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Q53T94 (TAF1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TAF1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.6 Ref.9 Ref.11 Ref.12

Subunit structure

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. Ref.1 Ref.8

Subcellular location

Nucleusnucleolus.

Domain

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 (Ref.11 and Ref.12).

Sequence similarities

Belongs to the RRN7/TAF1B family.

Contains 1 RRN7-type zinc finger.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA polymerase I transcriptional preinitiation complex assembly at the promoter for the nuclear large rRNA transcript

Inferred from direct assay Ref.12. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

termination of RNA polymerase I transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentRNA polymerase I core factor complex

Inferred from direct assay Ref.11Ref.12. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionRNA polymerase I CORE element sequence-specific DNA binding

Inferred from direct assay Ref.11Ref.12. Source: UniProtKB

RNA polymerase I CORE element sequence-specific DNA binding transcription factor recruiting transcription factor activity

Inferred from direct assay Ref.11Ref.12. Source: UniProtKB

TBP-class protein binding

Traceable author statement Ref.12. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q53T94-1)

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.
Isoform 2 (identifier: Q53T94-2)

The sequence of this isoform differs from the canonical sequence as follows:
     523-588: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q53T94-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-255: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588TATA box-binding protein-associated factor RNA polymerase I subunit B
PRO_0000261392

Regions

Zinc finger4 – 3936RRN7-type
Region40 – 6829B-reader
Region69 – 735B-linker
Region74 – 261188N-terminal cyclin fold
Region262 – 372111C-terminal cyclin fold

Sites

Metal binding131Zinc Probable
Metal binding161Zinc Probable
Metal binding311Zinc Probable
Metal binding341Zinc Probable

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13
Modified residue4401N6-acetyllysine Ref.10

Natural variations

Alternative sequence1 – 255255Missing in isoform 3.
VSP_042954
Alternative sequence523 – 58866Missing in isoform 2.
VSP_021677
Natural variant61A → S. Ref.1 Ref.4
Corresponds to variant rs2303914 [ dbSNP | Ensembl ].
VAR_029378
Natural variant2821V → I. Ref.1 Ref.2 Ref.4
Corresponds to variant rs396190 [ dbSNP | Ensembl ].
VAR_029379
Natural variant2921R → H.
Corresponds to variant rs16867223 [ dbSNP | Ensembl ].
VAR_057260
Natural variant3511T → A. Ref.1 Ref.2 Ref.4
Corresponds to variant rs1054565 [ dbSNP | Ensembl ].
VAR_029380
Natural variant4621E → D. Ref.1 Ref.2 Ref.4
Corresponds to variant rs1820965 [ dbSNP | Ensembl ].
VAR_029381
Natural variant4871T → M.
Corresponds to variant rs16867245 [ dbSNP | Ensembl ].
VAR_029382

Experimental info

Mutagenesis131C → A: Abolishes Pol I transcription but not recruitment of SL1/TIF-IB complex to rDNA promoters. Ref.12
Mutagenesis311C → A: Abolishes Pol I transcription but not recruitment of SL1/TIF-IB complex to rDNA promoters. Ref.12
Mutagenesis341C → A: Abolishes Pol I transcription but not recruitment of SL1/TIF-IB complex to rDNA promoters. Ref.12
Sequence conflict11M → L in AAA62863. Ref.1
Sequence conflict3721L → M in AAA62863. Ref.1
Sequence conflict5221C → W in AAA62863. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: CE45DE622E28FD6E

FASTA58868,832
        10         20         30         40         50         60 
MDLEEAEEFK ERCTQCAAVS WGLTDEGKYY CTSCHNVTER YQEVTNTDLI PNTQIKALNR 

        70         80         90        100        110        120 
GLKKKNNTEK GWDWYVCEGF QYILYQQAEA LKNLGVGPEL KNDVLHNFWK RYLQKSKQAY 

       130        140        150        160        170        180 
CKNPVYTTGR KPTVLEDNLS HSDWASEPEL LSDVSCPPFL ESGAESQSDI HTRKPFPVSK 

       190        200        210        220        230        240 
ASQSETSVCS GSLDGVEYSQ RKEKGIVKMT MPQTLAFCYL SLLWQREAIT LSDLLRFVEE 

       250        260        270        280        290        300 
DHIPYINAFQ HFPEQMKLYG RDRGIFGIES WPDYEDIYKK TVEVGTFLDL PRFPDITEDC 

       310        320        330        340        350        360 
YLHPNILCMK YLMEVNLPDE MHSLTCHVVK MTGMGEVDFL TFDPIAKMAK TVKYDVQAVA 

       370        380        390        400        410        420 
IIVVVLKLLF LLDDSFEWSL SNLAEKHNEK NKKDKPWFDF RKWYQIMKKA FDEKKQKWEE 

       430        440        450        460        470        480 
ARAKYLWKSE KPLYYSFVDK PVAYKKREMV VNLQKQFSTL VESTATAGKK SPSSFQFNWT 

       490        500        510        520        530        540 
EEDTDRTCFH GHSLQGVLKE KGQSLLTKNS LYWLSTQKFC RCYCTHVTTY EESNYSLSYQ 

       550        560        570        580 
FILNLFSFLL RIKTSLLHEE VSLVEKKLFE KKYSVKRKKS RSKKVRRH 

« Hide

Isoform 2 [UniParc].

Checksum: A0277EAF25B4F50F
Show »

FASTA52260,790
Isoform 3 [UniParc].

Checksum: 6E716737AB58736B
Show »

FASTA33339,533

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L39061 mRNA. Translation: AAA62863.1. Different initiation.
AK295402 mRNA. Translation: BAG58354.1.
AC010969 Genomic DNA. Translation: AAX93272.1.
BC018137 mRNA. Translation: AAH18137.1.
PIRI61581.
RefSeqNP_005671.2. NM_005680.2.
UniGeneHs.584833.

3D structure databases

ProteinModelPortalQ53T94.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114483. 33 interactions.
IntActQ53T94. 7 interactions.
MINTMINT-4543781.
STRING9606.ENSP00000263663.

PTM databases

PhosphoSiteQ53T94.

Polymorphism databases

DMDM74726856.

Proteomic databases

PaxDbQ53T94.
PRIDEQ53T94.

Protocols and materials databases

DNASU9014.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263663; ENSP00000263663; ENSG00000115750. [Q53T94-1]
ENST00000396242; ENSP00000379542; ENSG00000115750. [Q53T94-3]
GeneID9014.
KEGGhsa:9014.
UCSCuc002qzy.4. human. [Q53T94-1]

Organism-specific databases

CTD9014.
GeneCardsGC02P009983.
H-InvDBHIX0001812.
HGNCHGNC:11533. TAF1B.
MIM604904. gene.
neXtProtNX_Q53T94.
PharmGKBPA36308.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72502.
HOGENOMHOG000124571.
HOVERGENHBG053463.
InParanoidQ53T94.
KOK15213.
OMALSTQKFC.
OrthoDBEOG7V1FS7.
PhylomeDBQ53T94.
TreeFamTF324353.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ53T94.
BgeeQ53T94.
CleanExHS_TAF1B.
GenevestigatorQ53T94.

Family and domain databases

InterProIPR021752. TF_Rrn7.
[Graphical view]
PfamPF11781. RRN7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTAF1B.
GenomeRNAi9014.
NextBio33771.
PROQ53T94.
SOURCESearch...

Entry information

Entry nameTAF1B_HUMAN
AccessionPrimary (citable) accession number: Q53T94
Secondary accession number(s): B4DI42 expand/collapse secondary AC list , F8WD72, Q15574, Q8WVC3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM