ID GT2D1_HUMAN Reviewed; 959 AA. AC Q9UHL9; O95444; Q75MX7; Q86UM3; Q8WVC4; Q9UHK8; Q9UI91; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 01-MAY-2007, entry version 57. DE General transcription factor II-I repeat domain-containing protein 1 DE (GTF2I repeat domain-containing protein 1) (Muscle TFII-I repeat DE domain-containing protein 1) (General transcription factor III) (Slow- DE muscle-fiber enhancer-binding protein) (USE B1-binding protein) DE (MusTRD1/BEN) (Williams-Beuren syndrome chromosome region 11 protein). GN Name=GTF2IRD1; GN Synonyms=CREAM1, GTF3, MUSTRD1, RBAP2, WBSCR11, WBSCR12; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Muscle; RX MEDLINE=98449952; PubMed=9774679; RA O'Mahoney J.V., Guven K.L., Lin J., Joya J.E., Robinson C.S., RA Wade R.P., Hardeman E.C.; RT "Identification of a novel slow-muscle-fiber enhancer binding protein, RT MUSTRD1."; RL Mol. Cell. Biol. 18:6641-6652(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Colon carcinoma; RX MEDLINE=99216421; PubMed=10198167; DOI=10.1006/geno.1999.5784; RA Osborne L.R., Campbell T., Daradich A., Scherer S.W., Tsui L.-C.; RT "Identification of a putative transcription factor gene (WBSCR11) that RT is commonly deleted in Williams-Beuren syndrome."; RL Genomics 57:279-284(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX MEDLINE=20037629; PubMed=10573005; DOI=10.1038/sj.ejhg.5200396; RA Tassabehji M., Carette M., Wilmot C., Donnai D., Read A.P., RA Metcalfe K.; RT "A transcription factor involved in skeletal muscle gene expression is RT deleted in patients with Williams syndrome."; RL Eur. J. Hum. Genet. 7:737-747(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX MEDLINE=20044629; PubMed=10575229; RA Franke Y., Peoples R.J., Francke U.; RT "Identification of GTF2IRD1, a putative transcription factor within RT the Williams-Beuren syndrome deletion at 7q11.23."; RL Cytogenet. Cell Genet. 86:296-304(1999). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1, AND RP MUTAGENESIS. RC TISSUE=Cervix carcinoma, Fetal spleen, and Placenta; RX MEDLINE=20115113; PubMed=10642537; DOI=10.1042/0264-6021:3450749; RA Yan X., Zhao X., Qian M., Guo N., Gong X., Zhu X.; RT "Characterization and gene structure of a novel retinoblastoma- RT protein-associated protein similar to the transcription regulator RT TFII-I."; RL Biochem. J. 345:749-757(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP FUNCTION. RX MEDLINE=21332325; PubMed=11438732; DOI=10.1073/pnas.141222298; RA Tussie-Luna M.I., Bayarsaihan D., Ruddle F.H., Roy A.L.; RT "Repression of TFII-I-dependent transcription by nuclear exclusion."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7789-7794(2001). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND MASS RP SPECTROMETRY. RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND MASS RP SPECTROMETRY. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). CC -!- FUNCTION: May be a transcription regulator involved in cell-cycle CC progression and skeletal muscle differentiation. May repress GTF2I CC transcriptional functions, by preventing its nuclear residency, or CC by inhibiting its transcriptional activation. May contribute to CC slow-twitch fiber type specificity during myogenesis and in CC regenerating muscles. Binds troponin I slow-muscle fiber enhancer CC (USE B1). Binds specifically and with high affinity to the EFG CC sequences derived from the early enhancer of HOXC8 (By CC similarity). CC -!- SUBUNIT: Interacts with the retinoblastoma protein (RB1) via its CC C-terminus. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UHL9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UHL9-2; Sequence=VSP_003873; CC -!- TISSUE SPECIFICITY: Highly expressed in adult skeletal muscle, CC heart, fibroblast, bone and fetal tissues. Expressed at lower CC levels in all other tissues tested. CC -!