GTF2I_RAT
ID GTF2I_RAT Reviewed; 979 AA.
AC Q5U2Y1; Q80SX4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=General transcription factor II-I;
DE Short=GTFII-I;
DE Short=TFII-I;
GN Name=Gtf2i;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=DA, and E3;
RX PubMed=12461526; DOI=10.1038/ng1058;
RA Olofsson P., Holmberg J., Tordsson J., Lu S., Akerstrom B., Holmdahl R.;
RT "Positional identification of Ncf1 as a gene that regulates arthritis
RT severity in rats.";
RL Nat. Genet. 33:25-32(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Interacts with the basal transcription machinery by
CC coordinating the formation of a multiprotein complex at the C-FOS
CC promoter, and linking specific signal responsive activator complexes.
CC Promotes the formation of stable high-order complexes of SRF and PHOX1
CC and interacts cooperatively with PHOX1 to promote serum-inducible
CC transcription of a reporter gene deriven by the C-FOS serum response
CC element (SRE). Acts as a coregulator for USF1 by binding independently
CC two promoter elements, a pyrimidine-rich initiator (Inr) and an
CC upstream E-box (By similarity). Required for the formation of
CC functional ARID3A DNA-binding complexes and for activation of
CC immunoglobulin heavy-chain transcription upon B-lymphocyte activation
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (Potential). Interacts with SRF and PHOX1. Binds a
CC pyrimidine-rich initiator (Inr) and a recognition site (E-box) for
CC upstream stimulatory factor 1 (USF1). Associates with the PH domain of
CC Bruton's tyrosine kinase (BTK) (By similarity). May be a component of a
CC BHC histone deacetylase complex that contains HDAC1, HDAC2,
CC HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3,
CC GSE1 and GTF2I. Interacts with BTK and ARID3A (By similarity).
CC Interacts with isoform beta of PRKG1 (By similarity). {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Colocalizes with BTK in
CC the cytoplasm. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5U2Y1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5U2Y1-2; Sequence=VSP_034698;
CC -!- PTM: Transiently phosphorylated on tyrosine residues by BTK in response
CC to B-cell receptor stimulation. Phosphorylation on Tyr-248 and Tyr-379,
CC and perhaps, on Tyr-484 contributes to BTK-mediated transcriptional
CC activation (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFII-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00484}.
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DR EMBL; AF547390; AAO32678.1; -; mRNA.
DR EMBL; AF547391; AAO32679.1; -; mRNA.
DR EMBL; BC085815; AAH85815.1; -; mRNA.
DR RefSeq; NP_001001512.2; NM_001001512.2. [Q5U2Y1-2]
DR RefSeq; XP_017453850.1; XM_017598361.1. [Q5U2Y1-1]
DR AlphaFoldDB; Q5U2Y1; -.
DR SMR; Q5U2Y1; -.
DR BioGRID; 261874; 2.
DR IntAct; Q5U2Y1; 1.
DR STRING; 10116.ENSRNOP00000002020; -.
DR iPTMnet; Q5U2Y1; -.
DR PhosphoSitePlus; Q5U2Y1; -.
DR jPOST; Q5U2Y1; -.
DR PaxDb; Q5U2Y1; -.
DR PRIDE; Q5U2Y1; -.
DR Ensembl; ENSRNOT00000002020; ENSRNOP00000002020; ENSRNOG00000001479. [Q5U2Y1-1]
DR Ensembl; ENSRNOT00000040356; ENSRNOP00000040835; ENSRNOG00000001479. [Q5U2Y1-2]
DR GeneID; 353256; -.
DR KEGG; rno:353256; -.
DR UCSC; RGD:727961; rat. [Q5U2Y1-1]
DR CTD; 2969; -.
DR RGD; 727961; Gtf2i.
DR eggNOG; ENOG502QWD0; Eukaryota.
DR GeneTree; ENSGT00940000160349; -.
DR HOGENOM; CLU_011773_0_0_1; -.
DR InParanoid; Q5U2Y1; -.
DR PhylomeDB; Q5U2Y1; -.
DR PRO; PR:Q5U2Y1; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001479; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; Q5U2Y1; baseline and differential.
