ZN567_HUMAN
ID ZN567_HUMAN Reviewed; 647 AA.
AC Q8N184; B3KX49; Q6N044;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger protein 567;
GN Name=ZNF567;
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] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 2).
RC TISSUE=Prostate;
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 MRNA] (ISOFORM 1).
RC TISSUE=Liver;
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 [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-173, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-173; LYS-202; LYS-217; LYS-233
RP AND LYS-447, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 -!- INTERACTION:
CC Q8N184; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-749400, EBI-10175124;
CC Q8N184; Q9NYL2: MAP3K20; NbExp=3; IntAct=EBI-749400, EBI-602273;
CC Q8N184; Q9NYL2-2: MAP3K20; NbExp=7; IntAct=EBI-749400, EBI-10255081;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q8N184-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8N184-1; Sequence=VSP_016383;
CC Name=2;
CC IsoId=Q8N184-2; Sequence=VSP_016384;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK126691; BAG54361.1; -; mRNA.
DR EMBL; BX640706; CAE45826.1; -; mRNA.
DR EMBL; BC033849; AAH33849.2; -; mRNA.
DR CCDS; CCDS12495.1; -. [Q8N184-1]
DR CCDS; CCDS74349.1; -. [Q8N184-3]
DR RefSeq; NP_001287908.1; NM_001300979.1. [Q8N184-3]
DR RefSeq; NP_001309840.1; NM_001322911.1. [Q8N184-1]
DR RefSeq; NP_001309841.1; NM_001322912.1. [Q8N184-1]
DR RefSeq; NP_001309842.1; NM_001322913.1. [Q8N184-3]
DR RefSeq; NP_001309843.1; NM_001322914.1. [Q8N184-3]
DR RefSeq; NP_001309844.1; NM_001322915.1. [Q8N184-3]
DR RefSeq; NP_001309845.1; NM_001322916.1. [Q8N184-3]
DR RefSeq; NP_001309846.1; NM_001322917.1. [Q8N184-3]
DR RefSeq; NP_001309847.1; NM_001322918.1. [Q8N184-3]
DR RefSeq; NP_001309848.1; NM_001322919.1. [Q8N184-3]
DR RefSeq; NP_001309849.1; NM_001322920.1. [Q8N184-3]
DR RefSeq; NP_689816.2; NM_152603.4. [Q8N184-1]
DR RefSeq; XP_011524886.1; XM_011526584.2. [Q8N184-1]
DR RefSeq; XP_016881906.1; XM_017026417.1. [Q8N184-3]
DR RefSeq; XP_016881907.1; XM_017026418.1. [Q8N184-3]
DR RefSeq; XP_016881909.1; XM_017026420.1. [Q8N184-1]
DR RefSeq; XP_016881910.1; XM_017026421.1. [Q8N184-1]
DR AlphaFoldDB; Q8N184; -.
DR SMR; Q8N184; -.
DR BioGRID; 127848; 7.
DR IntAct; Q8N184; 5.
DR MINT; Q8N184; -.
DR STRING; 9606.ENSP00000441838; -.
DR iPTMnet; Q8N184; -.
DR PhosphoSitePlus; Q8N184; -.
DR BioMuta; ZNF567; -.
DR DMDM; 150387826; -.
DR jPOST; Q8N184; -.
DR MassIVE; Q8N184; -.
DR MaxQB; Q8N184; -.
DR PaxDb; Q8N184; -.
DR PeptideAtlas; Q8N184; -.
DR PRIDE; Q8N184; -.
DR ProteomicsDB; 71570; -. [Q8N184-3]
DR ProteomicsDB; 71571; -. [Q8N184-1]
DR ProteomicsDB; 71572; -. [Q8N184-2]
DR Antibodypedia; 16328; 50 antibodies from 13 providers.
DR DNASU; 163081; -.
