ID   ZNF28_HUMAN             Reviewed;         718 AA.
AC   P17035; A8KAK9; B4E3G0; B9EIK7; Q5H9V1; Q5HYM9; Q6ZML9; Q6ZN56;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 5.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Zinc finger protein 28;
DE   AltName: Full=Zinc finger protein KOX24;
GN   Name=ZNF28; Synonyms=KOX24;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP   GLN-465 AND THR-524.
RC   TISSUE=Cerebellum, and Uterus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-465
RP   AND THR-524.
RC   TISSUE=Rectum tumor, and Seminoma;
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   [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] (ISOFORM 2).
RC   TISSUE=Brain;
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 215-270 (ISOFORMS 1/2).
RC   TISSUE=Lymphoid tissue;
RX   PubMed=2288909;
RA   Thiesen H.-J.;
RT   "Multiple genes encoding zinc finger domains are expressed in human T
RT   cells.";
RL   New Biol. 2:363-374(1990).
RN   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-89 AND LYS-428, AND
RP   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).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P17035-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P17035-2; Sequence=VSP_029007;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD18706.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK131368; BAD18519.1; -; mRNA.
DR   EMBL; AK131574; BAD18706.1; ALT_INIT; mRNA.
DR   EMBL; AK293074; BAF85763.1; -; mRNA.
DR   EMBL; AK304704; BAG65472.1; -; mRNA.
DR   EMBL; CR933598; CAI45923.1; -; mRNA.
DR   EMBL; BX640767; CAI46258.1; -; mRNA.
DR   EMBL; AC008813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC140720; AAI40721.1; -; mRNA.
DR   EMBL; X52355; CAA36581.1; -; mRNA.
DR   CCDS; CCDS33093.2; -. [P17035-1]
DR   CCDS; CCDS92676.1; -. [P17035-2]
DR   PIR; I37964; I37964.
DR   RefSeq; NP_008900.3; NM_006969.3. [P17035-1]
DR   RefSeq; XP_011525564.1; XM_011527262.2.
DR   AlphaFoldDB; P17035; -.
DR   SMR; P17035; -.
DR   BioGRID; 113406; 9.
DR   IntAct; P17035; 3.
DR   STRING; 9606.ENSP00000397693; -.
DR   GlyGen; P17035; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P17035; -.
DR   PhosphoSitePlus; P17035; -.
DR   BioMuta; ZNF28; -.
DR   DMDM; 313104321; -.
DR   EPD; P17035; -.
DR   jPOST; P17035; -.
DR   MassIVE; P17035; -.
DR   MaxQB; P17035; -.
DR   PaxDb; 9606-ENSP00000397693; -.
DR   PeptideAtlas; P17035; -.
DR   ProteomicsDB; 53436; -. [P17035-1]
DR   ProteomicsDB; 53437; -. [P17035-2]
DR   Antibodypedia; 56951; 62 antibodies from 13 providers.
DR   DNASU; 7576; -.
DR   Ensembl; ENST00000438150.2; ENSP00000412143.2; ENSG00000198538.11. [P17035-2]
DR   Ensembl; ENST00000457749.7; ENSP00000397693.2; ENSG00000198538.11. [P17035-1]
DR   GeneID; 7576; -.
DR   KEGG; hsa:7576; -.
DR   MANE-Select; ENST00000457749.7; ENSP00000397693.2; NM_006969.5; NP_008900.3.
DR   UCSC; uc002qad.4; human. [P17035-1]
DR   AGR; HGNC:13073; -.
DR   CTD; 7576; -.
DR   DisGeNET; 7576; -.
DR   GeneCards; ZNF28; -.
DR   HGNC; HGNC:13073; ZNF28.
DR   HPA; ENSG00000198538; Low tissue specificity.
DR   MIM; 620466; gene.
DR   neXtProt; NX_P17035; -.
DR   OpenTargets; ENSG00000198538; -.
DR   PharmGKB; PA37649; -.
DR   VEuPathDB; HostDB:ENSG00000198538; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000165246; -.
DR   HOGENOM; CLU_002678_17_1_1; -.
DR   InParanoid; P17035; -.
DR   OMA; ASQRICC; -.
DR   OrthoDB; 4330832at2759; -.
DR   PhylomeDB; P17035; -.
DR   TreeFam; TF341892; -.
