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TAF1D_HUMAN
ID   TAF1D_HUMAN             Reviewed;         278 AA.
AC   Q9H5J8; Q6I9Y6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit D;
DE   AltName: Full=RNA polymerase I-specific TBP-associated factor 41 kDa;
DE            Short=TAFI41;
DE   AltName: Full=TATA box-binding protein-associated factor 1D;
DE            Short=TBP-associated factor 1D;
DE   AltName: Full=Transcription initiation factor SL1/TIF-IB subunit D;
GN   Name=TAF1D; Synonyms=JOSD3;
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], AND SUBCELLULAR LOCATION.
RX   PubMed=15520167; DOI=10.1158/0008-5472.can-04-2801;
RA   Wang L., Bhattacharyya N., Chelsea D.M., Escobar P.F., Banerjee S.;
RT   "A novel nuclear protein, MGC5306 interacts with DNA polymerase beta and
RT   has a potential role in cellular phenotype.";
RL   Cancer Res. 64:7673-7677(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix;
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   [5]
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   [6]
RP   FUNCTION, IDENTIFICATION IN THE SL1/TIF-IB COMPLEX, INTERACTION WITH UBTF,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=17318177; DOI=10.1038/sj.emboj.7601601;
RA   Gorski J.J., Pathak S., Panov K., Kasciukovic T., Panova T., Russell J.,
RA   Zomerdijk J.C.B.M.;
RT   "A novel TBP-associated factor of SL1 functions in RNA polymerase I
RT   transcription.";
RL   EMBO J. 26:1560-1568(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-234, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Component of the transcription factor SL1/TIF-IB complex,
CC       which is involved in the assembly of the PIC (preinitiation 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:17318177}.
CC   -!- SUBUNIT: Component of the transcription factor SL1/TIF-IB complex,
CC       composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. Interacts
CC       with UBTF. {ECO:0000269|PubMed:17318177}.
CC   -!- INTERACTION:
CC       Q9H5J8; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-716128, EBI-739624;
CC       Q9H5J8; Q02577: NHLH2; NbExp=3; IntAct=EBI-716128, EBI-5378683;
CC       Q9H5J8; P06746: POLB; NbExp=4; IntAct=EBI-716128, EBI-713836;
CC       Q9H5J8; Q9H5J8: TAF1D; NbExp=3; IntAct=EBI-716128, EBI-716128;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15520167,
CC       ECO:0000269|PubMed:17318177}.
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DR   EMBL; AK027016; BAB15628.1; -; mRNA.
DR   EMBL; CR457369; CAG33650.1; -; mRNA.
DR   EMBL; BC001972; AAH01972.1; -; mRNA.
DR   CCDS; CCDS8293.1; -.
DR   RefSeq; NP_077021.1; NM_024116.3.
DR   AlphaFoldDB; Q9H5J8; -.
DR   BioGRID; 122548; 95.
DR   IntAct; Q9H5J8; 51.
DR   MINT; Q9H5J8; -.
DR   STRING; 9606.ENSP00000410409; -.
DR   iPTMnet; Q9H5J8; -.
DR   PhosphoSitePlus; Q9H5J8; -.
DR   BioMuta; TAF1D; -.
DR   DMDM; 74733586; -.
DR   EPD; Q9H5J8; -.
DR   jPOST; Q9H5J8; -.
DR   MassIVE; Q9H5J8; -.
DR   MaxQB; Q9H5J8; -.
DR   PaxDb; Q9H5J8; -.
DR   PeptideAtlas; Q9H5J8; -.
DR   PRIDE; Q9H5J8; -.
DR   ProteomicsDB; 80916; -.
DR   Antibodypedia; 53987; 61 antibodies from 11 providers.
DR   DNASU; 79101; -.
DR   Ensembl; ENST00000323981.6; ENSP00000314971.2; ENSG00000166012.17.
DR   Ensembl; ENST00000448108.7; ENSP00000410409.2; ENSG00000166012.17.
DR   Ensembl; ENST00000526015.5; ENSP00000435087.1; ENSG00000166012.17.
DR   GeneID; 79101; -.
DR   KEGG; hsa:79101; -.
DR   MANE-Select; ENST00000448108.7; ENSP00000410409.2; NM_024116.4; NP_077021.1.
DR   UCSC; uc001ped.5; human.
DR   CTD; 79101; -.
DR   DisGeNET; 79101; -.
DR   GeneCards; TAF1D; -.
DR   HGNC; HGNC:28759; TAF1D.
DR   HPA; ENSG00000166012; Low tissue specificity.
DR   MIM; 612823; gene.
DR   neXtProt; NX_Q9H5J8; -.
DR   OpenTargets; ENSG00000166012; -.
DR   PharmGKB; PA164726421; -.
DR   VEuPathDB; HostDB:ENSG00000166012; -.
DR   eggNOG; ENOG502SQMW; Eukaryota.
DR   GeneTree; ENSGT00390000009061; -.
DR   InParanoid; Q9H5J8; -.
DR   OMA; CFIISTE; -.
DR   OrthoDB; 1263117at2759; -.
DR   PhylomeDB; Q9H5J8; -.
DR   TreeFam; TF335756; -.
DR   PathwayCommons; Q9H5J8; -.
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; Q9H5J8; -.
DR   BioGRID-ORCS; 79101; 359 hits in 1050 CRISPR screens.
DR   ChiTaRS; TAF1D; human.
DR   GenomeRNAi; 79101; -.
DR   Pharos; Q9H5J8; Tdark.
DR   PRO; PR:Q9H5J8; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9H5J8; protein.
DR   Bgee; ENSG00000166012; Expressed in body of pancreas and 200 other tissues.
DR   ExpressionAtlas; Q9H5J8; baseline and differential.
DR   Genevisible; Q9H5J8; HS.
DR   GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR027976; TAF1D.
DR   PANTHER; PTHR14562; PTHR14562; 1.
DR   Pfam; PF15333; TAF1D; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..278
FT                   /note="TATA box-binding protein-associated factor RNA
FT                   polymerase I subunit D"
FT                   /id="PRO_0000250717"
FT   REGION          20..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   CONFLICT        14
FT                   /note="S -> T (in Ref. 3; CAG33650)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="R -> G (in Ref. 3; CAG33650)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="M -> I (in Ref. 3; CAG33650)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  32058 MW;  4BA37C73BB387446 CRC64;
     MDKSGIDSLD HVTSDAVELA NRSDNSSDSS LFKTQCIPYS PKGEKRNPIR KFVRTPESVH
     ASDSSSDSSF EPIPLTIKAI FERFKNRKKR YKKKKKRRYQ PTGRPRGRPE GRRNPIYSLI
     DKKKQFRSRG SGFPFLESEN EKNAPWRKIL TFEQAVARGF FNYIEKLKYE HHLKESLKQM
     NVGEDLENED FDSRRYKFLD DDGSISPIEE STAEDEDATH LEDNECDIKL AGDSFIVSSE
     FPVRLSVYLE EEDITEEAAL SKKRATKAKN TGQRGLKM
 
 
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