ZN454_HUMAN
ID ZN454_HUMAN Reviewed; 522 AA.
AC Q8N9F8; Q2M1P2; Q2M323;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger protein 454;
GN Name=ZNF454;
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 VARIANTS TYR-152 AND ALA-166.
RC TISSUE=Brain, and Testis;
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-166.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-152 AND ALA-166.
RC TISSUE=Cerebellum;
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: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK094763; BAC04418.1; -; mRNA.
DR EMBL; AK292317; BAF85006.1; -; mRNA.
DR EMBL; AC104117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471165; EAW53822.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53823.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53824.1; -; Genomic_DNA.
DR EMBL; BC105061; AAI05062.1; -; mRNA.
DR EMBL; BC112276; AAI12277.1; -; mRNA.
DR CCDS; CCDS4441.1; -.
DR RefSeq; NP_001171560.1; NM_001178089.2.
DR RefSeq; NP_001171561.1; NM_001178090.2.
DR RefSeq; NP_001310235.1; NM_001323306.1.
DR RefSeq; NP_872400.2; NM_182594.3.
DR AlphaFoldDB; Q8N9F8; -.
DR SMR; Q8N9F8; -.
DR BioGRID; 130176; 5.
DR STRING; 9606.ENSP00000326249; -.
DR iPTMnet; Q8N9F8; -.
DR PhosphoSitePlus; Q8N9F8; -.
DR BioMuta; ZNF454; -.
DR DMDM; 269849529; -.
DR EPD; Q8N9F8; -.
DR jPOST; Q8N9F8; -.
DR MassIVE; Q8N9F8; -.
DR PaxDb; Q8N9F8; -.
DR PeptideAtlas; Q8N9F8; -.
DR PRIDE; Q8N9F8; -.
DR ProteomicsDB; 72529; -.
DR Antibodypedia; 17628; 129 antibodies from 16 providers.
DR DNASU; 285676; -.
DR Ensembl; ENST00000320129.7; ENSP00000326249.3; ENSG00000178187.8.
DR Ensembl; ENST00000519564.2; ENSP00000430354.1; ENSG00000178187.8.
DR GeneID; 285676; -.
DR KEGG; hsa:285676; -.
DR MANE-Select; ENST00000519564.2; ENSP00000430354.1; NM_001178089.3; NP_001171560.1.
DR UCSC; uc003mjo.3; human.
DR CTD; 285676; -.
DR GeneCards; ZNF454; -.
DR HGNC; HGNC:21200; ZNF454.
DR HPA; ENSG00000178187; Low tissue specificity.
DR neXtProt; NX_Q8N9F8; -.
DR OpenTargets; ENSG00000178187; -.
DR PharmGKB; PA134974337; -.
DR VEuPathDB; HostDB:ENSG00000178187; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162181; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; Q8N9F8; -.
DR OMA; CDESGKH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8N9F8; -.
DR TreeFam; TF336820; -.
DR PathwayCommons; Q8N9F8; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 285676; 6 hits in 1091 CRISPR screens.
DR GenomeRNAi; 285676; -.
DR Pharos; Q8N9F8; Tdark.
DR PRO; PR:Q8N9F8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8N9F8; protein.
DR Bgee; ENSG00000178187; Expressed in cortical plate and 108 other tissues.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
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; 11.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..522
FT /note="Zinc finger protein 454"
FT /id="PRO_0000047600"
FT DOMAIN 14..84
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 178..200
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 216..238
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..266
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..490
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 147..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 152
FT /note="C -> Y (in dbSNP:rs6867221)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_059919"
FT VARIANT 166
FT /note="D -> A (in dbSNP:rs12719860)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_033568"
SQ SEQUENCE 522 AA; 60008 MW; 77713F1487E01B4F CRC64;
MAVSHLPTMV QESVTFKDVA ILFTQEEWGQ LSPAQRALYR DVMLENYSNL VSLGLLGPKP
DTFSQLEKRE VWMPEDTPGG FCLDWMTMPA SKKSTVKAEI PEEELDQWTI KERFSSSSHW
KCASLLEWQC GGQEISLQRV VLTHPNTPSQ ECDESGSTMS SSLHSDQSQG FQPSKNAFEC
SECGKVFSKS STLNKHQKIH NEKNANQKIH IKEKRYECRE CGKAFHQSTH LIHHQRIHTG
EKPYECKECG KAFSVSSSLT YHQKIHTGEK PFECNLCGKA FIRNIHLAHH HRIHTGEKPF
KCNICEKAFV CRAHLTKHQN IHSGEKPYKC NECGKAFNQS TSFLQHQRIH TGEKPFECNE
CGKAFRVNSS LTEHQRIHTG EKPYKCNECG KAFRDNSSFA RHRKIHTGEK PYRCGLCEKA
FRDQSALAQH QRIHTGEKPY TCNICEKAFS DHSALTQHKR IHTREKPYKC KICEKAFIRS
THLTQHQRIH TGEKPYKCNK CGKAFNQTAN LIQHQRHHIG EK
