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P21675

- TAF1_HUMAN

UniProt

P21675 - TAF1_HUMAN

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Protein

Transcription initiation factor TFIID subunit 1

Gene
TAF1, BA2R, CCG1, CCGS, TAF2A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 H4.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Cofactori

Magnesium.

Enzyme regulationi

Autophosphorylates on Ser residues. Inhibited by retinoblastoma tumor suppressor protein, RB1. Binding to TAF1 or CIITA inhibits the histone acetyltransferase activity.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi1195 – 127379HMG boxAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. histone acetyltransferase activity Source: UniProtKB
  3. lysine-acetylated histone binding Source: BHF-UCL
  4. p53 binding Source: BHF-UCL
  5. protein binding Source: UniProtKB
  6. protein serine/threonine kinase activity Source: UniProtKB
  7. sequence-specific DNA binding Source: BHF-UCL
  8. TBP-class protein binding Source: BHF-UCL
  9. transcription coactivator activity Source: BHF-UCL
  10. transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: BHF-UCL
  2. DNA-templated transcription, initiation Source: BHF-UCL
  3. gene expression Source: Reactome
  4. histone acetylation Source: GOC
  5. peptidyl-serine phosphorylation Source: BHF-UCL
  6. peptidyl-threonine phosphorylation Source: BHF-UCL
  7. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  8. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  9. positive regulation of transcription initiation from RNA polymerase II promoter Source: BHF-UCL
  10. protein autophosphorylation Source: UniProtKB
  11. regulation of transcription involved in G2/M transition of mitotic cell cycle Source: BHF-UCL
  12. RNA polymerase II transcriptional preinitiation complex assembly Source: BHF-UCL
  13. transcription elongation from RNA polymerase II promoter Source: Reactome
  14. transcription from RNA polymerase II promoter Source: Reactome
  15. transcription initiation from RNA polymerase II promoter Source: Reactome
  16. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TAF1
Synonyms:BA2R, CCG1, CCGS, TAF2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11535. TAF1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. MLL1 complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. transcription factor TFIID complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi137 – 1371S → A: No decrease in kinase activity.
Mutagenesisi145 – 1451D → A: Reduces kinase activity; when associated with A-147; A-149; A-150; A-152 and A-154.
Mutagenesisi147 – 1471D → A: Reduces kinase activity; when associated with A-145; A-149; A-150; A-152 and A-154.
Mutagenesisi149 – 1491E → A: Reduces kinase activity; when associated with A-145; A-147; A-150; A-152 and A-154.
Mutagenesisi150 – 1501D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-152 and A-154.
Mutagenesisi152 – 1521D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-154.
Mutagenesisi154 – 1541K → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-152.
Mutagenesisi305 – 3051C → A: Reduces kinase activity; when associated with A-307; A-308; A-309 and A-310.
Mutagenesisi307 – 3071S → A: Reduces kinase activity; when associated with A-305; A-308; A-309 and A-310.
Mutagenesisi308 – 3081D → A: Reduces kinase activity; when associated with A-305; A-307; A-309 and A-310.
Mutagenesisi309 – 3091D → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-310.
Mutagenesisi310 – 3101E → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-309.
Mutagenesisi721 – 7211E → Q: 25% decrease in histone acetylation. 1 Publication
Mutagenesisi827 – 8293Missing: Dramatic decrease in histone acetylation. 1 Publication

Keywords - Diseasei

Dystonia, Parkinsonism

Organism-specific databases

MIMi314250. phenotype.
Orphaneti53351. X-linked dystonia-parkinsonism.
PharmGKBiPA36310.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18721872Transcription initiation factor TFIID subunit 1PRO_0000211215Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei137 – 1371Phosphoserine; by autocatalysis1 Publication
Modified residuei307 – 3071Phosphoserine; by autocatalysis1 Publication
Modified residuei544 – 5441N6-acetyllysine By similarity
Disulfide bondi1364 ↔ 1619
Modified residuei1826 – 18261Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by casein kinase II in vitro.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP21675.
PaxDbiP21675.
PRIDEiP21675.

PTM databases

PhosphoSiteiP21675.

