ZN410_HUMAN
ID ZN410_HUMAN Reviewed; 478 AA.
AC Q86VK4; B4DDV5; B4DR78; O00153; Q9BQ19;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Zinc finger protein 410 {ECO:0000305};
DE AltName: Full=Another partner for ARF 1 {ECO:0000303|PubMed:12370286};
GN Name=ZNF410 {ECO:0000303|PubMed:33301730, ECO:0000312|HGNC:HGNC:20144};
GN Synonyms=APA1 {ECO:0000303|PubMed:12370286};
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Lung;
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).
RN [3]
RP FUNCTION, SUMOYLATION, INDUCTION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP CDKN2A.
RX PubMed=12370286; DOI=10.1128/mcb.22.21.7385-7397.2002;
RA Benanti J.A., Williams D.K., Robinson K.L., Ozer H.L., Galloway D.A.;
RT "Induction of extracellular matrix-remodeling genes by the senescence-
RT associated protein APA-1.";
RL Mol. Cell. Biol. 22:7385-7397(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=30078215; DOI=10.1002/jcp.26803;
RA Chen Y., Liu R., Chu Z., Le B., Zeng H., Zhang X., Wu Q., Zhu G., Chen Y.,
RA Liu Y., Sun F., Lu Z., Qiao Y., Wang J.;
RT "High glucose stimulates proliferative capacity of liver cancer cells
RT possibly via O-GlcNAcylation-dependent transcriptional regulation of
RT GJC1.";
RL J. Cell. Physiol. 234:606-618(2018).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=33859416; DOI=10.1038/s41588-021-00843-w;
RA Vinjamur D.S., Yao Q., Cole M.A., McGuckin C., Ren C., Zeng J., Hossain M.,
RA Luk K., Wolfe S.A., Pinello L., Bauer D.E.;
RT "ZNF410 represses fetal globin by singular control of CHD4.";
RL Nat. Genet. 53:719-728(2021).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 217-362 IN COMPLEX WITH DNA AND
RP ZINC, FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=33301730; DOI=10.1016/j.molcel.2020.11.006;
RA Lan X., Ren R., Feng R., Ly L.C., Lan Y., Zhang Z., Aboreden N., Qin K.,
RA Horton J.R., Grevet J.D., Mayuranathan T., Abdulmalik O., Keller C.A.,
RA Giardine B., Hardison R.C., Crossley M., Weiss M.J., Cheng X., Shi J.,
RA Blobel G.A.;
RT "ZNF410 uniquely activates the NuRD component CHD4 to silence fetal
RT hemoglobin expression.";
RL Mol. Cell 81:239-254(2021).
CC -!- FUNCTION: Transcription factor that binds to the sequence motif 5'-
CC CATCCCATAATA-3', and is specifically required to silence expression of
CC fetal hemoglobin in adult erythroid cells (PubMed:33859416,
CC PubMed:33301730). Prevents expression of fetal hemoglobin genes HBG1
CC and HBG2 through CHD4: acts as a direct transcriptional activator of
CC CHD4, a central component of the NuRD complex that represses
CC transcription of fetal hemoglobin genes HBG1 and HBG2 in erythroid
CC cells (PubMed:33859416, PubMed:33301730). May also activate
CC transcription of matrix-remodeling genes such as MMP1 during fibroblast
CC senescence (PubMed:12370286). May activate transcription of the gap
CC junction gene GJC1, perhaps in response to increasing glucose
CC (PubMed:30078215). However, recent studies suggest that ZNF410 is
CC dedicated to regulate expression of a single gene: CHD4
CC (PubMed:33859416, PubMed:33301730). {ECO:0000269|PubMed:12370286,
CC ECO:0000269|PubMed:30078215, ECO:0000269|PubMed:33301730,
CC ECO:0000269|PubMed:33859416}.
CC -!- SUBUNIT: Interacts with CDKN2A/p14ARF. {ECO:0000269|PubMed:12370286}.