DR   PathwayCommons; P17035; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; P17035; -.
DR   BioGRID-ORCS; 7576; 10 hits in 1144 CRISPR screens.
DR   ChiTaRS; ZNF28; human.
DR   GenomeRNAi; 7576; -.
DR   Pharos; P17035; Tdark.
DR   PRO; PR:P17035; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P17035; Protein.
DR   Bgee; ENSG00000198538; Expressed in adrenal tissue and 108 other cell types or tissues.
DR   ExpressionAtlas; P17035; baseline and differential.
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; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 18.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24377; IP01015P-RELATED; 1.
DR   PANTHER; PTHR24377:SF765; ZINC FINGER PROTEIN 765; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 14.
DR   Pfam; PF13465; zf-H2C2_2; 1.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 18.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10.
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; 18.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..718
FT                   /note="Zinc finger protein 28"
FT                   /id="PRO_0000047357"
FT   DOMAIN          8..81
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         215..237
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         243..265
FT                   /note="C2H2-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         271..293
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         299..321
FT                   /note="C2H2-type 4; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         327..349
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         355..377
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         383..405
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         411..433
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         439..461
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         467..489
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         495..517
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         523..545
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         551..573
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         579..601
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         607..629
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         635..657
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         663..685
FT                   /note="C2H2-type 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         691..713
FT                   /note="C2H2-type 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        89
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        428
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..53
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029007"
FT   VARIANT         179
FT                   /note="R -> G (in dbSNP:rs13382164)"
FT                   /id="VAR_036841"
FT   VARIANT         465
FT                   /note="K -> Q (in dbSNP:rs10417163)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:17974005"
FT                   /id="VAR_036842"
FT   VARIANT         524
FT                   /note="M -> T (in dbSNP:rs8107444)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:17974005"
FT                   /id="VAR_036843"
FT   CONFLICT        65
FT                   /note="N -> D (in Ref. 1; BAD18519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="M -> T (in Ref. 1; BAF85763)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="C -> G (in Ref. 2; CAI46258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="K -> E (in Ref. 2; CAI45923)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        403
FT                   /note="R -> T (in Ref. 1; BAD18706 and 2; CAI46258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412
FT                   /note="K -> E (in Ref. 1; BAG65472)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        418
FT                   /note="K -> R (in Ref. 2; CAI46258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        498
FT                   /note="K -> T (in Ref. 2; CAI45923)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   718 AA;  83658 MW;  CF602657CFEC8633 CRC64;
     MALPQGLLTF RDVAIEFSQE EWKCLDPAQR TLYRDVMLEN YRNLVSLDIS SKCMMKTFFS
     TGQGNTEAFH TGTLQRQASH HIGDFCFQKI EKDIHGFQFQ WKEDETNDHA APMTEIKELT
     GSTGQHDQRH AGNKHIKDQL GLSFHSHLPE LHIFQPEGKI GNQVEKSINN ASSVSTSQRI
     CCRPKTHISN KYGNNSLHSS LLTQKRNVHM REKSFQCIES GKSFNCSSLL KKHQITHLEE
     KQCKCDVYGK VFNQKRYLAC HRRSHIDEKP YKCNECGKIF GHNTSLFLHK ALHTADKPYE
     CEECDKVFSR KSHLETHKII YTGGKPYKCK VCDKAFTCNS YLAKHTIIHT GEKPYKCNEC
     GKVFNRLSTL ARHRRLHTGE KPYECEECEK VFSRKSHLER HKRIHTGEKP YKCKVCDKAF
     AYNSYLAKHS IIHTGEKPYK CNECGKVFNQ QSTLARHHRL HTAEKPYKCE ECDKVFRCKS
     HLERHRRIHT GEKPYKCKVC DKAFRSDSCL TEHQRVHTGE KPYMCNECGK VFSTKANLAC
     HHKLHTAEKP YKCEECEKVF SRKSHMERHR RIHTGEKPYK CKVCDKAFRR DSHLAQHQRV
     HTGEKPYKCN ECGKTFRQTS SLIIHRRLHT GEKPYKCNEC GKTFSQMSSL VYHHRLHSGE
     KPYKCNECGK VFNQQAHLAQ HQRVHTGEKP YKCNECGKTF SQMSNLVYHH RLHSGEKP
//