ZN589_HUMAN
ID ZN589_HUMAN Reviewed; 364 AA.
AC Q86UQ0; Q86UC9; Q9BRI6; Q9BRY3; Q9Y611; Q9Y612;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Zinc finger protein 589;
DE AltName: Full=Stem cell zinc finger protein 1;
GN Name=ZNF589; Synonyms=SZF1;
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 [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, AND VARIANT ARG-216.
RX PubMed=10029171; DOI=10.1016/s0301-472x(98)00035-6;
RA Liu C., Levenstein M., Chen J., Tsifrina E., Yonescu R., Griffin C.,
RA Civin C.I., Small D.;
RT "SZF1: a novel KRAB-zinc finger gene expressed in CD34+ stem/progenitor
RT cells.";
RL Exp. Hematol. 27:313-325(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Shan Y.X., Yu L.;
RT "Cloning and characterization of a novel KRAB-zinc finger protein.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-12 AND
RP ARG-216.
RC TISSUE=Eye, Lung, and Muscle;
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 [6]
RP INTERACTION WITH TRIM28, AND FUNCTION.
RX PubMed=12097288;
RA Peng H., Zheng L., Lee W.H., Rux J.J., Rauscher F.J. III;
RT "A common DNA-binding site for SZF1 and the BRCA1-associated zinc finger
RT protein, ZBRK1.";
RL Cancer Res. 62:3773-3781(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=23665872; DOI=10.1007/s00018-013-1359-4;
RA Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M.,
RA Huang Z.;
RT "Novel activity of KRAB domain that functions to reinforce nuclear
RT localization of KRAB-containing zinc finger proteins by interacting with
RT KAP1.";
RL Cell. Mol. Life Sci. 70:3947-3958(2013).
CC -!- FUNCTION: May play a role in hematopoietic stem/progenitor cell
CC differentiation. May play a role as a DNA binding-dependent
CC transcriptional repressor. {ECO:0000269|PubMed:10029171,
CC ECO:0000269|PubMed:12097288}.
CC -!- SUBUNIT: Interacts with TRIM28. {ECO:0000269|PubMed:12097288}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23665872}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86UQ0-1; Sequence=Displayed;
CC Name=2; Synonyms=SZF1-2;
CC IsoId=Q86UQ0-2; Sequence=VSP_028449, VSP_028450;
CC Name=3; Synonyms=SZF1-1;
CC IsoId=Q86UQ0-3; Sequence=VSP_028449, VSP_028450, VSP_028451;
CC -!- TISSUE SPECIFICITY: Isoform 2 is widely expressed. Isoform 3 is only
CC expressed in CD34(+) cells. {ECO:0000269|PubMed:10029171}.
CC -!- DOMAIN: The KRAB domain mediates interaction with TRIM28.
CC -!- MISCELLANEOUS: [Isoform 2]: Probable target of nonsense-mediated mRNA
CC decay. The proposed CDS is dubious. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Probable target of nonsense-mediated mRNA
CC decay. The proposed CDS is dubious. Isoform produced through aberrant
CC splice sites. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05859.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH06247.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH48798.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF114816; AAD38879.1; -; mRNA.
DR EMBL; AF114817; AAD38880.1; -; mRNA.
DR EMBL; AY258146; AAP14679.1; -; mRNA.
DR EMBL; AL832831; CAI46129.1; -; mRNA.
DR EMBL; CH471055; EAW64856.1; -; Genomic_DNA.
DR EMBL; BC005859; AAH05859.2; ALT_INIT; mRNA.
DR EMBL; BC006247; AAH06247.2; ALT_INIT; mRNA.
DR EMBL; BC048798; AAH48798.1; ALT_INIT; mRNA.
DR CCDS; CCDS43085.1; -. [Q86UQ0-1]
DR RefSeq; NP_057173.2; NM_016089.2. [Q86UQ0-1]
DR AlphaFoldDB; Q86UQ0; -.
DR SMR; Q86UQ0; -.
DR BioGRID; 119515; 7.
DR IntAct; Q86UQ0; 5.
DR STRING; 9606.ENSP00000346729; -.
DR iPTMnet; Q86UQ0; -.
DR PhosphoSitePlus; Q86UQ0; -.
DR BioMuta; ZNF589; -.
DR DMDM; 74759403; -.
DR EPD; Q86UQ0; -.
DR jPOST; Q86UQ0; -.
DR MassIVE; Q86UQ0; -.
DR MaxQB; Q86UQ0; -.
