ZN383_HUMAN
ID ZN383_HUMAN Reviewed; 475 AA.
AC Q8NA42; Q6X2C7;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger protein 383;
GN Name=ZNF383; ORFNames=HSD17;
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 DEVELOPMENTAL STAGE.
RC TISSUE=Embryonic heart;
RX PubMed=15964543; DOI=10.1016/j.bbrc.2005.05.193;
RA Cao L., Wang Z., Zhu C., Zhao Y., Yuan W., Li J., Wang Y., Ying Z., Li Y.,
RA Yu W., Wu X., Liu M.;
RT "ZNF383, a novel KRAB-containing zinc finger protein, suppresses MAPK
RT signaling pathway.";
RL Biochem. Biophys. Res. Commun. 333:1050-1059(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RA Hu T.H., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
RT "A new spermatogenesis-related gene.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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).
CC -!- FUNCTION: May function as a transcriptional repressor, suppressing
CC transcriptional activities mediated by MAPK signaling pathways.
CC {ECO:0000269|PubMed:15964543}.
CC -!- INTERACTION:
CC Q8NA42; O94818-2: NOL4; NbExp=3; IntAct=EBI-20110775, EBI-10190763;
CC Q8NA42; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-20110775, EBI-1504830;
CC Q8NA42; Q08117-2: TLE5; NbExp=3; IntAct=EBI-20110775, EBI-11741437;
CC Q8NA42; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-20110775, EBI-11962760;
CC Q8NA42; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-20110775, EBI-10172590;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15964543}. Cytoplasm
CC {ECO:0000269|PubMed:15964543}. Note=Shuttling between the nucleus and
CC cytoplasm may occur under different stimulation and growth conditions.
CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, liver, pancreas and
CC with a higher level in skeletal muscle. {ECO:0000269|PubMed:15964543}.
CC -!- DEVELOPMENTAL STAGE: In tissues from a six months embryo, highly
CC expressed in heart, testis and skeletal muscle, lower expression levels
CC in kidney, intestines and prostate. {ECO:0000269|PubMed:15964543}.
CC -!- DOMAIN: The KRAB domain is responsible for the transcriptional
CC repressor activity.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY438646; AAR14184.1; -; mRNA.
DR EMBL; AY260141; AAP20067.1; -; mRNA.
DR EMBL; AK093182; BAC04086.1; -; mRNA.
DR CCDS; CCDS12501.1; -.
DR RefSeq; NP_001332876.1; NM_001345947.1.
DR RefSeq; NP_001332877.1; NM_001345948.1.
DR RefSeq; NP_001332878.1; NM_001345949.1.
DR RefSeq; NP_689817.1; NM_152604.2.
DR RefSeq; XP_005258642.1; XM_005258585.2.
DR RefSeq; XP_011524888.1; XM_011526586.2.
DR RefSeq; XP_011524889.1; XM_011526587.2.
DR RefSeq; XP_011524890.1; XM_011526588.2.
DR RefSeq; XP_011524891.1; XM_011526589.2.
DR RefSeq; XP_011524892.1; XM_011526590.2.
DR RefSeq; XP_016881911.1; XM_017026422.1.
DR RefSeq; XP_016881912.1; XM_017026423.1.
DR RefSeq; XP_016881913.1; XM_017026424.1.
DR AlphaFoldDB; Q8NA42; -.
DR SMR; Q8NA42; -.
DR BioGRID; 127849; 20.
DR IntAct; Q8NA42; 6.
DR STRING; 9606.ENSP00000340132; -.
DR iPTMnet; Q8NA42; -.
DR PhosphoSitePlus; Q8NA42; -.
DR BioMuta; ZNF383; -.
DR DMDM; 74760056; -.
DR jPOST; Q8NA42; -.
DR MassIVE; Q8NA42; -.
DR MaxQB; Q8NA42; -.
DR PaxDb; Q8NA42; -.
DR PeptideAtlas; Q8NA42; -.
DR PRIDE; Q8NA42; -.
DR Antibodypedia; 29883; 64 antibodies from 13 providers.
DR DNASU; 163087; -.
DR Ensembl; ENST00000352998.7; ENSP00000340132.2; ENSG00000188283.12.
DR Ensembl; ENST00000589413.5; ENSP00000464871.1; ENSG00000188283.12.
DR Ensembl; ENST00000590503.5; ENSP00000466101.1; ENSG00000188283.12.
DR Ensembl; ENST00000684119.1; ENSP00000507972.1; ENSG00000188283.12.
DR GeneID; 163087; -.
DR KEGG; hsa:163087; -.
DR MANE-Select; ENST00000684119.1; ENSP00000507972.1; NM_001387601.1; NP_001374530.1.
DR UCSC; uc002oft.2; human.
DR CTD; 163087; -.
DR DisGeNET; 163087; -.
DR GeneCards; ZNF383; -.
DR HGNC; HGNC:18609; ZNF383.
DR HPA; ENSG00000188283; Low tissue specificity.
DR MIM; 619499; gene.
DR neXtProt; NX_Q8NA42; -.
DR OpenTargets; ENSG00000188283; -.
DR PharmGKB; PA134903145; -.
DR VEuPathDB; HostDB:ENSG00000188283; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156284; -.
DR HOGENOM; CLU_002678_0_10_1; -.
DR InParanoid; Q8NA42; -.
DR OMA; YIPKPQV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8NA42; -.
DR PathwayCommons; Q8NA42; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q8NA42; -.
DR BioGRID-ORCS; 163087; 18 hits in 1066 CRISPR screens.
DR ChiTaRS; ZNF383; human.
DR GenomeRNAi; 163087; -.
DR Pharos; Q8NA42; Tdark.
DR PRO; PR:Q8NA42; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8NA42; protein.
DR Bgee; ENSG00000188283; Expressed in granulocyte and 121 other tissues.
DR ExpressionAtlas; Q8NA42; baseline and differential.
DR Genevisible; Q8NA42; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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 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; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
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..475
FT /note="Zinc finger protein 383"
FT /id="PRO_0000047550"
FT DOMAIN 6..77
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 170..192
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 198..220
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 226..248
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 254..276
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..304
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..332
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 338..360
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 394..416
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 422..444
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 450..472
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CONFLICT 11
FT /note="V -> A (in Ref. 2; AAP20067)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="Y -> H (in Ref. 2; AAP20067)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="I -> V (in Ref. 2; AAP20067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 54613 MW; 2F47070F5C2E582B CRC64;
MAEGSVMFSD VSIDFSQEEW DCLDPVQRDL YRDVMLENYG NLVSMGLYTP KPQVISLLEQ
GKEPWMVGRE LTRGLCSDLE SMCETKLLSL KKEVYEIELC QREIMGLTKH GLEYSSFGDV
LEYRSHLAKQ LGYPNGHFSQ EIFTPEYMPT FIQQTFLTLH QIINNEDRPY ECKKCGKAFS
QNSQFIQHQR IHIGEKSYEC KECGKFFSCG SHVTRHLKIH TGEKPFECKE CGKAFSCSSY
LSQHQRIHTG KKPYECKECG KAFSYCSNLI DHQRIHTGEK PYECKVCGKA FTKSSQLFQH
ARIHTGEKPY ECKECGKAFT QSSKLVQHQR IHTGEKPYEC KECGKAFSSG SALTNHQRIH
TGEKPYDCKE CGKAFTQSSQ LRQHQRIHAG EKPFECLECG KAFTQNSQLF QHQRIHTDEK
PYECNECGKA FNKCSNLTRH LRIHTGEKPY NCKECGKAFS SGSDLIRHQG IHTNK