DR Genevisible; Q5U2Y1; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0100026; P:positive regulation of DNA repair by transcription from RNA polymerase II promoter; ISO:RGD.
DR Gene3D; 3.90.1460.10; -; 6.
DR InterPro; IPR004212; GTF2I.
DR InterPro; IPR036647; GTF2I-like_rpt_sf.
DR InterPro; IPR016659; TF_II-I.
DR Pfam; PF02946; GTF2I; 6.
DR PIRSF; PIRSF016441; TF_II-I; 1.
DR SUPFAM; SSF117773; SSF117773; 6.
DR PROSITE; PS51139; GTF2I; 6.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CHAIN 2..979
FT /note="General transcription factor II-I"
FT /id="PRO_0000343749"
FT REPEAT 103..197
FT /note="GTF2I-like 1"
FT REPEAT 333..427
FT /note="GTF2I-like 2"
FT REPEAT 438..532
FT /note="GTF2I-like 3"
FT REPEAT 543..637
FT /note="GTF2I-like 4"
FT REPEAT 705..799
FT /note="GTF2I-like 5"
FT REPEAT 840..934
FT /note="GTF2I-like 6"
FT REGION 205..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 300..307
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 304..320
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 130
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 248
FT /note="Phosphotyrosine; by BTK"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 334
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8"
FT MOD_RES 379
FT /note="Phosphotyrosine; by BTK"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 393
FT /note="Phosphoserine; by PKG/PRKG1"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 431
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8"
FT MOD_RES 484
FT /note="Phosphotyrosine; by BTK"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8"
FT MOD_RES 539
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 696
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 765
FT /note="Phosphoserine; by PKG/PRKG1"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 475
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 507
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 542
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 641
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 651
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 661
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 696
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 808
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 842
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 845
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 860
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 872
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 972
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 972
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT VAR_SEQ 229..294
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034698"
FT MOD_RES Q5U2Y1-2:228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 979 AA; 110215 MW; 82D35A08122C210D CRC64;
MAQVAMSALP AEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE
RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKCTTQAN RMSVDAVEIE TLRKTVEDYF
CFCYGKALGK STVVPVPYEK MLRDQSAVAV QGLPEGVAFK HPEHYDLATL KWILENKAGI
SFIIKRPFLE PKKHLGGRVM AADADRPMLS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK
EESEDPDYYQ YNIQGSHHSS EGNEGAEVEV PAEDSTQHVP SETSEDPEVE VTIEDDDYSP
PTKRPKSSEP PPPPPVPEPT NAGKRKVREF NFEKWNARIT DLRKQVEELF ERKYAQAIKA
KGPVTIPYPL FQSHVEDLYV EGLPEGIPFR RPSTYGIPRL ERILLAKERI RFVIKKHELL
NSTREDLQLD KPASGVKEEW YARITKLRKM VDQLFCKKFA EALGSTEAKA VPYQKFEAYP
NDLYVEGLPE NIPFRSPSWY GIPRLEKIIQ VGNRIKFVIK RPELLTHSTT EVTQPRTNTP
VKEDWNVRIT KLRKQVEEIF NLKFAQALGL TEAVKVPYPV FESNPEFLYV EGLPEGIPFR
SPTWFGIPRL ERIVRGSNKI KFVVKKPELV VSYLPPGMAS KINTKALQSP KRPRSPGSNS
KVPEIEVTVE GPNNNSPQTS TVRTPTQTNG SNVPFKPRGR EFSFEAWNAK ITDLKQKVEN
LFNEKCGEAL GLKQAVKVPF ALFESFPEDF YVEGLPEGVP FRRPSTFGIP RLEKILRNKA
KIKFIIKKPE MFETAIKEST SSKSPPRKTN SSPSVNTTAS GVEDLNIIQV TIPDDDNERL
SKVEKARQLR EQVNDLFSRK FGEAIGMGFP VKVPYRKITI NPGCVVVDGM PPGVSFKAPS
YLEISSMRRI LDSAEFIKFT VIRPFPGLVI NNQLVDQNES EGPVIQESAE ASQLEVPATE
EIKETDGSSQ IKQEPDPTW
