ZGPAT_HUMAN
ID ZGPAT_HUMAN Reviewed; 531 AA.
AC Q8N5A5; E1P5K1; Q4VXN9; Q5JWI9; Q5JWJ0; Q8NC55; Q8WUV4; Q96JI0; Q96JU4;
AC Q9H401;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
DE AltName: Full=G patch domain-containing protein 6;
DE AltName: Full=Zinc finger CCCH domain-containing protein 9;
DE AltName: Full=Zinc finger and G patch domain-containing protein;
GN Name=ZGPAT; Synonyms=GPATC6, GPATCH6, KIAA1847, ZC3H9, ZC3HDC9, ZIP;
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 2), AND VARIANT ARG-61.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-61.
RC TISSUE=Thyroid;
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 GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-61.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ARG-61.
RC TISSUE=Placenta, and Uterus;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, TISSUE SPECIFICITY, AND
RP INTERACTION WITH CHD4.
RX PubMed=19644445; DOI=10.1038/emboj.2009.211;
RA Li R., Zhang H., Yu W., Chen Y., Gui B., Liang J., Wang Y., Sun L.,
RA Yang X., Zhang Y., Shi L., Li Y., Shang Y.;
RT "ZIP: a novel transcription repressor, represses EGFR oncogene and
RT suppresses breast carcinogenesis.";
RL EMBO J. 28:2763-2776(2009).
RN [8]
RP ALTERNATIVE SPLICING (ISOFORM 4), FUNCTION (ISOFORM 4), AND SUBCELLULAR
RP LOCATION (ISOFORM 4).
RX PubMed=20233718; DOI=10.1074/jbc.m110.107508;
RA Yu W., Li R., Gui B., Shang Y.;
RT "sZIP, an alternative splice variant of ZIP, antagonizes transcription
RT repression and growth inhibition by ZIP.";
RL J. Biol. Chem. 285:14301-14307(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP UBIQUITINATION.
RX PubMed=24116224; DOI=10.1371/journal.pone.0077320;
RA Maudet C., Sourisce A., Dragin L., Lahouassa H., Rain J.C., Bouaziz S.,
RA Ramirez B.C., Margottin-Goguet F.;
RT "HIV-1 Vpr Induces the Degradation of ZIP and sZIP, Adaptors of the NuRD
RT Chromatin Remodeling Complex, by Hijacking DCAF1/VprBP.";
RL PLoS ONE 8:E77320-E77320(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 120-268 IN COMPLEX WITH ZINC
RP IONS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the zinc finger of ZGPAT.";
RL Submitted (FEB-2013) to the PDB data bank.
CC -!- FUNCTION: Transcription repressor that specifically binds the 5'-
CC GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by
CC recruiting the chromatin multiprotein complex NuRD to target promoters.
CC Negatively regulates expression of EGFR, a gene involved in cell
CC proliferation, survival and migration. Its ability to repress genes of
CC the EGFR pathway suggest it may act as a tumor suppressor. Able to
CC suppress breast carcinogenesis. {ECO:0000269|PubMed:19644445}.
CC -!- FUNCTION: [Isoform 4]: Antagonizes the transcription repression by
CC isoform 1 by competing for the binding of the NuRD complex. Does not
CC bind DNA. {ECO:0000269|PubMed:19644445}.
CC -!- SUBUNIT: Interacts with CHD4/Mi-2; the interaction is direct.
CC {ECO:0000269|PubMed:19644445, ECO:0000269|Ref.12}.
CC -!- INTERACTION:
CC Q8N5A5; Q13155: AIMP2; NbExp=3; IntAct=EBI-3439227, EBI-745226;
CC Q8N5A5; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-3439227, EBI-10187270;
CC Q8N5A5; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-3439227, EBI-724373;
CC Q8N5A5; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-3439227, EBI-2548012;
CC Q8N5A5; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-3439227, EBI-2808286;
CC Q8N5A5; O95273: CCNDBP1; NbExp=4; IntAct=EBI-3439227, EBI-748961;
CC Q8N5A5; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-3439227, EBI-739624;
CC Q8N5A5; O43143: DHX15; NbExp=6; IntAct=EBI-3439227, EBI-1237044;
CC Q8N5A5; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-3439227, EBI-740680;
CC Q8N5A5; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-3439227, EBI-10175124;
CC Q8N5A5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-3439227, EBI-618309;
CC Q8N5A5; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-3439227, EBI-747204;
CC Q8N5A5; Q9BVG8: KIFC3; NbExp=4; IntAct=EBI-3439227, EBI-2125614;
CC Q8N5A5; P19012: KRT15; NbExp=3; IntAct=EBI-3439227, EBI-739566;
CC Q8N5A5; Q6A162: KRT40; NbExp=3; IntAct=EBI-3439227, EBI-10171697;
CC Q8N5A5; O95751: LDOC1; NbExp=5; IntAct=EBI-3439227, EBI-740738;
CC Q8N5A5; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-3439227, EBI-741037;
CC Q8N5A5; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-3439227, EBI-10172526;
CC Q8N5A5; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-3439227, EBI-2548751;
CC Q8N5A5; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-3439227, EBI-713786;
CC Q8N5A5; Q9Y2D8: SSX2IP; NbExp=4; IntAct=EBI-3439227, EBI-2212028;
CC Q8N5A5; Q96MF2: STAC3; NbExp=3; IntAct=EBI-3439227, EBI-745680;
CC Q8N5A5; Q9UBB9: TFIP11; NbExp=5; IntAct=EBI-3439227, EBI-1105213;
CC Q8N5A5; Q08117: TLE5; NbExp=4; IntAct=EBI-3439227, EBI-717810;
CC Q8N5A5; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-3439227, EBI-10175039;
CC Q8N5A5; P14373: TRIM27; NbExp=4; IntAct=EBI-3439227, EBI-719493;
CC Q8N5A5; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-3439227, EBI-2130429;
CC Q8N5A5; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-3439227, EBI-742740;
CC Q8N5A5-2; Q13155: AIMP2; NbExp=12; IntAct=EBI-10183064, EBI-745226;
CC Q8N5A5-2; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-10183064, EBI-746752;
CC Q8N5A5-2; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-10183064, EBI-10187270;
CC Q8N5A5-2; Q9H2G9: BLZF1; NbExp=6; IntAct=EBI-10183064, EBI-2548012;
CC Q8N5A5-2; Q13901: C1D; NbExp=3; IntAct=EBI-10183064, EBI-3844053;
CC Q8N5A5-2; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-10183064, EBI-11530605;
CC Q8N5A5-2; Q5BKX8: CAVIN4; NbExp=3; IntAct=EBI-10183064, EBI-12836558;
CC Q8N5A5-2; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-10183064, EBI-10961312;
CC Q8N5A5-2; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-10183064, EBI-10181422;
CC Q8N5A5-2; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-10183064, EBI-10961624;
CC Q8N5A5-2; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-10183064, EBI-10175300;
CC Q8N5A5-2; Q96GN5: CDCA7L; NbExp=9; IntAct=EBI-10183064, EBI-5278764;
CC Q8N5A5-2; Q01850: CDR2; NbExp=6; IntAct=EBI-10183064, EBI-1181367;
CC Q8N5A5-2; Q8NHQ1: CEP70; NbExp=9; IntAct=EBI-10183064, EBI-739624;
CC Q8N5A5-2; Q969H4: CNKSR1; NbExp=3; IntAct=EBI-10183064, EBI-741671;
CC Q8N5A5-2; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-10183064, EBI-11962928;
CC Q8N5A5-2; O43143: DHX15; NbExp=12; IntAct=EBI-10183064, EBI-1237044;
CC Q8N5A5-2; A0A0A0MR80: EP400; NbExp=3; IntAct=EBI-10183064, EBI-12089140;
CC Q8N5A5-2; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-10183064, EBI-10175124;
CC Q8N5A5-2; Q8WXI9: GATAD2B; NbExp=3; IntAct=EBI-10183064, EBI-923440;
CC Q8N5A5-2; Q08379: GOLGA2; NbExp=12; IntAct=EBI-10183064, EBI-618309;
CC Q8N5A5-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-10183064, EBI-5916454;
CC Q8N5A5-2; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-10183064, EBI-10961706;
CC Q8N5A5-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-10183064, EBI-7116203;
CC Q8N5A5-2; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-10183064, EBI-747204;
