ZN274_HUMAN
ID ZN274_HUMAN Reviewed; 653 AA.
AC Q96GC6; Q53XU4; Q6MZG1; Q8WY37; Q8WY38; Q92969; Q9UII0; Q9UII1;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Neurotrophin receptor-interacting factor homolog;
DE AltName: Full=Zinc finger protein 274;
DE AltName: Full=Zinc finger protein HFB101;
DE AltName: Full=Zinc finger protein with KRAB and SCAN domains 19;
DE AltName: Full=Zinc finger protein zfp2;
DE Short=Zf2;
GN Name=ZNF274; Synonyms=ZKSCAN19; ORFNames=SP2114;
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), SUBCELLULAR LOCATION,
RP FUNCTION AS A REPRESSOR, AND VARIANT ILE-147.
RC TISSUE=Fetal brain;
RX PubMed=10777669; DOI=10.1006/geno.2000.6140;
RA Yano K., Ueki N., Oda T., Seki N., Masuho Y., Muramatsu M.;
RT "Identification and characterization of human ZNF274 cDNA, Which encodes a
RT novel kruppel-type zinc-finger protein having nucleolar targeting
RT ability.";
RL Genomics 65:75-80(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP ILE-147.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Salivary gland;
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 MRNA] (ISOFORM 1), AND VARIANT ILE-147.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-147.
RC TISSUE=Skin;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 503-653.
RX PubMed=10520746; DOI=10.3109/10425179809072191;
RA Petroni D., Bartolini E., Chiaramonte R., Ottolenghi S., Comi P.;
RT "Computer sequence analysis of human highly conserved zinc finger
RT modules.";
RL DNA Seq. 9:163-169(1998).
RN [8]
RP DNA-BINDING, AND INTERACTION WITH SETDB1 AND TRIM28.
RX PubMed=21170338; DOI=10.1371/journal.pone.0015082;
RA Frietze S., O'Geen H., Blahnik K.R., Jin V.X., Farnham P.J.;
RT "ZNF274 recruits the histone methyltransferase SETDB1 to the 3' ends of ZNF
RT genes.";
RL PLoS ONE 5:E15082-E15082(2010).
RN [9]
RP FUNCTION, INTERACTION WITH ATRX, AND FORMATION OF A COMPLEX WITH ATRX;
RP TRIM28 AND SETDB1.
RX PubMed=27029610; DOI=10.1080/15592294.2016.1169351;
RA Valle-Garcia D., Qadeer Z.A., McHugh D.S., Ghiraldini F.G., Chowdhury A.H.,
RA Hasson D., Dyer M.A., Recillas-Targa F., Bernstein E.;
RT "ATRX binds to atypical chromatin domains at the 3' exons of zinc finger
RT genes to preserve H3K9me3 enrichment.";
RL Epigenetics 11:398-414(2016).
CC -!- FUNCTION: Probable transcription repressor. Specifically binds to the
CC 3'-end of zinc-finger coding genes and recruiting chromatin-modifying
CC proteins such as SETDB1 and TRIM28/KAP1, leading to transcription
CC repression. The SETDB1-TRIM28-ZNF274 complex may play a role in
CC recruiting ATRX to the 3'-exons of zinc-finger coding genes with
CC atypical chromatin signatures to establish or maintain/protect H3K9me3
CC at these transcriptionally active regions (PubMed:27029610).
CC {ECO:0000269|PubMed:10777669, ECO:0000269|PubMed:27029610}.
CC -!- SUBUNIT: Interacts with SETDB1 and TRIM28/KAP1. Interacts with ATRX.
CC Forms a complex with ATRX, SETDB1 and TRIM28 (PubMed:27029610).
