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TAF1B_BOVIN
ID   TAF1B_BOVIN             Reviewed;         590 AA.
AC   Q1JQD6; E1BGL1;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit B;
DE   AltName: Full=RNA polymerase I-specific TBP-associated factor 63 kDa;
DE            Short=TAFI63;
DE   AltName: Full=TATA box-binding protein-associated factor 1B;
DE            Short=TBP-associated factor 1B;
DE   AltName: Full=Transcription initiation factor SL1/TIF-IB subunit B;
GN   Name=TAF1B;
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 GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of RNA polymerase I core factor complex that acts
CC       as a GTF2B/TFIIB-like factor and plays a key role in multiple steps
CC       during transcription initiation such as pre-initiation complex (PIC)
CC       assembly and postpolymerase recruitment events in polymerase I (Pol I)
CC       transcription. Binds rDNA promoters and plays a role in Pol I
CC       recruitment as a component of the SL1/TIF-IB complex and, possibly,
CC       directly through its interaction with RRN3 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FLNA (via N-terminus) (By similarity).
CC       Component of the transcription factor SL1/TIF-IB complex, composed of
CC       TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the complex
CC       interacts directly with TBP, TAF1A and TAF1C. Interaction of the
CC       SL1/TIF-IB subunits with TBP excludes interaction of TBP with the
CC       transcription factor IID (TFIID) subunits. Interacts with TBP and RRN3
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- DOMAIN: Although it shares weak sequence similarity with GTF2B/TFIIB,
CC       displays a similar subdomain organization as GTF2B/TFIIB, with a N-
CC       terminal zinc finger, a connecting region (composed of B-reader and B-
CC       linker regions), followed by 2 cyclin folds. The RRN7-type zinc finger
CC       plays an essential postrecruitment role in Pol I transcription at a
CC       step preceding synthesis of the first 40 nucleotides (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RRN7/TAF1B family. {ECO:0000305}.
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DR   EMBL; DAAA02031936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02031937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03016422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03016423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03016426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03034356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03034357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC116032; AAI16033.1; -; mRNA.
DR   RefSeq; NP_001068971.1; NM_001075503.1.
DR   AlphaFoldDB; Q1JQD6; -.
DR   STRING; 9913.ENSBTAP00000041230; -.
DR   PaxDb; Q1JQD6; -.
DR   PRIDE; Q1JQD6; -.
DR   Ensembl; ENSBTAT00000043676; ENSBTAP00000041230; ENSBTAG00000007543.
DR   GeneID; 511236; -.
DR   KEGG; bta:511236; -.
DR   CTD; 9014; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007543; -.
DR   VGNC; VGNC:35570; TAF1B.
DR   eggNOG; ENOG502QVGU; Eukaryota.
DR   GeneTree; ENSGT00440000033827; -.
DR   HOGENOM; CLU_032815_0_0_1; -.
DR   InParanoid; Q1JQD6; -.
DR   OMA; PRSFVWL; -.
DR   OrthoDB; 329399at2759; -.
DR   TreeFam; TF324353; -.
DR   Reactome; R-BTA-5250924; B-WICH complex positively regulates rRNA expression.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000007543; Expressed in oocyte and 104 other tissues.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0070860; C:RNA polymerase I core factor complex; IBA:GO_Central.
DR   GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; ISS:UniProtKB.
DR   InterPro; IPR033599; TAF1B/Rrn7.
DR   InterPro; IPR021752; TF_Rrn7_Zf.
DR   PANTHER; PTHR31576; PTHR31576; 1.
DR   Pfam; PF11781; zf-RRN7; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..590
FT                   /note="TATA box-binding protein-associated factor RNA
FT                   polymerase I subunit B"
FT                   /id="PRO_0000416868"
FT   ZN_FING         4..39
FT                   /note="RRN7-type"
FT   REGION          40..68
FT                   /note="B-reader"
FT                   /evidence="ECO:0000250"
FT   REGION          69..73
FT                   /note="B-linker"
FT                   /evidence="ECO:0000250"
FT   REGION          74..262
FT                   /note="N-terminal cyclin fold"
FT                   /evidence="ECO:0000250"
FT   REGION          263..373
FT                   /note="C-terminal cyclin fold"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53T94"
SQ   SEQUENCE   590 AA;  69126 MW;  91572AE2A36EC5B8 CRC64;
     MDLEEAREFR ERCSQCAAVS WGLTDEGKYY CTSCHNVTER SREVIDTGAI PNTKIQAINR
     GLKRKRKLEK GWDWYVCEGF QHILYQQAEA LQSLGVGPEL KNEVLHNFWK RYLQKSKQAY
     CKNPVYTSRR KTTVLEDNLS HSDWESEPEL LSDMSCLSFA ESGAESQPDV RTPKPFPIIK
     ASHSETTSVC SGSLDGVEYS LRKEKGVMKM SVPRTLAFCY LSLLWQRETI TLSDLLRFVE
     EEHIPYIHAF QHFPEEMKLY GRDKGIFAIE SWPNYEVIFK KIIEVATFLD LPRFPDITEN
     CYLHPNILCM KYLMEVNLPD EMHNVTCLVV KSTGIGEVDF LRFDPIAKKA KTVKYDVQAV
     AVIVVALKLL FLLDDNLEWS LSNIAKKYNE KNKEDKPWFD FRKWYQVMKK AIDEKKQKWE
     EARAKFLWKG EKPLYYSAID RPVVYKRREM VVSLQKQFST LVDSAPNVEK KKPSSFQFNW
     TEEDSERPCF HGHSLQGVLQ QKGQSLTTKN SLYWLSTQKF CKSHCKHVTT YEESNFSLSY
     QFILNLFSFL LRIKTSFLHE EVSLIEKRLF KAKYNKTNKK SSRSRKTRKY
 
 
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