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GABP1_BOVIN
ID   GABP1_BOVIN             Reviewed;         383 AA.
AC   Q1RMI3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=GA-binding protein subunit beta-1;
DE            Short=GABP subunit beta-1;
DE            Short=GABPB-1;
DE   AltName: Full=GABP subunit beta-2;
DE            Short=GABPB-2;
GN   Name=GABPB1; Synonyms=GABPB2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor capable of interacting with purine rich
CC       repeats (GA repeats). Acts as a a master regulator of nuclear-encoded
CC       mitochondrial genes. {ECO:0000250|UniProtKB:Q00420}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. Interacts
CC       with HCFC1, causing repression of transcriptional activity.
CC       {ECO:0000250|UniProtKB:Q06547}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06547}.
CC   -!- PTM: Acetylated by EP300/p300. Deacetylated by SIRT7, promoting
CC       heterotetramerization and activity. {ECO:0000250|UniProtKB:Q00420}.
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DR   EMBL; BC114881; AAI14882.1; -; mRNA.
DR   RefSeq; NP_001069272.1; NM_001075804.1.
DR   RefSeq; XP_003586626.3; XM_003586578.3.
DR   RefSeq; XP_015320604.1; XM_015465118.1.
DR   AlphaFoldDB; Q1RMI3; -.
DR   SMR; Q1RMI3; -.
DR   STRING; 9913.ENSBTAP00000030917; -.
DR   PaxDb; Q1RMI3; -.
DR   PRIDE; Q1RMI3; -.
DR   Ensembl; ENSBTAT00000076865; ENSBTAP00000071985; ENSBTAG00000022801.
DR   GeneID; 520313; -.
DR   KEGG; bta:520313; -.
DR   CTD; 2553; -.
DR   VEuPathDB; HostDB:ENSBTAG00000022801; -.
DR   VGNC; VGNC:106750; GABPB1.
DR   eggNOG; ENOG502QRTX; Eukaryota.
DR   GeneTree; ENSGT00940000157875; -.
DR   HOGENOM; CLU_000134_12_1_1; -.
DR   InParanoid; Q1RMI3; -.
DR   OrthoDB; 1514706at2759; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000022801; Expressed in oocyte and 109 other tissues.
DR   ExpressionAtlas; Q1RMI3; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
PE   2: Evidence at transcript level;
KW   Acetylation; ANK repeat; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q06547"
FT   CHAIN           2..383
FT                   /note="GA-binding protein subunit beta-1"
FT                   /id="PRO_0000318945"
FT   REPEAT          5..34
FT                   /note="ANK 1"
FT   REPEAT          37..66
FT                   /note="ANK 2"
FT   REPEAT          70..99
FT                   /note="ANK 3"
FT   REPEAT          103..132
FT                   /note="ANK 4"
FT   REPEAT          136..166
FT                   /note="ANK 5"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06547"
FT   MOD_RES         69
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00420"
FT   MOD_RES         340
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00420"
FT   MOD_RES         369
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00420"
SQ   SEQUENCE   383 AA;  41321 MW;  07E7081A60016288 CRC64;
     MSLVDLGKKL LEAARAGQDD EVRILMANGA PFTTDWLGTS PLHLAAQYGH YSTTEVLLRA
     GVSRDARTKV DRTPLHMAAS EGHASIVEVL LKHGADVNAK DMLKMTALHW ATEHNHQEVV
     ELLIKYGADV HTQSKFCKTA FDISIDNGNE DLAEILQIAM QNQINTNPES PDTVTIHAAT
     PQFIIGPGGV VNLTDETGVS AVQFGNSSTS VLATLAALAE ASAPLSNSSE TPVVATEEVV
     TAESVDGAIQ QVVSSGGQQV ITIVTDGIQL GNLHSIPTSG IGQPIIVTMP DGQQVLTVPA
     TDIAEETVIS EEPPAKRQCI EIIENRVESA EIEEREALQK QLDEANREAQ KYRQQLLKKE
     QEAEAYRQKL EAMTRLQTNK EAV
 
 
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