Q9H5J8 (TAF1D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TATA box-binding protein-associated factor RNA polymerase I subunit D

Alternative name(s):
RNA polymerase I-specific TBP-associated factor 41 kDa
Short name=TAFI41
TATA box-binding protein-associated factor 1D
Short name=TBP-associated factor 1D
Transcription initiation factor SL1/TIF-IB subunit D

Gene names

Name:	TAF1D
Synonyms:	JOSD3

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	278 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.5 Ref.6
Subunit structure	Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. Interacts with UBTF. Ref.6
Subcellular location	Nucleus Ref.1 Ref.6.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.1. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
POLB	P06746	4	EBI-716128,EBI-713836

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 278	278	TATA box-binding protein-associated factor RNA polymerase I subunit D		PRO_0000250717
Amino acid modifications
	Modified residue	138	1	Phosphoserine Ref.7 Ref.8
	Modified residue	234	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	14	1	S → T in CAG33650. Ref.3
	Sequence conflict	97	1	R → G in CAG33650. Ref.3
	Sequence conflict	278	1	M → I in CAG33650. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9H5J8 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 4BA37C73BB387446	FASTA	278	32,058
	10 20 30 40 50 60 MDKSGIDSLD HVTSDAVELA NRSDNSSDSS LFKTQCIPYS PKGEKRNPIR KFVRTPESVH 70 80 90 100 110 120 ASDSSSDSSF EPIPLTIKAI FERFKNRKKR YKKKKKRRYQ PTGRPRGRPE GRRNPIYSLI 130 140 150 160 170 180 DKKKQFRSRG SGFPFLESEN EKNAPWRKIL TFEQAVARGF FNYIEKLKYE HHLKESLKQM 190 200 210 220 230 240 NVGEDLENED FDSRRYKFLD DDGSISPIEE STAEDEDATH LEDNECDIKL AGDSFIVSSE 250 260 270 FPVRLSVYLE EEDITEEAAL SKKRATKAKN TGQRGLKM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel nuclear protein, MGC5306 interacts with DNA polymerase beta and has a potential role in cellular phenotype." Wang L., Bhattacharyya N., Chelsea D.M., Escobar P.F., Banerjee S. Cancer Res. 64:7673-7677(2004) [PubMed: 15520167] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix.
[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]	"A novel TBP-associated factor of SL1 functions in RNA polymerase I transcription." Gorski J.J., Pathak S., Panov K., Kasciukovic T., Panova T., Russell J., Zomerdijk J.C.B.M. EMBO J. 26:1560-1568(2007) [PubMed: 17318177] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SL1/TIF-IB COMPLEX, INTERACTION WITH UBTF, SUBCELLULAR LOCATION.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-234, MASS SPECTROMETRY. Tissue: Leukemic T-cell.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK027016 mRNA. Translation: BAB15628.1. CR457369 mRNA. Translation: CAG33650.1. BC001972 mRNA. Translation: AAH01972.1.
IPI	IPI00012225.
RefSeq	NP_077021.1. NM_024116.3.
UniGene	Hs.355750.
3D structure databases
ProteinModelPortal	Q9H5J8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H5J8. 21 interactions.
STRING	Q9H5J8.
PTM databases
PhosphoSite	Q9H5J8.
Polymorphism databases
DMDM	74733586.
Proteomic databases
PRIDE	Q9H5J8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000323981; ENSP00000314971; ENSG00000166012. ENST00000448108; ENSP00000410409; ENSG00000166012.
GeneID	79101.
KEGG	hsa:79101.
UCSC	uc001ped.1. human.
Organism-specific databases
CTD	79101.
GeneCards	GC11M093503.
H-InvDB	HIX0010025.
HGNC	HGNC:28759. TAF1D.
MIM	612823. gene.
neXtProt	NX_Q9H5J8.
PharmGKB	PA164726421.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05000.
GeneTree	ENSGT00390000009061.
HOGENOM	HBG127159.
HOVERGEN	HBG096071.
InParanoid	Q9H5J8.
OMA	KRKYKPT.
OrthoDB	EOG4D7Z76.
PhylomeDB	Q9H5J8.
Gene expression databases
ArrayExpress	Q9H5J8.
Bgee	Q9H5J8.
CleanEx	HS_TAF1D.
Genevestigator	Q9H5J8.
GermOnline	ENSG00000166012. Homo sapiens.
Family and domain databases
KO	K15215.
ProtoNet	Search...
Other
NextBio	67969.
SOURCE	Search...

Entry information

Entry name

TAF1D_HUMAN

Accession

Primary (citable) accession number: Q9H5J8
Secondary accession number(s): Q6I9Y6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 72 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.