ID   FIZ1_HUMAN              Reviewed;         496 AA.
AC   Q96SL8; A2RU72; Q6ZMJ7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Flt3-interacting zinc finger protein 1;
DE   AltName: Full=Zinc finger protein 798;
GN   Name=FIZ1; Synonyms=ZNF798;
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], AND VARIANT ALA-391.
RC   TISSUE=Spleen, and 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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-391.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-391.
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).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12566383; DOI=10.1093/hmg/ddg035;
RA   Mitton K.P., Swain P.K., Khanna H., Dowd M., Apel I.J., Swaroop A.;
RT   "Interaction of retinal bZIP transcription factor NRL with Flt3-interacting
RT   zinc-finger protein Fiz1: possible role of Fiz1 as a transcriptional
RT   repressor.";
RL   Hum. Mol. Genet. 12:365-373(2003).
RN   [6]
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).
CC   -!- FUNCTION: May be a transcriptional repressor of NRL function in
CC       photoreceptors. Does not repress CRX-mediated transactivation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FLT3 cytoplasmic catalytic domain, following
CC       receptor stimulation, in a kinase-independent manner. Does not interact
CC       with other structurally related receptor tyrosine kinases, including
CC       KIT, CSF1R and PDGFR. Interacts with NRL (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12566383}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD18728.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK027674; BAB55286.1; -; mRNA.
DR   EMBL; AK160385; BAD18728.1; ALT_INIT; mRNA.
DR   EMBL; AC008735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471135; EAW72392.1; -; Genomic_DNA.
DR   EMBL; BC132777; AAI32778.1; -; mRNA.
DR   EMBL; BC136512; AAI36513.1; -; mRNA.
DR   CCDS; CCDS12928.1; -.
DR   RefSeq; NP_116225.2; NM_032836.2.
DR   RefSeq; XP_005259409.1; XM_005259352.4.
DR   AlphaFoldDB; Q96SL8; -.
DR   SMR; Q96SL8; -.
DR   BioGRID; 124357; 17.
DR   IntAct; Q96SL8; 6.
DR   MINT; Q96SL8; -.
DR   STRING; 9606.ENSP00000221665; -.
DR   iPTMnet; Q96SL8; -.
DR   PhosphoSitePlus; Q96SL8; -.
DR   BioMuta; FIZ1; -.
DR   DMDM; 296434506; -.
DR   EPD; Q96SL8; -.
DR   jPOST; Q96SL8; -.
DR   MassIVE; Q96SL8; -.
DR   MaxQB; Q96SL8; -.
DR   PaxDb; 9606-ENSP00000221665; -.
DR   PeptideAtlas; Q96SL8; -.
DR   ProteomicsDB; 78127; -.
DR   Pumba; Q96SL8; -.
DR   Antibodypedia; 33128; 177 antibodies from 24 providers.
DR   DNASU; 84922; -.
DR   Ensembl; ENST00000221665.5; ENSP00000221665.2; ENSG00000179943.8.
DR   GeneID; 84922; -.
DR   KEGG; hsa:84922; -.
DR   MANE-Select; ENST00000221665.5; ENSP00000221665.2; NM_032836.3; NP_116225.2.
DR   UCSC; uc002qli.4; human.
DR   AGR; HGNC:25917; -.
DR   CTD; 84922; -.
DR   GeneCards; FIZ1; -.
DR   HGNC; HGNC:25917; FIZ1.
DR   HPA; ENSG00000179943; Low tissue specificity.
DR   MIM; 609133; gene.
DR   neXtProt; NX_Q96SL8; -.
DR   OpenTargets; ENSG00000179943; -.
DR   PharmGKB; PA162388597; -.
DR   VEuPathDB; HostDB:ENSG00000179943; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000153306; -.
DR   HOGENOM; CLU_047914_0_0_1; -.
DR   InParanoid; Q96SL8; -.
DR   OMA; CECGTFF; -.
DR   OrthoDB; 5311231at2759; -.
DR   PhylomeDB; Q96SL8; -.
DR   TreeFam; TF337381; -.
DR   PathwayCommons; Q96SL8; -.
DR   SignaLink; Q96SL8; -.
DR   SIGNOR; Q96SL8; -.
DR   BioGRID-ORCS; 84922; 13 hits in 1181 CRISPR screens.
DR   GenomeRNAi; 84922; -.
DR   Pharos; Q96SL8; Tdark.
DR   PRO; PR:Q96SL8; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q96SL8; Protein.
DR   Bgee; ENSG00000179943; Expressed in cardiac muscle of right atrium and 171 other cell types or tissues.
DR   ExpressionAtlas; Q96SL8; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISS:ARUK-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:ARUK-UCL.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:ARUK-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 9.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24383:SF13; FLT3-INTERACTING ZINC FINGER PROTEIN 1; 1.
DR   PANTHER; PTHR24383; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
DR   Genevisible; Q96SL8; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..496
FT                   /note="Flt3-interacting zinc finger protein 1"
FT                   /id="PRO_0000046937"
FT   ZN_FING         23..45
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         51..73
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         79..101
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         107..130
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         200..222
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         228..250
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         331..352
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         358..381
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         414..436
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         442..464
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         470..492
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          250..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..395
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   VARIANT         391
FT                   /note="T -> A (in dbSNP:rs7247236)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT                   /id="VAR_060269"
FT   CONFLICT        127
FT                   /note="K -> R (in Ref. 1; BAB55286)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   496 AA;  51996 MW;  D4DD7E435249B0C5 CRC64;
     MDDVPAPTPA PAPPAAAAPR VPFHCSECGK SFRYRSDLRR HFARHTALKP HACPRCGKGF
     KHSFNLANHL RSHTGERPYR CSACPKGFRD STGLLHHQVV HTGEKPYCCL VCELRFSSRS
     SLGRHLKRQH RGVLPSPLQP GPGLPALSAP CSVCCNVGPC SVCGGSGAGG GEGPEGAGAG
     LGSWGLAEAA AAAAASLPPF ACGACARRFD HGRELAAHWA AHTDVKPFKC PRCERDFNAP
     ALLERHKLTH DLQGPGAPPA QAWAAGPGAG PETAGEGTAA EAGDAPLASD RRLLLGPAGG
     GVPKLGGLLP EGGGEAPAPA AAAEPSEDTL YQCDCGTFFA SAAALASHLE AHSGPATYGC
     GHCGALYAAL AALEEHRRVS HGEGGGEEAA TAAREREPAS GEPPSGSGRG KKIFGCSECE
     KLFRSPRDLE RHVLVHTGEK PFPCLECGKF FRHECYLKRH RLLHGTERPF PCHICGKGFI
     TLSNLSRHLK LHRGMD
//