DR Ensembl; ENST00000360729.8; ENSP00000353957.3; ENSG00000189042.14. [Q8N184-1]
DR Ensembl; ENST00000536254.6; ENSP00000441838.1; ENSG00000189042.14. [Q8N184-3]
DR Ensembl; ENST00000585696.5; ENSP00000467379.1; ENSG00000189042.14. [Q8N184-1]
DR Ensembl; ENST00000682579.1; ENSP00000507048.1; ENSG00000189042.14. [Q8N184-3]
DR GeneID; 163081; -.
DR KEGG; hsa:163081; -.
DR MANE-Select; ENST00000682579.1; ENSP00000507048.1; NM_001322917.1; NP_001309846.1.
DR UCSC; uc002oep.5; human. [Q8N184-3]
DR CTD; 163081; -.
DR GeneCards; ZNF567; -.
DR HGNC; HGNC:28696; ZNF567.
DR HPA; ENSG00000189042; Low tissue specificity.
DR neXtProt; NX_Q8N184; -.
DR OpenTargets; ENSG00000189042; -.
DR PharmGKB; PA134986394; -.
DR VEuPathDB; HostDB:ENSG00000189042; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162697; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; Q8N184; -.
DR OMA; THKGENM; -.
DR PhylomeDB; Q8N184; -.
DR TreeFam; TF337898; -.
DR PathwayCommons; Q8N184; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q8N184; -.
DR BioGRID-ORCS; 163081; 12 hits in 1101 CRISPR screens.
DR ChiTaRS; ZNF567; human.
DR GenomeRNAi; 163081; -.
DR Pharos; Q8N184; Tdark.
DR PRO; PR:Q8N184; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N184; protein.
DR Bgee; ENSG00000189042; Expressed in endothelial cell and 168 other tissues.
DR ExpressionAtlas; Q8N184; baseline and differential.
DR Genevisible; Q8N184; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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; 13.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
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..647
FT /note="Zinc finger protein 567"
FT /id="PRO_0000047658"
FT DOMAIN 6..77
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 210..232
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 253..275
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 281..303
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..331
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..359
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..387
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 393..415
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 421..443
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 449..471
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 477..499
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 505..527
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 533..555
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 561..583
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 589..611
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 617..639
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 447
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016383"
FT VAR_SEQ 579..634
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016384"
FT CONFLICT 59
FT /note="E -> G (in Ref. 2; CAE45826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 75164 MW; 0A384AF156FA2B78 CRC64;
MAQGSVSFND VTVDFTQEEW QHLDHAQKTL YMDVMLENYC HLISVGCHMT KPDVILKLER
GEEPWTSFAG HTCLEENWKA EDFLVKFKEH QEKYSRSVVS INHKKLVKEK SKIYEKTFTL
GKNPVNSKNL PPEYDTHGRI LKNVSELIIS NLNPARKRLS EYNGYGKSLL STKQETTHPE
VKSHNQSARA FSHNEVLMQY QKTETPAQSF GYNDCEKSFL QRGGLITHSR PYKGENPSVY
NKKRRATNIE KKHTCNECGK SFCRKSVLIL HQGIHSEEKP YQCHQCGNAF RRKSYLIDHQ
RTHTGEKPFV CNECGKSFRL KTALTDHQRT HTGEKSYECL QCRNAFRLKS HLIRHQRTHT
GEKPYECNDC GKSFRQKTTL SLHQRIHTGE KPYICKECGK SFHQKANLTV HQRTHTGEKP
YICNECGKSF SQKTTLALHE KTHNEEKPYI CSECGKSFRQ KTTLVAHQRT HTGEKSYECP
HCGKAFRMKS YLIDHHRTHT GEKPYECNEC GKSFSQKTNL NLHQRIHTGE KPYVCNECGK
SFRQKATLTV HQKIHTGQKS YECPQCGKAF SRKSYLIHHQ RTHTGEKPYK CSECGKCFRQ
KTNLIVHQRT HTGEKPYVCN ECGKSFSYKR NLIVHQRTHK GENIEMQ
