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Protein

Transcription initiation factor IIA subunit 1

Gene

Gtf2a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei276 – 2772Cleavage; by TASP1

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. protein heterodimerization activity Source: MGI
  3. RNA polymerase II repressing transcription factor binding Source: MGI
  4. TBP-class protein binding Source: MGI
  5. transcription factor binding Source: MGI

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription from RNA polymerase II promoter Source: MGI
  3. transcription initiation from RNA polymerase II promoter Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_230204. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_232708. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_244380. RNA Polymerase II Transcription Initiation.
REACT_255009. RNA Polymerase II Pre-transcription Events.
REACT_255334. RNA Polymerase II Promoter Escape.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor IIA subunit 1
Alternative name(s):
General transcription factor IIA subunit 1
Cleaved into the following 2 chains:
Alternative name(s):
TFIIA p35 subunit
Alternative name(s):
TFIIA p19 subunit
Gene namesi
Name:Gtf2a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1933277. Gtf2a1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleoplasm Source: MGI
  3. nucleus Source: MGI
  4. transcription factor TFIIA complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 378377Transcription initiation factor IIA subunit 1PRO_0000042595Add
BLAST
Chaini2 – 276275Transcription initiation factor IIA alpha chainPRO_0000042596Add
BLAST
Chaini277 – 378102Transcription initiation factor IIA beta chainPRO_0000042597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei282 – 2821Phosphoserine; by TAF1By similarity
Modified residuei283 – 2831Phosphoserine; by TAF1By similarity
Modified residuei318 – 3181Phosphoserine; by TAF1By similarity
Modified residuei323 – 3231Phosphoserine; by TAF1By similarity

Post-translational modificationi

The alpha and beta subunits are postranslationally produced from the precursor form by TASP1. The cleavage promotes proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99PM3.
PaxDbiQ99PM3.
PRIDEiQ99PM3.

PTM databases

PhosphoSiteiQ99PM3.

Expressioni

Tissue specificityi

Expressed in pachytene spermatocytes and spermatids.1 Publication

Inductioni

Up-regulated during germ cell differentiation in testis.1 Publication

Gene expression databases

BgeeiQ99PM3.
CleanExiMM_GTF2A1.
ExpressionAtlasiQ99PM3. baseline and differential.
GenevestigatoriQ99PM3.

Interactioni

Subunit structurei

TFIIA is a heterodimer of a unprocessed large subunit 1 and a small subunit gamma. It was originally believed to be a heterotrimer of an alpha, a beta and a gamma subunit. TFIIA forms a complex with TBP (By similarity).By similarity

Protein-protein interaction databases

BioGridi219952. 13 interactions.
MINTiMINT-1348159.

Structurei

3D structure databases

ProteinModelPortaliQ99PM3.
SMRiQ99PM3. Positions 9-51, 332-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi71 – 8010Poly-Gln
Compositional biasi81 – 888Poly-His

Sequence similaritiesi

Belongs to the TFIIA subunit 1 family.Curated

Phylogenomic databases

eggNOGiCOG5149.
GeneTreeiENSGT00530000063152.
HOGENOMiHOG000015236.
HOVERGENiHBG052771.
InParanoidiQ99PM3.
KOiK03122.
OMAiKAPRFAS.
OrthoDBiEOG7KWSJM.
PhylomeDBiQ99PM3.
TreeFamiTF350445.

Family and domain databases

Gene3Di1.10.287.100. 1 hit.
2.30.18.10. 1 hit.
InterProiIPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view]
PANTHERiPTHR12694. PTHR12694. 1 hit.
PfamiPF03153. TFIIA. 1 hit.
[Graphical view]
SUPFAMiSSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99PM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL
60 70 80 90 100
MQSRAVDGFH SEEQQLLLQV QQQHQPQQQQ HHHHHHQHQQ AQPQQTVPQQ
110 120 130 140 150
AQTQQVLIPA SQQATAPQVI VPDSKLLQHM NASSITSAAA TAATLALPAG
160 170 180 190 200
VTPVQQLLTN SGQLLQVVRA ANGAQYILQP QQSVVLQQQV IPQMQPGGVQ
210 220 230 240 250
APVIQQVLAP LPGGISPQTG VIIQPQQILF TGNKTQVIPT TVAAPAPAQA
260 270 280 290 300
PMPAAGQQQP QAQPAQQQAP LVLQVDGTGD TSSEEDEDEE EDYDDDEEED
310 320 330 340 350
KEKDGAEDGQ VEEEPLNSED DVSDEEGQEL FDTENVVVCQ YDKIHRSKNK
360 370
WKFHLKDGIM NLNGRDYIFS KAIGDAEW
Length:378
Mass (Da):41,614
Last modified:June 7, 2005 - v2
Checksum:iFE28AA688662457E
GO