CC -!- INTERACTION:
CC Q86VK4; Q9H2G9: BLZF1; NbExp=4; IntAct=EBI-720304, EBI-2548012;
CC Q86VK4; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-720304, EBI-739624;
CC Q86VK4; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-720304, EBI-10175124;
CC Q86VK4; A1L4K1: FSD2; NbExp=3; IntAct=EBI-720304, EBI-5661036;
CC Q86VK4; Q08379: GOLGA2; NbExp=3; IntAct=EBI-720304, EBI-618309;
CC Q86VK4; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-720304, EBI-742948;
CC Q86VK4; Q96QF0: RAB3IP; NbExp=3; IntAct=EBI-720304, EBI-747844;
CC Q86VK4; Q53GC0: SERTAD1; NbExp=3; IntAct=EBI-720304, EBI-2826300;
CC Q86VK4; Q12933: TRAF2; NbExp=3; IntAct=EBI-720304, EBI-355744;
CC Q86VK4; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-720304, EBI-744794;
CC Q86VK4; Q8NF99: ZNF397; NbExp=3; IntAct=EBI-720304, EBI-10213894;
CC Q86VK4-3; Q96I13: ABHD8; NbExp=3; IntAct=EBI-11741890, EBI-17180442;
CC Q86VK4-3; O95994: AGR2; NbExp=3; IntAct=EBI-11741890, EBI-712648;
CC Q86VK4-3; O43307: ARHGEF9; NbExp=3; IntAct=EBI-11741890, EBI-3447299;
CC Q86VK4-3; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-11741890, EBI-11524452;
CC Q86VK4-3; Q9H2G9: BLZF1; NbExp=7; IntAct=EBI-11741890, EBI-2548012;
CC Q86VK4-3; P20807-4: CAPN3; NbExp=3; IntAct=EBI-11741890, EBI-11532021;
CC Q86VK4-3; Q03692: COL10A1; NbExp=3; IntAct=EBI-11741890, EBI-2528309;
CC Q86VK4-3; P67870: CSNK2B; NbExp=3; IntAct=EBI-11741890, EBI-348169;
CC Q86VK4-3; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-11741890, EBI-742054;
CC Q86VK4-3; A0A0U1RQF7: DPEP2NB; NbExp=3; IntAct=EBI-11741890, EBI-18398199;
CC Q86VK4-3; Q14192: FHL2; NbExp=3; IntAct=EBI-11741890, EBI-701903;
CC Q86VK4-3; A1L4K1: FSD2; NbExp=3; IntAct=EBI-11741890, EBI-5661036;
CC Q86VK4-3; P14136: GFAP; NbExp=3; IntAct=EBI-11741890, EBI-744302;
CC Q86VK4-3; O76003: GLRX3; NbExp=3; IntAct=EBI-11741890, EBI-374781;
CC Q86VK4-3; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-11741890, EBI-5916454;
CC Q86VK4-3; P14652: HOXB2; NbExp=3; IntAct=EBI-11741890, EBI-5329558;
CC Q86VK4-3; Q8NA54: IQUB; NbExp=3; IntAct=EBI-11741890, EBI-10220600;
CC Q86VK4-3; Q5VVH5: IRAK1BP1; NbExp=3; IntAct=EBI-11741890, EBI-9658404;
CC Q86VK4-3; Q6A162: KRT40; NbExp=3; IntAct=EBI-11741890, EBI-10171697;
CC Q86VK4-3; P48059-3: LIMS1; NbExp=3; IntAct=EBI-11741890, EBI-12864460;
CC Q86VK4-3; P25791-3: LMO2; NbExp=5; IntAct=EBI-11741890, EBI-11959475;
CC Q86VK4-3; P61968: LMO4; NbExp=3; IntAct=EBI-11741890, EBI-2798728;
CC Q86VK4-3; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-11741890, EBI-473196;
CC Q86VK4-3; P50221: MEOX1; NbExp=3; IntAct=EBI-11741890, EBI-2864512;
CC Q86VK4-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11741890, EBI-16439278;
CC Q86VK4-3; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-11741890, EBI-10172526;
CC Q86VK4-3; O14561: NDUFAB1; NbExp=3; IntAct=EBI-11741890, EBI-1246261;
CC Q86VK4-3; P19404: NDUFV2; NbExp=3; IntAct=EBI-11741890, EBI-713665;
CC Q86VK4-3; Q9Y314: NOSIP; NbExp=3; IntAct=EBI-11741890, EBI-1051889;
CC Q86VK4-3; P26367: PAX6; NbExp=3; IntAct=EBI-11741890, EBI-747278;
CC Q86VK4-3; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-11741890, EBI-9640281;
CC Q86VK4-3; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-11741890, EBI-79165;
CC Q86VK4-3; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-11741890, EBI-1389308;
CC Q86VK4-3; P62487: POLR2G; NbExp=3; IntAct=EBI-11741890, EBI-347928;
CC Q86VK4-3; P78424: POU6F2; NbExp=3; IntAct=EBI-11741890, EBI-12029004;
CC Q86VK4-3; Q8N3J5: PPM1K; NbExp=3; IntAct=EBI-11741890, EBI-3923368;
CC Q86VK4-3; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-11741890, EBI-10293968;
CC Q86VK4-3; P31321: PRKAR1B; NbExp=3; IntAct=EBI-11741890, EBI-2805516;
CC Q86VK4-3; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-11741890, EBI-11984839;
CC Q86VK4-3; Q86WH2: RASSF3; NbExp=3; IntAct=EBI-11741890, EBI-2845202;
CC Q86VK4-3; Q15293: RCN1; NbExp=3; IntAct=EBI-11741890, EBI-948278;
CC Q86VK4-3; Q96P16-3: RPRD1A; NbExp=3; IntAct=EBI-11741890, EBI-12840198;
CC Q86VK4-3; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-11741890, EBI-748601;
CC Q86VK4-3; P51692: STAT5B; NbExp=3; IntAct=EBI-11741890, EBI-1186119;
CC Q86VK4-3; Q12933: TRAF2; NbExp=3; IntAct=EBI-11741890, EBI-355744;
CC Q86VK4-3; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-11741890, EBI-17716262;
CC Q86VK4-3; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-11741890, EBI-744794;
CC Q86VK4-3; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-11741890, EBI-9090990;
CC Q86VK4-3; Q96PU4-2: UHRF2; NbExp=3; IntAct=EBI-11741890, EBI-12878912;
CC Q86VK4-3; P61758: VBP1; NbExp=3; IntAct=EBI-11741890, EBI-357430;
CC Q86VK4-3; P17028: ZNF24; NbExp=3; IntAct=EBI-11741890, EBI-707773;
CC Q86VK4-3; Q8N5D4; NbExp=3; IntAct=EBI-11741890, EBI-10266435;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:33301730,
CC ECO:0000305|PubMed:33859416}. Chromosome {ECO:0000269|PubMed:33301730,
CC ECO:0000269|PubMed:33859416}. Note=Directly binds to the sequence motif
CC 5'-CATCCCATAATA-3'. {ECO:0000269|PubMed:33301730,
CC ECO:0000269|PubMed:33859416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q86VK4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VK4-2; Sequence=VSP_008485, VSP_008486;
CC Name=3;
CC IsoId=Q86VK4-3; Sequence=VSP_008487;
CC Name=4;
CC IsoId=Q86VK4-4; Sequence=VSP_042424;
CC Name=5;
CC IsoId=Q86VK4-5; Sequence=VSP_043417, VSP_043418;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12370286}.
CC -!- INDUCTION: During fibroblast senescence. {ECO:0000269|PubMed:12370286}.
