Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P21675 (TAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription initiation factor TFIID subunit 1

EC=2.3.1.48
EC=2.7.11.1
Alternative name(s):
Cell cycle gene 1 protein
TBP-associated factor 250 kDa
Short name=p250
Transcription initiation factor TFIID 250 kDa subunit
Short name=TAF(II)250
Short name=TAFII-250
Short name=TAFII250
Gene names
Name:TAF1
Synonyms:BA2R, CCG1, CCGS, TAF2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1872 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Largest component and core scaffold of the TFIID basal transcription factor complex. Contains novel N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on Ser residues. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Exhibits histone acetyltransferase activity towards histones H3 and H4. Ref.1 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17 Ref.20

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Cofactor

Magnesium.

Enzyme regulation

Autophosphorylates on Ser residues. Inhibited by retinoblastoma tumor suppressor protein, RB1. Binding to TAF1 or CIITA inhibits the histone acetyltransferase activity. Ref.26

Subunit structure

TAF1 is the largest component of transcription factor TFIID that is composed of TBP and a variety of TBP-associated factors. TAF1, when part of the TFIID complex, interacts with C-terminus of TP53. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. RB1 interacts with the N-terminal domain of TAF1. Interacts with ASF1A and ASF1B. Interacts with SV40 Large T antigen. Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H1.4, H2A, H2B, H3 and H4 (in vitro). Ref.3 Ref.13 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.29

Subcellular location

Nucleus Ref.1.

Post-translational modification

Phosphorylated by casein kinase II in vitro. Ref.12

Involvement in disease

Dystonia 3, torsion, X-linked (DYT3) [MIM:314250]: A X-linked dystonia-parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT3 is characterized by severe progressive torsion dystonia followed by parkinsonism. It has a well-defined pathology of extensive neuronal loss and mosaic gliosis in the striatum (caudate nucleus and putamen) which appears to resemble that in Huntington disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.8

Miscellaneous

Isoforms including the downstream (d) exons are preferencially expressed in brain, and may play a role in the regulation of genes involved in dopamine processing and transport.

Sequence similarities

Belongs to the TAF1 family.

Contains 2 bromo domains.

Contains 1 HMG box DNA-binding domain.

Contains 2 protein kinase domains.

Ontologies

Keywords
   Biological processCell cycle
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDystonia
Parkinsonism
   DomainBromodomain
Repeat
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionAcyltransferase
Kinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA-templated transcription, initiation

Inferred from sequence or structural similarity. Source: BHF-UCL

RNA polymerase II transcriptional preinitiation complex assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to DNA damage stimulus

Inferred by curator Ref.20. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

histone acetylation

Inferred from direct assay PubMed 8980232. Source: GOC

peptidyl-serine phosphorylation

Inferred from direct assay Ref.12. Source: BHF-UCL

peptidyl-threonine phosphorylation

Inferred from direct assay Ref.20. Source: BHF-UCL

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.20. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17996705. Source: BHF-UCL

positive regulation of transcription initiation from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

protein autophosphorylation

Traceable author statement Ref.20. Source: UniProtKB

regulation of transcription involved in G2/M transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentMLL1 complex

Inferred from direct assay Ref.21. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor TFIID complex

Inferred from direct assay Ref.12. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

TBP-class protein binding

Inferred from physical interaction Ref.14. Source: BHF-UCL

histone acetyltransferase activity

Inferred from direct assay PubMed 8980232. Source: UniProtKB

lysine-acetylated histone binding

Inferred from direct assay PubMed 17996705. Source: BHF-UCL

p53 binding

Inferred from physical interaction Ref.20. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 7590250PubMed 7667268Ref.3PubMed 7729427PubMed 7824954Ref.15. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.12. Source: UniProtKB

sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription coactivator activity

Inferred from direct assay PubMed 17996705. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction Ref.12. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P032553EBI-491289,EBI-2603114From a different organism.
GTF2F1P352693EBI-491289,EBI-457886
TBPP202265EBI-491289,EBI-355371

