Q53T94 (TAF1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

TAF1B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits. Ref.1 Ref.5
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 RRN3. Ref.1 Ref.4
Subcellular location	Nucleus.
Sequence similarities	Belongs to the TAF1 family.
Sequence caution	The sequence AAA62863.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	termination of RNA polymerase I transcription Traceable author statement. Source: Reactome transcription elongation from RNA polymerase I promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase I promoter Traceable author statement. Source: Reactome
Cellular component	nucleoplasm Traceable author statement. Source: Reactome
Molecular function	DNA 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...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 588	588	TATA box-binding protein-associated factor RNA polymerase I subunit B		PRO_0000261392
Amino acid modifications
	Modified residue	440	1	N6-acetyllysine Ref.6
Natural variations
	Alternative sequence	523 – 588	66	Missing in isoform 2.		VSP_021677
	Natural variant	6	1	A → S. Ref.1 Ref.3 Corresponds to variant rs2303914 [ dbSNP | Ensembl ].		VAR_029378
	Natural variant	282	1	V → I. Ref.1 Ref.3 Corresponds to variant rs396190 [ dbSNP | Ensembl ].		VAR_029379
	Natural variant	292	1	R → H. Corresponds to variant rs16867223 [ dbSNP | Ensembl ].		VAR_057260
	Natural variant	351	1	T → A. Ref.1 Ref.3 Corresponds to variant rs1054565 [ dbSNP | Ensembl ].		VAR_029380
	Natural variant	462	1	E → D. Ref.1 Ref.3 Corresponds to variant rs1820965 [ dbSNP | Ensembl ].		VAR_029381
	Natural variant	487	1	T → M. Corresponds to variant rs16867245 [ dbSNP | Ensembl ].		VAR_029382
Experimental info
	Sequence conflict	1	1	M → L in AAA62863. Ref.1
	Sequence conflict	372	1	L → M in AAA62863. Ref.1
	Sequence conflict	522	1	C → W in AAA62863. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: CE45DE622E28FD6E	FASTA	588	68,832
	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
	Isoform 2 [UniParc]. Checksum: A0277EAF25B4F50F	FASTA	522	60,790
	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 EEDTDRTCFH GHSLQGVLKE KGQSLLTKNS LYWLSTQKFC RC

References

	« Hide 'large scale' referencesShow '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: 7801123] [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]	"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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-6; ILE-282; ALA-351 AND ASP-462. Tissue: Colon.
[4]	"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: 11250903] [Abstract] Cited for: INTERACTION WITH RRN3.
[5]	"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: 15970593] [Abstract] Cited for: FUNCTION OF THE SL1/TIF-IB COMPLEX.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-440, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L39061 mRNA. Translation: AAA62863.1. Different initiation. AC010969 Genomic DNA. Translation: AAX93272.1. BC018137 mRNA. Translation: AAH18137.1.
IPI	IPI00291416. IPI00807704.
PIR	I61581.
RefSeq	NP_005671.2. NM_005680.2.
UniGene	Hs.584833.
3D structure databases
ProteinModelPortal	Q53T94.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q53T94. 2 interactions.
MINT	MINT-4543781.
STRING	Q53T94.
PTM databases
PhosphoSite	Q53T94.
Polymorphism databases
DMDM	74726856.
Proteomic databases
PRIDE	Q53T94.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263663; ENSP00000263663; ENSG00000115750.
GeneID	9014.
KEGG	hsa:9014.
UCSC	uc002qzy.2. human. uc002qzz.1. human.
Organism-specific databases
CTD	9014.
GeneCards	GC02P009934.
H-InvDB	HIX0001812.
HGNC	HGNC:11533. TAF1B.
MIM	604904. gene.
neXtProt	NX_Q53T94.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07029.
GeneTree	ENSGT00440000033827.
HOGENOM	HBG713720.
HOVERGEN	HBG053463.
InParanoid	Q53T94.
OMA	YLHPNIL.
OrthoDB	EOG4CVG6V.
PhylomeDB	Q53T94.
Enzyme and pathway databases
Reactome	REACT_1788. Transcription.
Gene expression databases
ArrayExpress	Q53T94.
Bgee	Q53T94.
CleanEx	HS_TAF1B.
Genevestigator	Q53T94.
GermOnline	ENSG00000115750. Homo sapiens.
Family and domain databases
InterPro	IPR021752. TF_Rrn7. [Graphical view]
KO	K15213.
Pfam	PF11781. RRN7. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	33771.
SOURCE	Search...

Entry information

Entry name

TAF1B_HUMAN

Accession

Primary (citable) accession number: Q53T94
Secondary accession number(s): Q15574, Q8WVC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	May 24, 2005
Last modified:	January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.