ID   ZN418_HUMAN             Reviewed;         676 AA.
AC   Q8TF45; Q2M1S2; Q670L5; Q96N18;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Zinc finger protein 418 {ECO:0000305};
GN   Name=ZNF418; Synonyms=KIAA1956;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DOMAIN.
RX   PubMed=18084723; DOI=10.1007/s11010-007-9674-4;
RA   Li Y., Yang D., Bai Y., Mo X., Huang W., Yuan W., Yin Z., Deng Y.,
RA   Murashko O., Wang Y., Fan X., Zhu C., Ocorr K., Bodmer R., Wu X.;
RT   "ZNF418, a novel human KRAB/C2H2 zinc finger protein, suppresses MAPK
RT   signaling pathway.";
RL   Mol. Cell. Biochem. 310:141-151(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA   Nagase T., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XXII. The
RT   complete sequences of 50 new cDNA clones which code for large proteins.";
RL   DNA Res. 8:319-327(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
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   [5]
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).
CC   -!- FUNCTION: Transcriptional repressor (PubMed:18084723). May play a role
CC       as regulator of the ubiquitin-proteasome system and autophagy-lysosomal
CC       pathway (By similarity). {ECO:0000250|UniProtKB:Q8BFS8,
CC       ECO:0000269|PubMed:18084723}.
CC   -!- INTERACTION:
CC       Q8TF45; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-3446851, EBI-12012928;
CC       Q8TF45; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-3446851, EBI-10172290;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18084723}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart.
CC       {ECO:0000269|PubMed:18084723}.
CC   -!- DOMAIN: The KRAB domain mediates the transcription repressor activity.
CC       {ECO:0000269|PubMed:18084723}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB85542.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY695825; AAU05132.1; -; mRNA.
DR   EMBL; AB075836; BAB85542.1; ALT_INIT; mRNA.
DR   EMBL; AK056113; BAB71096.1; -; mRNA.
DR   EMBL; AC010326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC112244; AAI12245.1; -; mRNA.
DR   EMBL; BC113707; AAI13708.1; -; mRNA.
DR   CCDS; CCDS42642.1; -.
DR   RefSeq; NP_001303956.1; NM_001317027.1.
DR   RefSeq; NP_001303957.1; NM_001317028.1.
DR   RefSeq; NP_001303958.1; NM_001317029.1.
DR   RefSeq; NP_001303959.1; NM_001317030.1.
DR   RefSeq; NP_597717.1; NM_133460.2.
DR   RefSeq; XP_016881801.1; XM_017026312.1.
DR   RefSeq; XP_016881802.1; XM_017026313.1.
DR   AlphaFoldDB; Q8TF45; -.
DR   SMR; Q8TF45; -.
DR   BioGRID; 127074; 22.
DR   IntAct; Q8TF45; 3.
DR   STRING; 9606.ENSP00000407039; -.
DR   iPTMnet; Q8TF45; -.
DR   PhosphoSitePlus; Q8TF45; -.
DR   BioMuta; ZNF418; -.
DR   DMDM; 23396985; -.
DR   MassIVE; Q8TF45; -.
DR   PaxDb; 9606-ENSP00000379451; -.
DR   PeptideAtlas; Q8TF45; -.
DR   ProteomicsDB; 74554; -.
DR   Pumba; Q8TF45; -.
DR   Antibodypedia; 33292; 57 antibodies from 16 providers.
DR   DNASU; 147686; -.
DR   Ensembl; ENST00000396147.6; ENSP00000379451.1; ENSG00000196724.13.
DR   Ensembl; ENST00000595830.5; ENSP00000471652.1; ENSG00000196724.13.
DR   Ensembl; ENST00000616958.1; ENSP00000483763.1; ENSG00000196724.13.
DR   GeneID; 147686; -.
DR   KEGG; hsa:147686; -.
DR   MANE-Select; ENST00000396147.6; ENSP00000379451.1; NM_133460.3; NP_597717.1.
DR   UCSC; uc002qqs.1; human.