Expressioni

Gene expression databases

ArrayExpressiP21675.
BgeeiP21675.
GenevestigatoriP21675.

Organism-specific databases

HPAiCAB016283.
HPA001075.

Interactioni

Subunit structurei

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).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P032553EBI-491289,EBI-2603114From a different organism.
GTF2F1P352693EBI-491289,EBI-457886
TBPP202265EBI-491289,EBI-355371

Protein-protein interaction databases

BioGridi112735. 51 interactions.
DIPiDIP-147N.
IntActiP21675. 26 interactions.
MINTiMINT-1211825.

Structurei

Secondary structure

1
1872
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1381 – 139717
Helixi1403 – 14053
Beta strandi1406 – 14083
Turni1411 – 14133
Helixi1417 – 14204
Helixi1427 – 14359
Helixi1442 – 146019
Beta strandi1462 – 14643
Helixi1465 – 148319
Helixi1485 – 149511
Turni1497 – 15004
Helixi1502 – 151716
Turni1518 – 15214
Helixi1526 – 15283
Turni1534 – 15363
Helixi1540 – 15434
Helixi1550 – 15589
Helixi1565 – 158319
Helixi1588 – 160619
Helixi1608 – 162114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQFX-ray2.10A1359-1638[»]
3AADX-ray3.30A1342-1629[»]
3UV4X-ray1.89A/B1501-1635[»]
3UV5X-ray2.03A1373-1635[»]
ProteinModelPortaliP21675.
SMRiP21675. Positions 1359-1625.

Miscellaneous databases

EvolutionaryTraceiP21675.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 414414Protein kinase 1Add
BLAST
Domaini1397 – 146771Bromo 1Add
BLAST
Domaini1425 – 1872448Protein kinase 2Add
BLAST
Domaini1520 – 159071Bromo 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni517 – 976460Histone acetyltransferase (HAT)Add
BLAST
Regioni1342 – 1629288Interaction with ASF1A and ASF1BAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1351 – 13588Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi157 – 1659Pro-rich
Compositional biasi1627 – 1872246Asp/Glu-rich (acidic tail)Add
BLAST

Sequence similaritiesi

Belongs to the TAF1 family.
Contains 2 bromo domains.

Keywords - Domaini

Bromodomain, Repeat

Phylogenomic databases

eggNOGiCOG5076.
HOVERGENiHBG050223.
KOiK03125.
OMAiDEFYYPK.
OrthoDBiEOG7QNVK2.
PhylomeDBiP21675.
TreeFamiTF313573.

Family and domain databases

Gene3Di1.10.1100.10. 1 hit.
1.20.920.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR011177. TAF1_animal.
IPR009067. TAF_II_230-bd.
IPR022591. TFIID_sub1_DUF3591.
[Graphical view]
PfamiPF00439. Bromodomain. 2 hits.
PF12157. DUF3591. 1 hit.
PF09247. TBP-binding. 1 hit.
[Graphical view]
PIRSFiPIRSF003047. TAF1_animal. 1 hit.
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMiSSF47055. SSF47055. 1 hit.
SSF47370. SSF47370. 2 hits.
PROSITEiPS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]

Sequences (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. Align

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) [UniParc]FASTAAdd to Basket

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.

« Hide

MGPGCDLLLR TAATITAAAI MSDTDSDEDS AGGGPFSLAG FLFGNINGAG     50
QLEGESVLDD ECKKHLAGLG ALGLGSLITE LTANEELTGT DGALVNDEGW 100
VRSTEDAVDY SDINEVAEDE SRRYQQTMGS LQPLCHSDYD EDDYDADCED 150
IDCKLMPPPP PPPGPMKKDK DQDSITGEKV DFSSSSDSES EMGPQEATQA 200
ESEDGKLTLP LAGIMQHDAT KLLPSVTELF PEFRPGKVLR FLRLFGPGKN 250
VPSVWRSARR KRKKKHRELI QEEQIQEVEC SVESEVSQKS LWNYDYAPPP 300
PPEQCLSDDE ITMMAPVESK FSQSTGDIDK VTDTKPRVAE WRYGPARLWY 350
DMLGVPEDGS GFDYGFKLRK TEHEPVIKSR MIEEFRKLEE NNGTDLLADE 400
NFLMVTQLHW EDDIIWDGED VKHKGTKPQR ASLAGWLPSS MTRNAMAYNV 450
QQGFAATLDD DKPWYSIFPI DNEDLVYGRW EDNIIWDAQA MPRLLEPPVL 500
TLDPNDENLI LEIPDEKEEA TSNSPSKESK KESSLKKSRI LLGKTGVIKE 550
EPQQNMSQPE VKDPWNLSND EYYYPKQQGL RGTFGGNIIQ HSIPAVELRQ 600
PFFPTHMGPI KLRQFHRPPL KKYSFGALSQ PGPHSVQPLL KHIKKKAKMR 650
EQERQASGGG EMFFMRTPQD LTGKDGDLIL AEYSEENGPL MMQVGMATKI 700
KNYYKRKPGK DPGAPDCKYG ETVYCHTSPF LGSLHPGQLL QAFENNLFRA 750
PIYLHKMPET DFLIIRTRQG YYIRELVDIF VVGQQCPLFE VPGPNSKRAN 800
THIRDFLQVF IYRLFWKSKD RPRRIRMEDI KKAFPSHSES SIRKRLKLCA 850
DFKRTGMDSN WWVLKSDFRL PTEEEIRAMV SPEQCCAYYS MIAAEQRLKD 900
AGYGEKSFFA PEEENEEDFQ MKIDDEVRTA PWNTTRAFIA AMKGKCLLEV 950
TGVADPTGCG EGFSYVKIPN KPTQQKDDKE PQPVKKTVTG TDADLRRLSL 1000
KNAKQLLRKF GVPEEEIKKL SRWEVIDVVR TMSTEQARSG EGPMSKFARG 1050
SRFSVAEHQE RYKEECQRIF DLQNKVLSST EVLSTDTDSS SAEDSDFEEM 1100
GKNIENMLQN KKTSSQLSRE REEQERKELQ RMLLAAGSAA SGNNHRDDDT 1150
ASVTSLNSSA TGRCLKIYRT FRDEEGKEYV RCETVRKPAV IDAYVRIRTT 1200
KDEEFIRKFA LFDEQHREEM RKERRRIQEQ LRRLKRNQEK EKLKGPPEKK 1250
PKKMKERPDL KLKCGACGAI GHMRTNKFCP LYYQTNAPPS NPVAMTEEQE 1300
EELEKTVIHN DNEELIKVEG TKIVLGKQLI ESADEVRRKS LVLKFPKQQL 1350
PPKKKRRVGT TVHCDYLNRP HKSIHRRRTD PMVTLSSILE SIINDMRDLP 1400
NTYPFHTPVN AKVVKDYYKI ITRPMDLQTL RENVRKRLYP SREEFREHLE 1450
LIVKNSATYN GPKHSLTQIS QSMLDLCDEK LKEKEDKLAR LEKAINPLLD 1500
DDDQVAFSFI LDNIVTQKMM AVPDSWPFHH PVNKKFVPDY YKVIVNPMDL 1550
ETIRKNISKH KYQSRESFLD DVNLILANSV KYNGPESQYT KTAQEIVNVC 1600
YQTLTEYDEH LTQLEKDICT AKEAALEEAE LESLDPMTPG PYTPQPPDLY 1650
DTNTSLSMSR DASVFQDESN MSVLDIPSAT PEKQVTQEGE DGDGDLADEE 1700
EGTVQQPQAS VLYEDLLMSE GEDDEEDAGS DEEGDNPFSA IQLSESGSDS 1750
DVGSGGIRPK QPRMLQENTR MDMENEESMM SYEGDGGEAS HGLEDSNISY 1800
GSYEEPDPKS NTQDTSFSSI GGYEVSEEEE DEEEEEQRSG PSVLSQVHLS 1850
EDEEDSEDFH SIAGDSDLDS DE 1872
Length:1,872
Mass (Da):212,677
Last modified:May 1, 1992 - v2
Checksum:i93BE3D181A72ABEB
GO
Isoform 2 (identifier: P21675-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     177-177: G → GVSENGEGIILPSIIAPSSLAS

Show »
Length:1,893
Mass (Da):214,714
Checksum:iAE148C222B418BB4
GO
Isoform 3 (identifier: P21675-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,832
Mass (Da):208,364
Checksum:i6C51A0F5885FF667
GO
Isoform 4 (identifier: P21675-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP

Note: Contains a phosphoserine at position 1700.

Show »
Length:1,906
Mass (Da):216,451
Checksum:i8880885A3D444515
GO
Isoform 2a (identifier: P21675-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,835
Mass (Da):208,693
Checksum:i4EF338B27B304C13
GO
Isoform 2c (identifier: P21675-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ

Show »
Length:1,801
Mass (Da):204,919
Checksum:i245D4080FB804D6D
GO
Isoform 2d (identifier: P21675-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1645-1645: Q → QAK
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ

Show »
Length:1,803
Mass (Da):205,118
Checksum:i1B90B7A234BDB92C
GO
Isoform 2e (identifier: P21675-8) [UniParc]FASTAAdd to Basket

Also known as: 2F

The sequence of this isoform differs from the canonical sequence as follows:
     1585-1592: PESQYTKT → YMCTTCRT
     1593-1872: Missing.

Show »
Length:1,592
Mass (Da):182,054
Checksum:i72C8271DD47EE24D
GO
Isoform 2g (identifier: P21675-9) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,837
Mass (Da):208,892
Checksum:i5165FAF620722AD3
GO
Isoform 2h (identifier: P21675-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1525-1528: SWPF → IITK
     1529-1872: Missing.

Show »
Length:1,528
Mass (Da):174,433
Checksum:i75267CFDD8211DD6
GO
Isoform 2i (identifier: P21675-11) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1525-1540: SWPFHHPVNKKFVPDY → VSCLCAKYFLAISSPS
     1541-1872: Missing.

Show »
Length:1,540
Mass (Da):175,648
Checksum:i4DC37D3B71D7AA10
GO
Isoform N-TAF1 (identifier: P21675-12) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,895
Mass (Da):214,913
Checksum:i68B48D4582D8A090
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti269 – 2691L → V.2 Publications
Corresponds to variant rs28382158 [ dbSNP | Ensembl ].
VAR_020678
Natural varianti297 – 2971A → G.1 Publication
Corresponds to variant rs35317750 [ dbSNP | Ensembl ].
VAR_041930
Natural varianti453 – 4531G → D in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041931
Natural varianti651 – 6511E → K in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041932
Natural varianti691 – 6911M → I in a lung bronchoalveolar carcinoma sample; somatic mutation. 1 Publication
VAR_041933
Natural varianti1383 – 13831V → I.
Corresponds to variant rs7050748 [ dbSNP | Ensembl ].
VAR_048433

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei177 – 1771G → GVSENGEGIILPSIIAPSSL AS in isoform 2 and isoform N-TAF1. VSP_012362
Alternative sequencei1525 – 154016SWPFH…FVPDY → VSCLCAKYFLAISSPS in isoform 2i. VSP_053376Add
BLAST
Alternative sequencei1525 – 15284SWPF → IITK in isoform 2h. VSP_053375
Alternative sequencei1529 – 1872344Missing in isoform 2h. VSP_053377Add
BLAST
Alternative sequencei1541 – 1872332Missing in isoform 2i. VSP_053378Add
BLAST
Alternative sequencei1585 – 15928PESQYTKT → YMCTTCRT in isoform 2e. VSP_053379
Alternative sequencei1593 – 1872280Missing in isoform 2e. VSP_053380Add
BLAST
Alternative sequencei1645 – 16451Q → QAK in isoform 2d, isoform 2g and isoform N-TAF1. VSP_053381
Alternative sequencei1684 – 16863Missing in isoform 3. VSP_053382
Alternative sequencei1687 – 16871Q → QMRQGRGRLGEEDSDVDIEG YDDEEEDGKPKTPAP in isoform 2g, isoform 2a, isoform 3 and isoform 4. VSP_053383
Alternative sequencei1799 – 187274SYGSY…LDSDE → RYQ in isoform 2g, isoform 2a, isoform 2c, isoform 2d and isoform 3. VSP_053384Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14412.1. [P21675-2]
CCDS35325.1. [P21675-1]
CCDS69783.1. [P21675-12]
PIRiA40262.
RefSeqiNP_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]
UniGeneiHs.158560.

Genome annotation databases

EnsembliENST00000276072; ENSP00000276072; ENSG00000147133. [P21675-2]
ENST00000373790; ENSP00000362895; ENSG00000147133. [P21675-1]
ENST00000423759; ENSP00000406549; ENSG00000147133. [P21675-12]
ENST00000449580; ENSP00000389000; ENSG00000147133. [P21675-4]
GeneIDi6872.
KEGGihsa:6872.
UCSCiuc004dzt.4. human. [P21675-2]
uc004dzu.4. human. [P21675-1]
uc004dzv.4. human. [P21675-4]

Polymorphism databases

DMDMi115942.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14412.1. [P21675-2 ]
CCDS35325.1. [P21675-1 ]
CCDS69783.1. [P21675-12 ]
PIRi A40262.
RefSeqi NP_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 ]
UniGenei Hs.158560.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P21675.
SMRi P21675. Positions 1359-1625.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112735. 51 interactions.
DIPi DIP-147N.
IntActi P21675. 26 interactions.
MINTi MINT-1211825.

PTM databases

PhosphoSitei P21675.

Polymorphism databases

DMDMi 115942.

Proteomic databases

MaxQBi P21675.
PaxDbi P21675.
PRIDEi P21675.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000276072 ; ENSP00000276072 ; ENSG00000147133 . [P21675-2 ]
ENST00000373790 ; ENSP00000362895 ; ENSG00000147133 . [P21675-1 ]
ENST00000423759 ; ENSP00000406549 ; ENSG00000147133 . [P21675-12 ]
ENST00000449580 ; ENSP00000389000 ; ENSG00000147133 . [P21675-4 ]
GeneIDi 6872.
KEGGi hsa:6872.
UCSCi uc004dzt.4. human. [P21675-2 ]
uc004dzu.4. human. [P21675-1 ]
uc004dzv.4. human. [P21675-4 ]

Organism-specific databases

CTDi 6872.
GeneCardsi GC0XP070586.
GeneReviewsi TAF1.
HGNCi HGNC:11535. TAF1.
HPAi CAB016283.
HPA001075.
MIMi 313650. gene.
314250. phenotype.
neXtProti NX_P21675.
Orphaneti 53351. X-linked dystonia-parkinsonism.
PharmGKBi PA36310.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
HOVERGENi HBG050223.
KOi K03125.
OMAi DEFYYPK.
OrthoDBi EOG7QNVK2.
PhylomeDBi P21675.
TreeFami TF313573.

Enzyme and pathway databases

Reactomei REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Miscellaneous databases

EvolutionaryTracei P21675.
GeneWikii TAF1.
GenomeRNAii 6872.
NextBioi 26827.
PROi P21675.
SOURCEi Search...

Gene expression databases

ArrayExpressi P21675.
Bgeei P21675.
Genevestigatori P21675.

Family and domain databases

Gene3Di 1.10.1100.10. 1 hit.
1.20.920.10. 2 hits.
InterProi IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR011177. TAF1_animal.
IPR009067. TAF_II_230-bd.
IPR022591. TFIID_sub1_DUF3591.
[Graphical view ]
Pfami PF00439. Bromodomain. 2 hits.
PF12157. DUF3591. 1 hit.
PF09247. TBP-binding. 1 hit.
[Graphical view ]
PIRSFi PIRSF003047. TAF1_animal. 1 hit.
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 2 hits.
[Graphical view ]
SUPFAMi SSF47055. SSF47055. 1 hit.
SSF47370. SSF47370. 2 hits.
PROSITEi PS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.
    , 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.

Entry informationi

Entry nameiTAF1_HUMAN
AccessioniPrimary (citable) accession number: P21675
Secondary accession number(s): A5CVC8
, A5CVC9, A5CVD0, A5CVD1, B1Q2X3, Q59FZ3, Q6IUZ1, Q70Q86, Q70Q87, Q70T00, Q70T01, Q70T02, Q70T03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1992
Last modified: September 3, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi