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ZFOI1_MOUSE
ID   ZFOI1_MOUSE             Reviewed;         680 AA.
AC   E9Q8G5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Zinc finger protein OBI1 {ECO:0000305};
DE   AltName: Full=Osteoblast inducer-1 {ECO:0000303|PubMed:30654721};
DE            Short=ObI-1 {ECO:0000303|PubMed:30654721};
GN   Name=ObI1; Synonyms=A430033K04Rik {ECO:0000312|MGI:MGI:3583896};
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 [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   [2]
RP   TISSUE SPECIFICITY, FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND
RP   UBIQUITINATION.
RX   PubMed=30654721; DOI=10.1089/scd.2018.0152;
RA   Querques F., D'Agostino A., Cozzolino C., Cozzuto L., Lombardo B.,
RA   Leggiero E., Ruosi C., Pastore L.;
RT   "Identification of a Novel Transcription Factor Required for Osteogenic
RT   Differentiation of Mesenchymal Stem Cells.";
RL   Stem Cells Dev. 28:370-383(2019).
CC   -!- FUNCTION: May modulate osteogenic differentiation, at least in part,
CC       through the bone morphogenetic protein (BMP) signaling pathway,
CC       increasing RUNX2 activation and leading to osteoblast commitment and
CC       maturation. {ECO:0000269|PubMed:30654721}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30654721}.
CC   -!- TISSUE SPECIFICITY: Expressed during osteogenic differentiation where
CC       levels increase from the first days of differentiation and remain high
CC       during the whole process (PubMed:30654721). Highly expressed in lung
CC       (PubMed:30654721). {ECO:0000269|PubMed:30654721}.
CC   -!- INDUCTION: Up-regulated during osteogenic differentiation.
CC       {ECO:0000269|PubMed:30654721}.
CC   -!- PTM: Polyubiquitinated, leading to its degradation via the ubiquitin-
CC       proteasome pathway. {ECO:0000269|PubMed:30654721}.
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DR   EMBL; AC125115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC242503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_898846.2; NM_183025.2.
DR   AlphaFoldDB; E9Q8G5; -.
DR   SMR; E9Q8G5; -.
DR   STRING; 10090.ENSMUSP00000067316; -.
DR   PaxDb; E9Q8G5; -.
DR   PRIDE; E9Q8G5; -.
DR   ProteomicsDB; 355325; -.
DR   DNASU; 243308; -.
DR   Ensembl; ENSMUST00000069862; ENSMUSP00000067316; ENSMUSG00000056014.
DR   GeneID; 243308; -.
DR   KEGG; mmu:243308; -.
DR   UCSC; uc009afu.2; mouse.
DR   MGI; MGI:3583896; A430033K04Rik.
DR   VEuPathDB; HostDB:ENSMUSG00000056014; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00950000182890; -.
DR   HOGENOM; CLU_002678_44_5_1; -.
DR   InParanoid; E9Q8G5; -.
DR   OMA; FCHESEN; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; E9Q8G5; -.
DR   TreeFam; TF339594; -.
DR   BioGRID-ORCS; 243308; 0 hits in 65 CRISPR screens.
DR   ChiTaRS; A430033K04Rik; mouse.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; E9Q8G5; protein.
DR   Bgee; ENSMUSG00000056014; Expressed in animal zygote and 186 other tissues.
DR   ExpressionAtlas; E9Q8G5; baseline and differential.
DR   Genevisible; E9Q8G5; MM.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IBA:GO_Central.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; 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; 6.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 6.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..680
FT                   /note="Zinc finger protein OBI1"
FT                   /id="PRO_0000454385"
FT   DOMAIN          16..87
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         263..280
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         455..477
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         483..505
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         511..533
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         539..561
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         567..589
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         595..617
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         623..645
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         651..673
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
SQ   SEQUENCE   680 AA;  79457 MW;  4F92FA6E3BF2DFF2 CRC64;
     MVRRRQRLPE VDMGLVSFED VAVDFTWQEW QELDAAQRTL YRDVMLENYR SLVWLGHCLA
     KPELISKLEE GFEPWGVAEA TEQCLPGVRK WSAPVEKGQQ SQEKYLRQVK IIKKNTPDED
     KVEVENTYNV DSNCISNMTL KNEVCSRVFF QELVNPLLDV PLPTEAGERQ STEVPHDLNR
     TQEVLSYPKH FTHHSKDQYS QCCFQYFGPD EAFHTKAILT PEMFYVQETS RTCNNYDKSF
     DEVTIPAQYM TQLRKQTLGW NICHKIFPNK TELSNHDAMH TGENDDKCDY EKPIINKSLY
     LTKHQEAHAG IEPQAHKENI KFFCLDAELQ TVDPELHGEK QVYECKVSGK TFRHQPEHIS
     QQRPHACERA CQAKEHGEAG CDEPALTQHQ RLCTEEKACE GKACSKAFHH KSLLPQYQSA
     RADEQQSDCK ELMKIYFYVS SPTQHHGPPP PEKPFRCNDC LKTFSHKSQL ERHQRMHTGE
     KPHECKECRK AFCHKSHLIR HQGIHAPEKP YECNECKKSF YLRSQLTLHE RTHTGEKPFE
     CKECRKAFSR NSHLTQHQKI HTGEKPHKCK ECGNAFARKS HLIQHQKTHT GERPYECKEC
     RKAFSRKSQL MQHETTHTGE RAYECKECRK TFYLKAYLTR HQVIHQSEKP FECKKCGKAF
     SRKSYLTRHQ KIHKGQTLSG
 
 
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