ZN207_XENLA
ID ZN207_XENLA Reviewed; 452 AA.
AC Q7ZXV8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=BUB3-interacting and GLEBS motif-containing protein ZNF207 {ECO:0000250|UniProtKB:O43670};
DE Short=BuGZ {ECO:0000250|UniProtKB:O43670};
DE Short=xBuGZ {ECO:0000303|PubMed:26388440};
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};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH BUB3.
RX PubMed=24462186; DOI=10.1016/j.devcel.2013.12.013;
RA Jiang H., He X., Wang S., Jia J., Wan Y., Wang Y., Zeng R., Yates J. III,
RA Zhu X., Zheng Y.;
RT "A microtubule-associated zinc finger protein, BuGZ, regulates mitotic
RT chromosome alignment by ensuring Bub3 stability and kinetochore
RT targeting.";
RL Dev. Cell 28:268-281(2014).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF TYR-117;
RP PHE-129; PHE-138; PHE-256; PHE-274; PHE-292; TYR-295; TYR-352; TYR-402;
RP TYR-412; PHE-420; PHE-430 AND TYR-452.
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. {ECO:0000269|PubMed:26388440}.
CC -!- SUBUNIT: Interacts (via GLEBS region) with bub3.
CC {ECO:0000269|PubMed:24462186}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43670}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O43670}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26388440}.
CC Note=Localizes primarily to the nucleus in interphase, concentrates at
CC kinetochores prior to nuclear envelope breakdown and during early
CC prometaphase, and disappears from kinetochores upon microtubule-
CC binding. {ECO:0000250|UniProtKB:O43670}.
CC -!- DOMAIN: The GLEBS region mediates interaction with bub3.
CC {ECO:0000250|UniProtKB:O43670}.
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 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; BC044099; AAH44099.1; -; mRNA.
DR RefSeq; NP_001080324.1; NM_001086855.1.
DR AlphaFoldDB; Q7ZXV8; -.
DR SMR; Q7ZXV8; -.
DR DNASU; 380016; -.
DR GeneID; 380016; -.
DR KEGG; xla:380016; -.
DR CTD; 380016; -.
DR Xenbase; XB-GENE-997707; znf207.S.
DR OrthoDB; 1453306at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 380016; Expressed in gastrula and 19 other tissues.
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:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:1990047; C:spindle matrix; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; IDA: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 Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Kinetochore; Metal-binding; Microtubule; Mitosis;
KW Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..452
FT /note="BUB3-interacting and GLEBS motif-containing protein
FT ZNF207"
FT /id="PRO_0000428734"
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..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..361
FT /note="GLEBS"
FT /evidence="ECO:0000250|UniProtKB:O43670"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 117
FT /note="Y->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-129; S-138; S-256; S-274; S-292; S-295;
FT S-352; S-402; S-412; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 129
FT /note="F->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-138; S-256; S-274; S-292; S-295;
FT S-352; S-402; S-412; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 138
FT /note="F->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-256; S-274; S-292; S-295;
FT S-352; S-402; S-412; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 256
FT /note="F->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-274; S-292; S-295;
FT S-352; S-402; S-412; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 274
FT /note="F->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-256; S-292; S-295;
FT S-352; S-402; S-412; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 292
FT /note="F->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-256; S-274; S-295;
FT S-352; S-402; S-412; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 295
FT /note="Y->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-256; S-274; S-292;
FT S-352; S-402; S-412; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 352
FT /note="Y->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-256; S-274; S-292;
FT S-295; S-402; S-412; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 402
FT /note="Y->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-256; S-274; S-292;
FT S-295; S-352; S-412; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 412
FT /note="Y->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-256; S-274; S-292;
FT S-295; S-352; S-402; S-420; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 420
FT /note="F->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-256; S-274; S-292;
FT S-295; S-352; S-402; S-412; S-430 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 430
FT /note="F->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-256; S-274; S-292;
FT S-295; S-352; S-402; S-412; S-420 and S-452."
FT /evidence="ECO:0000269|PubMed:26388440"
FT MUTAGEN 452
FT /note="Y->S: In xBuGZ13S: Impaired coacervation; when
FT associated with S-117; S-129; S-138; S-256; S-274; S-292;
FT S-295; S-352; S-402; S-412; S-420 and S-430."
FT /evidence="ECO:0000269|PubMed:26388440"
SQ SEQUENCE 452 AA; 48549 MW; B02A4DA4F7ED6ED1 CRC64;
MGRKKKKQLK PWCWYCNRDF DDEKILIQHQ KAKHFKCHIC HKKLYTGPGL AIHCMQVHKE
TIDAVPNAIP GRTDIELEIY GMEGIPEKDM EERRRILEQK TQVDGQKKKT NQDDSDYDDD
DDTAPSTSFQ QMQTQQAFMP TMGQPGIPGL PGAPGMPPGI TSLMPAVPPL ISGIPHVMAG
MHPHGMMSMG GMMHPHRPGI PPMMAGLPPG VPPPGLRPGI PPVTQAQPAL SQAVVSRLPV
PSTSAPALQS VPKPLFPSAG QAQAHISGPV GTDFKPLNNI PATTAEHPKP TFPAYTQSTM
STTSTTNSTA SKPSTSITSK PATLTTTSAT SKLVHPDEDI SLEEKRAQLP KYQRNLPRPG
QAPISNMGST AVGPLGAMMA PRPGLPPQQH GMRHPLPPHG QYGAPLQGMA GYHPGTMPPF
GQGPPMVPPF QGGPPRPLMG IRPPVMSQGG RY