CC Q8N5A5-2; Q86T90: KIAA1328; NbExp=5; IntAct=EBI-10183064, EBI-3437878;
CC Q8N5A5-2; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-10183064, EBI-2125614;
CC Q8N5A5-2; Q9BVG8-5: KIFC3; NbExp=6; IntAct=EBI-10183064, EBI-14069005;
CC Q8N5A5-2; P19012: KRT15; NbExp=3; IntAct=EBI-10183064, EBI-739566;
CC Q8N5A5-2; Q15323: KRT31; NbExp=3; IntAct=EBI-10183064, EBI-948001;
CC Q8N5A5-2; Q6A162: KRT40; NbExp=6; IntAct=EBI-10183064, EBI-10171697;
CC Q8N5A5-2; O95447: LCA5L; NbExp=3; IntAct=EBI-10183064, EBI-8473670;
CC Q8N5A5-2; O95751: LDOC1; NbExp=3; IntAct=EBI-10183064, EBI-740738;
CC Q8N5A5-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10183064, EBI-739832;
CC Q8N5A5-2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-10183064, EBI-1216080;
CC Q8N5A5-2; Q9BRK4: LZTS2; NbExp=9; IntAct=EBI-10183064, EBI-741037;
CC Q8N5A5-2; Q9UJV3-2: MID2; NbExp=9; IntAct=EBI-10183064, EBI-10172526;
CC Q8N5A5-2; Q8TD10: MIPOL1; NbExp=6; IntAct=EBI-10183064, EBI-2548751;
CC Q8N5A5-2; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-10183064, EBI-743811;
CC Q8N5A5-2; O76041: NEBL; NbExp=3; IntAct=EBI-10183064, EBI-2880203;
CC Q8N5A5-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-10183064, EBI-748974;
CC Q8N5A5-2; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-10183064, EBI-713786;
CC Q8N5A5-2; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-10183064, EBI-1105153;
CC Q8N5A5-2; P60903: S100A10; NbExp=3; IntAct=EBI-10183064, EBI-717048;
CC Q8N5A5-2; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-10183064, EBI-748391;
CC Q8N5A5-2; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-10183064, EBI-748621;
CC Q8N5A5-2; P09661: SNRPA1; NbExp=3; IntAct=EBI-10183064, EBI-876439;
CC Q8N5A5-2; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-10183064, EBI-2212028;
CC Q8N5A5-2; Q96MF2: STAC3; NbExp=3; IntAct=EBI-10183064, EBI-745680;
CC Q8N5A5-2; Q86TJ2-3: TADA2B; NbExp=3; IntAct=EBI-10183064, EBI-18173581;
CC Q8N5A5-2; Q9Y242: TCF19; NbExp=3; IntAct=EBI-10183064, EBI-7413767;
CC Q8N5A5-2; Q9UBB9: TFIP11; NbExp=9; IntAct=EBI-10183064, EBI-1105213;
CC Q8N5A5-2; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-10183064, EBI-741515;
CC Q8N5A5-2; Q8TBB0: THAP6; NbExp=3; IntAct=EBI-10183064, EBI-3925505;
CC Q8N5A5-2; Q08117: TLE5; NbExp=3; IntAct=EBI-10183064, EBI-717810;
CC Q8N5A5-2; Q08117-2: TLE5; NbExp=9; IntAct=EBI-10183064, EBI-11741437;
CC Q8N5A5-2; Q05BL1: TP53BP2; NbExp=6; IntAct=EBI-10183064, EBI-11952721;
CC Q8N5A5-2; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-10183064, EBI-10175039;
CC Q8N5A5-2; Q14142: TRIM14; NbExp=3; IntAct=EBI-10183064, EBI-2820256;
CC Q8N5A5-2; P14373: TRIM27; NbExp=9; IntAct=EBI-10183064, EBI-719493;
CC Q8N5A5-2; Q5T124-6: UBXN11; NbExp=3; IntAct=EBI-10183064, EBI-11524408;
CC Q8N5A5-2; Q5TFG8: ZC2HC1B; NbExp=3; IntAct=EBI-10183064, EBI-12275374;
CC Q8N5A5-2; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-10183064, EBI-12272076;
CC Q8N5A5-2; P17028: ZNF24; NbExp=3; IntAct=EBI-10183064, EBI-707773;
CC Q8N5A5-2; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-10183064, EBI-7233259;
CC Q8N5A5-2; P13682: ZNF35; NbExp=3; IntAct=EBI-10183064, EBI-11041653;
CC Q8N5A5-2; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-10183064, EBI-743265;
CC Q8N5A5-2; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-10183064, EBI-6427977;
CC Q8N5A5-2; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-10183064, EBI-4395732;
CC Q8N5A5-2; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-10183064, EBI-7138235;
CC Q8N5A5-2; P10073: ZSCAN22; NbExp=3; IntAct=EBI-10183064, EBI-10178224;
CC Q8N5A5-2; P98169: ZXDB; NbExp=3; IntAct=EBI-10183064, EBI-17493569;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19644445}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus
CC {ECO:0000269|PubMed:20233718}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8N5A5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5A5-2; Sequence=VSP_007754;
CC Name=3;
CC IsoId=Q8N5A5-3; Sequence=VSP_038121;
CC Name=4; Synonyms=sZIP;
CC IsoId=Q8N5A5-4; Sequence=VSP_053599;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19644445}.
