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TAF1D_MOUSE
ID   TAF1D_MOUSE             Reviewed;         322 AA.
AC   Q9D4V4; Q149X7; Q8C7I5; Q9CZG0; Q9D5U6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 127.
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   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 MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Liver, Mammary gland, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9D4V4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D4V4-2; Sequence=VSP_020729;
CC       Name=3;
CC         IsoId=Q9D4V4-3; Sequence=VSP_020730;
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DR   EMBL; AK050165; BAC34104.1; -; mRNA.
DR   EMBL; AK012662; BAB28391.1; -; mRNA.
DR   EMBL; AK014920; BAB29621.1; -; mRNA.
DR   EMBL; AK016109; BAB30118.1; -; mRNA.
DR   EMBL; AK166329; BAE38709.1; -; mRNA.
DR   EMBL; BC110660; AAI10661.1; -; mRNA.
DR   EMBL; BC117068; AAI17069.1; -; mRNA.
DR   EMBL; BC117070; AAI17071.1; -; mRNA.
DR   CCDS; CCDS22836.1; -. [Q9D4V4-1]
DR   CCDS; CCDS52726.1; -. [Q9D4V4-2]
DR   RefSeq; NP_081537.1; NM_027261.3. [Q9D4V4-2]
DR   RefSeq; NP_083524.2; NM_029248.2. [Q9D4V4-1]
DR   RefSeq; XP_006510726.1; XM_006510663.2.
DR   RefSeq; XP_011240922.1; XM_011242620.2. [Q9D4V4-1]
DR   AlphaFoldDB; Q9D4V4; -.
DR   STRING; 10090.ENSMUSP00000034415; -.
DR   iPTMnet; Q9D4V4; -.
DR   PhosphoSitePlus; Q9D4V4; -.
DR   MaxQB; Q9D4V4; -.
DR   PaxDb; Q9D4V4; -.
DR   PeptideAtlas; Q9D4V4; -.
DR   PRIDE; Q9D4V4; -.
DR   ProteomicsDB; 254493; -. [Q9D4V4-1]
DR   ProteomicsDB; 254494; -. [Q9D4V4-2]
DR   ProteomicsDB; 254495; -. [Q9D4V4-3]
DR   Antibodypedia; 53987; 61 antibodies from 11 providers.
DR   Ensembl; ENSMUST00000034415; ENSMUSP00000034415; ENSMUSG00000031939. [Q9D4V4-1]
DR   Ensembl; ENSMUST00000164079; ENSMUSP00000129141; ENSMUSG00000031939. [Q9D4V4-2]
DR   Ensembl; ENSMUST00000213763; ENSMUSP00000150356; ENSMUSG00000031939. [Q9D4V4-3]
DR   Ensembl; ENSMUST00000214054; ENSMUSP00000150937; ENSMUSG00000031939. [Q9D4V4-3]
DR   Ensembl; ENSMUST00000216825; ENSMUSP00000149377; ENSMUSG00000031939. [Q9D4V4-3]
DR   GeneID; 75316; -.
DR   KEGG; mmu:75316; -.
DR   UCSC; uc009ofp.2; mouse. [Q9D4V4-1]
DR   UCSC; uc009ofq.2; mouse. [Q9D4V4-2]
DR   CTD; 79101; -.
DR   MGI; MGI:1922566; Taf1d.
DR   VEuPathDB; HostDB:ENSMUSG00000031939; -.
DR   eggNOG; ENOG502SQMW; Eukaryota.
DR   GeneTree; ENSGT00390000009061; -.
DR   HOGENOM; CLU_071614_1_0_1; -.
DR   InParanoid; Q9D4V4; -.
DR   OMA; CFIISTE; -.
DR   OrthoDB; 1263117at2759; -.
DR   PhylomeDB; Q9D4V4; -.
DR   TreeFam; TF335756; -.
DR   Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR   BioGRID-ORCS; 75316; 19 hits in 77 CRISPR screens.
DR   ChiTaRS; Taf1d; mouse.
DR   PRO; PR:Q9D4V4; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9D4V4; protein.
DR   Bgee; ENSMUSG00000031939; Expressed in ileal epithelium and 271 other tissues.
DR   ExpressionAtlas; Q9D4V4; baseline and differential.
DR   Genevisible; Q9D4V4; MM.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:MGI.
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   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..322
FT                   /note="TATA box-binding protein-associated factor RNA
FT                   polymerase I subunit D"
FT                   /id="PRO_0000250718"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..111
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H5J8"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H5J8"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H5J8"
FT   VAR_SEQ         286..322
FT                   /note="DSRPQPRPFAHLQSKVMKKGELEYLEVHHLCGLSQPL -> GKEHR (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020729"
FT   VAR_SEQ         286..322
FT                   /note="DSRPQPRPFAHLQSKVMKKGELEYLEVHHLCGLSQPL -> GLS (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020730"
FT   CONFLICT        8
FT                   /note="S -> F (in Ref. 1; BAB29621)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="K -> R (in Ref. 1; BAB29621)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="L -> P (in Ref. 1; BAB29621)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="K -> E (in Ref. 1; BAB30118)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   322 AA;  36977 MW;  BDA75165CEC29301 CRC64;
     MAQSEVNSVC VASDRAGDTG DQSDDSSDGS LFKTQCAPSP IQKQRHPTVK RVTLPASVET
     DSSSDSSIEP RPLTLKAIFE RFKKKKRKKR KKRKYEPKLR PRGRPRGKPS GTRITRRSQI
     DAKQIKDKGA VFPFLESESG RKPLPWKKIL TYEQAVARGF FHHIEKLKYE HHLKECLKQM
     HAGEDLEKED LDSRRHKYMD DDGSLSPIEE PLTEDEATNP QAECDIKLVE DSCFIISSEF
     SRKRNLEQEK IKKESTFSKK AKDATHREKG HRRTLKGNEH VTIEEDSRPQ PRPFAHLQSK
     VMKKGELEYL EVHHLCGLSQ PL
 
 
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