ZFP28_HUMAN
ID ZFP28_HUMAN Reviewed; 868 AA.
AC Q8NHY6; A0JNV6; K7ES88; Q8NHU8; Q9BY30; Q9P2B6;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Zinc finger protein 28 homolog;
DE Short=Zfp-28;
DE AltName: Full=Krueppel-like zinc finger factor X6;
GN Name=ZFP28; Synonyms=KIAA1431;
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).
RX PubMed=12127974; DOI=10.1016/s0006-291x(02)00759-3;
RA Zhou L., Zhu C., Luo K., Li Y., Pi H., Yuan W., Wang Y., Huang C., Liu M.,
RA Wu X.;
RT "Identification and characterization of two novel zinc finger genes, ZNF359
RT and ZFP28, in human development.";
RL Biochem. Biophys. Res. Commun. 295:862-868(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
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 446-868 (ISOFORM 1).
RC TISSUE=Heart muscle;
RA Brand N.J., Mullen A.J., Barton P.J.R.;
RT "Identification of C2H2 zinc finger factor sequences in human heart.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP STRUCTURE BY NMR OF 415-812.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C2H2 type zinc finger region of human zinc
RT finger protein 28 homolog.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: May be involved in transcriptional regulation. May have a
CC role in embryonic development.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NHY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NHY6-2; Sequence=VSP_055934, VSP_055935;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92669.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF507045; AAM28892.1; -; mRNA.
DR EMBL; AB037852; BAA92669.1; ALT_INIT; mRNA.
DR EMBL; AC005498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028416; AAH28416.1; -; mRNA.
DR EMBL; BC099903; AAH99903.1; -; mRNA.
DR EMBL; BC127003; AAI27004.1; -; mRNA.
DR EMBL; AF226995; AAK28320.1; -; mRNA.
DR CCDS; CCDS12946.1; -. [Q8NHY6-1]
DR CCDS; CCDS77363.1; -. [Q8NHY6-2]
DR RefSeq; NP_001295369.1; NM_001308440.1. [Q8NHY6-2]
DR RefSeq; NP_065879.1; NM_020828.1. [Q8NHY6-1]
DR PDB; 2EM2; NMR; -; A=584-616.
DR PDB; 2EM3; NMR; -; A=640-672.
DR PDB; 2EM4; NMR; -; A=724-756.
DR PDB; 2EMJ; NMR; -; A=612-644.
DR PDB; 2EMK; NMR; -; A=668-700.
DR PDB; 2EML; NMR; -; A=752-784.
DR PDB; 2EN9; NMR; -; A=415-447.
DR PDB; 2ENH; NMR; -; A=556-588.
DR PDB; 2EOH; NMR; -; A=780-812.
DR PDB; 2EP0; NMR; -; A=528-560.
DR PDB; 2EPX; NMR; -; A=471-504.
DR PDB; 2EPZ; NMR; -; A=500-532.
DR PDB; 2YTM; NMR; -; A=696-728.
DR PDBsum; 2EM2; -.
DR PDBsum; 2EM3; -.
DR PDBsum; 2EM4; -.
DR PDBsum; 2EMJ; -.
DR PDBsum; 2EMK; -.
DR PDBsum; 2EML; -.
DR PDBsum; 2EN9; -.
DR PDBsum; 2ENH; -.
DR PDBsum; 2EOH; -.
DR PDBsum; 2EP0; -.
DR PDBsum; 2EPX; -.
DR PDBsum; 2EPZ; -.
DR PDBsum; 2YTM; -.
DR AlphaFoldDB; Q8NHY6; -.
DR SMR; Q8NHY6; -.
DR BioGRID; 126637; 5.
DR IntAct; Q8NHY6; 6.
DR MINT; Q8NHY6; -.
DR STRING; 9606.ENSP00000301318; -.
DR iPTMnet; Q8NHY6; -.
DR PhosphoSitePlus; Q8NHY6; -.
DR BioMuta; ZFP28; -.
DR DMDM; 33517131; -.
DR jPOST; Q8NHY6; -.
DR MassIVE; Q8NHY6; -.
DR MaxQB; Q8NHY6; -.
