ZN207_MOUSE
ID ZN207_MOUSE Reviewed; 495 AA.
AC Q9JMD0; E9PW12; Q99LA2; Q9Z326;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=BUB3-interacting and GLEBS motif-containing protein ZNF207 {ECO:0000250|UniProtKB:O43670};
DE Short=BuGZ {ECO:0000250|UniProtKB:O43670};
DE AltName: Full=49 kDa zinc finger protein;
DE AltName: Full=Zinc finger protein 207 {ECO:0000250|UniProtKB:O43670};
GN Name=Znf207 {ECO:0000250|UniProtKB:O43670};
GN Synonyms=Bugz {ECO:0000250|UniProtKB:O43670},
GN Zep {ECO:0000303|PubMed:9832628}, Zfp207 {ECO:0000312|MGI:MGI:1340045};
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] (ISOFORM 4), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9832628; DOI=10.1093/oxfordjournals.jbchem.a022241;
RA Taguchi E., Muramatsu H., Fan Q.W., Kurosawa N., Sobue G., Muramatsu T.;
RT "Zep: A novel zinc finger protein containing a large proline-rich domain.";
RL J. Biochem. 124:1220-1228(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Misawa K., Kitamura T., Nosaka T.;
RT "Mouse zinc finger transcription factor (ZNF207) mRNA, complete cds.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, DOMAIN, INTERACTION WITH BUB3, AND MUTAGENESIS OF
RP 391-GLU-GLU-392.
RX PubMed=26388440; DOI=10.1016/j.cell.2015.08.010;
RA Jiang H., Wang S., Huang Y., He X., Cui H., Zhu X., Zheng Y.;
RT "Phase transition of spindle-associated protein regulate spindle apparatus
RT assembly.";
RL Cell 163:108-122(2015).
CC -!- FUNCTION: Kinetochore- and microtubule-binding protein that plays a key
CC role in spindle assembly. ZNF207/BuGZ is mainly composed of disordered
CC low-complexity regions and undergoes phase transition or coacervation
CC to form temperature-dependent liquid droplets. Coacervation promotes
CC microtubule bundling and concentrates tubulin, promoting microtubule
CC polymerization and assembly of spindle and spindle matrix by
CC concentrating its building blocks (PubMed:26388440). Also acts as a
CC regulator of mitotic chromosome alignment by mediating the stability
CC and kinetochore loading of BUB3. Mechanisms by which BUB3 is protected
CC are unclear: according to a first report, ZNF207/BuGZ may act by
CC blocking ubiquitination and proteasomal degradation of BUB3. According
CC to another report, the stabilization is independent of the proteasome
CC (By similarity). {ECO:0000250|UniProtKB:O43670,
CC ECO:0000269|PubMed:26388440}.
CC -!- SUBUNIT: Interacts (via GLEBS region) with BUB3.
CC {ECO:0000269|PubMed:26388440}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9832628}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:O43670}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:O43670}. Note=Localizes
CC primarily to the nucleus in interphase, concentrates at kinetochores
CC prior to nuclear envelope breakdown and during early prometaphase, and
CC disappears from kinetochores upon microtubule-binding.
CC {ECO:0000250|UniProtKB:O43670}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9JMD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JMD0-2; Sequence=VSP_054255;
CC Name=3;
CC IsoId=Q9JMD0-3; Sequence=VSP_054257;
CC Name=4;
CC IsoId=Q9JMD0-4; Sequence=VSP_054256, VSP_054257;
CC -!- TISSUE SPECIFICITY: In day-13 embryo, strongly expressed in the nervous
CC system (brain, spinal cord and dorsal root ganglia), with strong to
CC weak expression in other regions. Continues to be strongly expressed in
CC the neonatal brain while expression is weak in the brain and spinal
CC cord of adult. {ECO:0000269|PubMed:9832628}.
CC -!- DOMAIN: Mainly composed of disordered low-complexity regions outside of
CC the C2H2-type zinc fingers. Coacervation depends on hydrophobic and
CC aromatic Phe and Tyr in the disordered low-complexity region, that may
CC promote coacervation by forming intermolecular hydrophobic
CC interactions. {ECO:0000269|PubMed:26388440}.
CC -!- DOMAIN: The GLEBS region mediates interaction with BUB3.
CC {ECO:0000250|UniProtKB:O43670}.
CC -!- DOMAIN: The microtubule-binding region is required for efficient
CC loading of BUB3 onto kinetochores and proper mitosis.
CC {ECO:0000250|UniProtKB:O43670}.
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DR EMBL; AB013357; BAA37094.1; -; mRNA.
DR EMBL; AB032196; BAA92375.1; -; mRNA.
DR EMBL; AK087885; BAC40034.1; -; mRNA.
DR EMBL; AK146787; BAE27431.1; -; mRNA.
DR EMBL; AK159683; BAE35286.1; -; mRNA.
DR EMBL; AL591146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL15636.1; -; Genomic_DNA.
DR EMBL; CH466556; EDL15638.1; -; Genomic_DNA.
DR EMBL; BC003715; AAH03715.1; -; mRNA.
DR CCDS; CCDS48863.1; -. [Q9JMD0-1]
DR CCDS; CCDS48864.1; -. [Q9JMD0-3]
DR CCDS; CCDS48865.1; -. [Q9JMD0-2]
DR PIR; JE0367; JE0367.
