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Q99PM3 (TF2AA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription initiation factor IIA subunit 1
Alternative name(s):
General transcription factor IIA subunit 1

Cleaved into the following 2 chains:

  1. Transcription initiation factor IIA alpha chain
    Alternative name(s):
    TFIIA p35 subunit
  2. Transcription initiation factor IIA beta chain
    Alternative name(s):
    TFIIA p19 subunit
Gene names
Name:Gtf2a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in pachytene spermatocytes and spermatids. Ref.1

Induction

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

Post-translational modification

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

Sequence similarities

Belongs to the TFIIA subunit 1 family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 378377Transcription initiation factor IIA subunit 1
PRO_0000042595
Chain2 – 276275Transcription initiation factor IIA alpha chain
PRO_0000042596
Chain277 – 378102Transcription initiation factor IIA beta chain
PRO_0000042597

Regions

Compositional bias71 – 8010Poly-Gln
Compositional bias81 – 888Poly-His

Sites

Site276 – 2772Cleavage; by TASP1

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2821Phosphoserine; by TAF1 By similarity
Modified residue2831Phosphoserine; by TAF1 By similarity
Modified residue3181Phosphoserine; by TAF1 By similarity
Modified residue3231Phosphoserine; by TAF1 By similarity

Experimental info

Sequence conflict1211V → G in AAG50431. Ref.1
Sequence conflict3241D → G in AAG50431. Ref.1
Sequence conflict3331T → A in AAG50431. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99PM3 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: FE28AA688662457E

FASTA37841,614
        10         20         30         40         50         60 
MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH 

        70         80         90        100        110        120 
SEEQQLLLQV QQQHQPQQQQ HHHHHHQHQQ AQPQQTVPQQ AQTQQVLIPA SQQATAPQVI 

       130        140        150        160        170        180 
VPDSKLLQHM NASSITSAAA TAATLALPAG VTPVQQLLTN SGQLLQVVRA ANGAQYILQP 

       190        200        210        220        230        240 
QQSVVLQQQV IPQMQPGGVQ APVIQQVLAP LPGGISPQTG VIIQPQQILF TGNKTQVIPT 

       250        260        270        280        290        300 
TVAAPAPAQA PMPAAGQQQP QAQPAQQQAP LVLQVDGTGD TSSEEDEDEE EDYDDDEEED 

       310        320        330        340        350        360 
KEKDGAEDGQ VEEEPLNSED DVSDEEGQEL FDTENVVVCQ YDKIHRSKNK WKFHLKDGIM 

       370 
NLNGRDYIFS KAIGDAEW 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF250834 mRNA. Translation: AAG50431.1.
AK048711 mRNA. Translation: BAC33430.1. Different initiation.
CCDSCCDS26089.1.
RefSeqNP_113568.2. NM_031391.2.
NP_780544.1. NM_175335.3.
UniGeneMm.275728.
Mm.432242.

3D structure databases

ProteinModelPortalQ99PM3.
SMRQ99PM3. Positions 9-51, 332-378.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid219952. 13 interactions.
MINTMINT-1348159.

PTM databases

PhosphoSiteQ99PM3.

Proteomic databases

MaxQBQ99PM3.
PaxDbQ99PM3.
PRIDEQ99PM3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021345; ENSMUSP00000021345; ENSMUSG00000020962.
GeneID83602.
KEGGmmu:83602.
UCSCuc007okr.2. mouse.

Organism-specific databases

CTD2957.
MGIMGI:1933277. Gtf2a1.

Phylogenomic databases

eggNOGCOG5149.
GeneTreeENSGT00530000063152.
HOGENOMHOG000015236.
HOVERGENHBG052771.
InParanoidQ99PM3.
KOK03122.
OMAHMSATGM.
OrthoDBEOG7KWSJM.
PhylomeDBQ99PM3.
TreeFamTF350445.

Gene expression databases

ArrayExpressQ99PM3.
BgeeQ99PM3.
CleanExMM_GTF2A1.
GenevestigatorQ99PM3.

Family and domain databases

Gene3D1.10.287.100. 1 hit.
2.30.18.10. 1 hit.
InterProIPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view]
PANTHERPTHR12694. PTHR12694. 1 hit.
PfamPF03153. TFIIA. 1 hit.
[Graphical view]
SUPFAMSSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.
ProtoNetSearch...

Other

NextBio350672.
PROQ99PM3.
SOURCESearch...

Entry information

Entry nameTF2AA_MOUSE
AccessionPrimary (citable) accession number: Q99PM3
Secondary accession number(s): Q8C812
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot