ID   ZN382_HUMAN             Reviewed;         550 AA.
AC   Q96SR6; A3KMP6; A8MT55; C9K0V5; Q53ZY8; Q5JPJ2;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 3.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Zinc finger protein 382;
DE   AltName: Full=KRAB/zinc finger suppressor protein 1;
DE            Short=KS1;
DE   AltName: Full=Multiple zinc finger and krueppel-associated box protein KS1;
GN   Name=ZNF382;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Embryonic heart;
RX   PubMed=12459182; DOI=10.1016/s0006-291x(02)02700-6;
RA   Luo K., Yuan W., Zhu C., Li Y., Wang Y., Zeng W., Jiao W., Liu M., Wu X.;
RT   "Expression of a novel Kruppel-like zinc-finger gene, ZNF382, in human
RT   heart.";
RL   Biochem. Biophys. Res. Commun. 299:606-612(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Urrutia R., Folch-Puy E., Fernandez-Zapico M.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Teratocarcinoma;
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 MRNA] (ISOFORM 3), AND VARIANT GLY-168.
RC   TISSUE=Lymph node;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-168.
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: Functions as a sequence-specific transcriptional repressor.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TRIM28; enhances the transcriptional repressor
CC       activity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q96SR6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96SR6-2; Sequence=VSP_036224;
CC       Name=3;
CC         IsoId=Q96SR6-3; Sequence=VSP_036225;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in heart with a weaker
CC       expression also detected in skeletal muscle.
CC       {ECO:0000269|PubMed:12459182}.
CC   -!- DEVELOPMENTAL STAGE: Primarily detected in 34 day-old embryos. Widely
CC       expressed at different levels during embryonic development where it is
CC       predominantly expressed in cerebellum, kidney, and cerebrum and to a
CC       lesser extent in lung, heart, skeletal muscle, tongue, and adrenal
CC       gland. {ECO:0000269|PubMed:12459182}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF513816; AAM48246.1; -; mRNA.
DR   EMBL; AY227449; AAO72308.1; -; mRNA.
DR   EMBL; AK027592; BAB55217.1; -; mRNA.
DR   EMBL; AL832265; CAI46159.1; -; mRNA.
DR   EMBL; AC074138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC132675; AAI32676.2; -; mRNA.
DR   CCDS; CCDS33004.1; -. [Q96SR6-1]
DR   CCDS; CCDS58659.1; -. [Q96SR6-2]
DR   RefSeq; NP_001243767.1; NM_001256838.1. [Q96SR6-2]
DR   RefSeq; NP_116214.2; NM_032825.4. [Q96SR6-1]
DR   AlphaFoldDB; Q96SR6; -.
DR   SMR; Q96SR6; -.
DR   BioGRID; 124348; 7.
DR   IntAct; Q96SR6; 1.
DR   STRING; 9606.ENSP00000292928; -.
DR   iPTMnet; Q96SR6; -.
DR   PhosphoSitePlus; Q96SR6; -.
DR   BioMuta; ZNF382; -.
DR   DMDM; 313104256; -.
DR   jPOST; Q96SR6; -.
DR   MassIVE; Q96SR6; -.
DR   MaxQB; Q96SR6; -.
DR   PaxDb; 9606-ENSP00000292928; -.
DR   PeptideAtlas; Q96SR6; -.
DR   ProteomicsDB; 78140; -. [Q96SR6-1]
DR   ProteomicsDB; 78141; -. [Q96SR6-2]
DR   ProteomicsDB; 78142; -. [Q96SR6-3]
DR   Antibodypedia; 16319; 32 antibodies from 15 providers.
DR   DNASU; 84911; -.
DR   Ensembl; ENST00000292928.7; ENSP00000292928.2; ENSG00000161298.19. [Q96SR6-1]
DR   Ensembl; ENST00000435416.1; ENSP00000410113.1; ENSG00000161298.19. [Q96SR6-3]
DR   Ensembl; ENST00000439428.5; ENSP00000407593.1; ENSG00000161298.19. [Q96SR6-2]
DR   GeneID; 84911; -.
DR   KEGG; hsa:84911; -.
DR   MANE-Select; ENST00000292928.7; ENSP00000292928.2; NM_032825.5; NP_116214.2.
DR   UCSC; uc002oek.5; human. [Q96SR6-1]
DR   AGR; HGNC:17409; -.
