Transcription initiation factor TFIID subunit 1

Protein attributes

Sequence length	1872 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.17
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Autophosphorylates on Ser residues. Inhibited by retinoblastoma tumor suppressor protein, RB1.
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 MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, CHD8, E2F6, HSP70, IN80C, KIAA1267, LAS1L, MAX, MCRS1, MGA, MYST1/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. Ref.12 Ref.17 Ref.3 Ref.10 Ref.13 Ref.15 Ref.16
Subcellular location	Nucleus Ref.1.
Post-translational modification	Phosphorylated by casein kinase II in vitro. Ref.9 Ref.19
Involvement in disease	Defects in TAF1 are the cause of dystonia type 3 (DYT3) [MIM:314250]; also called X-linked dystonia-parkinsonism (XDP). DYT3 is 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. Its prevalence is high in the Philippines. DYT3 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. Ref.6 Ref.21
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 process	Cell cycle Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Bromodomain Repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	G1 phase of mitotic cell cycle Ref.11 Inferred from genetic interaction. Source: UniProtKB RNA elongation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome RNA polymerase II transcriptional preinitiation complex assembly Inferred from sequence or structural similarity. Source: UniProtKB cellular response to DNA damage stimulus Ref.17 Inferred by curator. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-serine phosphorylation Ref.9 Inferred from direct assay. Source: UniProtKB peptidyl-threonine phosphorylation Ref.17 Inferred from direct assay. Source: UniProtKB positive regulation of gene-specific transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB positive regulation of proteasomal ubiquitin-dependent protein catabolic process Ref.17 Inferred from direct assay. Source: UniProtKB positive regulation of transcription initiation from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid autophosphorylation Ref.9 Ref.17 Traceable author statement. Source: UniProtKB regulation of transcription involved in G2/M-phase of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	MLL1 complex Ref.18 Inferred from direct assay. Source: UniProtKB transcription factor TFIID complex Ref.9 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW TATA-binding protein binding Ref.11 Inferred from physical interaction. Source: UniProtKB histone acetyl-lysine binding Inferred from direct assay. Source: UniProtKB histone acetyltransferase activity Inferred from direct assay. Source: UniProtKB p53 binding Ref.17 Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Ref.9 Ref.17 Inferred from direct assay. Source: UniProtKB sequence-specific DNA binding Inferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
E2	P03120	2	EBI-491313,EBI-1779322	From a different organism.
GTF2F1	P35269	2	EBI-491289,EBI-457886
RB1	P06400	1	EBI-491289,EBI-491274
TBP	P20226	1	EBI-491289,EBI-355371

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

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

Isoform 4 (identifier: P21675-4) The sequence of this isoform differs from the canonical sequence as follows: 1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1872

1872

Transcription initiation factor TFIID subunit 1

PRO_0000211215

Regions

Domain

1 – 414

414

Protein kinase 1

Domain

1397 – 1467

71

Bromo 1

Domain

1425 – 1872

448

Protein kinase 2

Domain

1520 – 1590

71

Bromo 2

DNA binding

1195 – 1273

79

HMG box

Region

1342 – 1629

288

Interaction with ASF1A and ASF1B

Motif

1351 – 1358

8

Nuclear localization signal Potential

Compositional bias

157 – 165

9

Pro-rich

Compositional bias

1627 – 1872

246

Asp/Glu-rich (acidic tail)

Amino acid modifications

Modified residue

137

1

Phosphoserine; by autocatalysis Ref.9

Modified residue

307

1

Phosphoserine; by autocatalysis Ref.9

Modified residue

1826

1

Phosphoserine Ref.19

Disulfide bond

1364 ↔ 1619

Natural variations

Alternative sequence

177

1

G → GVSENGEGIILPSIIAPSSL AS in isoform 2.

VSP_012362

Alternative sequence

1684 – 1686

3

Missing in isoform 3.

VSP_023318

Alternative sequence

1687

1

Q → QMRQGRGRLGEEDSDVDIEG YDDEEEDGKPKTPAP in isoform 3 and isoform 4.

VSP_023319

Natural variant

269

1

L → V: dbSNP rs28382158. Ref.4 Ref.22

VAR_020678

Natural variant

297

1

A → G: dbSNP rs35317750. Ref.22

VAR_041930

Natural variant

453

1

G → D in a colorectal adenocarcinoma sample; somatic mutation. Ref.22

VAR_041931

Natural variant

651

1

E → K in a metastatic melanoma sample; somatic mutation. Ref.22

VAR_041932

Natural variant

691

1

M → I in a lung bronchoalveolar carcinoma sample; somatic mutation. Ref.22

VAR_041933

Natural variant

1383

1

V → I: dbSNP rs7050748.

