ZN425_HUMAN
ID ZN425_HUMAN Reviewed; 752 AA.
AC Q6IV72; B3KPM1; Q08AG3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Zinc finger protein 425;
GN Name=ZNF425;
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, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Heart;
RX PubMed=21266108; DOI=10.5483/bmbrep.2011.44.1.58;
RA Wang Y., Ye X., Zhou J., Wan Y., Xie H., Deng Y., Yan Y., Li Y., Fan X.,
RA Yuan W., Mo X., Wu X.;
RT "A novel human KRAB-related zinc finger gene ZNF425 inhibits mitogen-
RT activated protein kinase signaling pathway.";
RL BMB Rep. 44:58-63(2011).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: Acts as a transcriptional repressor.
CC {ECO:0000269|PubMed:21266108}.
CC -!- INTERACTION:
CC Q6IV72; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10250516, EBI-10172290;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21266108}. Cytoplasm
CC {ECO:0000269|PubMed:21266108}. Note=Predominantly expressed in the
CC nucleus.
CC -!- DEVELOPMENTAL STAGE: Expressed in 30 days old embryos. Almost
CC undetectable in 60 days old embryos and in adults.
CC {ECO:0000269|PubMed:21266108}.
CC -!- DOMAIN: The C2H2 domain is necessary for the transcriptional
CC repression.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY621067; AAT40438.1; -; mRNA.
DR EMBL; AK056498; BAG51733.1; -; mRNA.
DR EMBL; AC073422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125189; AAI25190.1; -; mRNA.
DR CCDS; CCDS34773.1; -.
DR RefSeq; NP_001001661.1; NM_001001661.2.
DR AlphaFoldDB; Q6IV72; -.
DR SMR; Q6IV72; -.
DR BioGRID; 127572; 1.
DR IntAct; Q6IV72; 1.
DR STRING; 9606.ENSP00000367300; -.
DR iPTMnet; Q6IV72; -.
DR PhosphoSitePlus; Q6IV72; -.
DR BioMuta; ZNF425; -.
DR DMDM; 74762333; -.
DR MassIVE; Q6IV72; -.
DR PaxDb; Q6IV72; -.
DR PeptideAtlas; Q6IV72; -.
DR PRIDE; Q6IV72; -.
DR ProteomicsDB; 66500; -.
DR Antibodypedia; 64196; 13 antibodies from 7 providers.
DR DNASU; 155054; -.
DR Ensembl; ENST00000378061.7; ENSP00000367300.2; ENSG00000204947.9.
DR GeneID; 155054; -.
DR KEGG; hsa:155054; -.
DR MANE-Select; ENST00000378061.7; ENSP00000367300.2; NM_001001661.3; NP_001001661.1.
DR UCSC; uc003wfj.4; human.
DR CTD; 155054; -.
DR GeneCards; ZNF425; -.
DR HGNC; HGNC:20690; ZNF425.
DR HPA; ENSG00000204947; Low tissue specificity.
DR MIM; 619507; gene.
DR neXtProt; NX_Q6IV72; -.
DR OpenTargets; ENSG00000204947; -.
DR PharmGKB; PA134984453; -.
DR VEuPathDB; HostDB:ENSG00000204947; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163692; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q6IV72; -.
DR OMA; CLHKGER; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6IV72; -.
DR TreeFam; TF326846; -.
DR PathwayCommons; Q6IV72; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q6IV72; -.
DR BioGRID-ORCS; 155054; 26 hits in 1096 CRISPR screens.
DR ChiTaRS; ZNF425; human.
DR GenomeRNAi; 155054; -.
DR Pharos; Q6IV72; Tdark.
DR PRO; PR:Q6IV72; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q6IV72; protein.
DR Bgee; ENSG00000204947; Expressed in secondary oocyte and 97 other tissues.
DR ExpressionAtlas; Q6IV72; baseline and differential.
DR Genevisible; Q6IV72; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR003655; aKRAB.
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; 14.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 11.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..752
FT /note="Zinc finger protein 425"
FT /id="PRO_0000234577"
FT DOMAIN 9..80
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 190..212
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 246..268
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 274..296
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 302..324
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 330..352
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..380
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..464
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 470..492
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..520
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 526..548
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 554..576
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 582..604
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 610..632
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 638..660
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 666..688
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 694..716
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 722..744
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VARIANT 166
FT /note="D -> V (in dbSNP:rs6965052)"
FT /id="VAR_033565"
FT CONFLICT 289
FT /note="L -> P (in Ref. 4; AAI25190)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="T -> A (in Ref. 2; BAG51733)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="G -> V (in Ref. 2; BAG51733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 87721 MW; EDAADCD608517131 CRC64;
MAEPASVTVT FDDVALYFSE QEWEILEKWQ KQMYKQEMKT NYETLDSLGY AFSKPDLITW
MEQGRMLLIS EQGCLDKTRR TTSPPTDEQL NMKNTGKLLC FDDEGTPRTK EEDCRLNGPQ
KQDLCAALRG KERKILLAQT ATFQSPSLRE TEILNKKVSI TAYDPDKKDL RHKPRETPGR
LEIPTGPRCY SCYVCRKVFQ VRRDLLKHKR SHSKSQLCRY PKYKNSSRGK SELRRTQRLL
CQKKRFQCSE CEKSYFLKGS LVTHQVVHTG QRPYPCPECD KTFRYRANLK KHLCLHRGER
PFCCGECGRA FVQQCELTEH LRLHSGEKPF QCPQCDRCFR LKRGMKVHLT QHSGKRPFHC
PECGRSFSRK AALKTHQRTH SEEKPFSCGE CGRKFIYKIK LDEHIRVHTG EKPFSCPECN
KSFRLKRSLK AHGLQHIGKR PFQCPECSRG FFWRNAMRAH QRLHSEQKPF PCAECGKRFT
RPSKLACHTR VHDRQKEFPC GECKKTFSQQ SRLTQHLKVH TTEKPFSCAE CGRSFRRRAH
LTEHTRLHSG EEPFQCPECD KSFSWKASMK FHQRMHRDEK PFACGECDKT YTHQSQLTEH
LRLHSGEKPY QCPECEKTFR LKGNLKSHLL QHSGQKPFSC VMCGKSFTQQ YRLTEHIRVH
SGEKPFQCPE CDKSYCIRGS LKVHLYKHSG ERPFQCPECG KGFLQKRSLK AHLCLHSGER
PFSCDECGRS FTYVGALKTH IAVHAKEKPS SL