DR   CTD; 84911; -.
DR   DisGeNET; 84911; -.
DR   GeneCards; ZNF382; -.
DR   HGNC; HGNC:17409; ZNF382.
DR   HPA; ENSG00000161298; Tissue enhanced (brain, retina).
DR   MIM; 609516; gene.
DR   neXtProt; NX_Q96SR6; -.
DR   OpenTargets; ENSG00000161298; -.
DR   PharmGKB; PA134869965; -.
DR   VEuPathDB; HostDB:ENSG00000161298; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162338; -.
DR   HOGENOM; CLU_002678_44_5_1; -.
DR   InParanoid; Q96SR6; -.
DR   OMA; HKVETMR; -.
DR   OrthoDB; 5252528at2759; -.
DR   PhylomeDB; Q96SR6; -.
DR   TreeFam; TF337898; -.
DR   PathwayCommons; Q96SR6; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q96SR6; -.
DR   SIGNOR; Q96SR6; -.
DR   BioGRID-ORCS; 84911; 182 hits in 1168 CRISPR screens.
DR   ChiTaRS; ZNF382; human.
DR   GenomeRNAi; 84911; -.
DR   Pharos; Q96SR6; Tbio.
DR   PRO; PR:Q96SR6; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q96SR6; Protein.
DR   Bgee; ENSG00000161298; Expressed in right hemisphere of cerebellum and 114 other cell types or tissues.
DR   ExpressionAtlas; Q96SR6; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; 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: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; 10.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24390:SF197; GH18834P-RELATED; 1.
DR   PANTHER; PTHR24390; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 9.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
DR   Genevisible; Q96SR6; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..550
FT                   /note="Zinc finger protein 382"
FT                   /id="PRO_0000047549"
FT   DOMAIN          7..78
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         212..234
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         296..318
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         324..346
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         352..374
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         380..402
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         408..430
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         436..458
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         464..486
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         492..514
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         520..542
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..105
FT                   /note="Mediates interaction with TRIM28"
FT                   /evidence="ECO:0000250"
FT   REGION          5..46
FT                   /note="Represses transcription"
FT                   /evidence="ECO:0000250"
FT   REGION          70..211
FT                   /note="Represses transcription"
FT                   /evidence="ECO:0000250"
FT   REGION          296..550
FT                   /note="Required for transcriptional repression activity;
FT                   probably mediates sequence-specific DNA-binding"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..3
FT                   /note="MPL -> MS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_036224"
FT   VAR_SEQ         78
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_036225"
FT   VARIANT         168
FT                   /note="E -> G (in dbSNP:rs3108171)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17974005"
FT                   /id="VAR_054226"
FT   CONFLICT        129..130
FT                   /note="Missing (in Ref. 1; AAM48246, 2; AAO72308 and 3;
FT                   BAB55217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        547
FT                   /note="T -> M (in Ref. 6; AAI32676)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   550 AA;  64010 MW;  6D0706EA069DDD0B CRC64;
     MPLQGSVSFK DVTVDFTQEE WQQLDPAQKA LYRDVMLENY CHFVSVGFHM AKPDMIRKLE
     QGEELWTQRI FPSYSYLEED GKTEDVLVKF KEYQDRHSRP LIFINHKKLI KERSNIYGKT
     FTLGKNRISK TILCEYKPDG KVLKNISELV IRNISPIKEK FGDSTGWEKS LLNTKHEKIH
     PAVNLHKQTE RVLSGKQELI QHQKVQAPEQ PFDHNECEKS FLMKGMLFTH TRAHRGERTF
     EYNKDGIAFI EKSSLSVHPS NLMEKKPSAY NKYGKFLCRK PVFIMPQRPQ TEEKPFHCPY
     CGNNFRRKSY LIEHQRIHTG EKPYVCNQCG KAFRQKTALT LHEKTHIEGK PFICIDCGKS
     FRQKATLTRH HKTHTGEKAY ECPQCGSAFR KKSYLIDHQR THTGEKPYQC NECGKAFIQK
     TTLTVHQRTH TGEKPYICNE CGKSFCQKTT LTLHQRIHTG EKPYICNECG KSFRQKAILT
     VHHRIHTGEK SNGCPQCGKA FSRKSNLIRH QKTHTGEKPY ECKQCGKFFS CKSNLIVHQK
     THKVETTGIQ
//