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Q53T94

- TAF1B_HUMAN

UniProt

Q53T94 - TAF1B_HUMAN

Protein

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

Gene

TAF1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      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 RRN3.6 Publications

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri4 – 3936RRN7-typeAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    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
    5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    6. TBP-class protein binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. RNA polymerase I transcriptional preinitiation complex assembly at the promoter for the nuclear large rRNA transcript Source: UniProtKB
    3. termination of RNA polymerase I transcription Source: Reactome
    4. transcription, DNA-templated Source: UniProtKB
    5. transcription elongation from RNA polymerase I promoter Source: Reactome
    6. transcription from RNA polymerase I promoter Source: Reactome
    7. transcription initiation from RNA polymerase I promoter Source: Reactome

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_953. RNA Polymerase I Transcription Initiation.

    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 63 kDa
    Short name:
    TAFI63
    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11533. TAF1B.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. RNA polymerase I core factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131C → A: Abolishes Pol I transcription but not recruitment of SL1/TIF-IB complex to rDNA promoters. 1 Publication
    Mutagenesisi31 – 311C → A: Abolishes Pol I transcription but not recruitment of SL1/TIF-IB complex to rDNA promoters. 1 Publication
    Mutagenesisi34 – 341C → A: Abolishes Pol I transcription but not recruitment of SL1/TIF-IB complex to rDNA promoters. 1 Publication

    Organism-specific databases

    PharmGKBiPA36308.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 588588TATA box-binding protein-associated factor RNA polymerase I subunit BPRO_0000261392Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei440 – 4401N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ53T94.
    PaxDbiQ53T94.
    PRIDEiQ53T94.

    PTM databases

    PhosphoSiteiQ53T94.

    Expressioni

    Gene expression databases

    ArrayExpressiQ53T94.
    BgeeiQ53T94.
    CleanExiHS_TAF1B.
    GenevestigatoriQ53T94.

    Interactioni

    Subunit structurei

    Interacts with FLNA (via N-terminus) By similarity. 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.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SETQ011053EBI-1560239,EBI-1053182
    TBPP202263EBI-1560239,EBI-355371

    Protein-protein interaction databases

    BioGridi114483. 33 interactions.
    IntActiQ53T94. 7 interactions.
    MINTiMINT-4543781.
    STRINGi9606.ENSP00000263663.

    Structurei

    3D structure databases

    ProteinModelPortaliQ53T94.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 6829B-readerAdd
    BLAST
    Regioni69 – 735B-linker
    Regioni74 – 261188N-terminal cyclin foldAdd
    BLAST
    Regioni262 – 372111C-terminal cyclin foldAdd
    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 (PubMed:21921198 and PubMed:21921199).

    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 fingeri4 – 3936RRN7-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG72502.
    HOGENOMiHOG000124571.
    HOVERGENiHBG053463.
    InParanoidiQ53T94.
    KOiK15213.
    OMAiCFHGHSL.
    OrthoDBiEOG7V1FS7.
    PhylomeDBiQ53T94.
    TreeFamiTF324353.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q53T94-1) [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

