ZN396_HUMAN
ID ZN396_HUMAN Reviewed; 335 AA.
AC Q96N95; A1L3V0; Q8NF98; Q8TD80;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Zinc finger protein 396;
DE AltName: Full=Zinc finger and SCAN domain-containing protein 14;
GN Name=ZNF396; Synonyms=ZSCAN14;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hepatoma;
RX PubMed=12801647; DOI=10.1016/s0378-1119(03)00551-1;
RA Wu Y., Yu L., Bi G., Luo K., Zhou G., Zhao S.;
RT "Identification and characterization of two novel human SCAN domain-
RT containing zinc finger genes ZNF396 and ZNF397.";
RL Gene 310:193-201(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
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].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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: Isoform 1 and isoform 2 act as DNA-dependent transcriptional
CC repressors. {ECO:0000269|PubMed:12801647}.
CC -!- SUBUNIT: Isoforms 1 and 2 can both homo- and hetero-associate.
CC {ECO:0000269|PubMed:12801647}.
CC -!- INTERACTION:
CC Q96N95-3; P55273: CDKN2D; NbExp=3; IntAct=EBI-12328453, EBI-745859;
CC Q96N95-3; Q2NL68: PROSER3; NbExp=5; IntAct=EBI-12328453, EBI-11336487;
CC Q96N95-3; P57086: SCAND1; NbExp=6; IntAct=EBI-12328453, EBI-745846;
CC Q96N95-3; Q6PJ21: SPSB3; NbExp=3; IntAct=EBI-12328453, EBI-3937206;
CC Q96N95-3; P17028: ZNF24; NbExp=5; IntAct=EBI-12328453, EBI-707773;
CC Q96N95-3; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-12328453, EBI-740232;
CC Q96N95-3; Q9Y5A6: ZSCAN21; NbExp=3; IntAct=EBI-12328453, EBI-10281938;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ZNF396-fu;
CC IsoId=Q96N95-1; Sequence=Displayed;
CC Name=2; Synonyms=Truncated, ZNF396-nf;
CC IsoId=Q96N95-2; Sequence=VSP_008768, VSP_006923;
CC Name=3;
CC IsoId=Q96N95-3; Sequence=VSP_020993;
CC -!- TISSUE SPECIFICITY: Expressed strongly in liver, moderately in skeletal
CC muscle and weakly in kidney, pancreas, spleen and prostate.
CC {ECO:0000269|PubMed:12801647}.
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; AF492004; AAM09559.3; -; mRNA.
DR EMBL; AF533251; AAM95992.1; -; mRNA.
DR EMBL; AK055775; BAB71010.1; -; mRNA.
DR EMBL; CH471088; EAX01352.1; -; Genomic_DNA.
DR EMBL; BC130288; AAI30289.1; -; mRNA.
DR EMBL; BC136314; AAI36315.1; -; mRNA.
DR CCDS; CCDS11913.1; -. [Q96N95-3]
DR CCDS; CCDS82246.1; -. [Q96N95-2]
DR CCDS; CCDS82247.1; -. [Q96N95-1]
DR RefSeq; NP_001309215.1; NM_001322286.1. [Q96N95-1]
DR RefSeq; NP_001309219.1; NM_001322290.1. [Q96N95-1]
DR RefSeq; NP_001309220.1; NM_001322291.1. [Q96N95-2]
DR RefSeq; NP_665699.1; NM_145756.2. [Q96N95-3]
DR RefSeq; XP_006722495.1; XM_006722432.3. [Q96N95-1]
DR RefSeq; XP_016881176.1; XM_017025687.1. [Q96N95-1]
DR RefSeq; XP_016881177.1; XM_017025688.1. [Q96N95-1]
DR AlphaFoldDB; Q96N95; -.
DR SMR; Q96N95; -.
DR BioGRID; 128934; 20.
DR IntAct; Q96N95; 18.
DR STRING; 9606.ENSP00000302310; -.
DR iPTMnet; Q96N95; -.
DR PhosphoSitePlus; Q96N95; -.
DR BioMuta; ZNF396; -.
DR DMDM; 38258950; -.
DR jPOST; Q96N95; -.
DR MassIVE; Q96N95; -.
DR MaxQB; Q96N95; -.
DR PaxDb; Q96N95; -.
DR PeptideAtlas; Q96N95; -.
DR PRIDE; Q96N95; -.
DR ProteomicsDB; 77486; -. [Q96N95-1]
DR TopDownProteomics; Q96N95-3; -. [Q96N95-3]
DR Antibodypedia; 1833; 121 antibodies from 22 providers.
DR DNASU; 252884; -.
DR Ensembl; ENST00000306346.5; ENSP00000302310.1; ENSG00000186496.12. [Q96N95-3]
DR Ensembl; ENST00000586687.5; ENSP00000467275.1; ENSG00000186496.12. [Q96N95-2]
DR Ensembl; ENST00000589332.7; ENSP00000466500.1; ENSG00000186496.12. [Q96N95-1]
DR GeneID; 252884; -.
DR KEGG; hsa:252884; -.
DR MANE-Select; ENST00000589332.7; ENSP00000466500.1; NM_001322286.2; NP_001309215.1.
DR UCSC; uc010xcf.1; human. [Q96N95-1]
DR CTD; 252884; -.
DR DisGeNET; 252884; -.
DR GeneCards; ZNF396; -.
DR HGNC; HGNC:18824; ZNF396.
DR HPA; ENSG00000186496; Low tissue specificity.
DR MIM; 609600; gene.
DR neXtProt; NX_Q96N95; -.
DR OpenTargets; ENSG00000186496; -.
DR PharmGKB; PA38697; -.
DR VEuPathDB; HostDB:ENSG00000186496; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163395; -.
DR HOGENOM; CLU_002678_49_3_1; -.
DR InParanoid; Q96N95; -.
DR OMA; GIELHYD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96N95; -.
DR TreeFam; TF338304; -.
DR PathwayCommons; Q96N95; -.
DR SignaLink; Q96N95; -.
DR BioGRID-ORCS; 252884; 21 hits in 1094 CRISPR screens.
DR ChiTaRS; ZNF396; human.
DR GenomeRNAi; 252884; -.
DR Pharos; Q96N95; Tbio.
DR PRO; PR:Q96N95; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q96N95; protein.
DR Bgee; ENSG00000186496; Expressed in buccal mucosa cell and 126 other tissues.
DR ExpressionAtlas; Q96N95; baseline and differential.
DR Genevisible; Q96N95; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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 GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
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: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; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..335
FT /note="Zinc finger protein 396"
FT /id="PRO_0000047563"
FT DOMAIN 52..134
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 251..273
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..301
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 307..329
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 188..210
FT /note="DEDIKTTNVKSASRQKTSLGIEL -> GEGAGFSSCWKVWGPSAHHTHLS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12801647"
FT /id="VSP_008768"
FT VAR_SEQ 211..335
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12801647"
FT /id="VSP_006923"
FT VAR_SEQ 303..335
FT /note="GEKPYKCHDCGKAFSQSSNLFRHRKRHIRKKVP -> DSKYEHAIAEAQKNM
FT YFKTRLKCPRSLSGGR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020993"
FT VARIANT 211
FT /note="H -> L (in dbSNP:rs9963473)"
FT /id="VAR_057418"
FT CONFLICT 125
FT /note="T -> A (in Ref. 1; AAM09559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38612 MW; 2EC72390016E3E4F CRC64;
MSAKLGKSSS LLTQTSEECN GILTEKMEEE EQTCDPDSSL HWSSSYSPET FRQQFRQFGY
QDSPGPHEAL SRLWELCHLW LRPEVHTKEQ ILELLVLEQF LAILPKELQA WVQKHHPENG
EETVTMLEDV ERELDGPKQI FFGRRKDMIA EKLAPSEITE ELPSSQLMPV KKQLQGASWE
LQSLRPHDED IKTTNVKSAS RQKTSLGIEL HCNVSNILHM NGSQSSTYRG TYEQDGRFEK
RQGNPSWKKQ QKCDECGKIF SQSSALILHQ RIHSGKKPYA CDECAKAFSR SAILIQHRRT
HTGEKPYKCH DCGKAFSQSS NLFRHRKRHI RKKVP