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Protein

Transcription initiation factor TFIID subunit 12

Gene

Taf12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription (By similarity).By similarity

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. histone acetyltransferase activity Source: Ensembl
  3. sequence-specific DNA binding transcription factor activity Source: Ensembl
  4. transcription coactivator activity Source: MGI
  5. transcription factor binding Source: MGI

GO - Biological processi

  1. DNA-templated transcription, initiation Source: MGI
  2. histone H3 acetylation Source: MGI
  3. positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  4. regulation of nucleic acid-templated transcription Source: MGI
  5. transcription initiation from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_282911. RNA Polymerase II Pre-transcription Events.
REACT_283211. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_291621. HATs acetylate histones.
REACT_329615. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_342690. RNA Polymerase II Transcription Initiation.
REACT_349121. RNA Polymerase II Promoter Escape.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 12
Alternative name(s):
Transcription initiation factor TFIID 20 kDa subunits
Short name:
TAFII-20
Short name:
TAFII20
Gene namesi
Name:Taf12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1913714. Taf12.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: MGI
  2. PCAF complex Source: MGI
  3. STAGA complex Source: MGI
  4. transcription factor TFIID complex Source: MGI
  5. transcription factor TFTC complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161Transcription initiation factor TFIID subunit 12PRO_0000118908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphothreonineBy similarity
Modified residuei51 – 511Phosphoserine2 Publications
Modified residuei59 – 591PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8VE65.
PaxDbiQ8VE65.
PRIDEiQ8VE65.

PTM databases

PhosphoSiteiQ8VE65.

Expressioni

Gene expression databases

BgeeiQ8VE65.
ExpressionAtlasiQ8VE65. baseline and differential.
GenevestigatoriQ8VE65.

Interactioni

Subunit structurei

TFIID and PCAF are composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TBP is not part of TFTC. Interacts directly with TBP; additional interactions between TAFII20 and TAFII28 or TAFII30 were detected. Component of the PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3, TAF5L, SUPT3H, TAF6L, TAF9, TAF10, TAF12 and TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Interacts with ATF7 (via its transactivation domain); the interaction promotes the transactivation of ATF7 and is prevented by sumoylation of ATF7 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-29178N.
IntActiQ8VE65. 3 interactions.
MINTiMINT-4136826.

Structurei

3D structure databases

ProteinModelPortaliQ8VE65.
SMRiQ8VE65. Positions 55-128.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TAF12 family.Curated
Contains 1 histone-fold domain.Curated

Phylogenomic databases

eggNOGiCOG5624.
GeneTreeiENSGT00390000002144.
HOVERGENiHBG055174.
InParanoidiQ8VE65.
KOiK03126.
OrthoDBiEOG769ZMW.
PhylomeDBiQ8VE65.
TreeFamiTF323652.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR003228. TFIID_sub.
[Graphical view]
PfamiPF03847. TFIID_20kDa. 1 hit.
[Graphical view]
ProDomiPD012998. PD012998. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8VE65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQFGPSALI NLSSFSSVKP EPASTPPQGS MANSTTVGKI AGTPGTGGRL
60 70 80 90 100
SPENNQVLTK KKLQDLVREV DPNEQLDEDV EEMLLQIADD FIESVVTAAC
110 120 130 140 150
QLARHRKSST LEVKDVQLHL ERQWNMWIPG FGSEEIRPYK KACTTEAHKQ
160
RMALIRKTTK K
Length:161
Mass (Da):17,875
Last modified:February 28, 2002 - v1
Checksum:iB3C11D70B6E94E35
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771D → G in BAB28669 (PubMed:16141072).Curated
Sequence conflicti126 – 1261M → I in BAB28669 (PubMed:16141072).Curated
Sequence conflicti157 – 1571K → N in BAB25276 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007811 mRNA. Translation: BAB25276.1.
AK013133 mRNA. Translation: BAB28669.1.
AK132927 mRNA. Translation: BAE21426.1.
BC019668 mRNA. Translation: AAH19668.1.
CCDSiCCDS18721.1.
RefSeqiNP_079855.2. NM_025579.3.
XP_006539170.2. XM_006539107.2.
XP_006539172.1. XM_006539109.1.
XP_006539173.1. XM_006539110.1.
UniGeneiMm.331926.

Genome annotation databases

EnsembliENSMUST00000030731; ENSMUSP00000030731; ENSMUSG00000028899.
GeneIDi66464.
KEGGimmu:66464.
UCSCiuc008vax.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007811 mRNA. Translation: BAB25276.1.
AK013133 mRNA. Translation: BAB28669.1.
AK132927 mRNA. Translation: BAE21426.1.
BC019668 mRNA. Translation: AAH19668.1.
CCDSiCCDS18721.1.
RefSeqiNP_079855.2. NM_025579.3.
XP_006539170.2. XM_006539107.2.
XP_006539172.1. XM_006539109.1.
XP_006539173.1. XM_006539110.1.
UniGeneiMm.331926.

3D structure databases

ProteinModelPortaliQ8VE65.
SMRiQ8VE65. Positions 55-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29178N.
IntActiQ8VE65. 3 interactions.
MINTiMINT-4136826.

PTM databases

PhosphoSiteiQ8VE65.

Proteomic databases

MaxQBiQ8VE65.
PaxDbiQ8VE65.
PRIDEiQ8VE65.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030731; ENSMUSP00000030731; ENSMUSG00000028899.
GeneIDi66464.
KEGGimmu:66464.
UCSCiuc008vax.3. mouse.

Organism-specific databases

CTDi6883.
MGIiMGI:1913714. Taf12.

Phylogenomic databases

eggNOGiCOG5624.
GeneTreeiENSGT00390000002144.
HOVERGENiHBG055174.
InParanoidiQ8VE65.
KOiK03126.
OrthoDBiEOG769ZMW.
PhylomeDBiQ8VE65.
TreeFamiTF323652.

Enzyme and pathway databases

ReactomeiREACT_282911. RNA Polymerase II Pre-transcription Events.
REACT_283211. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_291621. HATs acetylate histones.
REACT_329615. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_342690. RNA Polymerase II Transcription Initiation.
REACT_349121. RNA Polymerase II Promoter Escape.

Miscellaneous databases

NextBioi321768.
PROiQ8VE65.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VE65.
ExpressionAtlasiQ8VE65. baseline and differential.
GenevestigatoriQ8VE65.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR003228. TFIID_sub.
[Graphical view]
PfamiPF03847. TFIID_20kDa. 1 hit.
[Graphical view]
ProDomiPD012998. PD012998. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Pancreas and Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTAF12_MOUSE
AccessioniPrimary (citable) accession number: Q8VE65
Secondary accession number(s): Q3V0S7, Q9CZ11, Q9D8Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2004
Last sequence update: February 28, 2002
Last modified: March 31, 2015
This is version 108 of the entry and version 1 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.