CC -!- DOMAIN: The five zinc finger domains are necessary and sufficient to
CC bind to DNA. {ECO:0000269|PubMed:33301730}.
CC -!- PTM: Sumoylated (PubMed:12370286). Sumoylation increases its half-life,
CC possibly by blocking ubiquitin-mediated degradation (PubMed:12370286).
CC {ECO:0000269|PubMed:12370286}.
CC -!- PTM: O-glycosylated (PubMed:30078215). O-GlcNAcylation may occur in
CC response to increasing glucose levels and affect transcription factor
CC activity (PubMed:30078215). {ECO:0000269|PubMed:30078215}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; U90919; AAB51059.1; -; mRNA.
DR EMBL; AK293350; BAG56866.1; -; mRNA.
DR EMBL; AK299138; BAG61190.1; -; mRNA.
DR EMBL; AC005480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000330; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC004357; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC050683; AAH50683.1; -; mRNA.
DR CCDS; CCDS55929.1; -. [Q86VK4-5]
DR CCDS; CCDS55930.1; -. [Q86VK4-3]
DR CCDS; CCDS55931.1; -. [Q86VK4-4]
DR CCDS; CCDS9821.1; -. [Q86VK4-1]
DR RefSeq; NP_001229853.1; NM_001242924.1. [Q86VK4-5]
DR RefSeq; NP_001229855.1; NM_001242926.1. [Q86VK4-3]
DR RefSeq; NP_001229856.1; NM_001242927.1. [Q86VK4-4]
DR RefSeq; NP_067011.1; NM_021188.2. [Q86VK4-1]
DR PDB; 6WMI; X-ray; 2.75 A; A/D=217-366.
DR PDBsum; 6WMI; -.
DR AlphaFoldDB; Q86VK4; -.
DR SMR; Q86VK4; -.
DR BioGRID; 121792; 54.
DR IntAct; Q86VK4; 66.
DR MINT; Q86VK4; -.
DR STRING; 9606.ENSP00000407130; -.
DR GlyGen; Q86VK4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86VK4; -.
DR PhosphoSitePlus; Q86VK4; -.
DR BioMuta; ZNF410; -.
DR DMDM; 37538029; -.
DR EPD; Q86VK4; -.
DR MassIVE; Q86VK4; -.
DR MaxQB; Q86VK4; -.
DR PaxDb; Q86VK4; -.
DR PeptideAtlas; Q86VK4; -.
DR PRIDE; Q86VK4; -.
DR ProteomicsDB; 70028; -. [Q86VK4-1]
DR ProteomicsDB; 70029; -. [Q86VK4-2]
DR ProteomicsDB; 70030; -. [Q86VK4-3]
DR ProteomicsDB; 70031; -. [Q86VK4-4]
DR ProteomicsDB; 70032; -. [Q86VK4-5]
DR Antibodypedia; 126; 191 antibodies from 22 providers.
DR DNASU; 57862; -.
DR Ensembl; ENST00000324593.10; ENSP00000323293.6; ENSG00000119725.21. [Q86VK4-3]
DR Ensembl; ENST00000398139.7; ENSP00000381208.3; ENSG00000119725.21. [Q86VK4-2]
DR Ensembl; ENST00000442160.7; ENSP00000407130.3; ENSG00000119725.21. [Q86VK4-5]
DR Ensembl; ENST00000540593.5; ENSP00000442228.1; ENSG00000119725.21. [Q86VK4-4]
DR Ensembl; ENST00000555044.6; ENSP00000451763.2; ENSG00000119725.21. [Q86VK4-1]
DR Ensembl; ENST00000615736.4; ENSP00000483073.1; ENSG00000119725.21. [Q86VK4-5]
DR GeneID; 57862; -.
DR KEGG; hsa:57862; -.
DR MANE-Select; ENST00000555044.6; ENSP00000451763.2; NM_021188.3; NP_067011.1.
DR UCSC; uc001xoz.3; human. [Q86VK4-1]
DR CTD; 57862; -.
DR DisGeNET; 57862; -.
DR GeneCards; ZNF410; -.
DR HGNC; HGNC:20144; ZNF410.
DR HPA; ENSG00000119725; Low tissue specificity.
DR MIM; 619427; gene.
DR neXtProt; NX_Q86VK4; -.
DR PharmGKB; PA134958929; -.
DR VEuPathDB; HostDB:ENSG00000119725; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158098; -.
DR HOGENOM; CLU_043629_1_0_1; -.
DR InParanoid; Q86VK4; -.
DR OMA; XNDRSFI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q86VK4; -.
DR TreeFam; TF333498; -.
DR PathwayCommons; Q86VK4; -.
DR SignaLink; Q86VK4; -.
DR BioGRID-ORCS; 57862; 22 hits in 1111 CRISPR screens.
DR ChiTaRS; ZNF410; human.
DR GenomeRNAi; 57862; -.
DR Pharos; Q86VK4; Tbio.
DR PRO; PR:Q86VK4; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q86VK4; protein.
DR Bgee; ENSG00000119725; Expressed in islet of Langerhans and 97 other tissues.
DR ExpressionAtlas; Q86VK4; baseline and differential.
DR Genevisible; Q86VK4; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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; IMP:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromosome; DNA-binding;
KW Glycoprotein; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..478
FT /note="Zinc finger protein 410"
FT /id="PRO_0000047571"
FT ZN_FING 219..243
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 249..273
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..303
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..333
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 339..362
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 187..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:33301730,
FT ECO:0007744|PDB:6WMI"
FT VAR_SEQ 57..129
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042424"
FT VAR_SEQ 57
FT /note="D -> EPVPWREEDGKSGCSDLN (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043417"
FT VAR_SEQ 245..272
FT /note="NDRSFICPAEGCGKSFYVLQRLKVHMRT -> RLWEKLLCAAEAEGAHEDPQ
FT WREALYVP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008485"
FT VAR_SEQ 273..478
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008486"
FT VAR_SEQ 377..423
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008487"
FT VAR_SEQ 467..478
FT /note="LLNQGDLTERRT -> SLAPLPRLECSGAFSAHCNLCLPGSSDSPASAS
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043418"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:6WMI"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:6WMI"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:6WMI"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:6WMI"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:6WMI"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6WMI"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:6WMI"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:6WMI"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6WMI"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6WMI"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6WMI"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:6WMI"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:6WMI"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:6WMI"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:6WMI"
SQ SEQUENCE 478 AA; 52113 MW; 1D7F7E139618F863 CRC64;
MLSDELESKP ELLVQFVQNT SIPLGQGLVE SEAKDITCLS LLPVTEASEC SRLMLPDDTT
NHSNSSKEVP SSAVLRSLRV NVGPDGEETR AQTVQKSPEF LSTSESSSLL QDLQPSDSTS
FILLNLTRAG LGSSAEHLVF VQDEAEDSGN DFLSSESTDS SIPWFLRVQE LAHDSLIAAT
RAQLAKNAKT SSNGENVHLG SGDGQSKDSG PLPQVEKKLK CTVEGCDRTF VWPAHFKYHL
KTHRNDRSFI CPAEGCGKSF YVLQRLKVHM RTHNGEKPFM CHESGCGKQF TTAGNLKNHR
RIHTGEKPFL CEAQGCGRSF AEYSSLRKHL VVHSGEKPHQ CQVCGKTFSQ SGSRNVHMRK
HHLQLGAAGS QEQEQTAEPL MGSSLLEEAS VPSKNLVSMN SQPSLGGESL NLPNTNSILG
VDDEVLAEGS PRSLSSVPDV THHLVTMQSG RQSYEVSVLT AVNPQELLNQ GDLTERRT