CC -!- INDUCTION: Down-regulated in breast carcinomas.
CC -!- PTM: Ubiquitinated in case of infection by HIV-1, leading to its
CC degradation. Ubiquitination is mediated by the CUL4A-RBX1-DDB1-
CC DCAF1/VPRBP complex that is hijacked by HIV-1 via interaction between
CC HIV-1 Vpr and DCAF1/VPRBP. {ECO:0000269|PubMed:24116224}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47476.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11317.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB058750; BAB47476.3; ALT_INIT; mRNA.
DR EMBL; AK027878; BAB55426.1; -; mRNA.
DR EMBL; AK074961; BAC11317.1; ALT_FRAME; mRNA.
DR EMBL; AL121845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75223.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75226.1; -; Genomic_DNA.
DR EMBL; BC019338; AAH19338.1; -; mRNA.
DR EMBL; BC032612; AAH32612.1; -; mRNA.
DR CCDS; CCDS13534.1; -. [Q8N5A5-1]
DR CCDS; CCDS13535.1; -. [Q8N5A5-2]
DR CCDS; CCDS56203.1; -. [Q8N5A5-3]
DR RefSeq; NP_001076582.1; NM_001083113.1. [Q8N5A5-2]
DR RefSeq; NP_001182582.1; NM_001195653.1. [Q8N5A5-2]
DR RefSeq; NP_001182583.1; NM_001195654.1. [Q8N5A5-3]
DR RefSeq; NP_115916.3; NM_032527.4. [Q8N5A5-1]
DR RefSeq; NP_852150.2; NM_181485.2. [Q8N5A5-2]
DR PDB; 4II1; X-ray; 2.65 A; A/B/C/D=120-268.
DR PDBsum; 4II1; -.
DR AlphaFoldDB; Q8N5A5; -.
DR SMR; Q8N5A5; -.
DR BioGRID; 124150; 190.
DR IntAct; Q8N5A5; 113.
DR MINT; Q8N5A5; -.
DR STRING; 9606.ENSP00000332013; -.
DR GlyGen; Q8N5A5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N5A5; -.
DR PhosphoSitePlus; Q8N5A5; -.
DR BioMuta; ZGPAT; -.
DR DMDM; 147744602; -.
DR EPD; Q8N5A5; -.
DR jPOST; Q8N5A5; -.
DR MassIVE; Q8N5A5; -.
DR MaxQB; Q8N5A5; -.
DR PaxDb; Q8N5A5; -.
DR PeptideAtlas; Q8N5A5; -.
DR PRIDE; Q8N5A5; -.
DR ProteomicsDB; 72025; -. [Q8N5A5-1]
DR ProteomicsDB; 72026; -. [Q8N5A5-2]
DR ProteomicsDB; 72027; -. [Q8N5A5-3]
DR ABCD; Q8N5A5; 5 sequenced antibodies.
DR Antibodypedia; 29857; 120 antibodies from 25 providers.
DR DNASU; 84619; -.
DR Ensembl; ENST00000328969.5; ENSP00000332013.5; ENSG00000197114.12. [Q8N5A5-1]
DR Ensembl; ENST00000355969.11; ENSP00000348242.6; ENSG00000197114.12. [Q8N5A5-2]
DR Ensembl; ENST00000357119.8; ENSP00000349634.4; ENSG00000197114.12. [Q8N5A5-3]
DR Ensembl; ENST00000369967.7; ENSP00000358984.3; ENSG00000197114.12. [Q8N5A5-2]
DR Ensembl; ENST00000448100.6; ENSP00000391176.1; ENSG00000197114.12. [Q8N5A5-2]
DR GeneID; 84619; -.
DR KEGG; hsa:84619; -.
