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Q60544 (TAF1_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Transcription initiation factor TFIID subunit 1

EC=2.3.1.48
EC=2.7.11.1
Alternative name(s):
Cell cycle gene 1 protein
TBP-associated factor 250 kDa
Short name=p250
Transcription initiation factor TFIID 250 kDa subunit
Short name=TAF(II)250
Short name=TAFII-250
Short name=TAFII250
Gene names
Name:TAF1
Synonyms:CCG1
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length1865 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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

Cofactor

Magnesium By similarity.

Enzyme regulation

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

Subunit structure

TAF1 is the largest component of transcription factor TFIID that is composed of TBP and a variety of TBP-associated factors. TAF1, when part of the TFIID complex, interacts with C-terminus of TP53. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. RB1 interacts with the N-terminal domain of TAF1. Interacts with ASF1A and ASF1B. Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H1.4, H2A, H2B, H3 and H4 (in vitro) By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the TAF1 family.

Contains 2 bromo domains.

Contains 1 HMG box DNA-binding domain.

Contains 2 protein kinase domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18651865Transcription initiation factor TFIID subunit 1
PRO_0000278523

Regions

Domain1 – 409409Protein kinase 1
Domain1392 – 146271Bromo 1
Domain1420 – 1865446Protein kinase 2
Domain1515 – 158571Bromo 2
DNA binding1190 – 126879HMG box By similarity
Region512 – 971460Histone acetyltransferase (HAT) By similarity
Region1337 – 1624288Interaction with ASF1A and ASF1B By similarity
Motif1346 – 13538Nuclear localization signal Potential
Compositional bias152 – 1609Poly-Pro
Compositional bias178 – 1858Poly-Ser
Compositional bias293 – 2975Poly-Pro
Compositional bias1822 – 18298Poly-Glu

Amino acid modifications

Modified residue1311Phosphoserine; by autocatalysis By similarity
Modified residue3021Phosphoserine; by autocatalysis By similarity
Modified residue5391N6-acetyllysine By similarity
Modified residue18211Phosphoserine By similarity
Disulfide bond1359 ↔ 1614 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60544 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A81614946C0C0F24

FASTA1,865211,868
        10         20         30         40         50         60 
MLLPATGASR SAAIMSDTDS DEDSSGGGPF SLTGFLFGNI NGAGQLEGES VLDDECKKHL 

        70         80         90        100        110        120 
AGLGALGLGS LITELTANEE LAGTDGALVN DEGWIRSRED AVDYSDINEV AEDESRRYQQ 

       130        140        150        160        170        180 
TMGSLQPLCH SADYDEDDYD ADCEDIDCKL MPPPPPPPGP VKKEKDQDGL TGEKVDFSSS 

       190        200        210        220        230        240 
SDSESEMGPQ EAAQAESKDG KLTLPLAGIM QHDATKLLPS VTELFPEFRP GKVLRFLRLF 

       250        260        270        280        290        300 
GPGKNVPSVW RSARRKRKKK HREPIQEEQI QEEECSVELE VNQKSLWNYD YAPPPPPEQC 

       310        320        330        340        350        360 
LSDDEITMMA PVESKFSQST GDTDKVMDTK PRVAEWRYGP ARLWYDMLGV PEDGSGFDYG 

       370        380        390        400        410        420 
FKMRKTEHEP AIKCKMMTKL RKLEESNGID LLADENFLMV TQLHWEDDII WDGEDVKHKG 

       430        440        450        460        470        480 
TKPQRASLAG WLPSSMTRNA MAYNVQQGFA ATLDDDKPWY SIFPIDNEDL VYGRWEDNII 

       490        500        510        520        530        540 
WDAQAMPRIL EPPVLTLDPN DENLILEIPD EKEEATSNSP SKENKKESSL KKSRILLGKT 

       550        560        570        580        590        600 
GVIKEEPQQN MSQPEVKDPW NLSNDEYYYP KQQGLRGTFG GNIIQHSIPA VELRQPFFPT 

       610        620        630        640        650        660 
HMGPIKLRQF HRPPLKKYSF GALSQPGPHS VQPLLKHIKK KAKMREQERQ ASGGGEMFFM 

       670        680        690        700        710        720 
RTPQDLTGKD GDLILAEYSE ENGPLMMQVG MATKIKNYYK RKPGKDPGAP DCKYGETVYC 

       730        740        750        760        770        780 
HTSPFLGSLH PGQLLQAFEN NLFRAPIYLH KMPETDFLII RTRQGYYIRE LVDIFVVGQQ 

       790        800        810        820        830        840 
CPLFEVPGPN SKRANTHIRD FLQVFIYRLF WKSKDRPRRI RMEDIKKAFP SHSESSIRKR 

       850        860        870        880        890        900 
LKLCADFKRT GMDSNWWVLK SDFRLPTEEE IRAMVSPEQC CAYYSMIAAE QRLKDAGYGE 

       910        920        930        940        950        960 
KSFFAPEEEN EEDFQMKIDD EVRTAPWNTT RAFIAAMKGK CLLEVTGVAD PTGCGEGFSY 

       970        980        990       1000       1010       1020 
VKIPNKPTQQ KDDKEPQPVK KTVTGTDADL RRLSLKNAKQ LLRKFGVPEE EIKKLSRWEV 

      1030       1040       1050       1060       1070       1080 
IDVVRTMSTE QARSGEGPMS KFARGSRFSV AEHQERYKEE CQRIFDLQNK VLSSTEVLST 

      1090       1100       1110       1120       1130       1140 
DTDSSSAEDS DFEEMGKNIE NMLQNKKTSS QLSREREEQE RKELQRMLLA AGSASAGNNH 

      1150       1160       1170       1180       1190       1200 
RDDDTASVTS LNSSATGRCL KIYRTFRDEE GKEYVRCETV RKPAVIDAYV RIRTTKDEEF 

      1210       1220       1230       1240       1250       1260 
IRKFALFDEQ HREEMRKERR RIQEQLRRLK RNQEKEKLKG PPEKKPKKMK ERPDLKLKCG 

      1270       1280       1290       1300       1310       1320 
ACGAIGHMRT NKFCPLYYQT NAPPSNPVAM TEEQEEELEK TVIHNDNEEL IKVEGTKIVL 

      1330       1340       1350       1360       1370       1380 
GKQLIESADE VRRKSLVLKF PKQQLPPKKK RRVGTTVHCD YLNRPHKSIH RRRTDPMVTL 

      1390       1400       1410       1420       1430       1440 
SSILESIIND MRDLPNTYPF HTPVNAKVVK DYYKIITRPM DLQTLRENVR KRLYPSREEF 

      1450       1460       1470       1480       1490       1500 
REHLELIVKN SATYNGPKHS LTQISQSMLD LCDEKLKEKE DKLARLEKAI NPLLDDDDQV 

      1510       1520       1530       1540       1550       1560 
AFSFILDNIV TQKMMAVPDS WPFHHPVNKK FVPDYYKVIV SPMDLETIRK NISKHKYQSR 

      1570       1580       1590       1600       1610       1620 
ESFLDDVNLI LANSVKYNGS ESQYTKTAQE IVNVCYQTLT EYDEHLTQLE KDICTAKEAA 

      1630       1640       1650       1660       1670       1680 
LEEAELESLD PMTPGPYTPQ PPDLYDNSTS LSVSRDASVY QDESNMSVLD IPSATSEKQL 

      1690       1700       1710       1720       1730       1740 
TQEGEDGDGD LADEEEGTVQ QPQASVLYED LLMSEGEDDE EDAGSDEEGD NPFSAIQLSE 

      1750       1760       1770       1780       1790       1800 
SGSDSDVGSG SIRPKQPRVL QENTRMGMEN EESMMSYEGD GGEVSRGLED SNISYGSYEE 

      1810       1820       1830       1840       1850       1860 
PDPKSNTQDT SFSSIGGYEV SEEEEDEEEQ RSGPSVLSQV HLSEDEEDSE DFHSIAGDSD 


MDSDE 

« Hide

References

[1]"The CCG1/TAFII250 gene is mutated in thermosensitive G1 mutants of the BHK21 cell line derived from golden hamster."
Hayashida T., Sekiguchi T., Noguchi E., Sunamoto H., Ohba T., Nishimoto T.
Gene 141:267-270(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D26114 mRNA. Translation: BAA05110.1.
PIRI48155.
RefSeqNP_001268498.1. NM_001281569.1.

3D structure databases

ProteinModelPortalQ60544.
SMRQ60544. Positions 1354-1620.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ60544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101838159.

Organism-specific databases

CTD6872.

Phylogenomic databases

HOVERGENHBG050223.

Family and domain databases

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

Entry information

Entry nameTAF1_MESAU
AccessionPrimary (citable) accession number: Q60544
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families