ID ZN445_HUMAN Reviewed; 1031 AA. AC P59923; Q3MJD1; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2003, sequence version 1. DT 23-FEB-2022, entry version 154. DE RecName: Full=Zinc finger protein 445 {ECO:0000305}; DE Short=ZFP445 {ECO:0000303|PubMed:30602440}; DE AltName: Full=Zinc finger protein 168; DE AltName: Full=Zinc finger protein with KRAB and SCAN domains 15; GN Name=ZNF445 {ECO:0000312|HGNC:HGNC:21018}; GN Synonyms=ZFP445 {ECO:0000303|PubMed:30602440}, ZKSCAN15, ZNF168; 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]. RA Shan Y.X., Luo K.T., Guo Z.K., Tang W.W., Ye G.M., Yu L., Huang C.Q.; RT "Cloning and characterization of a novel zinc finger protein."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-938, 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 [4] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-28, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [5] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-938, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [6] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-317; LYS-374; LYS-375; LYS-399; RP LYS-567; LYS-654; LYS-736; LYS-758; LYS-938; LYS-956 AND LYS-975, 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). RN [7] RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. RX PubMed=30602440; DOI=10.1101/gad.320069.118; RA Takahashi N., Coluccio A., Thorball C.W., Planet E., Shi H., Offner S., RA Turelli P., Imbeault M., Ferguson-Smith A.C., Trono D.; RT "ZNF445 is a primary regulator of genomic imprinting."; RL Genes Dev. 33:49-54(2019). CC -!- FUNCTION: Transcription regulator required to maintain maternal and CC paternal gene imprinting, a process by which gene expression is CC restricted in a parent of origin-specific manner by epigenetic CC modification of genomic DNA and chromatin, including DNA methylation. CC Acts by controlling DNA methylation during the earliest multicellular CC stages of development at multiple imprinting control regions (ICRs) CC (PubMed:30602440). Acts together with ZFP57, but seems to be the major CC factor in human early embryonic imprinting maintenance. In contrast, in CC mice, ZFP57 plays the predominant role in imprinting maintenance CC (PubMed:30602440). {ECO:0000269|PubMed:30602440}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30602440}. Note=Binds CC various differentially methylated regions (DMR). CC {ECO:0000269|PubMed:30602440}. CC -!- DEVELOPMENTAL STAGE: Expressed in the oocyte, expression is maintained CC at least until blastocyst stage. {ECO:0000269|PubMed:30602440}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY262260; AAP36990.1; -; mRNA. DR EMBL; AY295873; AAP50258.1; -; mRNA. DR EMBL; BC101486; AAI01487.1; -; mRNA. DR CCDS; CCDS2713.1; -. DR RefSeq; NP_852466.1; NM_181489.5. DR RefSeq; XP_005265159.1; XM_005265102.2. DR RefSeq; XP_011531976.1; XM_011533674.2. DR SMR; P59923; -. DR BioGRID; 131672; 56. DR IntAct; P59923; 21. DR MINT; P59923; -. DR STRING; 9606.ENSP00000413073; -. DR iPTMnet; P59923; -. DR PhosphoSitePlus; P59923; -. DR BioMuta; ZNF445; -. DR DMDM; 45593854; -. DR EPD; P59923; -. DR jPOST; P59923; -. DR MassIVE; P59923; -. DR MaxQB; P59923; -. DR PaxDb; P59923; -. DR PeptideAtlas; P59923; -. DR PRIDE; P59923; -. DR ProteomicsDB; 57172; -. DR Antibodypedia; 29430; 48 antibodies from 13 providers. DR DNASU; 353274; -. DR Ensembl; ENST00000396077; ENSP00000379387; ENSG00000185219. DR Ensembl; ENST00000425708; ENSP00000413073; ENSG00000185219. DR Ensembl; ENST00000634579; ENSP00000489139; ENSG00000283034. DR Ensembl; ENST00000635479; ENSP00000489368; ENSG00000283034. DR GeneID; 353274; -. DR KEGG; hsa:353274; -. DR MANE-Select; ENST00000396077.8; ENSP00000379387.2; NM_181489.6; NP_852466.1. DR UCSC; uc003cnf.3; human. DR CTD; 353274; -. DR GeneCards; ZNF445; -. DR HGNC; HGNC:21018; ZNF445. DR HPA; ENSG00000185219; Low tissue specificity. DR MIM; 619508; gene. DR neXtProt; NX_P59923; -. DR OpenTargets; ENSG00000185219; -. DR PharmGKB; PA134904986; -. DR VEuPathDB; HostDB:ENSG00000185219; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00900000141186; -. DR HOGENOM; CLU_002678_23_0_1; -. DR InParanoid; P59923; -. DR OMA; LHQETHT; -. DR OrthoDB; 1318335at2759; -. DR PhylomeDB; P59923; -. DR TreeFam; TF350827; -. DR PathwayCommons; P59923; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; P59923; -. DR BioGRID-ORCS; 353274; 18 hits in 1078 CRISPR screens. DR ChiTaRS; ZNF445; human. DR GenomeRNAi; 353274; -. DR Pharos; P59923; Tdark. DR PRO; PR:P59923; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P59923; protein. DR Bgee; ENSG00000185219; Expressed in amniotic fluid and 225 other tissues. DR ExpressionAtlas; P59923; baseline and differential. DR Genevisible; P59923; HS. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:UniProtKB. 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:0010216; P:maintenance of DNA methylation; IMP:UniProtKB. DR GO; GO:2000653; P:regulation of genetic imprinting; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR CDD; cd07936; SCAN; 1. DR Gene3D; 1.10.4020.10; -; 1. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR003309; SCAN_dom. DR InterPro; IPR038269; SCAN_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF02023; SCAN; 1. DR Pfam; PF00096; zf-C2H2; 11. DR SMART; SM00349; KRAB; 1. DR SMART; SM00431; SCAN; 1. DR SMART; SM00355; ZnF_C2H2; 14. DR SUPFAM; SSF109640; SSF109640; 1. DR SUPFAM; SSF57667; SSF57667; 9. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS50804; SCAN_BOX; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14. 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..1031 FT /note="Zinc finger protein 445" FT /id="PRO_0000047594" FT DOMAIN 55..137 FT /note="SCAN box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187" FT DOMAIN 234..304 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 485..507 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 513..535 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 541..563 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 597..619 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 625..647 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 681..703 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 709..731 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 762..784 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 790..812 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 840..862 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 868..890 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 896..918 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 978..1000 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1006..1028 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 911..939 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..36 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CROSSLNK 28 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 317 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 374 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 375 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 399 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 567 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 654 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 736 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 758 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 938 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 956 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 975 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 428 FT /note="Y -> C (in dbSNP:rs11710965)" FT /id="VAR_052832" SQ SEQUENCE 1031 AA; 118963 MW; 39C288802894006E CRC64; MPPGRWHAAY PAQAQSSRER GRLQTVKKEE EDESYTPVQA ARPQTLNRPG QELFRQLFRQ LRYHESSGPL ETLSRLRELC RWWLRPDVLS KAQILELLVL EQFLSILPGE LRVWVQLHNP ESGEEAVALL EELQRDLDGT SWRDPGPAQS PDVHWMGTGA LRSAQIWSLA SPLRSSSALG DHLEPPYEIE ARDFLAGQSD TPAAQMPALF PREGCPGDQV TPTRSLTAQL QETMTFKDVE VTFSQDEWGW LDSAQRNLYR DVMLENYRNM ASLVGPFTKP ALISWLEARE PWGLNMQAAQ PKGNPVAAPT GDDLQSKTNK FILNQEPLEE AETLAVSSGC PATSVSEGIG LRESFQQKSR QKDQCENPIQ VRVKKEETNF SHRTGKDSEV SGSNSLDLKH VTYLRVSGRK ESLKHGCGKH FRMSSHHYDY KKYGKGLRHM IGGFSLHQRI HSGLKGNKKD VCGKDFSLSS HHQRGQSLHT VGVSFKCSDC GRTFSHSSHL AYHQRLHTQE KAFKCRVCGK AFRWSSNCAR HEKIHTGVKP YKCDLCEKAF RRLSAYRLHR ETHAKKKFLE LNQYRAALTY SSGFDHHLGD QSGEKLFDCS QCRKSFHCKS YVLEHQRIHT QEKPYKCTKC RKTFRWRSNF TRHMRLHEEE KFYKQDECRE GFRQSPDCSQ PQGAPAVEKT FLCQQCGKTF TRKKTLVDHQ RIHTGEKPYQ CSDCGKDFAY RSAFIVHKKK HAMKRKPEGG PSFSQDTVFQ VPQSSHSKEE PYKCSQCGKA FRNHSFLLIH QRVHTGEKPY KCRECGKAFR WSSNLYRHQR IHSLQKQYDC HESEKTPNVE PKILTGEKRF WCQECGKTFT RKRTLLDHKG IHSGEKRYKC NLCGKSYDRN YRLVNHQRIH STERPFKCQW CGKEFIGRHT LSSHQRKHTR AAQAERSPPA RSSSQDTKLR LQKLKPSEEM PLEDCKEACS QSSRLTGLQD ISIGKKCHKC SICGKTFNKS SQLISHKRFH TRERPFKCSK CGKTFRWSSN LARHMKNHIR D //