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]

Note: the TAF1/DYT3 multiple transcript system is composed of 38 evolutionary conserved exons plus 5 downstream exons referred to as exons d1-d5 that are primate-specific. Multiple highly polymorphic variants can be generated by splicing exons d3 and d4 to various combinations of exons 1-37.
Isoform 1 (identifier: P21675-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P21675-2)

The sequence of this isoform differs from the canonical sequence as follows:
     177-177: G → GVSENGEGIILPSIIAPSSLAS
Isoform 3 (identifier: P21675-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1684-1686: Missing.
     1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ
Note: Contains a phosphoserine at position 1697.
Isoform 4 (identifier: P21675-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP
Note: Contains a phosphoserine at position 1700.
Isoform 2a (identifier: P21675-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ
Note: Contains a phosphoserine at position 1700.
Isoform 2c (identifier: P21675-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ
Isoform 2d (identifier: P21675-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1645-1645: Q → QAK
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ
Isoform 2e (identifier: P21675-8)

Also known as: 2F;

The sequence of this isoform differs from the canonical sequence as follows:
     1585-1592: PESQYTKT → YMCTTCRT
     1593-1872: Missing.
Isoform 2g (identifier: P21675-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1645-1645: Q → QAK
     1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ
Note: Contains a phosphoserine at position 1702.
Isoform 2h (identifier: P21675-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1525-1528: SWPF → IITK
     1529-1872: Missing.
Isoform 2i (identifier: P21675-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1525-1540: SWPFHHPVNKKFVPDY → VSCLCAKYFLAISSPS
     1541-1872: Missing.
Isoform N-TAF1 (identifier: P21675-12)

Also known as: TA14-391;

The sequence of this isoform differs from the canonical sequence as follows:
     177-177: G → GVSENGEGIILPSIIAPSSLAS
     1645-1645: Q → QAK
Note: Only detected in brain, highest expression in the caudate nucleus.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18721872Transcription initiation factor TFIID subunit 1
PRO_0000211215

Regions

Domain1 – 414414Protein kinase 1
Domain1397 – 146771Bromo 1
Domain1425 – 1872448Protein kinase 2
Domain1520 – 159071Bromo 2
DNA binding1195 – 127379HMG box
Region517 – 976460Histone acetyltransferase (HAT)
Region1342 – 1629288Interaction with ASF1A and ASF1B
Motif1351 – 13588Nuclear localization signal Potential
Compositional bias157 – 1659Pro-rich
Compositional bias1627 – 1872246Asp/Glu-rich (acidic tail)

Amino acid modifications

Modified residue1371Phosphoserine; by autocatalysis Ref.12
Modified residue3071Phosphoserine; by autocatalysis Ref.12
Modified residue5441N6-acetyllysine By similarity
Modified residue18261Phosphoserine Ref.24
Disulfide bond1364 ↔ 1619