CC {ECO:0000269|PubMed:21170338, ECO:0000269|PubMed:27029610}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:10777669}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=SP2114a;
CC IsoId=Q96GC6-1; Sequence=Displayed;
CC Name=2; Synonyms=ZNF274a;
CC IsoId=Q96GC6-2; Sequence=VSP_006911;
CC Name=3; Synonyms=ZNF274b;
CC IsoId=Q96GC6-3; Sequence=VSP_006910;
CC Name=4; Synonyms=SP2114b;
CC IsoId=Q96GC6-4; Sequence=VSP_006912, VSP_006913;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AB029149; BAA88522.1; -; mRNA.
DR EMBL; AB029150; BAA88523.1; -; mRNA.
DR EMBL; AF275680; AAG24390.1; -; mRNA.
DR EMBL; AF275681; AAG24391.1; -; mRNA.
DR EMBL; BX641169; CAE46074.1; -; mRNA.
DR EMBL; BT007304; AAP35968.1; -; mRNA.
DR EMBL; AC008751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009763; AAH09763.1; -; mRNA.
DR EMBL; U71598; AAB16810.1; -; mRNA.
DR CCDS; CCDS74473.1; -. [Q96GC6-1]
DR CCDS; CCDS74474.1; -. [Q96GC6-2]
DR CCDS; CCDS74476.1; -. [Q96GC6-3]
DR RefSeq; NP_001265663.1; NM_001278734.1.
DR RefSeq; NP_057408.2; NM_016324.3. [Q96GC6-3]
DR RefSeq; NP_057409.1; NM_016325.3. [Q96GC6-2]
DR RefSeq; NP_598009.1; NM_133502.2. [Q96GC6-1]
DR RefSeq; XP_011524629.1; XM_011526327.1. [Q96GC6-3]
DR RefSeq; XP_016881663.1; XM_017026174.1. [Q96GC6-3]
DR AlphaFoldDB; Q96GC6; -.
DR SMR; Q96GC6; -.
DR BioGRID; 115999; 16.
DR IntAct; Q96GC6; 10.
DR STRING; 9606.ENSP00000478533; -.
DR iPTMnet; Q96GC6; -.
DR PhosphoSitePlus; Q96GC6; -.
DR BioMuta; ZNF274; -.
DR DMDM; 327478548; -.
DR EPD; Q96GC6; -.
DR jPOST; Q96GC6; -.
DR MassIVE; Q96GC6; -.
DR MaxQB; Q96GC6; -.
DR PaxDb; Q96GC6; -.
DR PeptideAtlas; Q96GC6; -.
DR PRIDE; Q96GC6; -.
DR ProteomicsDB; 76611; -. [Q96GC6-1]
DR ProteomicsDB; 76612; -. [Q96GC6-2]
DR ProteomicsDB; 76613; -. [Q96GC6-3]
DR ProteomicsDB; 76614; -. [Q96GC6-4]
DR Antibodypedia; 9924; 226 antibodies from 23 providers.
DR DNASU; 10782; -.
DR Ensembl; ENST00000345813.7; ENSP00000321187.5; ENSG00000171606.18. [Q96GC6-2]
DR Ensembl; ENST00000424679.6; ENSP00000409872.3; ENSG00000171606.18. [Q96GC6-3]
DR Ensembl; ENST00000610905.4; ENSP00000478533.1; ENSG00000171606.18. [Q96GC6-1]
DR Ensembl; ENST00000617501.5; ENSP00000484810.1; ENSG00000171606.18. [Q96GC6-1]
DR GeneID; 10782; -.
DR KEGG; hsa:10782; -.
DR MANE-Select; ENST00000617501.5; ENSP00000484810.1; NM_133502.3; NP_598009.1.
DR UCSC; uc032igq.2; human. [Q96GC6-1]
DR CTD; 10782; -.
DR DisGeNET; 10782; -.
DR GeneCards; ZNF274; -.
DR HGNC; HGNC:13068; ZNF274.
DR HPA; ENSG00000171606; Low tissue specificity.
DR MIM; 605467; gene.
DR neXtProt; NX_Q96GC6; -.
DR OpenTargets; ENSG00000171606; -.
