ID   ZN256_HUMAN             Reviewed;         627 AA.
AC   Q9Y2P7; B2RA92; Q53Y85; Q9BV71;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Zinc finger protein 256;
DE   AltName: Full=Bone marrow zinc finger 3;
DE            Short=BMZF-3;
GN   Name=ZNF256; Synonyms=BMZF3;
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 2).
RC   TISSUE=Bone marrow;
RX   PubMed=10585455; DOI=10.1074/jbc.274.50.35741;
RA   Han Z.-G., Zhang Q.-H., Ye M., Kan L.-X., Gu B.-W., He K.-L., Shi S.-L.,
RA   Zhou J., Fu G., Mao M., Chen S.-J., Yu L., Chen Z.;
RT   "Molecular cloning of six novel Kruppel-like zinc finger genes from
RT   hematopoietic cells and identification of a novel transregulatory domain
RT   KRNB.";
RL   J. Biol. Chem. 274:35741-35748(1999).
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=Tongue;
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   FUNCTION, INDUCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH
RP   TRIM28.
RX   PubMed=18060868; DOI=10.1016/j.bbrc.2007.11.118;
RA   Suzuki C., Murakumo Y., Kawase Y., Sato T., Morinaga T., Fukuda N.,
RA   Enomoto A., Ichihara M., Takahashi M.;
RT   "A novel GDNF-inducible gene, BMZF3, encodes a transcriptional repressor
RT   associated with KAP-1.";
RL   Biochem. Biophys. Res. Commun. 366:226-232(2008).
CC   -!- FUNCTION: Transcriptional repressor that plays a role in cell
CC       proliferation. Requires TRIM28 for its activity.
CC       {ECO:0000269|PubMed:18060868}.
CC   -!- SUBUNIT: Interacts with TRIM28. {ECO:0000269|PubMed:18060868}.
CC   -!- INTERACTION:
CC       Q9Y2P7; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-12223065, EBI-10172290;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18060868}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y2P7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y2P7-2; Sequence=VSP_037721;
CC   -!- INDUCTION: By GDNF/glial cell line-derived neurotrophic factor.
CC       {ECO:0000269|PubMed:18060868}.
CC   -!- DOMAIN: The KRAB domain mediates interaction with TRIM28 and is
CC       required for transcriptional repressor activity.
CC       {ECO:0000269|PubMed:18060868}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF067165; AAD32449.1; -; mRNA.
DR   EMBL; BT006853; AAP35499.1; -; mRNA.
DR   EMBL; AK314094; BAG36789.1; -; mRNA.
DR   EMBL; AC008969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC010326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001438; AAH01438.2; -; mRNA.
DR   CCDS; CCDS12966.1; -. [Q9Y2P7-1]
DR   RefSeq; NP_005764.2; NM_005773.2. [Q9Y2P7-1]
DR   RefSeq; XP_016881627.1; XM_017026138.1.
DR   AlphaFoldDB; Q9Y2P7; -.
DR   SMR; Q9Y2P7; -.
DR   BioGRID; 115474; 6.
DR   IntAct; Q9Y2P7; 2.
DR   STRING; 9606.ENSP00000282308; -.
DR   iPTMnet; Q9Y2P7; -.
DR   PhosphoSitePlus; Q9Y2P7; -.
DR   BioMuta; ZNF256; -.
DR   DMDM; 254763378; -.
DR   MassIVE; Q9Y2P7; -.
DR   MaxQB; Q9Y2P7; -.
DR   PaxDb; 9606-ENSP00000282308; -.
DR   PeptideAtlas; Q9Y2P7; -.
DR   ProteomicsDB; 85855; -. [Q9Y2P7-1]
DR   ProteomicsDB; 85856; -. [Q9Y2P7-2]
DR   Antibodypedia; 33319; 150 antibodies from 23 providers.
DR   DNASU; 10172; -.
DR   Ensembl; ENST00000282308.4; ENSP00000282308.2; ENSG00000152454.4. [Q9Y2P7-1]
DR   GeneID; 10172; -.
DR   KEGG; hsa:10172; -.
DR   MANE-Select; ENST00000282308.4; ENSP00000282308.2; NM_005773.3; NP_005764.2.
DR   UCSC; uc002qqu.4; human. [Q9Y2P7-1]
DR   AGR; HGNC:13049; -.
DR   CTD; 10172; -.
DR   GeneCards; ZNF256; -.
DR   HGNC; HGNC:13049; ZNF256.
DR   HPA; ENSG00000152454; Low tissue specificity.
DR   MIM; 606956; gene.
DR   neXtProt; NX_Q9Y2P7; -.
DR   OpenTargets; ENSG00000152454; -.
DR   PharmGKB; PA37627; -.
DR   VEuPathDB; HostDB:ENSG00000152454; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000154734; -.
DR   HOGENOM; CLU_002678_55_2_1; -.
DR   InParanoid; Q9Y2P7; -.
DR   OMA; SRERCYM; -.
DR   OrthoDB; 5155879at2759; -.
DR   PhylomeDB; Q9Y2P7; -.
DR   TreeFam; TF339848; -.
DR   PathwayCommons; Q9Y2P7; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q9Y2P7; -.
DR   BioGRID-ORCS; 10172; 13 hits in 1169 CRISPR screens.
DR   GenomeRNAi; 10172; -.
DR   Pharos; Q9Y2P7; Tdark.
DR   PRO; PR:Q9Y2P7; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9Y2P7; Protein.
DR   Bgee; ENSG00000152454; Expressed in oocyte and 120 other cell types or tissues.
DR   ExpressionAtlas; Q9Y2P7; baseline and differential.
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: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:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 15.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23232; KRAB DOMAIN C2H2 ZINC FINGER; 1.
DR   PANTHER; PTHR23232:SF143; ZINC FINGER PROTEIN 747; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 14.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 15.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 9.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
DR   Genevisible; Q9Y2P7; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..627
FT                   /note="Zinc finger protein 256"
FT                   /id="PRO_0000047489"
FT   DOMAIN          14..96
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         90..112
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         239..261
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         267..289
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         295..317
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         323..345
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         351..373
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         379..401
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         407..429
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         435..457
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         463..485
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         491..513
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         519..541
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         547..569
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         575..597
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         603..625
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          55..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..153
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10585455,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT                   /id="VSP_037721"
FT   VARIANT         304
FT                   /note="F -> I (in dbSNP:rs953619)"
FT                   /id="VAR_058326"
FT   CONFLICT        254
FT                   /note="L -> P (in Ref. 3; BAG36789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        552
FT                   /note="C -> F (in Ref. 3; BAG36789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        574
FT                   /note="P -> L (in Ref. 1; AAD32449)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   627 AA;  71871 MW;  F03506B03E4A6E86 CRC64;
     MAAAELTAPA QGIVTFEDVA VYFSWKEWGL LDEAQKCLYH DVMLENLTLT TSLGGSGAGD
     EEAPYQQSTS PQRVSQVRIP KALPSPQKTN PCEICGPVLR QILHLVEHQG THHGQKLYTD
     GACRKQLQFT AYLHQHQKQH VGQKHFRSNG GRDMFLSSCT FEVSGKPFTC KEVGKDFLVR
     SRFLQQQAAH TRKKSNRTKS AVAFHSVKNH YNWGECVKAF SYKHVRVQHQ GDLIRERSYM
     CSECGKSFST SCSLSDHLRV HTSEKPYTCG ECGKSYRQSS SLITHRRIHT GVRPHQCDEC
     GKLFNRKYDL LIHQRVHTGE RPYKCSECGK SFSHSSSLIT HQRIHTGMRP YECSECGKSF
     IHSSSLITHQ RVHTGTRPYM CSECGKSFSQ SCHLIKHRRL HIGEGPYECS ECGKLFTYRS
     RFFQHQRVHT GVRSHECHEC GKLFSRKFDL IVHERVHTGE RPYECSECGK SFTCKSYLIS
     HWKVHTGARP YECGECGKSF THSSTLLQHQ RVHTGERPYE CNECGKFFSQ SSSLIRHRRS
     HTGERPYECS ECWKSFSNHS SLVKHRRVHT GERPYECSEC GKSFSQSSNL TNHQRIHSGE
     RPYECSDCGK FFTFNSNLLK HQNVHKG
//