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P21675

- TAF1_HUMAN

UniProt

P21675 - TAF1_HUMAN

Protein

Transcription initiation factor TFIID subunit 1

Gene

TAF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (01 May 1992)
      Previous versions | rss
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    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

    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

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi137 – 1371S → A: No decrease in kinase activity. 1 Publication
    Mutagenesisi145 – 1451D → A: Reduces kinase activity; when associated with A-147; A-149; A-150; A-152 and A-154. 1 Publication
    Mutagenesisi147 – 1471D → A: Reduces kinase activity; when associated with A-145; A-149; A-150; A-152 and A-154. 1 Publication
    Mutagenesisi149 – 1491E → A: Reduces kinase activity; when associated with A-145; A-147; A-150; A-152 and A-154. 1 Publication
    Mutagenesisi150 – 1501D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-152 and A-154. 1 Publication
    Mutagenesisi152 – 1521D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-154. 1 Publication
    Mutagenesisi154 – 1541K → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-152. 1 Publication
    Mutagenesisi305 – 3051C → A: Reduces kinase activity; when associated with A-307; A-308; A-309 and A-310. 1 Publication
    Mutagenesisi307 – 3071S → A: Reduces kinase activity; when associated with A-305; A-308; A-309 and A-310. 1 Publication
    Mutagenesisi308 – 3081D → A: Reduces kinase activity; when associated with A-305; A-307; A-309 and A-310. 1 Publication
    Mutagenesisi309 – 3091D → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-310. 1 Publication
    Mutagenesisi310 – 3101E → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-309. 1 Publication
    Mutagenesisi721 – 7211E → Q: 25% decrease in histone acetylation. 2 Publications
    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-acetyllysineBy similarity
    Disulfide bondi1364 ↔ 1619
    Modified residuei1826 – 18261Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by casein kinase II in vitro.2 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21675.

    Family & Domainsi

    Domains and Repeats

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

    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.Curated
    Contains 2 bromo domains.PROSITE-ProRule annotation
    Contains 1 HMG box DNA-binding domain.Curated
    Contains 2 protein kinase domains.Curated

    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. 1 PublicationVSP_012362
    Alternative sequencei1525 – 154016SWPFH…FVPDY → VSCLCAKYFLAISSPS in isoform 2i. 1 PublicationVSP_053376Add
    BLAST
    Alternative sequencei1525 – 15284SWPF → IITK in isoform 2h. 1 PublicationVSP_053375
    Alternative sequencei1529 – 1872344Missing in isoform 2h. 1 PublicationVSP_053377Add
    BLAST
    Alternative sequencei1541 – 1872332Missing in isoform 2i. 1 PublicationVSP_053378Add
    BLAST
    Alternative sequencei1585 – 15928PESQYTKT → YMCTTCRT in isoform 2e. 2 PublicationsVSP_053379
    Alternative sequencei1593 – 1872280Missing in isoform 2e. 2 PublicationsVSP_053380Add
    BLAST
    Alternative sequencei1645 – 16451Q → QAK in isoform 2d, isoform 2g and isoform N-TAF1. 3 PublicationsVSP_053381
    Alternative sequencei1684 – 16863Missing in isoform 3. 1 PublicationVSP_053382
    Alternative sequencei1687 – 16871Q → QMRQGRGRLGEEDSDVDIEG YDDEEEDGKPKTPAP in isoform 2g, isoform 2a, isoform 3 and isoform 4. 3 PublicationsVSP_053383
    Alternative sequencei1799 – 187274SYGSY…LDSDE → RYQ in isoform 2g, isoform 2a, isoform 2c, isoform 2d and isoform 3. 2 PublicationsVSP_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]
    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 ]
    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

    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: October 1, 2014
    This is version 167 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