VAR_048433

Experimental info

Mutagenesis

137

1

S → A: No decrease in kinase activity.

Mutagenesis

145

1

D → A: Reduces kinase activity; when associated with A-147; A-149; A-150; A-152 and A-154.

Mutagenesis

147

1

D → A: Reduces kinase activity; when associated with A-145; A-149; A-150; A-152 and A-154.

Mutagenesis

149

1

E → A: Reduces kinase activity; when associated with A-145; A-147; A-150; A-152 and A-154.

Mutagenesis

150

1

D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-152 and A-154.

Mutagenesis

152

1

D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-154.

Mutagenesis

154

1

K → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-152.

Mutagenesis

305

1

C → A: Reduces kinase activity; when associated with A-307; A-308; A-309 and A-310.

Mutagenesis

307

1

S → A: Reduces kinase activity; when associated with A-305; A-308; A-309 and A-310.

Mutagenesis

308

1

D → A: Reduces kinase activity; when associated with A-305; A-307; A-309 and A-310.

Mutagenesis

309

1

D → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-310.

Mutagenesis

310

1

E → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-309.

Sequence conflict

1525 – 1528

4

SWPF → IITK in CAM98557. Ref.6

Sequence conflict

1585 – 1591

7

PESQYTK → YMCTTCR in CAD87528. Ref.6

Sequence conflict

1645

1

Q → QAK in CAD87527. Ref.6

Sequence conflict

1

S → R in CAD70490. Ref.6

Sequence conflict

1

S → R in CAD70491. Ref.6

Sequence conflict

1

S → R in CAD70492. Ref.6

Sequence conflict

1

S → R in CAD70493. Ref.6

Sequence conflict

1

S → R in CAD87527. Ref.6

Sequence conflict

1

G → Q in CAD70491. Ref.6

Sequence conflict

1

G → Q in CAD70492. Ref.6

Sequence conflict

1

G → Q in CAD70493. Ref.6

Sequence conflict

1

G → Q in CAD87527. Ref.6

Secondary structure

1

.

1872

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified May 1, 1992. Version 2. Checksum: 93BE3D181A72ABEB Show »	FASTA	1,872	212,677
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. Checksum: AE148C222B418BB4 Show »	FASTA	1,893	214,714
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 DQDSITGVSE 190 200 210 220 230 240 NGEGIILPSI IAPSSLASEK VDFSSSSDSE SEMGPQEATQ AESEDGKLTL PLAGIMQHDA 250 260 270 280 290 300 TKLLPSVTEL FPEFRPGKVL RFLRLFGPGK NVPSVWRSAR RKRKKKHREL IQEEQIQEVE 310 320 330 340 350 360 CSVESEVSQK SLWNYDYAPP PPPEQCLSDD EITMMAPVES KFSQSTGDID KVTDTKPRVA 370 380 390 400 410 420 EWRYGPARLW YDMLGVPEDG SGFDYGFKLR KTEHEPVIKS RMIEEFRKLE ENNGTDLLAD 430 440 450 460 470 480 ENFLMVTQLH WEDDIIWDGE DVKHKGTKPQ RASLAGWLPS SMTRNAMAYN VQQGFAATLD 490 500 510 520 530 540 DDKPWYSIFP IDNEDLVYGR WEDNIIWDAQ AMPRLLEPPV LTLDPNDENL ILEIPDEKEE 550 560 570 580 590 600 ATSNSPSKES KKESSLKKSR ILLGKTGVIK EEPQQNMSQP EVKDPWNLSN DEYYYPKQQG 610 620 630 640 650 660 LRGTFGGNII QHSIPAVELR QPFFPTHMGP IKLRQFHRPP LKKYSFGALS QPGPHSVQPL 670 680 690 700 710 720 LKHIKKKAKM REQERQASGG GEMFFMRTPQ DLTGKDGDLI LAEYSEENGP LMMQVGMATK 730 740 750 760 770 780 IKNYYKRKPG KDPGAPDCKY GETVYCHTSP FLGSLHPGQL LQAFENNLFR APIYLHKMPE 790 800 810 820 830 840 TDFLIIRTRQ GYYIRELVDI FVVGQQCPLF EVPGPNSKRA NTHIRDFLQV FIYRLFWKSK 850 860 870 880 890 900 DRPRRIRMED IKKAFPSHSE SSIRKRLKLC ADFKRTGMDS NWWVLKSDFR LPTEEEIRAM 910 920 930 940 950 960 VSPEQCCAYY SMIAAEQRLK DAGYGEKSFF APEEENEEDF QMKIDDEVRT APWNTTRAFI 970 980 990 1000 1010 1020 AAMKGKCLLE VTGVADPTGC GEGFSYVKIP NKPTQQKDDK EPQPVKKTVT GTDADLRRLS 1030 1040 1050 1060 1070 1080 LKNAKQLLRK FGVPEEEIKK LSRWEVIDVV RTMSTEQARS GEGPMSKFAR GSRFSVAEHQ 1090 1100 1110 1120 1130 1140 ERYKEECQRI FDLQNKVLSS TEVLSTDTDS SSAEDSDFEE MGKNIENMLQ NKKTSSQLSR 1150 1160 1170 1180 1190 1200 EREEQERKEL QRMLLAAGSA ASGNNHRDDD TASVTSLNSS ATGRCLKIYR TFRDEEGKEY 1210 1220 1230 1240 1250 1260 VRCETVRKPA VIDAYVRIRT TKDEEFIRKF ALFDEQHREE MRKERRRIQE QLRRLKRNQE 1270 1280 1290 1300 1310 1320 KEKLKGPPEK KPKKMKERPD LKLKCGACGA IGHMRTNKFC PLYYQTNAPP SNPVAMTEEQ 1330 1340 1350 1360 1370 1380 EEELEKTVIH NDNEELIKVE GTKIVLGKQL IESADEVRRK SLVLKFPKQQ LPPKKKRRVG 1390 1400 1410 1420 1430 1440 TTVHCDYLNR PHKSIHRRRT DPMVTLSSIL ESIINDMRDL PNTYPFHTPV NAKVVKDYYK 1450 1460 1470 1480 1490 1500 IITRPMDLQT LRENVRKRLY PSREEFREHL ELIVKNSATY NGPKHSLTQI SQSMLDLCDE 1510 1520 1530 1540 1550 1560 KLKEKEDKLA RLEKAINPLL DDDDQVAFSF ILDNIVTQKM MAVPDSWPFH HPVNKKFVPD 1570 1580 1590 1600 1610 1620 YYKVIVNPMD LETIRKNISK HKYQSRESFL DDVNLILANS VKYNGPESQY TKTAQEIVNV 1630 1640 1650 1660 1670 1680 CYQTLTEYDE HLTQLEKDIC TAKEAALEEA ELESLDPMTP GPYTPQPPDL YDTNTSLSMS 1690 1700 1710 1720 1730 1740 RDASVFQDES NMSVLDIPSA TPEKQVTQEG EDGDGDLADE EEGTVQQPQA SVLYEDLLMS 1750 1760 1770 1780 1790 1800 EGEDDEEDAG SDEEGDNPFS AIQLSESGSD SDVGSGGIRP KQPRMLQENT RMDMENEESM 1810 1820 1830 1840 1850 1860 MSYEGDGGEA SHGLEDSNIS YGSYEEPDPK SNTQDTSFSS IGGYEVSEEE EDEEEEEQRS 1870 1880 1890 GPSVLSQVHL SEDEEDSEDF HSIAGDSDLD SDE « Hide
Isoform 3. Checksum: 6B9CE52516EAEA58 Show »	FASTA	1,903	216,123
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 PEKQMRQGRG RLGEEDSDVD IEGYDDEEED GKPKTPAPEG EDGDGDLADE EEGTVQQPQA 1750 1760 1770 1780 1790 1800 SVLYEDLLMS EGEDDEEDAG SDEEGDNPFS AIQLSESGSD SDVGSGGIRP KQPRMLQENT 1810 1820 1830 1840 1850 1860 RMDMENEESM MSYEGDGGEA SHGLEDSNIS YGSYEEPDPK SNTQDTSFSS IGGYEVSEEE 1870 1880 1890 1900 EDEEEEEQRS GPSVLSQVHL SEDEEDSEDF HSIAGDSDLD SDE « Hide
Isoform 4. Checksum: 8880885A3D444515 Show »	FASTA	1,906	216,451
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 PEKQVTQMRQ GRGRLGEEDS DVDIEGYDDE EEDGKPKTPA PEGEDGDGDL ADEEEGTVQQ 1750 1760 1770 1780 1790 1800 PQASVLYEDL LMSEGEDDEE DAGSDEEGDN PFSAIQLSES GSDSDVGSGG IRPKQPRMLQ 1810 1820 1830 1840 1850 1860 ENTRMDMENE ESMMSYEGDG GEASHGLEDS NISYGSYEEP DPKSNTQDTS FSSIGGYEVS 1870 1880 1890 1900 EEEEDEEEEE QRSGPSVLSQ VHLSEDEEDS EDFHSIAGDS DLDSDE « Hide