DR PaxDb; Q8NHY6; -.
DR PeptideAtlas; Q8NHY6; -.
DR PRIDE; Q8NHY6; -.
DR ProteomicsDB; 73791; -. [Q8NHY6-1]
DR Antibodypedia; 33216; 66 antibodies from 16 providers.
DR DNASU; 140612; -.
DR Ensembl; ENST00000301318.8; ENSP00000301318.3; ENSG00000196867.8. [Q8NHY6-1]
DR Ensembl; ENST00000591844.5; ENSP00000468603.1; ENSG00000196867.8. [Q8NHY6-2]
DR GeneID; 140612; -.
DR KEGG; hsa:140612; -.
DR MANE-Select; ENST00000301318.8; ENSP00000301318.3; NM_020828.2; NP_065879.1.
DR UCSC; uc002qni.4; human. [Q8NHY6-1]
DR CTD; 140612; -.
DR GeneCards; ZFP28; -.
DR HGNC; HGNC:17801; ZFP28.
DR HPA; ENSG00000196867; Low tissue specificity.
DR neXtProt; NX_Q8NHY6; -.
DR OpenTargets; ENSG00000196867; -.
DR PharmGKB; PA38469; -.
DR VEuPathDB; HostDB:ENSG00000196867; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162376; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; Q8NHY6; -.
DR OMA; TFRENWD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8NHY6; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; Q8NHY6; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q8NHY6; -.
DR BioGRID-ORCS; 140612; 17 hits in 1096 CRISPR screens.
DR ChiTaRS; ZFP28; human.
DR EvolutionaryTrace; Q8NHY6; -.
DR GenomeRNAi; 140612; -.
DR Pharos; Q8NHY6; Tbio.
DR PRO; PR:Q8NHY6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8NHY6; protein.
DR Bgee; ENSG00000196867; Expressed in cortical plate and 125 other tissues.
DR ExpressionAtlas; Q8NHY6; baseline and differential.
DR Genevisible; Q8NHY6; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 2.
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; 2.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00349; KRAB; 2.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF109640; SSF109640; 2.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..868
FT /note="Zinc finger protein 28 homolog"
FT /id="PRO_0000047289"
FT DOMAIN 103..174
FT /note="KRAB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT DOMAIN 232..299
FT /note="KRAB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 420..442
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..470
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..499
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 505..527
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 533..555
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 561..583
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 589..611
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 617..639
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 645..667
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 673..695
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 701..723
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 729..751
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 757..779
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 785..807
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 813..835
FT /note="C2H2-type 15; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 301..349
FT /note="QRSVHETQELFPKQDSYAEGVTDRTSNTKLDCSSFRENWDSDYVFGRKL ->
FT ECRRAWCGKSTARESGAFTKKAASSLIYSRKLYPGSLGLERKLNSGSSK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055934"
FT VAR_SEQ 350..868
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055935"
FT VARIANT 141
FT /note="S -> W (in dbSNP:rs34136271)"
FT /id="VAR_052738"
FT VARIANT 620
FT /note="A -> V (in dbSNP:rs10409531)"
FT /id="VAR_024190"
FT CONFLICT 10
FT /note="R -> H (in Ref. 4; AAH28416/AAH99903)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="F -> S (in Ref. 2; BAA92669)"
FT /evidence="ECO:0000305"
FT CONFLICT 766..785
FT /note="Missing (in Ref. 5)"
FT /evidence="ECO:0000305"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:2EN9"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:2EN9"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:2EPX"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:2EPX"
