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P97358

- TAF1B_MOUSE

UniProt

P97358 - TAF1B_MOUSE

Protein

TATA box-binding protein-associated factor RNA polymerase I subunit B

Gene

Taf1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during trancription initiation such as preinitiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi13 – 131ZincBy similarity
    Metal bindingi16 – 161ZincBy similarity
    Metal bindingi31 – 311ZincBy similarity
    Metal bindingi34 – 341ZincBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri5 – 3935RRN7-typeAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. RNA polymerase I CORE element sequence-specific DNA binding Source: UniProtKB
    4. RNA polymerase I CORE element sequence-specific DNA binding transcription factor recruiting transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. RNA polymerase I transcriptional preinitiation complex assembly at the promoter for the nuclear large rRNA transcript Source: UniProtKB
    2. transcription from RNA polymerase I promoter Source: MGI

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_224328. SIRT1 negatively regulates rRNA Expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TATA box-binding protein-associated factor RNA polymerase I subunit B
    Alternative name(s):
    RNA polymerase I-specific TBP-associated factor 68 kDa
    Short name:
    TAFI68
    TATA box-binding protein-associated factor 1B
    Short name:
    TBP-associated factor 1B
    Transcription initiation factor SL1/TIF-IB subunit B
    Gene namesi
    Name:Taf1b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:109577. Taf1b.

    Subcellular locationi

    Nucleusnucleolus By similarity

    GO - Cellular componenti

    1. RNA polymerase I core factor complex Source: Ensembl
    2. RNA polymerase I transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 586586TATA box-binding protein-associated factor RNA polymerase I subunit BPRO_0000304406Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei438 – 4381N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP97358.

    PTM databases

    PhosphoSiteiP97358.

    Expressioni

    Gene expression databases

    BgeeiP97358.
    GenevestigatoriP97358.

    Interactioni

    Subunit structurei

    Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the complex interacts directly with TBP, TAF1A and TAF1C. Interaction of the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the transcription factor IID (TFIID) subunits. Interacts with TBP and RRN3. Interacts with FLNA (via N-terminus).3 Publications

    Protein-protein interaction databases

    BioGridi203957. 8 interactions.
    IntActiP97358. 1 interaction.
    MINTiMINT-249228.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 6829B-readerBy similarityAdd
    BLAST
    Regioni69 – 735B-linkerBy similarity
    Regioni74 – 259186N-terminal cyclin foldBy similarityAdd
    BLAST
    Regioni260 – 370111C-terminal cyclin foldBy similarityAdd
    BLAST

    Domaini

    Although it shares weak sequence similarity with GTF2B/TFIIB, displays a similar subdomain organization as GTF2B/TFIIB, with a N-terminal zinc finger, a connecting region (composed of B-reader and B-linker regions), followed by 2 cyclin folds. The RRN7-type zinc finger plays an essential postrecruitment role in Pol I transcription at a step preceding synthesis of the first 40 nucleotides By similarity.By similarity

    Sequence similaritiesi

    Belongs to the RRN7/TAF1B family.Curated
    Contains 1 RRN7-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri5 – 3935RRN7-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG72502.
    GeneTreeiENSGT00440000033827.
    HOGENOMiHOG000124571.
    HOVERGENiHBG053463.
    InParanoidiP97358.
    KOiK15213.
    OMAiCFHGHSL.
    OrthoDBiEOG7V1FS7.
    TreeFamiTF324353.

    Family and domain databases

    InterProiIPR021752. TF_Rrn7.
    [Graphical view]
    PfamiPF11781. RRN7. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P97358-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDVEEVKAFR DRCSQCAAVS WGLTDEGKYY CTSCHNVTDR SEEVVSAADI    50
    PNTKINSINR GLRQRSKHEK GWDWYVCEGF QCILYHQAKA LETLGVSPEL 100
    KNEVLHNFWK RYLQKSKQAY CKNPVRTSGR KAKVLEDSVQ SSDLGSDLEL 150
    LSDTTCPLES EAEFQSDPQI PKPFPVTKGS PKSASVCSGS VDGVEYSERK 200
    EKGLVKMTVP RTLALCSLSL LWQRETITVS DLLRFVEEDH IPYINAFKLF 250
    PEEMKVYGRD KGIFAIESWP DYEDIYKNMI ELAIFLDLPR FPDITEDCYL 300
    HPNTLCMKYL LEVNLPDEMH TLTCQVVKLT GIGEVDFLTF DPIAKTKRTV 350
    KYDVQAMAVI VVVLKLLFLL DDKLEWSYSD LAEAYNEQHR EDTPQFDFRK 400
    WYQVMKKTFD EKRRKWEEAR ARYAWKTKRP LYRSHIDKSV AYKRRKMVEN 450
    LQKQFSALVG SSPVVEKQAP SSFQFNWTEE GTDSPCFHGH SLQGLLIMKG 500
    QSMITKNSLY WLSTQKFCKS YCKHVTTYEE SNFSLSYQFI LNIFSFLLRI 550
    KTSALHEEVS LLEKKLFEKK YNESKKSSGS KKGRRH 586
    Length:586
    Mass (Da):67,954
    Last modified:July 27, 2011 - v2
    Checksum:i85E0EBB8C742EE71
    GO
    Isoform 2 (identifier: P97358-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.
         101-101: K → M

    Note: No experimental confirmation available.

