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ZN207_PONAB
ID   ZN207_PONAB             Reviewed;         494 AA.
AC   Q5R8K4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=Zinc finger protein 207 {ECO:0000250|UniProtKB:O43670};
GN   Name=ZNF207 {ECO:0000250|UniProtKB:O43670};
GN   Synonyms=BUGZ {ECO:0000250|UniProtKB:O43670};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Also acts as a regulator of mitotic
CC       chromosome alignment by mediating the stability and kinetochore loading
CC       of BUB3. Mechanisms by which BUB3 is protected are unclear: according
CC       to a first report, ZNF207/BuGZ may act by blocking ubiquitination and
CC       proteasomal degradation of BUB3. According to another report, the
CC       stabilization is independent of the proteasome.
CC       {ECO:0000250|UniProtKB:O43670}.
CC   -!- SUBUNIT: Interacts (via GLEBS region) with BUB3.
CC       {ECO:0000250|UniProtKB:O43670}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43670}.
CC       Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O43670}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O43670}.
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: The microtubule-binding region is required for efficient
CC       loading of BUB3 onto kinetochores and proper mitosis.
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:0000250|UniProtKB:Q9JMD0}.
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DR   EMBL; CR859748; CAH91906.1; -; mRNA.
DR   RefSeq; NP_001126104.1; NM_001132632.1.
DR   AlphaFoldDB; Q5R8K4; -.
DR   SMR; Q5R8K4; -.
DR   STRING; 9601.ENSPPYP00000009173; -.
DR   GeneID; 100173059; -.
DR   CTD; 7756; -.
DR   eggNOG; KOG2893; Eukaryota.
DR   InParanoid; Q5R8K4; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:1990047; C:spindle matrix; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; 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:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW   Cytoplasm; Cytoskeleton; DNA-binding; Kinetochore; Metal-binding;
KW   Microtubule; Mitosis; Nucleus; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..494
FT                   /note="BUB3-interacting and GLEBS motif-containing protein
FT                   ZNF207"
FT                   /id="PRO_0000301676"
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          100..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..407
FT                   /note="GLEBS"
FT                   /evidence="ECO:0000250|UniProtKB:O43670"
FT   REGION          455..494
FT                   /note="Disordered"
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..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..484
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  52580 MW;  28EE04241771AE46 CRC64;
     MGRKKKKQLK PWCWYCNRDF DDEKILTQHQ KAKHFKCHIC HKKLYTGPGL AIHCMQVHKE
     TIDAVPNAIP GRTDIELEIY GMEGIPEKDM DEGRRLLEQK TQESQKKKQQ DDSDEYDDDD
     SAASTSFQPQ PVQPQQGYIP PMAQPGLPPV PGAPGMPPGI PPLMPGVPPL MPGMPPVMPG
     MPPGLHHQRK YTQSFCGENI MMPMGGMMPP GPGIPPLMPG MPPGMPPPVP RPGIPPMTQA
     QAVSAPGILN RPPAPTATVP APQPPVTKPL FPSAGQMGTP VTSSSTASSN SESLSASSKA
     PFPSTAQAQV AVQGPVGTDF KPLNSTPATS TEPPKPTFPA YTQSTASTTS TTNSTAAKPA
     ASITSKPATL TTTSATSKLI HPDEDISLEE RRAQLPKYQR NLPRPGQAPI GNPPVGPIGG
     MMPPQPGIPQ QQGMRPPMPP HGQYGGHHQG MPGYLPGAMP PYGQGPPMVP PYQGGPPRPP
     MGMRPPVMSQ GGRY
 
 
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