ID   RRN3_HUMAN              Reviewed;         651 AA.
AC   Q9NYV6; A2RTY9; B4E0J7; B4E3T2; Q3MHU9; Q6IPL4; Q9H4F0;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=RNA polymerase I-specific transcription initiation factor RRN3;
DE   AltName: Full=Transcription initiation factor IA;
DE            Short=TIF-IA;
GN   Name=RRN3; Synonyms=TIFIA;
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), AND FUNCTION.
RX   PubMed=11265758; DOI=10.1093/embo-reports/kvd032;
RA   Bodem J., Dobreva G., Hoffmann-Rohrer U., Iben S., Zentgraf H., Delius H.,
RA   Vingron M., Grummt I.;
RT   "TIF-IA, the factor mediating growth-dependent control of ribosomal RNA
RT   synthesis, is the mammalian homolog of yeast Rrn3p.";
RL   EMBO Rep. 1:171-175(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX   PubMed=10758157; DOI=10.1073/pnas.080063997;
RA   Moorefield B., Greene E.A., Reeder R.H.;
RT   "RNA polymerase I transcription factor Rrn3 is functionally conserved
RT   between yeast and human.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:4724-4729(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   TISSUE=Hippocampus, Thymus, and Uterus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney, and Spleen;
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   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TAF1B AND TAF1C.
RX   PubMed=11250903; DOI=10.1093/emboj/20.6.1373;
RA   Miller G., Panov K.I., Friedrich J.K., Trinkle-Mulcahy L., Lamond A.I.,
RA   Zomerdijk J.C.B.M.;
RT   "hRRN3 is essential in the SL1-mediated recruitment of RNA polymerase I to
RT   rRNA gene promoters.";
RL   EMBO J. 20:1373-1382(2001).
RN   [8]
RP   INTERACTION WITH POLR1F; EIF3L; TAF1B AND TAF1C, AND MUTAGENESIS OF
RP   411-LEU--LYS-415.
RX   PubMed=12393749; DOI=10.1093/embo-reports/kvf212;
RA   Yuan X., Zhao J., Zentgraf H., Hoffmann-Rohrer U., Grummt I.;
RT   "Multiple interactions between RNA polymerase I, TIF-IA and TAF(I) subunits
RT   regulate preinitiation complex assembly at the ribosomal gene promoter.";
RL   EMBO Rep. 3:1082-1087(2002).
RN   [9]
RP   PHOSPHORYLATION AT THR-200 BY MAPK9/JNK2, AND FUNCTION.
RX   PubMed=15805466; DOI=10.1101/gad.333205;
RA   Mayer C., Bierhoff H., Grummt I.;
RT   "The nucleolus as a stress sensor: JNK2 inactivates the transcription
RT   factor TIF-IA and down-regulates rRNA synthesis.";
RL   Genes Dev. 19:933-941(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-172 AND SER-640, AND
RP   IDENTIFICATION BY 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640, 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   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
RP   IDENTIFICATION BY 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   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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: Required for efficient transcription initiation by RNA
CC       polymerase I (Pol I). Required for the formation of the competent pre-
CC       initiation complex (PIC). {ECO:0000250, ECO:0000269|PubMed:10758157,
CC       ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:11265758,
CC       ECO:0000269|PubMed:15805466}.
CC   -!- SUBUNIT: Part of Pol I pre-initiation complex (PIC), in which Pol I
CC       core assembles with RRN3 and promoter-bound UTBF and SL1/TIF-IB
CC       complex. Interacts with POLR1F, EIF3L, TAF1B and TAF1C.
CC       {ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:12393749}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11250903}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9NYV6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NYV6-2; Sequence=VSP_056338, VSP_056339;
CC       Name=3;
CC         IsoId=Q9NYV6-3; Sequence=VSP_056520;
CC       Name=4;
CC         IsoId=Q9NYV6-4; Sequence=VSP_056519, VSP_056521;
CC   -!- PTM: Phosphorylation is required for participation in rDNA
CC       transcription (By similarity). Phosphorylated at Thr-200 by MAPK9/JNK2,
CC       which abrogates initiation complex formation. {ECO:0000250,
CC       ECO:0000269|PubMed:15805466}.
CC   -!- SIMILARITY: Belongs to the RRN3 family. {ECO:0000305}.
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DR   EMBL; AJ272050; CAC07955.1; -; mRNA.
DR   EMBL; AF227156; AAF66160.1; -; mRNA.
DR   EMBL; AK303405; BAG64459.1; -; mRNA.
DR   EMBL; AK304856; BAG65594.1; -; mRNA.
DR   EMBL; AK314769; BAG37307.1; -; mRNA.
