P21675 (TAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription initiation factor TFIID subunit 1
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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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 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.10 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.24
Subcellular location	Nucleus Ref.1.
Post-translational modification	Phosphorylated by casein kinase II in vitro. Ref.9
Involvement in disease	Dystonia 3 (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.6 Ref.23
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
Disease	Dystonia Parkinsonism
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 Reference proteome
Gene Ontology (GO)
Biological_process	G1 phase of mitotic cell cycle Inferred from genetic interaction Ref.11. Source: BHF-UCL RNA polymerase II transcriptional preinitiation complex assembly Inferred from sequence or structural similarity. Source: BHF-UCL peptidyl-serine phosphorylation Inferred from direct assay Ref.9. Source: BHF-UCL peptidyl-threonine phosphorylation Inferred from direct assay Ref.17. Source: BHF-UCL positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.17. 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.17. Source: UniProtKB regulation of transcription involved in G2/M-phase of mitotic cell cycle Inferred from sequence or structural similarity. Source: BHF-UCL response to DNA damage stimulus Inferred by curator Ref.17. Source: BHF-UCL transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MLL1 complex Inferred from direct assay Ref.18. Source: UniProtKB transcription factor TFIID complex Inferred from direct assay Ref.9. Source: BHF-UCL
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histone acetyl-lysine binding Inferred from direct assay PubMed 17996705. Source: BHF-UCL histone acetyltransferase activity Inferred from direct assay PubMed 8980232. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.9. 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GTF2F1	P35269	3	EBI-491289,EBI-457886
TBP	P20226	5	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

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.

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.20

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. Ref.4 Ref.25
Corresponds to variant rs28382158 [ dbSNP | Ensembl ].

VAR_020678

Natural variant

297

1

A → G. Ref.25
Corresponds to variant rs35317750 [ dbSNP | Ensembl ].

VAR_041930

Natural variant

453

1

G → D in a colorectal adenocarcinoma sample; somatic mutation. Ref.25

VAR_041931

Natural variant

651

1

E → K in a metastatic melanoma sample; somatic mutation. Ref.25

VAR_041932

Natural variant

691

1

M → I in a lung bronchoalveolar carcinoma sample; somatic mutation. Ref.25

VAR_041933

Natural variant

1383

1

V → I.
Corresponds to variant rs7050748 [ dbSNP | Ensembl ].

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

1799

1

S → R in CAD70490. Ref.6

Sequence conflict

1799

1

S → R in CAD70491. Ref.6

Sequence conflict

1799

1

S → R in CAD70492. Ref.6

Sequence conflict

1799

1

S → R in CAD70493. Ref.6

Sequence conflict

1799

1

S → R in CAD87527. Ref.6

Sequence conflict

1801

1

G → Q in CAD70491. Ref.6

Sequence conflict

1801

1

G → Q in CAD70492. Ref.6

Sequence conflict

1801

1

G → Q in CAD70493. Ref.6

Sequence conflict

1801

1

G → Q in CAD87527. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1872

Helix Strand Turn

Details...

Helix

1381 – 1397

17

Helix

1403 – 1405

3

Beta strand

1406 – 1408

3

Turn

1411 – 1413

3

Helix

1417 – 1420

4

Helix

1427 – 1435

9

Helix

1442 – 1460

19

Beta strand

1462 – 1464

3

Helix

1465 – 1483

19

Helix

1485 – 1495

11

Turn

1497 – 1500

4

Helix

1502 – 1517

16

Turn

1518 – 1521

4

Helix

1526 – 1528

3

Turn

1534 – 1536

3

Helix

1540 – 1543

4

Helix

1550 – 1558

9

Helix

1565 – 1583

19

Helix

1588 – 1606

19

Helix

1608 – 1621

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1992. Version 2. Checksum: 93BE3D181A72ABEB	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
	Isoform 2 [UniParc]. Checksum: AE148C222B418BB4	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
	Isoform 3 [UniParc]. Checksum: 6B9CE52516EAEA58	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
	Isoform 4 [UniParc]. Checksum: 8880885A3D444515	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

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] [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]	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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[19]	"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.
[20]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"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-1697 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1700 (ISOFORM 4), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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.
[23]	"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: INVOLVEMENT IN DYT3.
[24]	"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.
[25]	"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. , 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

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. NM_004606.3.
NP_620278.1. NM_138923.2.

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	[»]
3AAD	X-ray	3.30	A	1342-1629	[»]
3UV4	X-ray	1.89	A/B	1501-1635	[»]
3UV5	X-ray	2.03	A	1373-1635	[»]

ProteinModelPortal

P21675.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-147N.
DIP-24198N.

IntAct

P21675. 23 interactions.

MINT

MINT-1211825.

PTM databases

PhosphoSite

P21675.

Polymorphism databases

DMDM

115942.

Proteomic databases

PaxDb

P21675.

PRIDE

P21675.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000276072; ENSP00000276072; ENSG00000147133.
ENST00000373790; ENSP00000362895; ENSG00000147133.
ENST00000449580; ENSP00000389000; ENSG00000147133.

GeneID

6872.

KEGG

hsa:6872.

UCSC

uc004dzt.4. human.
uc004dzu.4. human.
uc004dzv.4. human.

Organism-specific databases

CTD

6872.

GeneCards

GC0XP070586.

HGNC

HGNC:11535. TAF1.

HPA

CAB016283.
HPA001075.

MIM

313650. gene.
314250. phenotype.

neXtProt

NX_P21675.

Orphanet

53351. X-linked dystonia-parkinsonism.

PharmGKB

PA36310.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5076.

HOVERGEN

HBG050223.

KO

K03125.

OMA

DEFYYPK.

OrthoDB

EOG4K3KVC.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P21675.

Bgee

P21675.

Genevestigator

P21675.

GermOnline

ENSG00000147133. Homo sapiens.

Family and domain databases

Gene3D

1.10.1100.10. 1 hit.
1.20.920.10. 2 hits.

InterPro

IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR011177. TAF1_animal.
IPR009067. TAF_II_230-bd.
IPR022591. TFIID_sub1_DUF3591.
[Graphical view]

Pfam

PF00439. Bromodomain. 2 hits.
PF12157. DUF3591. 1 hit.
PF09247. TBP-binding. 1 hit.
[Graphical view]

PIRSF

PIRSF003047. TAF1_animal. 1 hit.

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 2 hits.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 2 hits.
SSF47055. TAF_II_230. 1 hit.

PROSITE

PS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
PS50118. HMG_BOX_2. False negative.
PS50011. PROTEIN_KINASE_DOM. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P21675.

GenomeRNAi

6872.

NextBio

26827.

SOURCE

Search...

Entry information

Entry name

TAF1_HUMAN

Accession

Primary (citable) accession number: P21675
Secondary accession number(s): A5CVD0 , 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:	May 1, 2013
This is version 152 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.