ZNF28_HUMAN
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 03-AUG-2022, entry version 187.
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 PIR; I37964; I37964.
DR RefSeq; NP_008900.3; NM_006969.3. [P17035-1]
DR RefSeq; XP_011525564.1; XM_011527262.2. [P17035-1]
DR AlphaFoldDB; P17035; -.
DR SMR; P17035; -.
DR BioGRID; 113406; 8.
DR IntAct; P17035; 3.
DR STRING; 9606.ENSP00000397693; -.
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; P17035; -.
DR PeptideAtlas; P17035; -.
DR PRIDE; P17035; -.
DR ProteomicsDB; 53436; -. [P17035-1]
DR ProteomicsDB; 53437; -. [P17035-2]
DR Antibodypedia; 56951; 59 antibodies from 12 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 CTD; 7576; -.
DR DisGeNET; 7576; -.
DR GeneCards; ZNF28; -.
DR HGNC; HGNC:13073; ZNF28.
DR HPA; ENSG00000198538; Low tissue specificity.
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; CDYSAMQ; -.
DR OrthoDB; 1318335at2759; -.
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 1066 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 107 other 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 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; 1.
DR Pfam; PF00096; zf-C2H2; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 18.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
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