Natural variations

Alternative sequence1771G → GVSENGEGIILPSIIAPSSL AS in isoform 2 and isoform N-TAF1.
VSP_012362
Alternative sequence1525 – 154016SWPFH…FVPDY → VSCLCAKYFLAISSPS in isoform 2i.
VSP_053376
Alternative sequence1525 – 15284SWPF → IITK in isoform 2h.
VSP_053375
Alternative sequence1529 – 1872344Missing in isoform 2h.
VSP_053377
Alternative sequence1541 – 1872332Missing in isoform 2i.
VSP_053378
Alternative sequence1585 – 15928PESQYTKT → YMCTTCRT in isoform 2e.
VSP_053379
Alternative sequence1593 – 1872280Missing in isoform 2e.
VSP_053380
Alternative sequence16451Q → QAK in isoform 2d, isoform 2g and isoform N-TAF1.
VSP_053381
Alternative sequence1684 – 16863Missing in isoform 3.
VSP_053382
Alternative sequence16871Q → QMRQGRGRLGEEDSDVDIEG YDDEEEDGKPKTPAP in isoform 2g, isoform 2a, isoform 3 and isoform 4.
VSP_053383
Alternative sequence1799 – 187274SYGSY…LDSDE → RYQ in isoform 2g, isoform 2a, isoform 2c, isoform 2d and isoform 3.
VSP_053384
Natural variant2691L → V. Ref.5 Ref.30
Corresponds to variant rs28382158 [ dbSNP | Ensembl ].
VAR_020678
Natural variant2971A → G. Ref.30
Corresponds to variant rs35317750 [ dbSNP | Ensembl ].
VAR_041930
Natural variant4531G → D in a colorectal adenocarcinoma sample; somatic mutation. Ref.30
VAR_041931
Natural variant6511E → K in a metastatic melanoma sample; somatic mutation. Ref.30
VAR_041932
Natural variant6911M → I in a lung bronchoalveolar carcinoma sample; somatic mutation. Ref.30
VAR_041933
Natural variant13831V → I.
Corresponds to variant rs7050748 [ dbSNP | Ensembl ].
VAR_048433

Experimental info

Mutagenesis1371S → A: No decrease in kinase activity.
Mutagenesis1451D → A: Reduces kinase activity; when associated with A-147; A-149; A-150; A-152 and A-154.
Mutagenesis1471D → A: Reduces kinase activity; when associated with A-145; A-149; A-150; A-152 and A-154.
Mutagenesis1491E → A: Reduces kinase activity; when associated with A-145; A-147; A-150; A-152 and A-154.
Mutagenesis1501D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-152 and A-154.
Mutagenesis1521D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-154.
Mutagenesis1541K → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-152.
Mutagenesis3051C → A: Reduces kinase activity; when associated with A-307; A-308; A-309 and A-310.
Mutagenesis3071S → A: Reduces kinase activity; when associated with A-305; A-308; A-309 and A-310.
Mutagenesis3081D → A: Reduces kinase activity; when associated with A-305; A-307; A-309 and A-310.
Mutagenesis3091D → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-310.
Mutagenesis3101E → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-309.
Mutagenesis7211E → Q: 25% decrease in histone acetylation. Ref.22
Mutagenesis827 – 8293Missing: Dramatic decrease in histone acetylation. Ref.22

Secondary structure

...................................... 1872
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: 93BE3D181A72ABEB

FASTA1,872212,677
        10         20         30         40         50         60 
MGPGCDLLLR TAATITAAAI MSDTDSDEDS AGGGPFSLAG FLFGNINGAG QLEGESVLDD 

        70         80         90        100        110        120 
ECKKHLAGLG ALGLGSLITE LTANEELTGT DGALVNDEGW VRSTEDAVDY SDINEVAEDE 

       130        140        150        160        170        180 
SRRYQQTMGS LQPLCHSDYD EDDYDADCED IDCKLMPPPP PPPGPMKKDK DQDSITGEKV 

       190        200        210        220        230        240 
DFSSSSDSES EMGPQEATQA ESEDGKLTLP LAGIMQHDAT KLLPSVTELF PEFRPGKVLR 

       250        260        270        280        290        300 
FLRLFGPGKN VPSVWRSARR KRKKKHRELI QEEQIQEVEC SVESEVSQKS LWNYDYAPPP 

       310        320        330        340        350        360 
PPEQCLSDDE ITMMAPVESK FSQSTGDIDK VTDTKPRVAE WRYGPARLWY DMLGVPEDGS 

       370        380        390        400        410        420 
GFDYGFKLRK TEHEPVIKSR MIEEFRKLEE NNGTDLLADE NFLMVTQLHW EDDIIWDGED 

       430        440        450        460        470        480 
VKHKGTKPQR ASLAGWLPSS MTRNAMAYNV QQGFAATLDD DKPWYSIFPI DNEDLVYGRW 

       490        500        510        520        530        540 
EDNIIWDAQA MPRLLEPPVL TLDPNDENLI LEIPDEKEEA TSNSPSKESK KESSLKKSRI 

       550        560        570        580        590        600 
LLGKTGVIKE EPQQNMSQPE VKDPWNLSND EYYYPKQQGL RGTFGGNIIQ HSIPAVELRQ 

       610        620        630        640        650        660 
PFFPTHMGPI KLRQFHRPPL KKYSFGALSQ PGPHSVQPLL KHIKKKAKMR EQERQASGGG 

       670        680        690        700        710        720 
EMFFMRTPQD LTGKDGDLIL AEYSEENGPL MMQVGMATKI KNYYKRKPGK DPGAPDCKYG 

       730        740        750        760        770        780 
ETVYCHTSPF LGSLHPGQLL QAFENNLFRA PIYLHKMPET DFLIIRTRQG YYIRELVDIF 

       790        800        810        820        830        840 
VVGQQCPLFE VPGPNSKRAN THIRDFLQVF IYRLFWKSKD RPRRIRMEDI KKAFPSHSES 

       850        860        870        880        890        900 
SIRKRLKLCA DFKRTGMDSN WWVLKSDFRL PTEEEIRAMV SPEQCCAYYS MIAAEQRLKD 

       910        920        930        940        950        960 
AGYGEKSFFA PEEENEEDFQ MKIDDEVRTA PWNTTRAFIA AMKGKCLLEV TGVADPTGCG 

       970        980        990       1000       1010       1020 
EGFSYVKIPN KPTQQKDDKE PQPVKKTVTG TDADLRRLSL KNAKQLLRKF GVPEEEIKKL 

      1030       1040       1050       1060       1070       1080 
SRWEVIDVVR TMSTEQARSG EGPMSKFARG SRFSVAEHQE RYKEECQRIF DLQNKVLSST 

      1090       1100       1110       1120       1130       1140 
EVLSTDTDSS SAEDSDFEEM GKNIENMLQN KKTSSQLSRE REEQERKELQ RMLLAAGSAA 

      1150       1160       1170       1180       1190       1200 
SGNNHRDDDT ASVTSLNSSA TGRCLKIYRT FRDEEGKEYV RCETVRKPAV IDAYVRIRTT 

      1210       1220       1230       1240       1250       1260 
KDEEFIRKFA LFDEQHREEM RKERRRIQEQ LRRLKRNQEK EKLKGPPEKK PKKMKERPDL 

      1270       1280       1290       1300       1310       1320 
KLKCGACGAI GHMRTNKFCP LYYQTNAPPS NPVAMTEEQE EELEKTVIHN DNEELIKVEG 

      1330       1340       1350       1360       1370       1380 
TKIVLGKQLI ESADEVRRKS LVLKFPKQQL PPKKKRRVGT TVHCDYLNRP HKSIHRRRTD 

      1390       1400       1410       1420       1430       1440 
PMVTLSSILE SIINDMRDLP NTYPFHTPVN AKVVKDYYKI ITRPMDLQTL RENVRKRLYP 

      1450       1460       1470       1480       1490       1500 
SREEFREHLE LIVKNSATYN GPKHSLTQIS QSMLDLCDEK LKEKEDKLAR LEKAINPLLD 

      1510       1520       1530       1540       1550       1560 
DDDQVAFSFI LDNIVTQKMM AVPDSWPFHH PVNKKFVPDY YKVIVNPMDL ETIRKNISKH 

      1570       1580       1590       1600       1610       1620 
KYQSRESFLD DVNLILANSV KYNGPESQYT KTAQEIVNVC YQTLTEYDEH LTQLEKDICT 

      1630       1640       1650       1660       1670       1680 
AKEAALEEAE LESLDPMTPG PYTPQPPDLY DTNTSLSMSR DASVFQDESN MSVLDIPSAT 

      1690       1700       1710       1720       1730       1740 
PEKQVTQEGE DGDGDLADEE EGTVQQPQAS VLYEDLLMSE GEDDEEDAGS DEEGDNPFSA 

      1750       1760       1770       1780       1790       1800 
IQLSESGSDS DVGSGGIRPK QPRMLQENTR MDMENEESMM SYEGDGGEAS HGLEDSNISY 

      1810       1820       1830       1840       1850       1860 
GSYEEPDPKS NTQDTSFSSI GGYEVSEEEE DEEEEEQRSG PSVLSQVHLS EDEEDSEDFH 

      1870 
SIAGDSDLDS DE 

« Hide

Isoform 2 [UniParc].