    MDLEEAEEFK ERCTQCAAVS WGLTDEGKYY CTSCHNVTER YQEVTNTDLI    50
    PNTQIKALNR GLKKKNNTEK GWDWYVCEGF QYILYQQAEA LKNLGVGPEL 100
    KNDVLHNFWK RYLQKSKQAY CKNPVYTTGR KPTVLEDNLS HSDWASEPEL 150
    LSDVSCPPFL ESGAESQSDI HTRKPFPVSK ASQSETSVCS GSLDGVEYSQ 200
    RKEKGIVKMT MPQTLAFCYL SLLWQREAIT LSDLLRFVEE DHIPYINAFQ 250
    HFPEQMKLYG RDRGIFGIES WPDYEDIYKK TVEVGTFLDL PRFPDITEDC 300
    YLHPNILCMK YLMEVNLPDE MHSLTCHVVK MTGMGEVDFL TFDPIAKMAK 350
    TVKYDVQAVA IIVVVLKLLF LLDDSFEWSL SNLAEKHNEK NKKDKPWFDF 400
    RKWYQIMKKA FDEKKQKWEE ARAKYLWKSE KPLYYSFVDK PVAYKKREMV 450
    VNLQKQFSTL VESTATAGKK SPSSFQFNWT EEDTDRTCFH GHSLQGVLKE 500
    KGQSLLTKNS LYWLSTQKFC RCYCTHVTTY EESNYSLSYQ FILNLFSFLL 550
    RIKTSLLHEE VSLVEKKLFE KKYSVKRKKS RSKKVRRH 588
    Length:588
    Mass (Da):68,832
    Last modified:May 24, 2005 - v1
    Checksum:iCE45DE622E28FD6E
    GO
    Isoform 2 (identifier: Q53T94-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         523-588: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:522
    Mass (Da):60,790
    Checksum:iA0277EAF25B4F50F
    GO
    Isoform 3 (identifier: Q53T94-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-255: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:333
    Mass (Da):39,533
    Checksum:i6E716737AB58736B
    GO

    Sequence cautioni

    The sequence AAA62863.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → L in AAA62863. (PubMed:7801123)Curated
    Sequence conflicti372 – 3721L → M in AAA62863. (PubMed:7801123)Curated
    Sequence conflicti522 – 5221C → W in AAA62863. (PubMed:7801123)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61A → S.2 Publications
    Corresponds to variant rs2303914 [ dbSNP | Ensembl ].
    VAR_029378
    Natural varianti282 – 2821V → I.3 Publications
    Corresponds to variant rs396190 [ dbSNP | Ensembl ].
    VAR_029379
    Natural varianti292 – 2921R → H.
    Corresponds to variant rs16867223 [ dbSNP | Ensembl ].
    VAR_057260
    Natural varianti351 – 3511T → A.3 Publications
    Corresponds to variant rs1054565 [ dbSNP | Ensembl ].
    VAR_029380
    Natural varianti462 – 4621E → D.3 Publications
    Corresponds to variant rs1820965 [ dbSNP | Ensembl ].
    VAR_029381
    Natural varianti487 – 4871T → M.
    Corresponds to variant rs16867245 [ dbSNP | Ensembl ].
    VAR_029382

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 255255Missing in isoform 3. 1 PublicationVSP_042954Add
    BLAST
    Alternative sequencei523 – 58866Missing in isoform 2. CuratedVSP_021677Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39061 mRNA. Translation: AAA62863.1. Different initiation.
    AK295402 mRNA. Translation: BAG58354.1.
    AC010969 Genomic DNA. Translation: AAX93272.1.
    BC018137 mRNA. Translation: AAH18137.1.
    CCDSiCCDS33143.1. [Q53T94-1]
    PIRiI61581.
    RefSeqiNP_005671.2. NM_005680.2.
    UniGeneiHs.584833.

    Genome annotation databases

    EnsembliENST00000263663; ENSP00000263663; ENSG00000115750. [Q53T94-1]
    GeneIDi9014.
    KEGGihsa:9014.
    UCSCiuc002qzy.4. human. [Q53T94-1]

    Polymorphism databases

    DMDMi74726856.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39061 mRNA. Translation: AAA62863.1 . Different initiation.
    AK295402 mRNA. Translation: BAG58354.1 .
    AC010969 Genomic DNA. Translation: AAX93272.1 .
    BC018137 mRNA. Translation: AAH18137.1 .
    CCDSi CCDS33143.1. [Q53T94-1 ]
    PIRi I61581.
    RefSeqi NP_005671.2. NM_005680.2.
    UniGenei Hs.584833.

    3D structure databases

    ProteinModelPortali Q53T94.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114483. 33 interactions.
    IntActi Q53T94. 7 interactions.
    MINTi MINT-4543781.
    STRINGi 9606.ENSP00000263663.

    PTM databases

    PhosphoSitei Q53T94.

    Polymorphism databases

    DMDMi 74726856.

    Proteomic databases

    MaxQBi Q53T94.
    PaxDbi Q53T94.
    PRIDEi Q53T94.

