ZN174_HUMAN
ID ZN174_HUMAN Reviewed; 407 AA.
AC Q15697; Q53Y68; Q9BQ34;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Zinc finger protein 174;
DE AltName: Full=AW-1;
DE AltName: Full=Zinc finger and SCAN domain-containing protein 8;
GN Name=ZNF174; Synonyms=ZSCAN8;
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] (ISOFORM 1), AND FUNCTION.
RX PubMed=7673192; DOI=10.1074/jbc.270.38.22143;
RA Williams A.J., Khachigian L.M., Shows T., Collins T.;
RT "Isolation and characterization of a novel zinc-finger protein with
RT transcription repressor activity.";
RL J. Biol. Chem. 270:22143-22152(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix, and Lung;
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26; LYS-204; LYS-230 AND LYS-271,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [5]
RP STRUCTURE BY NMR OF 37-132, AND SUBUNIT.
RX PubMed=15629724; DOI=10.1016/j.molcel.2004.12.015;
RA Ivanov D., Stone J.R., Maki J.L., Collins T., Wagner G.;
RT "Mammalian SCAN domain dimer is a domain-swapped homolog of the HIV capsid
RT C-terminal domain.";
RL Mol. Cell 17:137-143(2005).
CC -!- FUNCTION: Transcriptional repressor. {ECO:0000269|PubMed:7673192}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15629724}.
CC -!- INTERACTION:
CC Q15697-2; P57086: SCAND1; NbExp=3; IntAct=EBI-11158827, EBI-745846;
CC Q15697-2; P17028: ZNF24; NbExp=4; IntAct=EBI-11158827, EBI-707773;
CC Q15697-2; Q8TBC5: ZSCAN18; NbExp=3; IntAct=EBI-11158827, EBI-3919096;
CC Q15697-2; P10073: ZSCAN22; NbExp=3; IntAct=EBI-11158827, EBI-10178224;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15697-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15697-2; Sequence=VSP_006897, VSP_006898;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of organs, but most strongly
CC in adult testis and ovary followed by small intestine, colon, prostate,
CC thymus, spleen, pancreas, skeletal muscle, heart, brain and kidney.
CC Also expressed in umbilical vein endothelial cells, foreskin fibroblast
CC and Hep-G2 cells.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U31248; AAB04897.1; -; mRNA.
DR EMBL; BT006923; AAP35569.1; -; mRNA.
DR EMBL; BC000876; AAH00876.1; -; mRNA.
DR EMBL; BC001161; AAH01161.1; -; mRNA.
DR CCDS; CCDS10504.1; -. [Q15697-1]
DR CCDS; CCDS32380.1; -. [Q15697-2]
DR PIR; I39152; I39152.
DR RefSeq; NP_001027463.1; NM_001032292.2. [Q15697-2]
DR RefSeq; NP_001334797.1; NM_001347868.1. [Q15697-1]
DR RefSeq; NP_003441.1; NM_003450.2. [Q15697-1]
DR PDB; 1Y7Q; NMR; -; A/B=37-132.
DR PDBsum; 1Y7Q; -.
DR AlphaFoldDB; Q15697; -.
DR SMR; Q15697; -.
DR BioGRID; 113516; 63.
DR IntAct; Q15697; 20.
DR MINT; Q15697; -.
DR STRING; 9606.ENSP00000268655; -.
DR iPTMnet; Q15697; -.
DR PhosphoSitePlus; Q15697; -.
DR BioMuta; ZNF174; -.
DR DMDM; 3123173; -.
DR EPD; Q15697; -.
DR jPOST; Q15697; -.
DR MassIVE; Q15697; -.
DR MaxQB; Q15697; -.
DR PaxDb; Q15697; -.
DR PeptideAtlas; Q15697; -.
DR PRIDE; Q15697; -.
DR ProteomicsDB; 60705; -. [Q15697-1]
DR ProteomicsDB; 60706; -. [Q15697-2]
DR ABCD; Q15697; 2 sequenced antibodies.