Sequence cautioni

The sequence BAC33430.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211V → G in AAG50431 (PubMed:11159353).Curated
Sequence conflicti324 – 3241D → G in AAG50431 (PubMed:11159353).Curated
Sequence conflicti333 – 3331T → A in AAG50431 (PubMed:11159353).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250834 mRNA. Translation: AAG50431.1.
AK048711 mRNA. Translation: BAC33430.1. Different initiation.
CCDSiCCDS26089.1.
RefSeqiNP_113568.2. NM_031391.2.
NP_780544.1. NM_175335.3.
UniGeneiMm.275728.
Mm.432242.

Genome annotation databases

EnsembliENSMUST00000021345; ENSMUSP00000021345; ENSMUSG00000020962.
GeneIDi83602.
KEGGimmu:83602.
UCSCiuc007okr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250834 mRNA. Translation: AAG50431.1.
AK048711 mRNA. Translation: BAC33430.1. Different initiation.
CCDSiCCDS26089.1.
RefSeqiNP_113568.2. NM_031391.2.
NP_780544.1. NM_175335.3.
UniGeneiMm.275728.
Mm.432242.

3D structure databases

ProteinModelPortaliQ99PM3.
SMRiQ99PM3. Positions 9-51, 332-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219952. 13 interactions.
MINTiMINT-1348159.

PTM databases

PhosphoSiteiQ99PM3.

Proteomic databases

MaxQBiQ99PM3.
PaxDbiQ99PM3.
PRIDEiQ99PM3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021345; ENSMUSP00000021345; ENSMUSG00000020962.
GeneIDi83602.
KEGGimmu:83602.
UCSCiuc007okr.2. mouse.

Organism-specific databases

CTDi2957.
MGIiMGI:1933277. Gtf2a1.

Phylogenomic databases

eggNOGiCOG5149.
GeneTreeiENSGT00530000063152.
HOGENOMiHOG000015236.
HOVERGENiHBG052771.
InParanoidiQ99PM3.
KOiK03122.
OMAiKAPRFAS.
OrthoDBiEOG7KWSJM.
PhylomeDBiQ99PM3.
TreeFamiTF350445.

Enzyme and pathway databases

ReactomeiREACT_230204. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_232708. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_244380. RNA Polymerase II Transcription Initiation.
REACT_255009. RNA Polymerase II Pre-transcription Events.
REACT_255334. RNA Polymerase II Promoter Escape.

Miscellaneous databases

NextBioi350672.
PROiQ99PM3.
SOURCEiSearch...

Gene expression databases

BgeeiQ99PM3.
CleanExiMM_GTF2A1.
ExpressionAtlasiQ99PM3. baseline and differential.
GenevestigatoriQ99PM3.

Family and domain databases

Gene3Di1.10.287.100. 1 hit.
2.30.18.10. 1 hit.
InterProiIPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view]
PANTHERiPTHR12694. PTHR12694. 1 hit.
PfamiPF03153. TFIIA. 1 hit.
[Graphical view]
SUPFAMiSSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TFIIAalpha/beta-like factor is encoded by a germ cell-specific gene whose expression is up-regulated with other general transcription factors during spermatogenesis in the mouse."
    Han S., Zhou L., Upadhyaya A.B., Lee S.H., Parker K.L., DeJong J.
    Biol. Reprod. 64:507-517(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-378.
    Strain: C57BL/6J.
    Tissue: Cerebellum.

Entry informationi

Entry nameiTF2AA_MOUSE
AccessioniPrimary (citable) accession number: Q99PM3
Secondary accession number(s): Q8C812
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: March 4, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.