DR   EMBL; AC139256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471301; EAW54754.1; -; Genomic_DNA.
DR   EMBL; BC071868; AAH71868.1; -; mRNA.
DR   EMBL; BC104660; AAI04661.1; -; mRNA.
DR   EMBL; BC132688; AAI32689.1; -; mRNA.
DR   EMBL; BC132690; AAI32691.1; -; mRNA.
DR   CCDS; CCDS10559.1; -. [Q9NYV6-1]
DR   RefSeq; NP_060897.3; NM_018427.4. [Q9NYV6-1]
DR   PDB; 7OBA; EM; 3.10 A; O=1-651.
DR   PDBsum; 7OBA; -.
DR   AlphaFoldDB; Q9NYV6; -.
DR   EMDB; EMD-12796; -.
DR   SMR; Q9NYV6; -.
DR   BioGRID; 120102; 45.
DR   CORUM; Q9NYV6; -.
DR   IntAct; Q9NYV6; 8.
DR   MINT; Q9NYV6; -.
DR   STRING; 9606.ENSP00000198767; -.
DR   iPTMnet; Q9NYV6; -.
DR   MetOSite; Q9NYV6; -.
DR   PhosphoSitePlus; Q9NYV6; -.
DR   BioMuta; RRN3; -.
DR   DMDM; 74719591; -.
DR   EPD; Q9NYV6; -.
DR   jPOST; Q9NYV6; -.
DR   MassIVE; Q9NYV6; -.
DR   MaxQB; Q9NYV6; -.
DR   PaxDb; 9606-ENSP00000198767; -.
DR   PeptideAtlas; Q9NYV6; -.
DR   ProteomicsDB; 5679; -.
DR   ProteomicsDB; 5920; -.
DR   ProteomicsDB; 61783; -.
DR   ProteomicsDB; 83282; -. [Q9NYV6-1]
DR   Pumba; Q9NYV6; -.
DR   Antibodypedia; 11691; 260 antibodies from 31 providers.
DR   DNASU; 54700; -.
DR   Ensembl; ENST00000198767.11; ENSP00000198767.7; ENSG00000085721.13. [Q9NYV6-1]
DR   Ensembl; ENST00000327307.11; ENSP00000318484.7; ENSG00000085721.13. [Q9NYV6-3]
DR   Ensembl; ENST00000564131.1; ENSP00000454238.1; ENSG00000085721.13. [Q9NYV6-2]
DR   Ensembl; ENST00000616334.2; ENSP00000480743.1; ENSG00000278494.2. [Q9NYV6-1]
DR   Ensembl; ENST00000632541.1; ENSP00000488651.1; ENSG00000278494.2. [Q9NYV6-3]
DR   Ensembl; ENST00000634151.1; ENSP00000487821.1; ENSG00000278494.2. [Q9NYV6-2]
DR   GeneID; 54700; -.
DR   KEGG; hsa:54700; -.
DR   MANE-Select; ENST00000198767.11; ENSP00000198767.7; NM_018427.5; NP_060897.3.
DR   UCSC; uc002dde.4; human. [Q9NYV6-1]
DR   AGR; HGNC:30346; -.
DR   CTD; 54700; -.
DR   DisGeNET; 54700; -.
DR   GeneCards; RRN3; -.
DR   HGNC; HGNC:30346; RRN3.
DR   HPA; ENSG00000085721; Low tissue specificity.
DR   MIM; 605121; gene.
DR   neXtProt; NX_Q9NYV6; -.
DR   OpenTargets; ENSG00000085721; -.
DR   PharmGKB; PA134878601; -.
DR   VEuPathDB; HostDB:ENSG00000085721; -.
DR   eggNOG; KOG2434; Eukaryota.
DR   GeneTree; ENSGT00390000001488; -.
DR   HOGENOM; CLU_010579_3_1_1; -.
DR   InParanoid; Q9NYV6; -.
DR   OMA; VCSPAIV; -.
DR   OrthoDB; 227969at2759; -.
DR   PhylomeDB; Q9NYV6; -.
DR   TreeFam; TF312979; -.
DR   PathwayCommons; Q9NYV6; -.
DR   Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR   SignaLink; Q9NYV6; -.
DR   SIGNOR; Q9NYV6; -.
DR   BioGRID-ORCS; 54700; 757 hits in 1158 CRISPR screens.
DR   ChiTaRS; RRN3; human.
DR   GeneWiki; RRN3; -.
DR   GenomeRNAi; 54700; -.
DR   Pharos; Q9NYV6; Tbio.
DR   PRO; PR:Q9NYV6; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9NYV6; Protein.
DR   Bgee; ENSG00000085721; Expressed in cortical plate and 102 other cell types or tissues.
DR   ExpressionAtlas; Q9NYV6; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001042; F:RNA polymerase I core binding; IBA:GO_Central.
DR   GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IBA:GO_Central.
DR   GO; GO:0007028; P:cytoplasm organization; IEA:Ensembl.
DR   GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR   GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0007000; P:nucleolus organization; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:2000142; P:regulation of DNA-templated transcription initiation; IEA:Ensembl.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:Ensembl.
DR   GO; GO:0006361; P:transcription initiation at RNA polymerase I promoter; IBA:GO_Central.
DR   InterPro; IPR007991; RNA_pol_I_trans_ini_fac_RRN3.
DR   PANTHER; PTHR12790:SF0; RNA POLYMERASE I-SPECIFIC TRANSCRIPTION INITIATION FACTOR RRN3-RELATED; 1.
DR   PANTHER; PTHR12790; TRANSCRIPTION INITIATION FACTOR IA RRN3; 1.
DR   Pfam; PF05327; RRN3; 1.
DR   Genevisible; Q9NYV6; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..651
FT                   /note="RNA polymerase I-specific transcription initiation
FT                   factor RRN3"
FT                   /id="PRO_0000211426"
FT   REGION          500..651
FT                   /note="Interaction with POLR1F"
FT                   /evidence="ECO:0000269|PubMed:12393749"
FT   REGION          557..651
FT                   /note="Interaction with EIF3L"
FT                   /evidence="ECO:0000269|PubMed:12393749"
FT   REGION          624..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by MAPK9"
FT                   /evidence="ECO:0000269|PubMed:15805466"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   VAR_SEQ         1..149
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056519"
FT   VAR_SEQ         1..33
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056520"
FT   VAR_SEQ         223..255
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056521"
FT   VAR_SEQ         287..305
FT                   /note="DEDEETEHETKAGPERLDQ -> VSSLLMKVEMKFIIKGGNS (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056338"
FT   VAR_SEQ         306..651
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056339"
FT   VARIANT         348
FT                   /note="I -> M (in dbSNP:rs2941256)"
FT                   /id="VAR_051886"
FT   MUTAGEN         411..415
FT                   /note="Missing: Abolishes interaction with TAF1B and
FT                   TAF1C."
FT                   /evidence="ECO:0000269|PubMed:12393749"
FT   HELIX           110..113
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           127..138
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           141..144
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           145..153
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           182..196
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           199..203
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           205..210
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           219..235
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           240..256
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           309..328
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           342..354
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   TURN            355..357
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           365..371
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           376..391
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           397..412
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           419..439
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           454..469
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   TURN            470..474
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           484..486
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           487..495
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   STRAND          497..499
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   TURN            501..504
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           507..519
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           554..558
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   TURN            567..569
FT                   /evidence="ECO:0007829|PDB:7OBA"
FT   HELIX           571..574
FT                   /evidence="ECO:0007829|PDB:7OBA"
SQ   SEQUENCE   651 AA;  74107 MW;  C646DC6677C49895 CRC64;
     MAAPLLHTRL PGDAAASSSA VKKLGASRTG ISNMRALEND FFNSPPRKTV RFGGTVTEVL
     LKYKKGETND FELLKNQLLD PDIKDDQIIN WLLEFRSSIM YLTKDFEQLI SIILRLPWLN
     RSQTVVEEYL AFLGNLVSAQ TVFLRPCLSM IASHFVPPRV IIKEGDVDVS DSDDEDDNLP
     ANFDTCHRAL QIIARYVPST PWFLMPILVE KFPFVRKSER TLECYVHNLL RISVYFPTLR
     HEILELIIEK LLKLDVNASR QGIEDAEETA TQTCGGTDST EGLFNMDEDE ETEHETKAGP
     ERLDQMVHPV AERLDILMSL VLSYMKDVCY VDGKVDNGKT KDLYRDLINI FDKLLLPTHA
     SCHVQFFMFY LCSFKLGFAE AFLEHLWKKL QDPSNPAIIR QAAGNYIGSF LARAKFIPLI
     TVKSCLDLLV NWLHIYLNNQ DSGTKAFCDV ALHGPFYSAC QAVFYTFVFR HKQLLSGNLK
     EGLQYLQSLN FERIVMSQLN PLKICLPSVV NFFAAITNKY QLVFCYTIIE RNNRQMLPVI
     RSTAGGDSVQ ICTNPLDTFF PFDPCVLKRS KKFIDPIYQV WEDMSAEELQ EFKKPMKKDI
     VEDEDDDFLK GEVPQNDTVI GITPSSFDTH FRSPSSSVGS PPVLYMQPSP L
//