FIZ1_HUMAN
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 03-AUG-2022, entry version 157.
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 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; Q96SL8; -.
DR PeptideAtlas; Q96SL8; -.
DR PRIDE; Q96SL8; -.
DR ProteomicsDB; 78127; -.
DR Antibodypedia; 33128; 152 antibodies from 23 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 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; DCERDFN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96SL8; -.
DR TreeFam; TF337381; -.
DR PathwayCommons; Q96SL8; -.
DR SignaLink; Q96SL8; -.
DR SIGNOR; Q96SL8; -.
DR BioGRID-ORCS; 84922; 13 hits in 1103 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 170 other tissues.
DR ExpressionAtlas; Q96SL8; baseline and differential.
DR Genevisible; Q96SL8; HS.
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 GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
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
