TF2AA_MOUSE
ID TF2AA_MOUSE Reviewed; 378 AA.
AC Q99PM3; Q8C812;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Transcription initiation factor IIA subunit 1;
DE AltName: Full=General transcription factor IIA subunit 1;
DE Contains:
DE RecName: Full=Transcription initiation factor IIA alpha chain;
DE AltName: Full=TFIIA p35 subunit;
DE Contains:
DE RecName: Full=Transcription initiation factor IIA beta chain;
DE AltName: Full=TFIIA p19 subunit;
GN Name=Gtf2a1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11159353; DOI=10.1095/biolreprod64.2.507;
RA Han S., Zhou L., Upadhyaya A.B., Lee S.H., Parker K.L., DeJong J.;
RT "TFIIAalpha/beta-like factor is encoded by a germ cell-specific gene whose
RT expression is up-regulated with other general transcription factors during
RT spermatogenesis in the mouse.";
RL Biol. Reprod. 64:507-517(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-378.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: TFIIA is a component of the transcription machinery of RNA
CC polymerase II and plays an important role in transcriptional
CC activation. TFIIA in a complex with TBP mediates transcriptional
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: TFIIA is a heterodimer of a unprocessed large subunit 1 and a
CC small subunit gamma. It was originally believed to be a heterotrimer of
CC an alpha, a beta and a gamma subunit. TFIIA forms a complex with TBP
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in pachytene spermatocytes and
CC spermatids. {ECO:0000269|PubMed:11159353}.
CC -!- INDUCTION: Up-regulated during germ cell differentiation in testis.
CC {ECO:0000269|PubMed:11159353}.
CC -!- PTM: The alpha and beta subunits are postranslationally produced from
CC the precursor form by TASP1. The cleavage promotes proteasomal
CC degradation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFIIA subunit 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33430.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF250834; AAG50431.1; -; mRNA.
DR EMBL; AK048711; BAC33430.1; ALT_INIT; mRNA.
DR CCDS; CCDS26089.1; -.
DR RefSeq; NP_113568.2; NM_031391.2.
DR RefSeq; NP_780544.1; NM_175335.3.
DR AlphaFoldDB; Q99PM3; -.
DR BioGRID; 219952; 25.
DR ComplexPortal; CPX-743; Transcription factor complex TFIIA.
DR IntAct; Q99PM3; 12.
DR MINT; Q99PM3; -.
DR STRING; 10090.ENSMUSP00000021345; -.
DR iPTMnet; Q99PM3; -.
DR PhosphoSitePlus; Q99PM3; -.
DR EPD; Q99PM3; -.
DR MaxQB; Q99PM3; -.
DR PaxDb; Q99PM3; -.
DR PRIDE; Q99PM3; -.
DR ProteomicsDB; 263289; -.
DR Antibodypedia; 76; 313 antibodies from 32 providers.
DR DNASU; 83602; -.
DR Ensembl; ENSMUST00000021345; ENSMUSP00000021345; ENSMUSG00000020962.
DR GeneID; 83602; -.
DR KEGG; mmu:83602; -.
DR UCSC; uc007okr.2; mouse.
DR CTD; 2957; -.
DR MGI; MGI:1933277; Gtf2a1.
DR VEuPathDB; HostDB:ENSMUSG00000020962; -.
DR eggNOG; KOG2652; Eukaryota.
DR GeneTree; ENSGT00940000156726; -.
DR HOGENOM; CLU_030027_5_0_1; -.
DR InParanoid; Q99PM3; -.
DR OMA; EVCDASQ; -.
DR OrthoDB; 1443035at2759; -.
DR PhylomeDB; Q99PM3; -.
DR TreeFam; TF350445; -.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 83602; 15 hits in 70 CRISPR screens.
DR ChiTaRS; Gtf2a1; mouse.
DR PRO; PR:Q99PM3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q99PM3; protein.
DR Bgee; ENSMUSG00000020962; Expressed in animal zygote and 263 other tissues.
DR ExpressionAtlas; Q99PM3; baseline and differential.
DR Genevisible; Q99PM3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005672; C:transcription factor TFIIA complex; IDA:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR GO; GO:0097550; C:transcription preinitiation complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 2.30.18.10; -; 1.
DR InterPro; IPR004855; TFIIA_asu/bsu.
DR InterPro; IPR009088; TFIIA_b-brl.
DR PANTHER; PTHR12694; PTHR12694; 1.
DR Pfam; PF03153; TFIIA; 2.
DR SMART; SM01371; TFIIA; 1.
DR SUPFAM; SSF50784; SSF50784; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52655"
FT CHAIN 2..378
FT /note="Transcription initiation factor IIA subunit 1"
FT /id="PRO_0000042595"
FT CHAIN 2..276
FT /note="Transcription initiation factor IIA alpha chain"
FT /id="PRO_0000042596"
FT CHAIN 277..378
FT /note="Transcription initiation factor IIA beta chain"
FT /id="PRO_0000042597"
FT REGION 69..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..331
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 276..277
FT /note="Cleavage; by TASP1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52655"
FT MOD_RES 282
FT /note="Phosphoserine; by TAF1"
FT /evidence="ECO:0000250|UniProtKB:P52655"
FT MOD_RES 283
FT /note="Phosphoserine; by TAF1"
FT /evidence="ECO:0000250|UniProtKB:P52655"
FT MOD_RES 318
FT /note="Phosphoserine; by TAF1"
FT /evidence="ECO:0000250|UniProtKB:P52655"
FT MOD_RES 323
FT /note="Phosphoserine; by TAF1"
FT /evidence="ECO:0000250|UniProtKB:P52655"
FT CONFLICT 121
FT /note="V -> G (in Ref. 1; AAG50431)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="D -> G (in Ref. 1; AAG50431)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="T -> A (in Ref. 1; AAG50431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 41614 MW; FE28AA688662457E CRC64;
MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH
SEEQQLLLQV QQQHQPQQQQ HHHHHHQHQQ AQPQQTVPQQ AQTQQVLIPA SQQATAPQVI
VPDSKLLQHM NASSITSAAA TAATLALPAG VTPVQQLLTN SGQLLQVVRA ANGAQYILQP
QQSVVLQQQV IPQMQPGGVQ APVIQQVLAP LPGGISPQTG VIIQPQQILF TGNKTQVIPT
TVAAPAPAQA PMPAAGQQQP QAQPAQQQAP LVLQVDGTGD TSSEEDEDEE EDYDDDEEED
KEKDGAEDGQ VEEEPLNSED DVSDEEGQEL FDTENVVVCQ YDKIHRSKNK WKFHLKDGIM
NLNGRDYIFS KAIGDAEW
