GTF2I_BOVIN
ID GTF2I_BOVIN Reviewed; 978 AA.
AC A7MB80;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=General transcription factor II-I;
DE Short=GTFII-I;
DE Short=TFII-I;
GN Name=GTF2I;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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. Required for the formation of functional ARID3A DNA-
CC binding complexes and for activation of immunoglobulin heavy-chain
CC transcription upon B-lymphocyte activation (By similarity).
CC {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). May be a component of a BHC histone
CC deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A,
CC RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC Interacts with ARID3A. Interacts with isoform beta of PRKG1 (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Colocalizes with BTK in
CC the cytoplasm. {ECO:0000250}.
CC -!- PTM: Transiently phosphorylated on tyrosine residues by BTK in response
CC to B-cell receptor stimulation. Phosphorylation on Tyr-248 and Tyr-377,
CC and perhaps, on Tyr-482 contributes to BTK-mediated transcriptional
CC activation.
CC -!- PTM: Sumoylated.
CC -!- SIMILARITY: Belongs to the TFII-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00484}.
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DR EMBL; BC151387; AAI51388.1; -; mRNA.
DR RefSeq; NP_001095647.1; NM_001102177.1.
DR AlphaFoldDB; A7MB80; -.
DR SMR; A7MB80; -.
DR STRING; 9913.ENSBTAP00000012904; -.
DR PaxDb; A7MB80; -.
DR PRIDE; A7MB80; -.
DR Ensembl; ENSBTAT00000012904; ENSBTAP00000012904; ENSBTAG00000009780.
DR Ensembl; ENSBTAT00000074577; ENSBTAP00000058347; ENSBTAG00000009780.
DR GeneID; 534669; -.
DR KEGG; bta:534669; -.
DR CTD; 2969; -.
DR VEuPathDB; HostDB:ENSBTAG00000009780; -.
DR VGNC; VGNC:29699; GTF2I.
DR eggNOG; ENOG502QWD0; Eukaryota.
DR GeneTree; ENSGT00940000160349; -.
DR HOGENOM; CLU_011773_0_0_1; -.
DR InParanoid; A7MB80; -.
DR OrthoDB; 115381at2759; -.
DR TreeFam; TF352524; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000009780; Expressed in thyroid gland and 109 other tissues.
DR ExpressionAtlas; A7MB80; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW 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..978
FT /note="General transcription factor II-I"
FT /id="PRO_0000343748"
FT REPEAT 103..197
FT /note="GTF2I-like 1"
FT REPEAT 331..425
FT /note="GTF2I-like 2"
FT REPEAT 436..530
FT /note="GTF2I-like 3"
FT REPEAT 541..635
FT /note="GTF2I-like 4"
FT REPEAT 703..797
FT /note="GTF2I-like 5"
FT REPEAT 839..933
FT /note="GTF2I-like 6"
FT REGION 208..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 299..306
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 667..692
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 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
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 332
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8"
FT MOD_RES 377
FT /note="Phosphotyrosine; by BTK"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 391
FT /note="Phosphoserine; by PKG/PRKG1"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 429
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8"
FT MOD_RES 482
FT /note="Phosphotyrosine; by BTK"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 535
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 694
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 763
FT /note="Phosphoserine; by PKG/PRKG1"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT MOD_RES 803
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 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 322
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 429
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 540
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 643
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 694
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 795
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 807
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 841
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 844
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 859
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 871
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 971
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
FT CROSSLNK 971
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P78347"
SQ SEQUENCE 978 AA; 110125 MW; 3B919D92F149AF88 CRC64;
MAQVAVSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE
RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTAQAN RMSVDAVEIE TLRKTVEDYF
CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI
SFIIKRPFLE PKKHLGGRVM VTDAERSMIS PSGSCGPVKV KTEPSEDSGI SLEMAAVTVK
EESEDPDYYQ YNIQAGPSET DDVDDKLPLS KSLQGSHHSS EGNEGTEMEV PAEDDDYPPP
AKRPKSSEPP QPPVTEPANA GKRKVREFNF EKWNARITDL RKQVEELFER KYAQAIKAKG
PVTIPYPLFQ SHVEDLYVEG LPEGIPFRRP STYGIPRLER ILLAKERIRF VIKKHELLNS
TREDLQLDKP ASGVKEEWYA RITKLRKMVD QLFCKKFAEA LGSTEAKAVP YQKFEAHPND
LYVEGLPENI PFRSPSWYGI PRLEKIIQVG NRIKFVIKRP ELLTHSTTEV TQPRTNTPVK
EDWNVRITKL RKQVEEIFNL KFAQALGLTE AVKVPYPVFE SNPEFLYVEG LPEGIPFRSP
TWFGIPRLER IVRGSNKIKF VVKKPELVIS YLPPGMASKI NTKALQSPKR PRSPGSNSKV
PEIEVTVEGP NNSNPQTSAV RTPTQTNGSN VPFKPRGREF SFEAWNAKIT DLKQKVENLF
NEKCGEALGL KQAVKVPFAL FESFPEDFYV EGLPEGVPFR RPSTFGIPRL EKILRNKAKI
KFIIKKPEMF ETAIKESTSS SKSPPRKINS SPSVNTTASG VEDLNIIQVT IPDDDNERLS
KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN PGCVVVDGMP PGVSFKAPSY
LEISSMRRIL DSAEFIKFTV IRPFPGLVIN NQLVDQNESE GPVIQESAEP TQLEVPATEE
IKETDGNSQI KQEPDPTW
