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   13-FEB-2019, entry version 136.
DE   RecName: Full=Zinc finger protein 445;
DE   AltName: Full=Zinc finger protein 168;
DE   AltName: Full=Zinc finger protein with KRAB and SCAN domains 15;
GN   Name=ZNF445; Synonyms=ZKSCAN15, ZNF168;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   project: 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
RP   MASS 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
RP   MASS 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
RP   MASS 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
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and 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;
RP   LYS-399; LYS-567; LYS-654; LYS-736; LYS-758; LYS-938; LYS-956 AND
RP   LYS-975, 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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00187}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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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   UniGene; Hs.250481; -.
DR   ProteinModelPortal; P59923; -.
DR   BioGrid; 131672; 25.
DR   IntAct; P59923; 3.
DR   STRING; 9606.ENSP00000379387; -.
DR   iPTMnet; P59923; -.
DR   PhosphoSitePlus; P59923; -.
DR   BioMuta; ZNF445; -.
DR   DMDM; 45593854; -.
DR   EPD; P59923; -.
DR   jPOST; P59923; -.
DR   MaxQB; P59923; -.
DR   PaxDb; P59923; -.
DR   PeptideAtlas; P59923; -.
DR   PRIDE; P59923; -.
DR   ProteomicsDB; 57172; -.
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   UCSC; uc003cnf.3; human.
DR   CTD; 353274; -.
DR   DisGeNET; 353274; -.
DR   EuPathDB; HostDB:ENSG00000185219.16; -.
DR   GeneCards; ZNF445; -.
DR   HGNC; HGNC:21018; ZNF445.
DR   HPA; HPA006678; -.
DR   neXtProt; NX_P59923; -.
DR   OpenTargets; ENSG00000185219; -.
DR   PharmGKB; PA134904986; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00900000141186; -.
DR   HOGENOM; HOG000234619; -.
DR   HOVERGEN; HBG106583; -.
DR   InParanoid; P59923; -.
DR   KO; K09229; -.
DR   OMA; RHMKNHI; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P59923; -.
DR   TreeFam; TF350827; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   ChiTaRS; ZNF445; human.
DR   GenomeRNAi; 353274; -.
DR   PRO; PR:P59923; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000185219; Expressed in 210 organ(s), highest expression level in amniotic fluid.
DR   ExpressionAtlas; P59923; baseline and differential.
DR   Genevisible; P59923; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Polymorphism; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1031       Zinc finger protein 445.
FT                                /FTId=PRO_0000047594.
FT   DOMAIN       55    137       SCAN box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00187}.
FT   DOMAIN      234    304       KRAB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00119}.
FT   ZN_FING     485    507       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     513    535       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     541    563       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     597    619       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     625    647       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     681    703       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     709    731       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     762    784       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     790    812       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     840    862       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     868    890       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     896    918       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     978   1000       C2H2-type 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1006   1028       C2H2-type 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   CROSSLNK     28     28       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1).
FT                                {ECO:0000244|PubMed:25114211}.
FT   CROSSLNK    317    317       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    374    374       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    375    375       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    399    399       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    567    567       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    654    654       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    736    736       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    758    758       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    938    938       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    956    956       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    975    975       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VARIANT     428    428       Y -> C (in dbSNP:rs11710965).
FT                                /FTId=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
//