DR PharmGKB; PA37644; -.
DR VEuPathDB; HostDB:ENSG00000171606; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162111; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; Q96GC6; -.
DR OMA; VEDATWI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96GC6; -.
DR TreeFam; TF338018; -.
DR PathwayCommons; Q96GC6; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q96GC6; -.
DR BioGRID-ORCS; 10782; 11 hits in 290 CRISPR screens.
DR ChiTaRS; ZNF274; human.
DR GeneWiki; ZNF274; -.
DR GenomeRNAi; 10782; -.
DR Pharos; Q96GC6; Tbio.
DR PRO; PR:Q96GC6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96GC6; protein.
DR Bgee; ENSG00000171606; Expressed in left ovary and 199 other tissues.
DR ExpressionAtlas; Q96GC6; baseline and differential.
DR Genevisible; Q96GC6; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:GO_Central.
DR GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR CDD; cd07765; KRAB_A-box; 2.
DR CDD; cd07936; SCAN; 1.
DR DisProt; DP01556; -.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 2.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00349; KRAB; 2.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF109640; SSF109640; 2.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50805; KRAB; 2.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..653
FT /note="Neurotrophin receptor-interacting factor homolog"
FT /id="PRO_0000047501"
FT DOMAIN 14..85
FT /note="KRAB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT DOMAIN 161..243
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 287..360
FT /note="KRAB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 507..529
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 535..557
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 563..585
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 591..613
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 619..641
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 139..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..653
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..281
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498874,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_006912"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10777669"
FT /id="VSP_006910"
FT VAR_SEQ 55..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10777669"
FT /id="VSP_006911"
FT VAR_SEQ 282..284
FT /note="LPE -> MLQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498874,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_006913"
FT VARIANT 147
FT /note="V -> I (in dbSNP:rs7256349)"
FT /evidence="ECO:0000269|PubMed:10777669,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15498874,
FT ECO:0000269|Ref.4"
FT /id="VAR_064920"
FT CONFLICT 14
FT /note="V -> E (in Ref. 2; AAG24390)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="A -> T (in Ref. 2; AAG24390)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="F -> S (in Ref. 3; CAE46074)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="G -> W (in Ref. 1; BAA88522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 74177 MW; 8B91F51F4BEED925 CRC64;
MASRLPTAWS CEPVTFEDVT LGFTPEEWGL LDLKQKSLYR EVMLENYRNL VSVEHQLSKP
DVVSQLEEAE DFWPVERGIP QDTIPEYPEL QLDPKLDPLP AESPLMNIEV VEVLTLNQEV
AGPRNAQIQA LYAEDGSLSA DAPSEQVQQQ GKHPGDPEAA RQRFRQFRYK DMTGPREALD
QLRELCHQWL QPKARSKEQI LELLVLEQFL GALPVKLRTW VESQHPENCQ EVVALVEGVT
WMSEEEVLPA GQPAEGTTCC LEVTAQQEEK QEDAAICPVT VLPEEPVTFQ DVAVDFSREE
WGLLGPTQRT EYRDVMLETF GHLVSVGWET TLENKELAPN SDIPEEEPAP SLKVQESSRD
CALSSTLEDT LQGGVQEVQD TVLKQMESAQ EKDLPQKKHF DNRESQANSG ALDTNQVSLQ
KIDNPESQAN SGALDTNQVL LHKIPPRKRL RKRDSQVKSM KHNSRVKIHQ KSCERQKAKE
GNGCRKTFSR STKQITFIRI HKGSQVCRCS ECGKIFRNPR YFSVHKKIHT GERPYVCQDC
GKGFVQSSSL TQHQRVHSGE RPFECQECGR TFNDRSAISQ HLRTHTGAKP YKCQDCGKAF
RQSSHLIRHQ RTHTGERPYA CNKCGKAFTQ SSHLIGHQRT HNRTKRKKKQ PTS
