ZFP90_MOUSE
ID ZFP90_MOUSE Reviewed; 636 AA.
AC Q61967; Q3U4J5; Q543I6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Zinc finger protein 90;
DE Short=Zfp-90;
DE AltName: Full=Zinc finger protein NK10;
GN Name=Zfp90; Synonyms=Nk10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=7576184; DOI=10.1089/dna.1995.14.971;
RA Lange R., Christoph A., Thiesen H.-J., Vopper G., Johnson K.R., Lemaire L.,
RA Plomann M., Cremer H., Barthels D., Heinlein U.A.O.;
RT "Developmentally regulated mouse gene NK10 encodes a zinc finger repressor
RT protein with differential DNA-binding domains.";
RL DNA Cell Biol. 14:971-981(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Olfactory bulb, and Pancreatic islet;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [4]
RP FUNCTION, INTERACTION WITH REST, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21284946; DOI=10.1016/j.yjmcc.2011.01.017;
RA Hata L., Murakami M., Kuwahara K., Nakagawa Y., Kinoshita H., Usami S.,
RA Yasuno S., Fujiwara M., Kuwabara Y., Minami T., Yamada Y., Yamada C.,
RA Nakao K., Ueshima K., Nishikimi T., Nakao K.;
RT "Zinc-finger protein 90 negatively regulates neuron-restrictive silencer
RT factor-mediated transcriptional repression of fetal cardiac genes.";
RL J. Mol. Cell. Cardiol. 50:972-981(2011).
CC -!- FUNCTION: Inhibits the transcriptional repressor activity of REST by
CC inhibiting its binding to DNA, thereby derepressing transcription of
CC REST target genes. {ECO:0000269|PubMed:21284946,
CC ECO:0000269|PubMed:7576184}.
CC -!- SUBUNIT: Interacts (via N- and C-termini) with REST (via zinc-finger
CC DNA-binding domain); the interaction inhibits REST repressor activity.
CC {ECO:0000269|PubMed:21284946}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21284946,
CC ECO:0000269|PubMed:7576184}. Note=Colocalizes with REST in the nucleus.
CC {ECO:0000269|PubMed:21284946}.
CC -!- TISSUE SPECIFICITY: Brain, spleen, thymus, and testis (PubMed:7576184).
CC Expressed in heart (PubMed:7576184, PubMed:21284946).
CC {ECO:0000269|PubMed:21284946, ECO:0000269|PubMed:7576184}.
CC -!- DEVELOPMENTAL STAGE: There is a marked increase after postnatal stages
CC 18-20 (simultaneously to the appearance of haploid cell stages).
CC Maximal expression is observed around 2 weeks postnatally, with the
CC exception of brain and testis, where the expression is highest in
CC earlier developmental stages. {ECO:0000269|PubMed:7576184}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32436.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE32436.1; Type=Miscellaneous discrepancy; Note=After frameshift's correction, the CDS was not identified.; Evidence={ECO:0000305};
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DR EMBL; X79828; CAA56225.1; -; mRNA.
DR EMBL; AK032286; BAC27794.1; -; mRNA.
DR EMBL; AK050519; BAC34302.1; -; mRNA.
DR EMBL; AK154205; BAE32436.1; ALT_SEQ; mRNA.
DR EMBL; BC046298; AAH46298.1; -; mRNA.
DR CCDS; CCDS22635.1; -.
DR PIR; I48689; I48689.
DR RefSeq; NP_035894.1; NM_011764.3.
DR AlphaFoldDB; Q61967; -.
DR SMR; Q61967; -.
DR STRING; 10090.ENSMUSP00000034382; -.
DR iPTMnet; Q61967; -.
DR PhosphoSitePlus; Q61967; -.
DR jPOST; Q61967; -.
DR MaxQB; Q61967; -.
DR PaxDb; Q61967; -.
DR PRIDE; Q61967; -.
DR ProteomicsDB; 299550; -.
DR Antibodypedia; 29788; 76 antibodies from 18 providers.
DR DNASU; 22751; -.
DR Ensembl; ENSMUST00000034382; ENSMUSP00000034382; ENSMUSG00000031907.
DR Ensembl; ENSMUST00000212874; ENSMUSP00000148744; ENSMUSG00000031907.
DR GeneID; 22751; -.
DR KEGG; mmu:22751; -.
DR UCSC; uc009ngd.1; mouse.
DR CTD; 146198; -.
DR MGI; MGI:104786; Zfp90.
DR VEuPathDB; HostDB:ENSMUSG00000031907; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162132; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q61967; -.
DR OMA; TLEDTWD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q61967; -.
DR TreeFam; TF350822; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 22751; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Zfp90; mouse.
DR PRO; PR:Q61967; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61967; protein.
DR Bgee; ENSMUSG00000031907; Expressed in ganglionic eminence and 233 other tissues.
DR ExpressionAtlas; Q61967; baseline and differential.
DR Genevisible; Q61967; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
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; 11.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..636
FT /note="Zinc finger protein 90"
FT /id="PRO_0000047311"
FT DOMAIN 14..85
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 208..230
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 250..272
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 390..412
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..468
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..516
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..544
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..572
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 227..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TF47"
FT CONFLICT 53
FT /note="L -> A (in Ref. 2; BAE32436)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="T -> A (in Ref. 2; BAE32436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 72423 MW; 1269BEC7729E369F CRC64;
MAPRPPTAKP QESVTFKDVA VNFTQEEWHH VGPAQRSLYR DVMLENYNHL VSLGYQVSKP
EVIFKLEQGE EPWISEKEIQ RPFCPDWKTR PESSRSPQQG VSEVFLRTNV LSHTTIGDIW
NVAIQGHQES GRRHLGPEAS SQKKITTLEK KIEQNKVGED SSLSTDLVPQ LDISSSIRPS
DCKTFGNNLE HNSELVTQSN ILAKKKPYKC DKCRKSFIHR SSLNKHEKIH KGDPYSNGTD
QGAQSGRKHH ECADCGKTFL WRTQLTEHQR IHTGEKPFEC NVCGKAFRHS SSLGQHENAH
TGEKPYQCSL CGKAFQRSSS LVQHQRIHTG EKPYRCNLCG RSFRHSTSLT QHEVTHSGEK
PFQCKECGKA FSRCSSLVQH ERTHTGEKPF ECSICGRAFG QSPSLYKHMR IHKRSKPYQS
NNFSLAFVPN TPLPQGEGLL TEVKSYHCND CGKDFGHITD FSEHQRLHAG ENSYGSEQTL
LGQQSLSHPR EKPYQCNVCG KAFKRSTSFI EHHRIHTGEK PYECNECGEA FSRLSSLTQH
ERTHTGEKPY ECIDCGKAFS QSSSLIQHER THTGEKPYEC NECGRAFRKK TNLHDHQRTH
TGEKPYACKE CGRNFSRSSA LTKHHRVHAR NKLQES
