TAF1A_HUMAN
ID TAF1A_HUMAN Reviewed; 450 AA.
AC Q15573; B2RDZ8; D3DTB7; Q9NWA1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit A;
DE AltName: Full=RNA polymerase I-specific TBP-associated factor 48 kDa;
DE Short=TAFI48;
DE AltName: Full=TATA box-binding protein-associated factor 1A;
DE Short=TBP-associated factor 1A;
DE AltName: Full=Transcription factor SL1;
DE AltName: Full=Transcription initiation factor SL1/TIF-IB subunit A;
GN Name=TAF1A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 68-84; 113-123;
RP 155-169; 183-193; 205-219; 221-230; 404-413 AND 442-449, FUNCTION, AND
RP INTERACTION WITH TBP; TAF1B AND TAF1C.
RX PubMed=7801123; DOI=10.1126/science.7801123;
RA Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R.;
RT "Reconstitution of transcription factor SL1: exclusive binding of TBP by
RT SL1 or TFIID subunits.";
RL Science 266:1966-1972(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH UBTF.
RX PubMed=7491500; DOI=10.1126/science.270.5241.1506;
RA Beckmann H., Chen J.L., O'Brien T., Tjian R.;
RT "Coactivator and promoter-selective properties of RNA polymerase I TAFs.";
RL Science 270:1506-1509(1995).
RN [7]
RP FUNCTION OF THE SL1/TIF-IB COMPLEX.
RX PubMed=15970593; DOI=10.1074/jbc.m501595200;
RA Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.;
RT "TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex
RT formation and stabilizes upstream binding factor at the rDNA promoter.";
RL J. Biol. Chem. 280:29551-29558(2005).
RN [8]
RP INTERACTION WITH CEBPA.
RX PubMed=20075868; DOI=10.1038/emboj.2009.404;
RA Muller C., Bremer A., Schreiber S., Eichwald S., Calkhoven C.F.;
RT "Nucleolar retention of a translational C/EBPalpha isoform stimulates rDNA
RT transcription and cell size.";
RL EMBO J. 29:897-909(2010).
CC -!- FUNCTION: Component of the transcription factor SL1/TIF-IB complex,
CC which is involved in the assembly of the PIC (pre-initiation complex)
CC during RNA polymerase I-dependent transcription. The rate of PIC
CC formation probably is primarily dependent on the rate of association of
CC SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in
CC stabilization of nucleolar transcription factor 1/UBTF on rDNA.
CC Formation of SL1/TIF-IB excludes the association of TBP with TFIID
CC subunits. {ECO:0000269|PubMed:15970593, ECO:0000269|PubMed:7801123}.
CC -!- SUBUNIT: Component of the transcription factor SL1/TIF-IB complex,
CC composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the
CC complex interacts directly with TBP, TAF1A and TAF1B. Interaction of
CC the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the
CC transcription factor IID (TFIID) subunits. Interacts with UBFT.
CC Interacts with CEBPA (isoform 1 and isoform 4) (PubMed:20075868).
CC {ECO:0000269|PubMed:20075868, ECO:0000269|PubMed:7491500,
CC ECO:0000269|PubMed:7801123}.
CC -!- INTERACTION:
CC Q15573; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-2510647, EBI-3920396;
CC Q15573; Q6ZUT1-2: NKAPD1; NbExp=3; IntAct=EBI-2510647, EBI-10180231;
CC Q15573; Q01105: SET; NbExp=2; IntAct=EBI-2510647, EBI-1053182;
CC Q15573; P20226: TBP; NbExp=2; IntAct=EBI-2510647, EBI-355371;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15573-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15573-2; Sequence=VSP_017635;
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DR EMBL; L39060; AAA62862.1; -; mRNA.
DR EMBL; AK001054; BAA91482.1; -; mRNA.
DR EMBL; AK315740; BAG38095.1; -; mRNA.
DR EMBL; AL592148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93271.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93272.1; -; Genomic_DNA.
DR EMBL; BC013808; AAH13808.1; -; mRNA.
DR CCDS; CCDS1531.1; -. [Q15573-1]
DR CCDS; CCDS1532.1; -. [Q15573-2]
DR PIR; I61580; I61580.
DR RefSeq; NP_001188465.1; NM_001201536.1. [Q15573-1]
DR RefSeq; NP_005672.1; NM_005681.3. [Q15573-1]
DR RefSeq; NP_647603.1; NM_139352.2. [Q15573-2]
DR RefSeq; XP_006711676.1; XM_006711613.3. [Q15573-2]
DR RefSeq; XP_016858248.1; XM_017002759.1. [Q15573-2]
DR RefSeq; XP_016858249.1; XM_017002760.1. [Q15573-2]
DR AlphaFoldDB; Q15573; -.
DR BioGRID; 114484; 78.
DR CORUM; Q15573; -.
DR IntAct; Q15573; 20.
DR MINT; Q15573; -.
DR STRING; 9606.ENSP00000339976; -.
DR BindingDB; Q15573; -.
DR ChEMBL; CHEMBL4105882; -.
DR iPTMnet; Q15573; -.
DR PhosphoSitePlus; Q15573; -.
DR BioMuta; TAF1A; -.
DR DMDM; 74739864; -.
DR EPD; Q15573; -.
DR MassIVE; Q15573; -.
DR MaxQB; Q15573; -.
DR PaxDb; Q15573; -.
DR PeptideAtlas; Q15573; -.
DR PRIDE; Q15573; -.
DR ProteomicsDB; 60643; -. [Q15573-1]
DR ProteomicsDB; 60644; -. [Q15573-2]
DR Antibodypedia; 20741; 234 antibodies from 29 providers.
DR DNASU; 9015; -.
DR Ensembl; ENST00000350027.8; ENSP00000339976.4; ENSG00000143498.18. [Q15573-1]
DR Ensembl; ENST00000352967.9; ENSP00000327072.6; ENSG00000143498.18. [Q15573-1]
DR Ensembl; ENST00000366890.5; ENSP00000355856.1; ENSG00000143498.18. [Q15573-2]
DR GeneID; 9015; -.
DR KEGG; hsa:9015; -.
DR MANE-Select; ENST00000352967.9; ENSP00000327072.6; NM_005681.4; NP_005672.1.
DR UCSC; uc001hni.3; human. [Q15573-1]
DR CTD; 9015; -.
DR DisGeNET; 9015; -.
DR GeneCards; TAF1A; -.
DR HGNC; HGNC:11532; TAF1A.
DR HPA; ENSG00000143498; Low tissue specificity.
DR MalaCards; TAF1A; -.
DR MIM; 604903; gene.
DR neXtProt; NX_Q15573; -.
DR OpenTargets; ENSG00000143498; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR PharmGKB; PA36307; -.
DR VEuPathDB; HostDB:ENSG00000143498; -.
DR eggNOG; ENOG502R510; Eukaryota.
DR GeneTree; ENSGT00390000011405; -.
DR HOGENOM; CLU_049461_0_0_1; -.
DR InParanoid; Q15573; -.
DR OMA; EMIWRIG; -.
DR PhylomeDB; Q15573; -.
DR TreeFam; TF330958; -.
DR PathwayCommons; Q15573; -.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR SignaLink; Q15573; -.
DR BioGRID-ORCS; 9015; 448 hits in 1083 CRISPR screens.
DR GeneWiki; TAF1A; -.
DR GenomeRNAi; 9015; -.
DR Pharos; Q15573; Tbio.
DR PRO; PR:Q15573; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15573; protein.
DR Bgee; ENSG00000143498; Expressed in oocyte and 145 other tissues.
DR ExpressionAtlas; Q15573; baseline and differential.
DR Genevisible; Q15573; HS.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006360; P:transcription by RNA polymerase I; TAS:ProtInc.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR InterPro; IPR016629; RNA_pol_I_TAF1A/TAFI48_chr.
DR InterPro; IPR039495; TAF1A.
DR Pfam; PF14929; TAF1_subA; 1.
DR PIRSF; PIRSF015161; TAFI48; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..450
FT /note="TATA box-binding protein-associated factor RNA
FT polymerase I subunit A"
FT /id="PRO_0000227987"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017635"
FT VARIANT 98
FT /note="I -> M (in dbSNP:rs17163271)"
FT /id="VAR_052253"
SQ SEQUENCE 450 AA; 52676 MW; 130330D78493C4D8 CRC64;
MSDFSEELKG PVTDDEEVET SVLSGAGMHF PWLQTYVETV AIGGKRRKDF AQTTSACLSF
IQEALLKHQW QQAAEYMYSY FQTLEDSDSY KRQAAPEIIW KLGSEILFYH PKSNMESFNT
FANRMKNIGV MNYLKISLQH ALYLLHHGML KDAKRNLSEA ETWRHGENTS SREILINLIQ
AYKGLLQYYT WSEKKMELSK LDKDDYAYNA VAQDVFNHSW KTSANISALI KIPGVWDPFV
KSYVEMLEFY GDRDGAQEVL TNYAYDEKFP SNPNAHIYLY NFLKRQKAPR SKLISVLKIL
YQIVPSHKLM LEFHTLLRKS EKEEHRKLGL EVLFGVLDFA GCTKNITAWK YLAKYLKNIL
MGNHLAWVQE EWNSRKNWWP GFHFSYFWAK SDWKEDTALA CEKAFVAGLL LGKGCRYFRY
ILKQDHQILG KKIKRMKRSV KKYSIVNPRL
