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TAF1D_RAT
ID   TAF1D_RAT               Reviewed;         285 AA.
AC   Q5M948;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit D;
DE   AltName: Full=TATA box-binding protein-associated factor 1D;
DE            Short=TBP-associated factor 1D;
DE   AltName: Full=Transcription initiation factor SL1/TIF-IB subunit D;
GN   Name=Taf1d; Synonyms=Josd3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the transcription factor SL1/TIF-IB complex,
CC       which is involved in the assembly of the PIC (preinitiation complex)
CC       during RNA polymerase I-dependent transcription. The rate of PIC
CC       formation probably is primarily dependent on the rate of association of
CC       SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in
CC       stabilization of nucleolar transcription factor 1/UBTF on rDNA.
CC       Formation of SL1/TIF-IB excludes the association of TBP with TFIID
CC       subunits (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the transcription factor SL1/TIF-IB complex,
CC       composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. Interacts
CC       with UBTF (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; BC087647; AAH87647.1; -; mRNA.
DR   RefSeq; NP_001014229.1; NM_001014207.1.
DR   AlphaFoldDB; Q5M948; -.
DR   STRING; 10116.ENSRNOP00000014605; -.
DR   PaxDb; Q5M948; -.
DR   PRIDE; Q5M948; -.
DR   GeneID; 363017; -.
DR   KEGG; rno:363017; -.
DR   UCSC; RGD:1309627; rat.
DR   CTD; 79101; -.
DR   RGD; 1309627; Taf1d.
DR   eggNOG; ENOG502SQMW; Eukaryota.
DR   InParanoid; Q5M948; -.
DR   OrthoDB; 1263117at2759; -.
DR   PhylomeDB; Q5M948; -.
DR   Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR   PRO; PR:Q5M948; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR027976; TAF1D.
DR   PANTHER; PTHR14562; PTHR14562; 1.
DR   Pfam; PF15333; TAF1D; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..285
FT                   /note="TATA box-binding protein-associated factor RNA
FT                   polymerase I subunit D"
FT                   /id="PRO_0000250720"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..108
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H5J8"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H5J8"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H5J8"
SQ   SEQUENCE   285 AA;  32616 MW;  F2C644629A4889FB CRC64;
     MAQSEVDSVD CVTSDRDGDI GNQSDDSSNS SLFKTQCVPS PTRKQRIPTV KCVPSLASVE
     TDSSSDSSLE PRPLTLKAIF ERFKKKKRKK RKKRKYKPKL RRQGRPSGTR NIRRSQIDAK
     QIKDKGAVFP FLESESGRKT LPWKKILTYE QAVARGFFHH IEKLKYEHHL KECLSQMHAG
     EDLEKEDFDS RRHKYMDDDG PLSPIEEPST EDEATDPQSE CDIKLVEDSC FIISTEFPRK
     RNLEQGKIKK ESAFSKKSKA KDATQRGNRR SWKGGEHACL HSEVS
 
 
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