DR Antibodypedia; 1362; 221 antibodies from 29 providers.
DR DNASU; 7727; -.
DR Ensembl; ENST00000268655.5; ENSP00000268655.4; ENSG00000103343.13. [Q15697-1]
DR Ensembl; ENST00000344823.9; ENSP00000339781.5; ENSG00000103343.13. [Q15697-2]
DR Ensembl; ENST00000571936.5; ENSP00000460397.1; ENSG00000103343.13. [Q15697-1]
DR Ensembl; ENST00000575752.5; ENSP00000461502.1; ENSG00000103343.13. [Q15697-2]
DR GeneID; 7727; -.
DR KEGG; hsa:7727; -.
DR MANE-Select; ENST00000268655.5; ENSP00000268655.4; NM_003450.3; NP_003441.1.
DR UCSC; uc002cvb.4; human. [Q15697-1]
DR CTD; 7727; -.
DR DisGeNET; 7727; -.
DR GeneCards; ZNF174; -.
DR HGNC; HGNC:12963; ZNF174.
DR HPA; ENSG00000103343; Low tissue specificity.
DR MIM; 603900; gene.
DR neXtProt; NX_Q15697; -.
DR OpenTargets; ENSG00000103343; -.
DR PharmGKB; PA37545; -.
DR VEuPathDB; HostDB:ENSG00000103343; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162024; -.
DR HOGENOM; CLU_002678_53_2_1; -.
DR InParanoid; Q15697; -.
DR OMA; AQKPFTH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q15697; -.
DR TreeFam; TF338582; -.
DR PathwayCommons; Q15697; -.
DR SignaLink; Q15697; -.
DR BioGRID-ORCS; 7727; 24 hits in 1101 CRISPR screens.
DR ChiTaRS; ZNF174; human.
DR EvolutionaryTrace; Q15697; -.
DR GenomeRNAi; 7727; -.
DR Pharos; Q15697; Tbio.
DR PRO; PR:Q15697; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q15697; protein.
DR Bgee; ENSG00000103343; Expressed in endothelial cell and 124 other tissues.
DR ExpressionAtlas; Q15697; baseline and differential.
DR Genevisible; Q15697; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR027778; Zfp174.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23226:SF175; PTHR23226:SF175; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..407
FT /note="Zinc finger protein 174"
FT /id="PRO_0000047439"
FT DOMAIN 59..124
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 326..348
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 382..405
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 210..234
FT /note="APRMRSDNKENPQQEGAKGAKPCAV -> LLIEKTDPNMATDELPCKLWLSF
FT IA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_006897"
FT VAR_SEQ 235..407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_006898"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1Y7Q"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:1Y7Q"
FT HELIX 61..75
FT /evidence="ECO:0007829|PDB:1Y7Q"
FT HELIX 82..97
FT /evidence="ECO:0007829|PDB:1Y7Q"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:1Y7Q"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:1Y7Q"
SQ SEQUENCE 407 AA; 46455 MW; 1FAB4A631EA2ABCC CRC64;
MAAKMEITLS SNTEASSKQE RHIIAKLEEK RGPPLQKNCP DPELCRQSFR RFCYQEVSGP
QEALSQLRQL CRQWLQPELH TKEQILELLV MEQFLTILPP EIQARVRHRC PMSSKEIVTL
VEDFHRASKK PKQWVAVCMQ GQKVLLEKTG SQLGEQELPD FQPQTPRRDL RESSPAEPSQ
AGAYDRLSPH HWEKSPLLQE PTPKLAGTEA PRMRSDNKEN PQQEGAKGAK PCAVSAGRSK
GNGLQNPEPR GANMSEPRLS RRQVSSPNAQ KPFAHYQRHC RVEYISSPLK SHPLRELKKS
KGGKRSLSNR LQHLGHQPTR SAKKPYKCDD CGKSFTWNSE LKRHKRVHTG ERPYTCGECG
NCFGRQSTLK LHQRIHTGEK PYQCGQCGKS FRQSSNLHQH HRLHHGD