DR MANE-Select; ENST00000355969.11; ENSP00000348242.6; NM_181485.3; NP_852150.2. [Q8N5A5-2]
DR UCSC; uc002ygi.3; human. [Q8N5A5-1]
DR CTD; 84619; -.
DR DisGeNET; 84619; -.
DR GeneCards; ZGPAT; -.
DR HGNC; HGNC:15948; ZGPAT.
DR HPA; ENSG00000197114; Tissue enriched (liver).
DR MIM; 619577; gene.
DR neXtProt; NX_Q8N5A5; -.
DR OpenTargets; ENSG00000197114; -.
DR PharmGKB; PA134881248; -.
DR VEuPathDB; HostDB:ENSG00000197114; -.
DR eggNOG; KOG2185; Eukaryota.
DR GeneTree; ENSGT00390000000732; -.
DR HOGENOM; CLU_040504_1_0_1; -.
DR InParanoid; Q8N5A5; -.
DR OMA; SVDACMN; -.
DR OrthoDB; 1238995at2759; -.
DR PhylomeDB; Q8N5A5; -.
DR TreeFam; TF105970; -.
DR PathwayCommons; Q8N5A5; -.
DR SignaLink; Q8N5A5; -.
DR BioGRID-ORCS; 84619; 23 hits in 1087 CRISPR screens.
DR ChiTaRS; ZGPAT; human.
DR GeneWiki; ZGPAT; -.
DR GenomeRNAi; 84619; -.
DR Pharos; Q8N5A5; Tbio.
DR PRO; PR:Q8N5A5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8N5A5; protein.
DR Bgee; ENSG00000197114; Expressed in right lobe of liver and 96 other tissues.
DR ExpressionAtlas; Q8N5A5; baseline and differential.
DR Genevisible; Q8N5A5; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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; cd04508; TUDOR; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR043560; ZGPAT.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR46297; PTHR46297; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..531
FT /note="Zinc finger CCCH-type with G patch domain-containing
FT protein"
FT /id="PRO_0000213894"
FT DOMAIN 333..379
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 175..201
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 91..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM1"
FT VAR_SEQ 1..343
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_053599"
FT VAR_SEQ 282..310
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038121"
FT VAR_SEQ 291..310
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11347906,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007754"
FT VARIANT 61
FT /note="S -> R (in dbSNP:rs1291212)"
FT /evidence="ECO:0000269|PubMed:11347906,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5"
FT /id="VAR_025539"
FT CONFLICT 184
FT /note="L -> Q (in Ref. 3; BAB55426)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="C -> R (in Ref. 3; BAC11317)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="M -> V (in Ref. 3; BAB55426)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="G -> R (in Ref. 6; AAH19338)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="Q -> R (in Ref. 3; BAB55426)"
FT /evidence="ECO:0000305"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:4II1"
FT STRAND 146..157
FT /evidence="ECO:0007829|PDB:4II1"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:4II1"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4II1"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4II1"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:4II1"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4II1"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4II1"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4II1"
FT STRAND 233..244
FT /evidence="ECO:0007829|PDB:4II1"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:4II1"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4II1"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4II1"
SQ SEQUENCE 531 AA; 57359 MW; 36572156BABDA876 CRC64;
MDEESLESAL QTYRAQLQQV ELALGAGLDS SEQADLRQLQ GDLKELIELT EASLVSVRKS
SLLAALDEER PGRQEDAEYQ AFREAITEAV EAPAAARGSG SETVPKAEAG PESAAGGQEE
EEGEDEEELS GTKVSAPYYS SWGTLEYHNA MVVGTEEAED GSAGVRVLYL YPTHKSLKPC
PFFLEGKCRF KENCRFSHGQ VVSLDELRPF QDPDLSSLQA GSACLAKHQD GLWHAARITD
VDNGYYTVKF DSLLLREAVV EGDGILPPLR TEATESDSDS DGTGDSSYAR VVGSDAVDSA
QSSALCPSLA VVGSDAVDSG TCSSAFAGWE VHTRGIGSRL LTKMGYEFGK GLGRHAEGRV
EPIHAVVLPR GKSLDQCVET LQKQTRVGKA GTNKPPRCRG RGARPGGRPA PRNVFDFLNE
KLQGQAPGAL EAGAAPAGRR SKDMYHASKS AKRALSLRLF QTEEKIERTQ RDIRSIQEAL
ARNAGRHSVA SAQLQEKLAG AQRQLGQLRA QEAGLQQEQR KADTHKKMTE F