DR   AGR; HGNC:20647; -.
DR   CTD; 147686; -.
DR   DisGeNET; 147686; -.
DR   GeneCards; ZNF418; -.
DR   HGNC; HGNC:20647; ZNF418.
DR   HPA; ENSG00000196724; Low tissue specificity.
DR   MIM; 619509; gene.
DR   neXtProt; NX_Q8TF45; -.
DR   OpenTargets; ENSG00000196724; -.
DR   PharmGKB; PA134912102; -.
DR   VEuPathDB; HostDB:ENSG00000196724; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000164269; -.
DR   HOGENOM; CLU_002678_55_2_1; -.
DR   InParanoid; Q8TF45; -.
DR   OMA; LHRCEDW; -.
DR   OrthoDB; 5343198at2759; -.
DR   PhylomeDB; Q8TF45; -.
DR   TreeFam; TF339848; -.
DR   PathwayCommons; Q8TF45; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q8TF45; -.
DR   BioGRID-ORCS; 147686; 8 hits in 1169 CRISPR screens.
DR   ChiTaRS; ZNF418; human.
DR   GenomeRNAi; 147686; -.
DR   Pharos; Q8TF45; Tbio.
DR   PRO; PR:Q8TF45; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8TF45; Protein.
DR   Bgee; ENSG00000196724; Expressed in primordial germ cell in gonad and 113 other cell types or tissues.
DR   ExpressionAtlas; Q8TF45; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001217; F:DNA-binding transcription repressor activity; 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:0016237; P:microautophagy; ISS:UniProtKB.
DR   GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 16.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23226:SF394; FI01424P-RELATED; 1.
DR   PANTHER; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 15.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 17.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
DR   Genevisible; Q8TF45; HS.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..676
FT                   /note="Zinc finger protein 418"
FT                   /id="PRO_0000047573"
FT   DOMAIN          5..91
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         82..105
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         230..252
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         258..280
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         286..308
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         314..336
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         342..364
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         370..392
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         398..420
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         426..448
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         454..476
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         482..504
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         510..532
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         538..560
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         591..613
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         619..641
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         647..669
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CONFLICT        290
FT                   /note="E -> G (in Ref. 3; BAB71096)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   676 AA;  77858 MW;  1BB0F0064B8F3BD3 CRC64;
     MQGTVAFEDV AVNFSQEEWS LLSEVQRCLY HDVMLENWVL ISSLGCWCGS EDEEAPSKKS
     ISIQRVSQVS TPGAGVSPKK AHSCEMCGAI LGDILHLADH QGTHHKQKLH RCEAWGNKLY
     DSSNRPHQNQ YLGEKPYRSS VEEALFVKRC KFHVSEESSI FIQSGKDFLP SSGLLLQEAT
     HTGEKSNSKP ECESPFQWGD THYSCGECMK HSSTKHVFVQ QQRLPSREEC YCWECGKSFS
     KYDSVSNHQR VHTGKRPYEC GECGKSFSHK GSLVQHQRVH TGKRPYECGE CGKSFSHKGS
     LVQHQRVHTG ERPYECGECG KSFSQNGTLI KHQRVHTGER PYECEECGKC FTQKGNLIQH
     QRGHTSERPY ECEECGKCFS QKGTLTEHHR VHTRERPYEC GECGKSFSRK GHLRNHQRGH
     TGERPYECGE CGKSFSRKGN LIQHQRSHTG ERPYECRECR KLFRGKSHLI EHQRVHTGER
     PYECNECGKS FQDSSGFRVH QRVHTGEKPF ECSECGKSFP QSCSLLRHRR VHTGERPYEC
     GECGKSFHQS SSLLRHQKTH TAERPYECRE CGKFFSSLLE HRRVHTGERP YECRECGKTF
     TRRSAHFKHQ RLHTRGKPYE CSECGKSFAE TFSLTEHRRV HTGERPYECS ECGKSFHRSS
     SLLRHQRVHT ERSPYK
//