FT HELIX 488..495
FT /evidence="ECO:0007829|PDB:2EPX"
FT TURN 496..501
FT /evidence="ECO:0007829|PDB:2EPX"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:2EPZ"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:2EPZ"
FT HELIX 517..524
FT /evidence="ECO:0007829|PDB:2EPZ"
FT TURN 525..529
FT /evidence="ECO:0007829|PDB:2EPZ"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:2EP0"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:2EP0"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:2EP0"
FT HELIX 545..552
FT /evidence="ECO:0007829|PDB:2EP0"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:2EP0"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:2ENH"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:2ENH"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:2ENH"
FT HELIX 574..579
FT /evidence="ECO:0007829|PDB:2ENH"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:2ENH"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:2EM2"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:2EM2"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:2EM2"
FT HELIX 601..611
FT /evidence="ECO:0007829|PDB:2EM2"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:2EMJ"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:2EMJ"
FT STRAND 625..628
FT /evidence="ECO:0007829|PDB:2EMJ"
FT HELIX 629..639
FT /evidence="ECO:0007829|PDB:2EMJ"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:2EM3"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:2EM3"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:2EM3"
FT HELIX 657..667
FT /evidence="ECO:0007829|PDB:2EM3"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:2EMK"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:2EMK"
FT HELIX 685..695
FT /evidence="ECO:0007829|PDB:2EMK"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:2YTM"
FT TURN 704..707
FT /evidence="ECO:0007829|PDB:2YTM"
FT HELIX 713..724
FT /evidence="ECO:0007829|PDB:2YTM"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:2EM4"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:2EM4"
FT STRAND 737..740
FT /evidence="ECO:0007829|PDB:2EM4"
FT HELIX 741..751
FT /evidence="ECO:0007829|PDB:2EM4"
FT STRAND 752..755
FT /evidence="ECO:0007829|PDB:2EM4"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:2EML"
FT STRAND 760..762
FT /evidence="ECO:0007829|PDB:2EML"
FT STRAND 765..768
FT /evidence="ECO:0007829|PDB:2EML"
FT HELIX 769..776
FT /evidence="ECO:0007829|PDB:2EML"
FT HELIX 777..779
FT /evidence="ECO:0007829|PDB:2EML"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:2EOH"
FT HELIX 797..806
FT /evidence="ECO:0007829|PDB:2EOH"
FT CONFLICT Q8NHY6-2:324
FT /note="S -> F (in Ref. 4; AAH28416/AAH99903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 868 AA; 98705 MW; E5959243B41CE3F3 CRC64;
MRGAASASVR EPTPLPGRGA PRTKPRAGRG PTVGTPATLA LPARGRPRSR NGLASKGQRG
AAPTGPGHRA LPSRDTALPQ ERNKKLEAVG TGIEPKAMSQ GLVTFGDVAV DFSQEEWEWL
NPIQRNLYRK VMLENYRNLA SLGLCVSKPD VISSLEQGKE PWTVKRKMTR AWCPDLKAVW
KIKELPLKKD FCEGKLSQAV ITERLTSYNL EYSLLGEHWD YDALFETQPG LVTIKNLAVD
FRQQLHPAQK NFCKNGIWEN NSDLGSAGHC VAKPDLVSLL EQEKEPWMVK RELTGSLFSG
QRSVHETQEL FPKQDSYAEG VTDRTSNTKL DCSSFRENWD SDYVFGRKLA VGQETQFRQE
PITHNKTLSK ERERTYNKSG RWFYLDDSEE KVHNRDSIKN FQKSSVVIKQ TGIYAGKKLF
KCNECKKTFT QSSSLTVHQR IHTGEKPYKC NECGKAFSDG SSFARHQRCH TGKKPYECIE
CGKAFIQNTS LIRHWRYYHT GEKPFDCIDC GKAFSDHIGL NQHRRIHTGE KPYKCDVCHK
SFRYGSSLTV HQRIHTGEKP YECDVCRKAF SHHASLTQHQ RVHSGEKPFK CKECGKAFRQ
NIHLASHLRI HTGEKPFECA ECGKSFSISS QLATHQRIHT GEKPYECKVC SKAFTQKAHL
AQHQKTHTGE KPYECKECGK AFSQTTHLIQ HQRVHTGEKP YKCMECGKAF GDNSSCTQHQ
RLHTGQRPYE CIECGKAFKT KSSLICHRRS HTGEKPYECS VCGKAFSHRQ SLSVHQRIHS
GKKPYECKEC RKTFIQIGHL NQHKRVHTGE RSYNYKKSRK VFRQTAHLAH HQRIHTGESS
TCPSLPSTSN PVDLFPKFLW NPSSLPSP
