.073290408;
RA Hayes P.L., Lytle B.L., Volkman B.F., Peterson F.C.;
RT "The solution structure of ZNF593 from Homo sapiens reveals a zinc finger
RT in a predominantly unstructured protein.";
RL Protein Sci. 17:571-576(2008).
RN [14] {ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.13 ANGSTROMS) IN COMPLEX WITH PRE-60S
RP RIBOSOMAL PARTICLES, FUNCTION, AND INTERACTION WITH PRE-60S RIBOSOMAL
RP PARTICLES.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Involved in pre-60S ribosomal particles maturation by
CC promoting the nuclear export of the 60S ribosome (PubMed:32669547).
CC Negatively modulates the DNA binding activity of Oct-2 and therefore
CC its transcriptional regulatory activity (PubMed:9115366).
CC {ECO:0000269|PubMed:9115366, ECO:0000305|PubMed:32669547}.
CC -!- SUBUNIT: Associates with pre-60S ribosomal particles.
CC {ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC O00488; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-726769, EBI-742054;
CC O00488; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-726769, EBI-739832;
CC O00488; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-726769, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q08004}. Note=Shuttles between the
CC nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q08004}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in spleen, prostate, testis,
CC small intestine, colon and to a minor level in thymus and peripheral
CC blood leukocytes. {ECO:0000269|PubMed:9115366}.
CC -!- DOMAIN: The protein is largely disordered, with the exception of the
CC zinc finger domain. {ECO:0000269|PubMed:18287285}.
CC -!- SIMILARITY: Belongs to the ZNF593/BUD20 C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02580.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH19267.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA20369.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG34867.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK311926; BAG34867.1; ALT_INIT; mRNA.
DR EMBL; AL391650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07843.1; -; Genomic_DNA.
DR EMBL; BC002580; AAH02580.1; ALT_INIT; mRNA.
DR EMBL; BC019267; AAH19267.1; ALT_INIT; mRNA.
DR EMBL; D45213; BAA20369.1; ALT_INIT; mRNA.
DR CCDS; CCDS275.2; -.
DR RefSeq; NP_056955.2; NM_015871.4.
DR PDB; 1ZR9; NMR; -; A=20-134.
DR PDB; 6LSS; EM; 3.23 A; 9=1-134.
DR PDB; 6LU8; EM; 3.13 A; 9=1-134.
DR PDBsum; 1ZR9; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR AlphaFoldDB; O00488; -.
DR SMR; O00488; -.
DR BioGRID; 119241; 57.
DR IntAct; O00488; 22.
DR MINT; O00488; -.
DR STRING; 9606.ENSP00000363384; -.
DR iPTMnet; O00488; -.
DR PhosphoSitePlus; O00488; -.
DR BioMuta; ZNF593; -.
DR SWISS-2DPAGE; O00488; -.
DR EPD; O00488; -.
DR jPOST; O00488; -.
DR MassIVE; O00488; -.
DR MaxQB; O00488; -.
DR PaxDb; O00488; -.
DR PeptideAtlas; O00488; -.
DR PRIDE; O00488; -.
DR ProteomicsDB; 47933; -.
DR Antibodypedia; 30564; 75 antibodies from 20 providers.
DR DNASU; 51042; -.
DR Ensembl; ENST00000374266.7; ENSP00000363384.5; ENSG00000142684.9.
DR GeneID; 51042; -.
DR KEGG; hsa:51042; -.
DR MANE-Select; ENST00000374266.7; ENSP00000363384.5; NM_015871.5; NP_056955.2.
DR UCSC; uc001bll.5; human.
DR CTD; 51042; -.
DR DisGeNET; 51042; -.
DR GeneCards; ZNF593; -.
DR HGNC; HGNC:30943; ZNF593.
DR HPA; ENSG00000142684; Low tissue specificity.
DR MIM; 616698; gene.
DR neXtProt; NX_O00488; -.
DR OpenTargets; ENSG00000142684; -.
DR PharmGKB; PA134962156; -.
DR VEuPathDB; HostDB:ENSG00000142684; -.
DR eggNOG; KOG3408; Eukaryota.
DR GeneTree; ENSGT00390000004173; -.
DR HOGENOM; CLU_117291_1_2_1; -.
DR InParanoid; O00488; -.
DR OMA; TECAKWF; -.
DR OrthoDB; 1445352at2759; -.
DR PhylomeDB; O00488; -.
DR TreeFam; TF315114; -.
DR PathwayCommons; O00488; -.
DR SignaLink; O00488; -.
DR BioGRID-ORCS; 51042; 179 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF593; human.
DR EvolutionaryTrace; O00488; -.
DR GeneWiki; ZNF593; -.
DR GenomeRNAi; 51042; -.
DR Pharos; O00488; Tbio.
DR PRO; PR:O00488; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00488; protein.
DR Bgee; ENSG00000142684; Expressed in gastrocnemius and 173 other tissues.
DR ExpressionAtlas; O00488; baseline and differential.
DR Genevisible; O00488; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IMP:CAFA.
DR GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IGI:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:GO_Central.
DR DisProt; DP00549; -.
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 Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..134
FT /note="Zinc finger protein 593"
FT /id="PRO_0000047684"
FT ZN_FING 61..85
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..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..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 6
FT /note="R -> Q (in dbSNP:rs2232649)"
FT /id="VAR_059924"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1ZR9"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1ZR9"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1ZR9"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:1ZR9"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1ZR9"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1ZR9"
SQ SEQUENCE 134 AA; 15199 MW; 883BCE4F72459818 CRC64;
MGRSRRTGAH RAHSLARQMK AKRRRPDLDE IHRELRPQGS ARPQPDPNAE FDPDLPGGGL
HRCLACARYF IDSTNLKTHF RSKDHKKRLK QLSVEPYSQE EAERAAGMGS YVPPRRLAVP
TEVSTEVPEM DTST
