ZN283_HUMAN
ID ZN283_HUMAN Reviewed; 679 AA.
AC Q8N7M2; B4DGZ5; B7WP04; Q6RFR9; Q86WM6;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Zinc finger protein 283;
DE AltName: Full=Zinc finger protein HZF19;
GN Name=ZNF283;
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], AND VARIANT ILE-314.
RC TISSUE=Brain, and Trachea;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-242, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12743021; DOI=10.1101/gr.963903;
RA Shannon M., Hamilton A.T., Gordon L., Branscomb E., Stubbs L.;
RT "Differential expansion of zinc-finger transcription factor loci in
RT homologous human and mouse gene clusters.";
RL Genome Res. 13:1097-1110(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 172-679, AND VARIANT ILE-314.
RX PubMed=7865130; DOI=10.1089/dna.1995.14.125;
RA Abrink M., Aveskogh M., Hellman L.;
RT "Isolation of cDNA clones for 42 different Kruppel-related zinc finger
RT proteins expressed in the human monoblast cell line U-937.";
RL DNA Cell Biol. 14:125-136(1995).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-280; LYS-476 AND LYS-588, 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 -!- TISSUE SPECIFICITY: Detected in prostate, testis, and pancreas.
CC {ECO:0000269|PubMed:12743021}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05251.1; Type=Miscellaneous discrepancy; Note=Compared to the genome, the sequence lacks 6 bp for unexplained reasons.; Evidence={ECO:0000305};
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DR EMBL; AK098175; BAC05251.1; ALT_SEQ; mRNA.
DR EMBL; AK294852; BAG57956.1; -; mRNA.
DR EMBL; AC011508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY166784; AAO45833.1; -; mRNA.
DR EMBL; AY500359; AAS55109.1; -; mRNA.
DR CCDS; CCDS46097.1; -.
DR RefSeq; NP_001284681.1; NM_001297752.1.
DR RefSeq; NP_862828.1; NM_181845.1.
DR RefSeq; XP_016882117.1; XM_017026628.1.
DR RefSeq; XP_016882118.1; XM_017026629.1.
DR RefSeq; XP_016882119.1; XM_017026630.1.
DR RefSeq; XP_016882120.1; XM_017026631.1.
DR AlphaFoldDB; Q8N7M2; -.
DR SMR; Q8N7M2; -.
DR BioGRID; 129837; 1.
DR IntAct; Q8N7M2; 1.
DR STRING; 9606.ENSP00000484852; -.
DR iPTMnet; Q8N7M2; -.
DR PhosphoSitePlus; Q8N7M2; -.
DR BioMuta; ZNF283; -.
DR DMDM; 269849746; -.
DR jPOST; Q8N7M2; -.
DR MassIVE; Q8N7M2; -.
DR PaxDb; Q8N7M2; -.
DR PeptideAtlas; Q8N7M2; -.
DR PRIDE; Q8N7M2; -.
DR ProteomicsDB; 72307; -.
DR Antibodypedia; 29840; 7 antibodies from 6 providers.
DR DNASU; 284349; -.
DR Ensembl; ENST00000324461.9; ENSP00000327314.7; ENSG00000167637.18.
DR Ensembl; ENST00000618787.5; ENSP00000484852.1; ENSG00000167637.18.
DR GeneID; 284349; -.
DR KEGG; hsa:284349; -.
DR MANE-Select; ENST00000618787.5; ENSP00000484852.1; NM_181845.2; NP_862828.1.
DR UCSC; uc002oxr.5; human.
DR CTD; 284349; -.
DR GeneCards; ZNF283; -.
DR HGNC; HGNC:13077; ZNF283.
DR HPA; ENSG00000167637; Low tissue specificity.
DR neXtProt; NX_Q8N7M2; -.
DR OpenTargets; ENSG00000167637; -.
DR PharmGKB; PA37653; -.
DR VEuPathDB; HostDB:ENSG00000167637; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161267; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; Q8N7M2; -.
DR OMA; FKNNWKC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8N7M2; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; Q8N7M2; -.
DR SignaLink; Q8N7M2; -.
DR BioGRID-ORCS; 284349; 25 hits in 1106 CRISPR screens.
DR ChiTaRS; ZNF283; human.
DR GenomeRNAi; 284349; -.
DR Pharos; Q8N7M2; Tdark.
DR PRO; PR:Q8N7M2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N7M2; protein.
DR Bgee; ENSG00000167637; Expressed in adrenal tissue and 113 other tissues.
DR ExpressionAtlas; Q8N7M2; baseline and differential.
DR Genevisible; Q8N7M2; 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; 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; 9.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..679
FT /note="Zinc finger protein 283"
FT /id="PRO_0000047507"
FT DOMAIN 73..152
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 205..227
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 233..255
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 261..283
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..451
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 457..479
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 485..507
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..535
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 541..563
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 569..591
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 597..619
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 588
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 314
FT /note="T -> I (in dbSNP:rs2195980)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7865130"
FT /id="VAR_060605"
FT VARIANT 629
FT /note="R -> H (in dbSNP:rs1061768)"
FT /id="VAR_057416"
FT VARIANT 638
FT /note="C -> R (in dbSNP:rs2356437)"
FT /id="VAR_060606"
FT VARIANT 638
FT /note="C -> Y (in dbSNP:rs1061769)"
FT /id="VAR_060607"
FT VARIANT 646
FT /note="R -> I (in dbSNP:rs10417624)"
FT /id="VAR_057417"
FT CONFLICT 139..140
FT /note="Missing (in Ref. 1; BAG57956)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="E -> R (in Ref. 4; AAS55109)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="E -> K (in Ref. 4; AAS55109)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="C -> H (in Ref. 1; BAC05251/BAG57956 and 4;
FT AAS55109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 679 AA; 77942 MW; ADB64BFD18D49020 CRC64;
MESRSVAQAG VQWCDLGSLQ APPPGFTLFS CLSLLSSWDY SSGFSGFCAS PIEESHGALI
SSCNSRTMTD GLVTFRDVAI DFSQEEWECL DPAQRDLYVD VMLENYSNLV SLDLESKTYE
TKKIFSENDI FEINFSQWEM KDKSKTLGLE ASIFRNNWKC KSIFEGLKGH QEGYFSQMII
SYEKIPSYRK SKSLTPHQRI HNTEKSYVCK ECGKACSHGS KLVQHERTHT AEKHFECKEC
GKNYLSAYQL NVHQRFHTGE KPYECKECGK TFSWGSSLVK HERIHTGEKP YECKECGKAF
SRGYHLTQHQ KIHTGVKSYK CKECGKAFFW GSSLAKHEII HTGEKPYKCK ECGKAFSRGY
QLTQHQKIHT GKKPYECKIC GKAFCWGYQL TRHQIFHTGE KPYECKECGK AFNCGSSLIQ
HERIHTGEKP YECKECGKAF SRGYHLSQHQ KIHTGEKPFE CKECGKAFSW GSSLVKHERV
HTGEKSHECK ECGKTFCSGY QLTRHQVFHT GEKPYECKEC GKAFNCGSSL VQHERIHTGE
KPYECKECGK AFSRGYHLTQ HQKIHTGEKP FKCKECGKAF SWGSSLVKHE RVHTNEKSYE
CKDCGKAFGS GYQLSVHQRF HTGEKLYQRK EFGKTFTCGS KLVHERTHSN DKPYKYNECG
EAFLWTTYSN EKIDTDETL
