RRN3_HUMAN
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 03-AUG-2022, entry version 145.
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. Required for the formation of the competent preinitiation
CC complex (PIC). Dissociates from pol I as a consequence of
CC transcription. In vitro, cannot activate transcription in a subsequent
CC transcription reaction (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10758157, ECO:0000269|PubMed:11250903,
CC ECO:0000269|PubMed:11265758, ECO:0000269|PubMed:15805466}.
CC -!- SUBUNIT: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 SMR; Q9NYV6; -.
DR BioGRID; 120102; 39.
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; Q9NYV6; -.
DR PeptideAtlas; Q9NYV6; -.
DR PRIDE; Q9NYV6; -.
DR ProteomicsDB; 5679; -.
DR ProteomicsDB; 5920; -.
DR ProteomicsDB; 61783; -.
DR ProteomicsDB; 83282; -. [Q9NYV6-1]
DR Antibodypedia; 11691; 230 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 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; 855834at2759; -.
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; 724 hits in 1080 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 101 other tissues.
DR ExpressionAtlas; Q9NYV6; baseline and differential.
DR Genevisible; Q9NYV6; HS.
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 transcription, DNA-templated; 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 from RNA polymerase I promoter; IBA:GO_Central.
DR InterPro; IPR007991; RNA_pol_I_trans_ini_fac_RRN3.
DR PANTHER; PTHR12790; PTHR12790; 1.
DR Pfam; PF05327; RRN3; 1.
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