Checksum: AE148C222B418BB4
Show »

FASTA1,893214,714
Isoform 3 [UniParc].

Checksum: 6C51A0F5885FF667
Show »

FASTA1,832208,364
Isoform 4 [UniParc].

Checksum: 8880885A3D444515
Show »

FASTA1,906216,451
Isoform 2a [UniParc].

Checksum: 4EF338B27B304C13
Show »

FASTA1,835208,693
Isoform 2c [UniParc].

Checksum: 245D4080FB804D6D
Show »

FASTA1,801204,919
Isoform 2d [UniParc].

Checksum: 1B90B7A234BDB92C
Show »

FASTA1,803205,118
Isoform 2e (2F) [UniParc].

Checksum: 72C8271DD47EE24D
Show »

FASTA1,592182,054
Isoform 2g [UniParc].

Checksum: 5165FAF620722AD3
Show »

FASTA1,837208,892
Isoform 2h [UniParc].

Checksum: 75267CFDD8211DD6
Show »

FASTA1,528174,433
Isoform 2i [UniParc].

Checksum: 4DC37D3B71D7AA10
Show »

FASTA1,540175,648
Isoform N-TAF1 (TA14-391) [UniParc].

Checksum: 68B48D4582D8A090
Show »

FASTA1,895214,913

References

« Hide 'large scale' references
[1]"The human CCG1 gene, essential for progression of the G1 phase, encodes a 210-kilodalton nuclear DNA-binding protein."
Sekiguchi T., Nohiro Y., Nakamura Y., Hisamoto N., Nishimoto T.
Mol. Cell. Biol. 11:3317-3325(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
Tissue: Laryngeal carcinoma.
[2]"Molecular cloning of the cDNA of human X chromosomal gene (CCG1) which complements the temperature-sensitive G1 mutants, tsBN462 and ts13, of the BHK cell line."
Sekiguchi T., Miyata T., Nishimoto T.
EMBO J. 7:1683-1687(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation."
Ruppert S., Wang E.H., Tjian R.
Nature 362:175-179(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TBP AND TAFS.
[4]"Reduced neuron-specific expression of the TAF1 gene is associated with X-linked dystonia-parkinsonism."
Makino S., Kaji R., Ando S., Tomizawa M., Yasuno K., Goto S., Matsumoto S., Tabuena M.D., Maranon E., Dantes M., Lee L.V., Ogasawara K., Tooyama I., Akatsu H., Nishimura M., Tamiya G.
Am. J. Hum. Genet. 80:393-406(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N-TAF1), INVOLVEMENT IN DYT3.
Tissue: Brain.
[5]NIEHS SNPs program
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-269.
[6]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 837-1872 (ISOFORM 4).
Tissue: Brain.
[8]"Specific sequence changes in multiple transcript system DYT3 are associated with X-linked dystonia parkinsonism."
Nolte D., Niemann S., Muller U.
Proc. Natl. Acad. Sci. U.S.A. 100:10347-10352(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1347-1801 (ISOFORMS 2A; 2C AND 2D), NUCLEOTIDE SEQUENCE [MRNA] OF 1347-1592 (ISOFORM 2E), NUCLEOTIDE SEQUENCE [MRNA] OF 1498-1801 (ISOFORM 3), INVOLVEMENT IN DYT3.
Tissue: Fetal brain.
[9]Nolte D.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[10]"Structural and functional analysis of the human TAF1/DYT3 multiple transcript system."
Herzfeld T., Nolte D., Muller U.
Mamm. Genome 18:787-795(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1347-1801 (ISOFORMS 2E; 2G; 2H AND 2I), ALTERNATIVE SPLICING.
[11]"The p250 subunit of native TATA box-binding factor TFIID is the cell-cycle regulatory protein CCG1."
Hisatake K., Hasegawa S., Takada R., Nakatani Y., Horikoshi M., Roeder R.G.
Nature 362:179-181(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74."
Dikstein R., Ruppert S., Tjian R.
Cell 84:781-790(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-137 AND SER-307, ATP-BINDING.
[13]"TAF-like function of SV40 large T antigen."
Damania B., Alwine J.C.
Genes Dev. 10:1369-1381(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[14]"Functional analysis of the human TAFII250 N-terminal kinase domain."
O'Brien T., Tjian R.
Mol. Cell 1:905-911(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS.
[15]"Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250."
Siegert J.L., Robbins P.D.
Mol. Cell. Biol. 19:846-854(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RB1, ATP-BINDING.
[16]"A human homologue of yeast anti-silencing factor has histone chaperone activity."
Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M.