    Show »
    Length:486
    Mass (Da):56,601
    Checksum:i3306E944624DC8E1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21D → N in CAA71092. (PubMed:9050847)Curated
    Sequence conflicti2 – 21D → N in BAE38271. (PubMed:16141072)Curated
    Sequence conflicti2 – 21D → N in BAE41709. (PubMed:16141072)Curated
    Sequence conflicti2 – 21D → N in AAH57167. (PubMed:15489334)Curated
    Sequence conflicti2 – 21D → N in AAI25028. (PubMed:15489334)Curated
    Sequence conflicti2 – 21D → N in AAI25029. (PubMed:15489334)Curated
    Sequence conflicti178 – 1781K → T in AAI25029. (PubMed:15489334)Curated
    Sequence conflicti287 – 2871D → G in BAE20906. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_028024Add
    BLAST
    Alternative sequencei101 – 1011K → M in isoform 2. 1 PublicationVSP_028025

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09973 Genomic DNA. Translation: CAA71092.1.
    AK131963 mRNA. Translation: BAE20906.1.
    AK165580 mRNA. Translation: BAE38271.1.
    AK170313 mRNA. Translation: BAE41709.1.
    AC125067 Genomic DNA. No translation available.
    AC132587 Genomic DNA. No translation available.
    BC057167 mRNA. Translation: AAH57167.1.
    BC069907 mRNA. Translation: AAH69907.1.
    BC094035 mRNA. Translation: AAH94035.1.
    BC125027 mRNA. Translation: AAI25028.1.
    BC125028 mRNA. Translation: AAI25029.1.
    CCDSiCCDS36419.1. [P97358-1]
    RefSeqiNP_065639.2. NM_020614.2. [P97358-1]
    UniGeneiMm.39082.
    Mm.421402.

    Genome annotation databases

    EnsembliENSMUST00000075954; ENSMUSP00000075339; ENSMUSG00000059669. [P97358-1]
    GeneIDi21340.
    KEGGimmu:21340.
    UCSCiuc007nej.2. mouse. [P97358-1]
    uc007nel.2. mouse. [P97358-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09973 Genomic DNA. Translation: CAA71092.1 .
    AK131963 mRNA. Translation: BAE20906.1 .
    AK165580 mRNA. Translation: BAE38271.1 .
    AK170313 mRNA. Translation: BAE41709.1 .
    AC125067 Genomic DNA. No translation available.
    AC132587 Genomic DNA. No translation available.
    BC057167 mRNA. Translation: AAH57167.1 .
    BC069907 mRNA. Translation: AAH69907.1 .
    BC094035 mRNA. Translation: AAH94035.1 .
    BC125027 mRNA. Translation: AAI25028.1 .
    BC125028 mRNA. Translation: AAI25029.1 .
    CCDSi CCDS36419.1. [P97358-1 ]
    RefSeqi NP_065639.2. NM_020614.2. [P97358-1 ]
    UniGenei Mm.39082.
    Mm.421402.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203957. 8 interactions.
    IntActi P97358. 1 interaction.
    MINTi MINT-249228.

    PTM databases

    PhosphoSitei P97358.

    Proteomic databases

    PRIDEi P97358.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075954 ; ENSMUSP00000075339 ; ENSMUSG00000059669 . [P97358-1 ]
    GeneIDi 21340.
    KEGGi mmu:21340.
    UCSCi uc007nej.2. mouse. [P97358-1 ]
    uc007nel.2. mouse. [P97358-2 ]

    Organism-specific databases

    CTDi 9014.
    MGIi MGI:109577. Taf1b.

    Phylogenomic databases

    eggNOGi NOG72502.
    GeneTreei ENSGT00440000033827.
    HOGENOMi HOG000124571.
    HOVERGENi HBG053463.
    InParanoidi P97358.
    KOi K15213.
    OMAi CFHGHSL.
    OrthoDBi EOG7V1FS7.
    TreeFami TF324353.

    Enzyme and pathway databases

    Reactomei REACT_224328. SIRT1 negatively regulates rRNA Expression.

    Miscellaneous databases

    NextBioi 300516.
    PROi P97358.
    SOURCEi Search...

    Gene expression databases

    Bgeei P97358.
    Genevestigatori P97358.

    Family and domain databases

    InterProi IPR021752. TF_Rrn7.
    [Graphical view ]
    Pfami PF11781. RRN7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of murine RNA polymerase I-specific TAF factors: conserved interactions between the subunits of the species-specific transcription initiation factor TIF-IB/SL1."
      Heix J., Zomerdijk J.C.B.M., Ravanpay A., Tjian R., Grummt I.
      Proc. Natl. Acad. Sci. U.S.A. 94:1733-1738(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH TBP; TAF1A AND TAF1C.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C3H, C57BL/6J and NOD.
      Tissue: Brain, Dendritic cell and Embryonic stem cell.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. "Rrn3 phosphorylation is a regulatory checkpoint for ribosome biogenesis."
      Cavanaugh A.H., Hirschler-Laszkiewicz I., Hu Q., Dundr M., Smink T., Misteli T., Rothblum L.I.
      J. Biol. Chem. 277:27423-27432(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RRN3.
    6. "Identification of novel nuclear protein interactions with the N-terminal part of filamin A."
      Qiu H., Nomiyama R., Moriguchi K., Fukada T., Sugimoto K.
      Biosci. Biotechnol. Biochem. 75:145-147(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLNA.

    Entry informationi

    Entry nameiTAF1B_MOUSE
    AccessioniPrimary (citable) accession number: P97358
    Secondary accession number(s): E9QJY7
    , Q08AT7, Q3V292, Q6NSS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3