    Protocols and materials databases

    DNASUi 9014.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263663 ; ENSP00000263663 ; ENSG00000115750 . [Q53T94-1 ]
    GeneIDi 9014.
    KEGGi hsa:9014.
    UCSCi uc002qzy.4. human. [Q53T94-1 ]

    Organism-specific databases

    CTDi 9014.
    GeneCardsi GC02P009983.
    H-InvDB HIX0001812.
    HGNCi HGNC:11533. TAF1B.
    MIMi 604904. gene.
    neXtProti NX_Q53T94.
    PharmGKBi PA36308.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72502.
    HOGENOMi HOG000124571.
    HOVERGENi HBG053463.
    InParanoidi Q53T94.
    KOi K15213.
    OMAi CFHGHSL.
    OrthoDBi EOG7V1FS7.
    PhylomeDBi Q53T94.
    TreeFami TF324353.

    Enzyme and pathway databases

    Reactomei REACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_953. RNA Polymerase I Transcription Initiation.

    Miscellaneous databases

    GeneWikii TAF1B.
    GenomeRNAii 9014.
    NextBioi 33771.
    PROi Q53T94.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q53T94.
    Bgeei Q53T94.
    CleanExi HS_TAF1B.
    Genevestigatori Q53T94.

    Family and domain databases

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

    Publicationsi

    1. "Reconstitution of transcription factor SL1: exclusive binding of TBP by SL1 or TFIID subunits."
      Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R.
      Science 266:1966-1972(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-20; 42-56; 93-110; 123-135; 264-276; 281-289; 311-321; 331-340; 396-407; 429-444; 448-466 AND 471-480, FUNCTION, INTERACTION WITH TBP; TAF1A AND TAF1C, VARIANTS SER-6; ILE-282; ALA-351 AND ASP-462.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANTS ILE-282; ALA-351 AND ASP-462.
      Tissue: Corpus callosum.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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], VARIANTS SER-6; ILE-282; ALA-351 AND ASP-462.
      Tissue: Colon.
    5. "Assembly of transcriptionally active RNA polymerase I initiation factor SL1 from recombinant subunits."
      Zomerdijk J.C., Beckmann H., Comai L., Tjian R.
      Science 266:2015-2018(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Coactivator and promoter-selective properties of RNA polymerase I TAFs."
      Beckmann H., Chen J.L., O'Brien T., Tjian R.
      Science 270:1506-1509(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    7. "Genomic localization of the human genes TAF1A, TAF1B and TAF1C, encoding TAF(I)48, TAF(I)63 and TAF(I)110 subunits of class I general transcription initiation factor SL1."
      Di Pietro C., Rapisarda A., Amico V., Bonaiuto C., Viola A., Scalia M., Motta S., Amato A., Engel H., Messina A., Sichel G., Grzeschik K., Purrello M.
      Cytogenet. Cell Genet. 89:133-136(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    8. "hRRN3 is essential in the SL1-mediated recruitment of RNA polymerase I to rRNA gene promoters."
      Miller G., Panov K.I., Friedrich J.K., Trinkle-Mulcahy L., Lamond A.I., Zomerdijk J.C.B.M.
      EMBO J. 20:1373-1382(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RRN3.
    9. "TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex formation and stabilizes upstream binding factor at the rDNA promoter."
      Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.
      J. Biol. Chem. 280:29551-29558(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE SL1/TIF-IB COMPLEX.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Yeast Rrn7 and human TAF1B are TFIIB-related RNA polymerase I general transcription factors."
      Knutson B.A., Hahn S.
      Science 333:1637-1640(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "TAF1B is a TFIIB-like component of the basal transcription machinery for RNA polymerase I."
      Naidu S., Friedrich J.K., Russell J., Zomerdijk J.C.
      Science 333:1640-1642(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-13; CYS-31 AND CYS-34.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTAF1B_HUMAN
    AccessioniPrimary (citable) accession number: Q53T94
    Secondary accession number(s): B4DI42
    , F8WD72, Q15574, Q8WVC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

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