Z354B_MOUSE
ID Z354B_MOUSE Reviewed; 601 AA.
AC Q9QXT9; Q9CV15;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Zinc finger protein 354B;
DE AltName: Full=Kidney, ischemia, and developmentally-regulated protein 2;
GN Name=Znf354b; Synonyms=Kid2, Zfp354b;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv;
RX PubMed=10564808; DOI=10.1016/s0378-1119(99)00440-0;
RA Tekki-Kessaris N., Bonventre J.V., Boulter C.A.;
RT "Characterization of the mouse Kid1 gene and identification of a highly
RT related gene, Kid2.";
RL Gene 240:13-22(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-590.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and kidney. Lower levels in
CC lung, muscle, heart, testis, tongue and eye.
CC {ECO:0000269|PubMed:10564808}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 16.5 dpc in brain, heart, lung,
CC kidney and gut. {ECO:0000269|PubMed:10564808}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF184112; AAF01034.1; -; mRNA.
DR EMBL; AL627215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC107400; AAI07401.1; -; mRNA.
DR EMBL; BC107401; AAI07402.1; -; mRNA.
DR EMBL; AK010007; BAB26638.1; -; mRNA.
DR CCDS; CCDS24641.1; -.
DR RefSeq; NP_038772.1; NM_013744.3.
DR AlphaFoldDB; Q9QXT9; -.
DR SMR; Q9QXT9; -.
DR STRING; 10090.ENSMUSP00000104752; -.
DR iPTMnet; Q9QXT9; -.
DR PhosphoSitePlus; Q9QXT9; -.
DR jPOST; Q9QXT9; -.
DR PaxDb; Q9QXT9; -.
DR PRIDE; Q9QXT9; -.
DR ProteomicsDB; 275332; -.
DR Antibodypedia; 29455; 16 antibodies from 9 providers.
DR DNASU; 27274; -.
DR Ensembl; ENSMUST00000109124; ENSMUSP00000104752; ENSMUSG00000020335.
DR Ensembl; ENSMUST00000164280; ENSMUSP00000127671; ENSMUSG00000020335.
DR GeneID; 27274; -.
DR KEGG; mmu:27274; -.
DR UCSC; uc007itd.2; mouse.
DR CTD; 27274; -.
DR MGI; MGI:1351476; Zfp354b.
DR VEuPathDB; HostDB:ENSMUSG00000020335; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162570; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q9QXT9; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9QXT9; -.
DR TreeFam; TF341817; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 27274; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Zfp354b; mouse.
DR PRO; PR:Q9QXT9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QXT9; protein.
DR Bgee; ENSMUSG00000020335; Expressed in ureteric bud trunk and 179 other tissues.
DR Genevisible; Q9QXT9; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
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; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..601
FT /note="Zinc finger protein 354B"
FT /id="PRO_0000280407"
FT DOMAIN 14..85
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 206..228
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 234..256
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 262..284
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 290..312
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 343..365
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 371..393
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 399..421
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 427..449
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 455..477
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 483..505
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 511..533
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 539..561
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 567..589
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96LW1"
SQ SEQUENCE 601 AA; 68664 MW; 4CE1540A8FF8E8B1 CRC64;
MAPEQREGKS QVSVTFEDVA VLFTRDEWKK LVPSQRSLYR EVMLENYSNL ASLGFPFTKP
KMISVLQQGE EPWKSEKESH GCSPLGCHGS LQTTKSTQTK ESLFQELKRK QLKRDEAWDF
TSGKSCRPDN SFRTQDTNES LEIISINHTK ILTIDKSRKN FKFGPSVGLK SIGKQKIAGE
KTQRNSLEEN STLLSQPKLK TVEKRYKCST CEKAFIHNSS LRKHLKNHTG ERLFQCKDCL
KAFSQSSALI QHQRTHTGEK PYICKECGKA FSHSASLCKH LRTHTLEKSY TCKECGKSFS
RRSGLFLHQK IHARENPHKY NPGRKASTSL SGCQRIHSRK KTYLCNECGN TFKSSSSLRY
HQRIHTGEKP FKCSECGRAF SQSASLIQHE RIHTGEKPYR CSECGKGFTS ISRLNRHRII
HTGEKFYNCN ECGKALSSHS TLIIHERIHT GEKPCKCKVC GKAFRQSSAL IQHQRMHTGE
RPYKCNECGK TFRCNSSLSN HQRTHTGEKP YRCQECGMSF GQSAALIQHR RIHTGEKPFK
CNTCGKSFRQ SSSLIAHQRI HTGEKPYECS ACGKLFSQRS SLTNHYRIHI EEDALNIDLH
E