DR RefSeq; NP_001123641.1; NM_001130169.1. [Q9JMD0-1]
DR RefSeq; NP_001123642.1; NM_001130170.1. [Q9JMD0-2]
DR RefSeq; NP_001123643.1; NM_001130171.1. [Q9JMD0-3]
DR RefSeq; NP_035881.1; NM_011751.3. [Q9JMD0-4]
DR RefSeq; XP_006533252.1; XM_006533189.2. [Q9JMD0-1]
DR AlphaFoldDB; Q9JMD0; -.
DR SMR; Q9JMD0; -.
DR BioGRID; 204648; 14.
DR IntAct; Q9JMD0; 1.
DR STRING; 10090.ENSMUSP00000054168; -.
DR iPTMnet; Q9JMD0; -.
DR PhosphoSitePlus; Q9JMD0; -.
DR EPD; Q9JMD0; -.
DR MaxQB; Q9JMD0; -.
DR PaxDb; Q9JMD0; -.
DR PeptideAtlas; Q9JMD0; -.
DR PRIDE; Q9JMD0; -.
DR ProteomicsDB; 299572; -. [Q9JMD0-3]
DR ProteomicsDB; 299573; -. [Q9JMD0-4]
DR Antibodypedia; 1741; 326 antibodies from 24 providers.
DR DNASU; 22680; -.
DR Ensembl; ENSMUST00000017567; ENSMUSP00000017567; ENSMUSG00000017421. [Q9JMD0-3]
DR Ensembl; ENSMUST00000053740; ENSMUSP00000054168; ENSMUSG00000017421. [Q9JMD0-1]
DR Ensembl; ENSMUST00000165565; ENSMUSP00000132968; ENSMUSG00000017421. [Q9JMD0-2]
DR Ensembl; ENSMUST00000178665; ENSMUSP00000136727; ENSMUSG00000017421. [Q9JMD0-3]
DR Ensembl; ENSMUST00000188489; ENSMUSP00000139653; ENSMUSG00000017421. [Q9JMD0-3]
DR GeneID; 22680; -.
DR KEGG; mmu:22680; -.
DR UCSC; uc007kly.2; mouse. [Q9JMD0-4]
DR UCSC; uc007klz.2; mouse. [Q9JMD0-1]
DR UCSC; uc007kma.2; mouse. [Q9JMD0-3]
DR UCSC; uc007kmb.2; mouse. [Q9JMD0-2]
DR CTD; 22680; -.
DR MGI; MGI:1340045; Zfp207.
DR VEuPathDB; HostDB:ENSMUSG00000017421; -.
DR eggNOG; KOG2893; Eukaryota.
DR GeneTree; ENSGT00730000111057; -.
DR HOGENOM; CLU_037132_3_2_1; -.
DR InParanoid; Q9JMD0; -.
DR OMA; EPPKATF; -.
DR OrthoDB; 1453306at2759; -.
DR PhylomeDB; Q9JMD0; -.
DR TreeFam; TF313844; -.
DR BioGRID-ORCS; 22680; 23 hits in 76 CRISPR screens.
DR ChiTaRS; Zfp207; mouse.
DR PRO; PR:Q9JMD0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JMD0; protein.
DR Bgee; ENSMUSG00000017421; Expressed in undifferentiated genital tubercle and 264 other tissues.
DR ExpressionAtlas; Q9JMD0; baseline and differential.
DR Genevisible; Q9JMD0; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:1990047; C:spindle matrix; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IDA:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Kinetochore; Metal-binding;
KW Microtubule; Mitosis; Nucleus; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..495
FT /note="BUB3-interacting and GLEBS motif-containing protein
FT ZNF207"
FT /id="PRO_0000428733"
FT ZN_FING 11..34
FT /note="C2H2-type 1"
FT ZN_FING 35..58
FT /note="C2H2-type 2"
FT REGION 1..92
FT /note="Microtubule-binding region"
FT /evidence="ECO:0000250|UniProtKB:O43670"
FT REGION 99..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..408
FT /note="GLEBS"
FT /evidence="ECO:0000250|UniProtKB:O43670"
FT REGION 462..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 185..200
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054255"
FT VAR_SEQ 219..222
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9832628"
FT /id="VSP_054256"
FT VAR_SEQ 276..306
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9832628"
FT /id="VSP_054257"
FT MUTAGEN 390..391
FT /note="EE->AA: Abolishes interaction and stabilization of
FT BUB3."
FT /evidence="ECO:0000269|PubMed:26388440"
SQ SEQUENCE 495 AA; 52793 MW; 71EB32147BB6A5AD CRC64;
MGRKKKKQLK PWCWYCNRDF DDEKILIQHQ KAKHFKCHIC HKKLYTGPGL AIHCMQVHKE
TIDAVPNAIP GRTDIELEIY GMEGIPEKDM DERRRLLEQK TQESQKKKQQ DDSDEYDDDE
SAASTSFQPQ PVQPQQGYIP PMAQPGLPPV PGAPGMPPGI PPLMPGVPPL MPGMPPVMPG
MPPGLHHQRK YTQSFCGENI MMPMGGMMPP GPGIPPLMPG MPPGMPPPVP RPGIPPMTQA
QAVSAPGILN RPPAPTAAVP APQPPVTKPL FPSAGQMGTP VTSSSTASSN SESLSASSKA
LFPSTAQAQA AVQGPVGTDF KPLNSTPAAT TTEPPKPTFP AYTQSTASTT STTNSTAAKP
AASITSKPAT LTTTSATSKL IHPDEDISLE ERRAQLPKYQ RNLPRPGQTP IGNPPVGPIG
GMMPPQPGLP QQQAMRPPMP PHGQYGGHHQ GMPGYLPGAM PPYGQGPPMV PPYQGGPPRP
PMGMRPPVMS QGGRY