References

	« Hide 'large scale' referencesShow '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: 2038334] [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: 3169001] [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: 7680771] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TBP AND TAFS.
[4]	NIEHS SNPs program Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-269.
[5]	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.
[6]	"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: 12928496] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1347-1801 (ISOFORMS 1 AND 4), NUCLEOTIDE SEQUENCE [MRNA] OF 1498-1801 (ISOFORM 3), INVOLVEMENT IN DYT3. Tissue: Fetal brain.
[7]	Nolte D. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[8]	"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: 8450888] [Abstract] Cited for: FUNCTION.
[9]	"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: 8625415] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-137 AND SER-307, ATP-BINDING.
[10]	"TAF-like function of SV40 large T antigen." Damania B., Alwine J.C. Genes Dev. 10:1369-1381(1996) [PubMed: 8647434] [Abstract] Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[11]	"Functional analysis of the human TAFII250 N-terminal kinase domain." O'Brien T., Tjian R. Mol. Cell 1:905-911(1998) [PubMed: 9660973] [Abstract] Cited for: FUNCTION, MUTAGENESIS.
[12]	"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: 9858607] [Abstract] Cited for: FUNCTION, INTERACTION WITH RB1, ATP-BINDING.
[13]	"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: 10759893] [Abstract] Cited for: INTERACTION WITH ASF1A.
[14]	"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: 11278496] [Abstract] Cited for: FUNCTION.
[15]	"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: 12093919] [Abstract] Cited for: INTERACTION WITH ASF1A.
[16]	"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: 12842904] [Abstract] Cited for: INTERACTION WITH ASF1A AND ASF1B.
[17]	"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: 15053879] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53.
[18]	"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: 15960975] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[19]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1826, MASS SPECTROMETRY. Tissue: T-cell.
[20]	"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: 10827952] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1359-1638.
[21]	"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: 17273961] [Abstract] Cited for: INVOLVEMENT IN DYT3.
[22]	"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. Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-269; GLY-297; ASP-453; LYS-651 AND ILE-691.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D90359 mRNA. Translation: BAA14374.1.
X07024 mRNA. Translation: CAA30073.1. Sequence problems.
AY623109 Genomic DNA. Translation: AAT38105.1.
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.
AM711894 mRNA. Translation: CAM98557.1.

IPI

IPI00009891.
IPI00645793.
IPI00828032.
IPI00939191.

PIR

A40262.

RefSeq

NP_004597.2.
NP_620278.1.

UniGene

Hs.158560

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EQF	X-ray	2.10	A	1359-1638	[»]

ModBase

Protein-protein interaction databases

DIP

DIP-147N.
DIP-24198N.

IntAct

P21675. 11 interactions.

STRING

P21675.

PTM databases

PhosphoSite

P21675.

Proteomic databases

PRIDE

P21675.

Genome annotation databases

Ensembl

ENST00000373790; ENSP00000362895; ENSG00000147133; Homo sapiens. [Genome view]

GeneID

6872.

KEGG

hsa:6872.

UCSC

uc004dzt.2. human.
uc004dzu.2. human.

Organism-specific databases

CTD

6872.

GeneCards

GC0XP070502.

H-InvDB

HIX0056184.

HGNC

HGNC:11535. TAF1.

HPA

CAB016283.
HPA001075.

MIM

313650. gene.
314250. phenotype.

Orphanet

53351. Dystonia-parkinsonism, X-linked.

PharmGKB

PA25437.

GenAtlas

Phylogenomic databases

eggNOG

prNOG16035.

HOVERGEN

P21675.

OMA

EENNGTD.

OrthoDB

EOG93FKGN.

PhylomeDB

P21675.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Reactome

REACT_1788. Transcription.
REACT_6185. HIV Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P21675.

Bgee

P21675.

Genevestigator

P21675.

GermOnline

ENSG00000147133. Homo sapiens.

Family and domain databases

InterPro

IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR011177. TAF1_animal.
IPR009067. TAF_II_230_bd.
[Graphical view]

Gene3D

G3DSA:1.20.920.10. Bromodomain. 2 hits.

Pfam

PF00439. Bromodomain. 2 hits.
PF09247. TBP-binding. 1 hit.
[Graphical view]

PIRSF

PIRSF003047. TAF1_animal. 1 hit.

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 2 hits.
[Graphical view]

PROSITE

PS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
PS50118. HMG_BOX_2. False negative.
[Graphical view]

ProtoNet

Other Resources

NextBio

26827.

SOURCE

Entry information

Entry name

TAF1_HUMAN

Accession

Primary (citable) accession number: P21675
Secondary accession number(s): A5CVD0

Q70T03

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1992
Last modified:	February 9, 2010
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.