- DEVELOPMENTAL STAGE: Highly expressed in developing and CC regenerating muscles, at the time of myofiber diversification. CC -!- DOMAIN: The N-terminal half may have an activating activity. CC -!- DISEASE: Haploinsufficiency of GTF2IRD1 may be the cause of CC certain cardiovascular and musculo-skeletal abnormalities observed CC in Williams-Beuren syndrome (WBS), a rare developmental disorder. CC It is a contiguous gene deletion syndrome involving genes from CC chromosome band 7q11.23. CC -!- SIMILARITY: Belongs to the TFII-I family. CC -!- SIMILARITY: Contains 5 GTF2I-like repeats. CC -!- CAUTION: Ref.6 (AAS00362) sequence differs from that shown due to CC erroneous gene model prediction. 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; AF118270; AAD14687.2; -; mRNA. DR EMBL; AF104923; AAD27668.1; -; mRNA. DR EMBL; AF151354; AAF19786.1; -; mRNA. DR EMBL; AF156489; AAF17358.1; -; mRNA. DR EMBL; AF089107; AAF21796.1; -; mRNA. DR EMBL; AC004851; AAS00362.1; -; Genomic_DNA. DR EMBL; AC005231; AAP21877.1; -; Genomic_DNA. DR EMBL; BC018136; AAH18136.1; -; mRNA. DR UniGene; Hs.647056; -. DR PDB; 2DN5; NMR; A=802-877. DR Ensembl; ENSG00000006704; Homo sapiens. DR KEGG; hsa:9569; -. DR H-InvDB; HIX0006766; -. DR HGNC; HGNC:4661; GTF2IRD1. DR MIM; 194050; phenotype. DR MIM; 604318; gene. DR LinkHub; Q9UHL9; -. DR ArrayExpress; Q9UHL9; -. DR RZPD-ProtExp; IOH10904; -. DR RZPD-ProtExp; Z0404; -. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003705; F:RNA polymerase II transcription factor acti...; NAS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB. DR InterPro; IPR004212; GTF2I. DR Gene3D; G3DSA:3.90.1460.10; G3DSA:3.90.1460.10; 5. DR Pfam; PF02946; GTF2I; 5. DR PROSITE; PS51139; GTF2I; 5. KW 3D-structure; Alternative splicing; Developmental protein; KW DNA-binding; Nuclear protein; Phosphorylation; Polymorphism; Repeat; KW Transcription; Transcription regulation; Williams-Beuren syndrome. FT CHAIN 1 959 General transcription factor II-I repeat FT domain-containing protein 1. FT /FTId=PRO_0000083870. FT REPEAT 119 213 GTF2I-like 1. FT REPEAT 342 436 GTF2I-like 2. FT REPEAT 556 650 GTF2I-like 3. FT REPEAT 696 790 GTF2I-like 4. FT REPEAT 793 887 GTF2I-like 5. FT MOTIF 898 905 Nuclear localization signal (Potential). FT COMPBIAS 906 930 Ser-rich. FT MOD_RES 448 448 Phosphoserine. FT VAR_SEQ 656 670 Missing (in isoform 2). FT /FTId=VSP_003873. FT VARIANT 652 652 M -> V (in dbSNP:rs2301895). FT /FTId=VAR_013446. FT MUTAGEN 898 959 Missing: Cytoplasmic localization. FT CONFLICT 111 111 G -> S (in Ref. 1 and 2). FT CONFLICT 378 378 R -> Q (in Ref. 5). SQ SEQUENCE 959 AA; 106057 MW; 7DA3097879701540 CRC64; MALLGKRCDV PTNGCGPDRW NSAFTRKDEI ITSLVSALDS MCSALSKLNA EVACVAVHDE SAFVVGTEKG RMFLNARKEL QSDFLRFCRG PPWKDPEAEH PKKVQRGEGG GRSLPRSSLE HGSDVYLLRK MVEEVFDVLY SEALGRASVV PLPYERLLRE PGLLAVQGLP EGLAFRRPAE YDPKALMAIL EHSHRIRFKL KRPLEDGGRD SKALVELNGV SLIPKGSRDC GLHGQAPKVP PQDLPPTATS SSMASFLYST ALPNHAIREL KQEAPSCPLA PSDLGLSRPM PEPKATGAQD FSDCCGQKPT GPGGPLIQNV HASKRILFSI VHDKSEKWDA FIKETEDINT LRECVQILFN SRYAEALGLD HMVPVPYRKI ACDPEAVEIV GIPDKIPFKR PCTYGVPKLK RILEERHSIH FIIKRMFDER IFTGNKFTKD TTKLEPASPP EDTSAEVSRA TVLDLAGNAR SDKGSMSEDC GPGTSGELGG LRPIKIEPED LDIIQVTVPD PSPTSEEMTD SMPGHLPSED SGYGMEMLTD KGLSEDARPE ERPVEDSHGD VIRPLRKQVE LLFNTRYAKA IGISEPVKVP YSKFLMHPEE LFVVGLPEGI SLRRPNCFGI AKLRKILEAS NSIQFVIKRP ELLTEGVKEP IMDSQGTASS LGFSPPALPP ERDSGDPLVD ESLKRQGFQE NYDARLSRID IANTLREQVQ DLFNKKYGEA LGIKYPVQVP YKRIKSNPGS VIIEGLPPGI PFRKPCTFGS QNLERILAVA DKIKFTVTRP FQGLIPKPDE DDANRLGEKV ILREQVKELF NEKYGEALGL NRPVLVPYKL IRDSPDAVEV TGLPDDIPFR NPNTYDIHRL EKILKAREHV RMVIINQLQP FAEICNDAKV PAKDSSIPKR KRKRVSEGNS VSSSSSSSSS SSSNPDSVAS ANQISLVQWP MYMVDYAGLN VQLPGPLNY //