Genes Cells 5:221-233(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASF1A.
[17]"Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity."
Solow S., Salunek M., Ryan R., Lieberman P.M.
J. Biol. Chem. 276:15886-15892(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Identification and characterization of CIA/ASF1 as an interactor of bromodomains associated with TFIID."
Chimura T., Kuzuhara T., Horikoshi M.
Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASF1A.
[19]"Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis."
Umehara T., Horikoshi M.
J. Biol. Chem. 278:35660-35667(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASF1A AND ASF1B.
[20]"Phosphorylation on Thr-55 by TAF1 mediates degradation of p53: a role for TAF1 in cell G1 progression."
Li H.-H., Li A.G., Sheppard H.M., Liu X.
Mol. Cell 13:867-878(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53.
[21]"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[22]"TAF1 histone acetyltransferase activity in Sp1 activation of the cyclin D1 promoter."
Hilton T.L., Li Y., Dunphy E.L., Wang E.H.
Mol. Cell. Biol. 25:4321-4332(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: HISTONE ACETYLTRANSFERASE ACTIVITY, MUTAGENESIS OF GLU-721 AND 827-MET--ASP-829.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1700 (ISOFORMS 2A AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1702 (ISOFORM 2G), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1697 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Phosphorylation-dependent regulation of cyclin D1 and cyclin A gene transcription by TFIID subunits TAF1 and TAF7."
Kloet S.L., Whiting J.L., Gafken P., Ranish J., Wang E.H.
Mol. Cell. Biol. 32:3358-3369(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[27]"X-linked dystonia parkinsonism syndrome (XDP, lubag): disease-specific sequence change DSC3 in TAF1/DYT3 affects genes in vesicular transport and dopamine metabolism."
Herzfeld T., Nolte D., Grznarova M., Hofmann A., Schultze J.L., Muller U.
Hum. Mol. Genet. 22:941-951(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: MISCELLANEOUS.
[28]"Structure and function of a human TAFII250 double bromodomain module."
Jacobson R.H., Ladurner A.G., King D.S., Tjian R.
Science 288:1422-1425(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1359-1638.
[29]"Histone recognition and large-scale structural analysis of the human bromodomain family."
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S.
Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 1501-1635, SUBUNIT.
[30]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-269; GLY-297; ASP-453; LYS-651 AND ILE-691.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90359 mRNA. Translation: BAA14374.1.
X07024 mRNA. Translation: CAA30073.1. Sequence problems.
AB300418 mRNA. Translation: BAG15901.1.
AY623109 Genomic DNA. Translation: AAT38105.1.
AL590762 Genomic DNA. No translation available.
AL590763 Genomic DNA. No translation available.
AB209316 mRNA. Translation: BAD92553.1.
AJ549247 mRNA. Translation: CAD70490.1.
AJ549248 mRNA. Translation: CAD70491.3.
AJ549249 mRNA. Translation: CAD70492.2.
AJ549250 mRNA. Translation: CAD70493.3.
AJ555148 mRNA. Translation: CAD87527.2.
AJ555149 mRNA. Translation: CAD87528.2.
AM711892 mRNA. Translation: CAM98555.1.
AM711893 mRNA. Translation: CAM98556.1.
AM711894 mRNA. Translation: CAM98557.1.
AM711895 mRNA. Translation: CAM98558.1.
CCDSCCDS14412.1. [P21675-2]
CCDS35325.1. [P21675-1]
CCDS69783.1. [P21675-12]
PIRA40262.
RefSeqNP_001273003.1. NM_001286074.1. [P21675-12]
NP_004597.2. NM_004606.4. [P21675-2]
NP_620278.1. NM_138923.3. [P21675-1]
XP_005262354.1. XM_005262297.2. [P21675-4]
UniGeneHs.158560.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQFX-ray2.10A1359-1638[»]
3AADX-ray3.30A1342-1629[»]
3UV4X-ray1.89A/B1501-1635[»]
3UV5X-ray2.03A1373-1635[»]
ProteinModelPortalP21675.
SMRP21675. Positions 1359-1625.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112735. 51 interactions.
DIPDIP-147N.
IntActP21675. 26 interactions.
MINTMINT-1211825.

