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Protein

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

Gene

TAF1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. RNA polymerase I CORE element sequence-specific DNA binding Source: UniProtKB
  3. RNA polymerase I CORE element sequence-specific DNA binding transcription factor recruiting transcription factor activity Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. TBP-class protein binding Source: UniProtKB

GO - Biological processi

  1. chromatin silencing at rDNA Source: Reactome
  2. gene expression Source: Reactome
  3. negative regulation of gene expression, epigenetic Source: Reactome
  4. regulation of gene expression, epigenetic Source: Reactome
  5. RNA polymerase I transcriptional preinitiation complex assembly at the promoter for the nuclear large rRNA transcript Source: UniProtKB
  6. termination of RNA polymerase I transcription Source: Reactome
  7. transcription, DNA-templated Source: UniProtKB
  8. transcription elongation from RNA polymerase I promoter Source: Reactome
  9. transcription from RNA polymerase I promoter Source: Reactome
  10. transcription initiation from RNA polymerase I promoter Source: Reactome
Complete GO annotation...

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_2204. RNA Polymerase I Chain Elongation.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_264541. SIRT1 negatively regulates rRNA Expression.
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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11533. TAF1B.

Subcellular locationi

GO - Cellular componenti

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

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.

Polymorphism and mutation databases

BioMutaiTAF1B.
DMDMi74726856.

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

BgeeiQ53T94.
CleanExiHS_TAF1B.
ExpressionAtlasiQ53T94. baseline and differential.
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. 35 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.
GeneTreeiENSGT00440000033827.
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. AlignAdd to basket

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

        10         20         30         40         50
MDLEEAEEFK ERCTQCAAVS WGLTDEGKYY CTSCHNVTER YQEVTNTDLI
60 70 80 90 100
PNTQIKALNR GLKKKNNTEK GWDWYVCEGF QYILYQQAEA LKNLGVGPEL
110 120 130 140 150
KNDVLHNFWK RYLQKSKQAY CKNPVYTTGR KPTVLEDNLS HSDWASEPEL
160 170 180 190 200
LSDVSCPPFL ESGAESQSDI HTRKPFPVSK ASQSETSVCS GSLDGVEYSQ
210 220 230 240 250
RKEKGIVKMT MPQTLAFCYL SLLWQREAIT LSDLLRFVEE DHIPYINAFQ
260 270 280 290 300
HFPEQMKLYG RDRGIFGIES WPDYEDIYKK TVEVGTFLDL PRFPDITEDC
310 320 330 340 350
YLHPNILCMK YLMEVNLPDE MHSLTCHVVK MTGMGEVDFL TFDPIAKMAK
360 370 380 390 400
TVKYDVQAVA IIVVVLKLLF LLDDSFEWSL SNLAEKHNEK NKKDKPWFDF
410 420 430 440 450
RKWYQIMKKA FDEKKQKWEE ARAKYLWKSE KPLYYSFVDK PVAYKKREMV
460 470 480 490 500
VNLQKQFSTL VESTATAGKK SPSSFQFNWT EEDTDRTCFH GHSLQGVLKE
510 520 530 540 550
KGQSLLTKNS LYWLSTQKFC RCYCTHVTTY EESNYSLSYQ FILNLFSFLL
560 570 580
RIKTSLLHEE VSLVEKKLFE KKYSVKRKKS RSKKVRRH
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.Curated

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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiTAF1B.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ53T94.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114483. 35 interactions.
IntActiQ53T94. 7 interactions.
MINTiMINT-4543781.
STRINGi9606.ENSP00000263663.

PTM databases

PhosphoSiteiQ53T94.

Polymorphism and mutation databases

BioMutaiTAF1B.
DMDMi74726856.

Proteomic databases

MaxQBiQ53T94.
PaxDbiQ53T94.
PRIDEiQ53T94.

Protocols and materials databases

DNASUi9014.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9014.
GeneCardsiGC02P009983.
H-InvDBHIX0001812.
HGNCiHGNC:11533. TAF1B.
MIMi604904. gene.
neXtProtiNX_Q53T94.
PharmGKBiPA36308.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG72502.
GeneTreeiENSGT00440000033827.
HOGENOMiHOG000124571.
HOVERGENiHBG053463.
InParanoidiQ53T94.
KOiK15213.
OMAiCFHGHSL.
OrthoDBiEOG7V1FS7.
PhylomeDBiQ53T94.
TreeFamiTF324353.

Enzyme and pathway databases

ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_264541. SIRT1 negatively regulates rRNA Expression.
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

GeneWikiiTAF1B.
GenomeRNAii9014.
NextBioi33771.
PROiQ53T94.
SOURCEiSearch...

Gene expression databases

BgeeiQ53T94.
CleanExiHS_TAF1B.
ExpressionAtlasiQ53T94. baseline and differential.
GenevestigatoriQ53T94.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 95 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

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.