DR PaxDb; Q86UQ0; -.
DR PeptideAtlas; Q86UQ0; -.
DR PRIDE; Q86UQ0; -.
DR ProteomicsDB; 69858; -. [Q86UQ0-1]
DR ProteomicsDB; 69859; -. [Q86UQ0-2]
DR ProteomicsDB; 69860; -. [Q86UQ0-3]
DR Antibodypedia; 831; 107 antibodies from 16 providers.
DR DNASU; 51385; -.
DR Ensembl; ENST00000354698.8; ENSP00000346729.3; ENSG00000164048.14. [Q86UQ0-1]
DR Ensembl; ENST00000448461.5; ENSP00000404592.1; ENSG00000164048.14. [Q86UQ0-1]
DR GeneID; 51385; -.
DR KEGG; hsa:51385; -.
DR MANE-Select; ENST00000354698.8; ENSP00000346729.3; NM_016089.3; NP_057173.2.
DR UCSC; uc003csl.5; human. [Q86UQ0-1]
DR CTD; 51385; -.
DR DisGeNET; 51385; -.
DR GeneCards; ZNF589; -.
DR HGNC; HGNC:16747; ZNF589.
DR HPA; ENSG00000164048; Low tissue specificity.
DR MIM; 616702; gene.
DR neXtProt; NX_Q86UQ0; -.
DR OpenTargets; ENSG00000164048; -.
DR PharmGKB; PA134988473; -.
DR VEuPathDB; HostDB:ENSG00000164048; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164260; -.
DR HOGENOM; CLU_002678_0_7_1; -.
DR InParanoid; Q86UQ0; -.
DR OMA; YPTFRFY; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q86UQ0; -.
DR TreeFam; TF338096; -.
DR PathwayCommons; Q86UQ0; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q86UQ0; -.
DR BioGRID-ORCS; 51385; 10 hits in 1100 CRISPR screens.
DR ChiTaRS; ZNF589; human.
DR GenomeRNAi; 51385; -.
DR Pharos; Q86UQ0; Tbio.
DR PRO; PR:Q86UQ0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q86UQ0; protein.
DR Bgee; ENSG00000164048; Expressed in buccal mucosa cell and 148 other tissues.
DR ExpressionAtlas; Q86UQ0; baseline and differential.
DR Genevisible; Q86UQ0; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Zinc; Zinc-finger.
FT CHAIN 1..364
FT /note="Zinc finger protein 589"
FT /id="PRO_0000306325"
FT DOMAIN 35..108
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 248..270
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..298
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 304..326
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 332..354
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 103..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 1..32
FT /note="MWAPREQLLGWTAEALPAKDSAWPWEEKPRYL -> MIDFQMLNQLCRTIIN
FT PSVIPCLKYCGDQI (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10029171"
FT /id="VSP_028449"
FT VAR_SEQ 75
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10029171"
FT /id="VSP_028450"
FT VAR_SEQ 353..364
FT /note="IHTGDKPYVCRD -> CQVTVPLEEWSLHLTTSFCNCVLPLASMTLSCFIFF
FT YISSLCCFLSYPTFRFYSEFSLQPYNLRDTFTRSPS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10029171"
FT /id="VSP_028451"
FT VARIANT 12
FT /note="T -> A (in dbSNP:rs9847953)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052871"
FT VARIANT 216
FT /note="T -> R (in dbSNP:rs11718329)"
FT /evidence="ECO:0000269|PubMed:10029171,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_035290"
SQ SEQUENCE 364 AA; 41189 MW; EC335916B88993E3 CRC64;
MWAPREQLLG WTAEALPAKD SAWPWEEKPR YLGPVTFEDV AVLFTEAEWK RLSLEQRNLY
KEVMLENLRN LVSLAESKPE VHTCPSCPLA FGSQQFLSQD ELHNHPIPGF HAGNQLHPGN
PCPEDQPQSQ HPSDKNHRGA EAEDQRVEGG VRPLFWSTNE RGALVGFSSL FQRPPISSWG
GNRILEIQLS PAQNASSEEV DRISKRAETP GFGAVTFGEC ALAFNQKSNL FRQKAVTAEK
SSDKRQSQVC RECGRGFSRK SQLIIHQRTH TGEKPYVCGE CGRGFIVESV LRNHLSTHSG
EKPYVCSHCG RGFSCKPYLI RHQRTHTREK SFMCTVCGRG FREKSELIKH QRIHTGDKPY
VCRD