PTM databases

PhosphoSiteP21675.

Polymorphism databases

DMDM115942.

Proteomic databases

MaxQBP21675.
PaxDbP21675.
PRIDEP21675.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276072; ENSP00000276072; ENSG00000147133. [P21675-2]
ENST00000373790; ENSP00000362895; ENSG00000147133. [P21675-1]
ENST00000423759; ENSP00000406549; ENSG00000147133. [P21675-12]
ENST00000449580; ENSP00000389000; ENSG00000147133. [P21675-4]
GeneID6872.
KEGGhsa:6872.
UCSCuc004dzt.4. human. [P21675-2]
uc004dzu.4. human. [P21675-1]
uc004dzv.4. human. [P21675-4]

Organism-specific databases

CTD6872.
GeneCardsGC0XP070586.
GeneReviewsTAF1.
HGNCHGNC:11535. TAF1.
HPACAB016283.
HPA001075.
MIM313650. gene.
314250. phenotype.
neXtProtNX_P21675.
Orphanet53351. X-linked dystonia-parkinsonism.
PharmGKBPA36310.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOVERGENHBG050223.
KOK03125.
OMADEFYYPK.
OrthoDBEOG7QNVK2.
PhylomeDBP21675.
TreeFamTF313573.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP21675.
BgeeP21675.
GenevestigatorP21675.

Family and domain databases

Gene3D1.10.1100.10. 1 hit.
1.20.920.10. 2 hits.
InterProIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR011177. TAF1_animal.
IPR009067. TAF_II_230-bd.
IPR022591. TFIID_sub1_DUF3591.
[Graphical view]
PfamPF00439. Bromodomain. 2 hits.
PF12157. DUF3591. 1 hit.
PF09247. TBP-binding. 1 hit.
[Graphical view]
PIRSFPIRSF003047. TAF1_animal. 1 hit.
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMSSF47055. SSF47055. 1 hit.
SSF47370. SSF47370. 2 hits.
PROSITEPS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21675.
GeneWikiTAF1.
GenomeRNAi6872.
NextBio26827.
PROP21675.
SOURCESearch...

Entry information

Entry nameTAF1_HUMAN
AccessionPrimary (citable) accession number: P21675
Secondary accession number(s): A5CVC8 expand/collapse secondary AC list , A5CVC9, A5CVD0, A5CVD1, B1Q2X3, Q59FZ3, Q6IUZ1, Q70Q86, Q70Q87, Q70T00, Q70T01, Q70T02, Q70T03
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM