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Q80YV3 (TRRAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transformation/transcription domain-associated protein
Alternative name(s):
Tra1 homolog
Gene names
Name:Trrap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2565 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein, which is found in various multiprotein chromatin complexes with histone acetyltransferase activity (HAT), which gives a specific tag for epigenetic transcription activation. Component of the NuA4 histone acetyltransferase complex which is responsible for acetylation of nucleosomal histones H4 and H2A. Plays a central role in MYC transcription activation, and also participates in cell transformation by MYC. Required for p53/TP53-, E2F1- and E2F4-mediated transcription activation. Probably acts by linking transcription factors such as E1A, MYC or E2F1 to HAT complexes such as STAGA thereby allowing transcription activation. Probably not required in the steps following histone acetylation in processes of transcription activation. May be required for the mitotic checkpoint and normal cell cycle progression. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. Ref.3

Subunit structure

Interacts with MYC, E2F1 and E2F4 transcription factors. Interacts directly with p53/TP53. Interacts with GCN5L2. Component of various HAT complexes. Component of the PCAF complex, at least composed of TADA2L/ADA2, SUPT3H, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5, TAF10 and TRRAP. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of the STAGA complex, at least composed of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22. Component of the BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1, and TRRAP, which preferentially acetylates histone H4 (and H2A) within nucleosomes. Interacts with NPAT By similarity. Interaction with TELO2 AND TTI1. Component of a SWR1-like complex By similarity.

Subcellular location

Nucleus By similarity.

Domain

The PI3K/PI4K domain is required for the recruitment of HAT complexes, and the MYC-dependent transactivation. Although it is strongly related to the PI3/PI4-kinase family, it lacks the typical motifs that constitute the catalytic site of PI3/PI4-kinase proteins, and lacks such activity By similarity.

Sequence similarities

Belongs to the PI3/PI4-kinase family. TRA1 subfamily.

Contains 1 FAT domain.

Contains 1 FATC domain.

Contains 1 PI3K/PI4K domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kat2aQ9JHD23EBI-2942477,EBI-2943116

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25652565Transformation/transcription domain-associated protein
PRO_0000088852

Regions

Domain1403 – 1963561FAT
Domain2234 – 2532299PI3K/PI4K
Domain2533 – 256533FATC
Region710 – 1087378Interaction with TP53 By similarity
Motif745 – 76016Bipartite nuclear localization signal Potential

Amino acid modifications

Modified residue7491Phosphoserine By similarity
Modified residue7751Phosphoserine By similarity
Modified residue17661N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q80YV3 [UniParc].

Last modified November 28, 2003. Version 2.
Checksum: 702138B3F2642B21

FASTA2,565291,557
        10         20         30         40         50         60 
MTRKFVKRSI FLHLLRHQPA NAQIGLMEGN TFCTTLQPRL FTMDLNVVEH KVFYTELLNL 

        70         80         90        100        110        120 
CEAEDSALTK LPCYKSLPSL VPLRIAALNA LAACNYLPQS REKIIAALFK ALNSTNSELQ 

       130        140        150        160        170        180 
EAGEACMRKF LEGATIEVDQ IHTHMRPLLM MLGDYRSLTL NVVNRLTSVT RLFPNSFNDK 

       190        200        210        220        230        240 
FCDQMMQHLR KWMEVVVITH KGGQRSDGNE MKICSAIINL FHLIPAAPQT LVKPPLEVVM 

       250        260        270        280        290        300 
ETERAMLIEA GSPFREPLIK FLTRHPSQTV ELFMMGATLN DPQWSRMFMS FLKHKDARPL 

       310        320        330        340        350        360 
RDVLAANPNR FITLLLPGGA QTAVRPGSSS TSNMRLDLQF QAIKIISIIV KNDDAWLASQ 

       370        380        390        400        410        420 
HSLVSQLRRV WVSETFQERH RKENMAATNW KEPKLLAFCL LNYCKRNYGD IELLFQLLRA 

       430        440        450        460        470        480 
FTGRFLCNMT FLKEYMEEEI PKNYSIAQKR ALFFRFVEFN DPNFGDELKA KVLQHILNPA 

       490        500        510        520        530        540 
FLYSFEKGEG EQLLGPPNPE GDNPESITSV FITKVLDPEK QADMLDSLRI YLLQYATLLV 

       550        560        570        580        590        600 
EHAPHHIHDN NKNRNSKLRR LMTFAWPCLL SKACVDPACR YSGHLLLAHI IAKFAIHKKI 

       610        620        630        640        650        660 
VLQVFHSLLK AHAMEARAIV RQAMAILTPA VPARMEDGHQ MLTHWTRKII VEEGHTVPQL 

       670        680        690        700        710        720 
VHILHPIVQH FKVYYPVRHH LVQHMVSAMQ RLGFTPSVTI EQRRLAVDLS EVVIKWELQR 

       730        740        750        760        770        780 
IKDQQPDSDM DPNSSGEGVN SVSIKRGLSV DSAQEVKRFR AATGAISAVF GRSQSLPGAD 

       790        800        810        820        830        840 
SLLAKPIDKQ HTDTVVNFLI RVACQVNDNT NTAGSPGEVL SRRCVNLLKT ALRPDMWCKS 

       850        860        870        880        890        900 
ELKLQWFDKL LMTVEQPNQV NYGNICTGLE VLNFLLTVLQ SPAILSSFKP LQRGIAACMT 

       910        920        930        940        950        960 
CGNTKVLRAV HSLLSRLMSI FPTEPSTSSV ASKYEELECL YAAVGKVIYE GLTNYEKATS 

       970        980        990       1000       1010       1020 
ANPSQLFGTL MIHKSACCNN PSYIDRLISV FMRSLQKMVR EHLNPQTASG STEATAAGTS 

      1030       1040       1050       1060       1070       1080 
ELVMLSLDLV KTRLAVMSME MRKNFIQTIL TSLIEKSPDA KILRAVVKIV EEWVKNNSPM 

      1090       1100       1110       1120       1130       1140 
AANQTPTLRE KSILLVKMMT YIEKRFPEDL ELNAQFLDLV NYVYRDEALS GSELTAKLEP 

      1150       1160       1170       1180       1190       1200 
AFLSGLRCAQ PLIRAKFFEV FDNSMKRRVY ERLLYVTCSQ NWEAMGSHFW IKQCIELLLA 

      1210       1220       1230       1240       1250       1260 
VCEKSTAIGT SCQGAMLPSI TNVINLADSH DRAAFAMVTH VKQEPREREN SESKEEDVEI 

      1270       1280       1290       1300       1310       1320 
DIELAPGDQT STPKTKELSE KDIGNQLHML TNRHDKFLDT LREVKTGALL SAFVQLCHIS 

      1330       1340       1350       1360       1370       1380 
TTLAEKTWVQ LFPRLWKILS DRQQHALAGE ISPFLCSGSH QVQRDCQPSA LNCFVEAMSQ 

      1390       1400       1410       1420       1430       1440 
CVPPIPMRPC VLKYLGKTHN LWFRSTLMLE HQAFEKGLSL PIKPKQTTEF YEQESITPPQ 

      1450       1460       1470       1480       1490       1500 
QEILDSLAEL YSLLQEEDMW AGLWQKRCKF SETATAIAYE QHGFFEQAQE SYEKAMDKAK 

      1510       1520       1530       1540       1550       1560 
KEHERSNASP AIFPEYQLWE DHWIRCSKEL NQWEALTEFG QSKGHINPYL VLECAWRVSN 

      1570       1580       1590       1600       1610       1620 
WTAMKEALVQ VEVSCPKEMA WKVNMYRGYL AICHPEEQQL SFIERLVEMA SSLAIREWRR 

      1630       1640       1650       1660       1670       1680 
LPHVVSHVHT PLLQAAQQII ELQEAAQINA GLQPTNLGRN NSLHDMKTVV KTWRNRLPIV 

      1690       1700       1710       1720       1730       1740 
SDDLSHWSSV FMWRQHHYQA IVTAYENSSH HDPSSNNAML GVHASASAII QYGKIARKQG 

      1750       1760       1770       1780       1790       1800 
LVNVALDILS RIHTIPTVPI VDCFQKIRQQ VKCYLQLAGV MGKNECMQGL EVIESTNLKY 

      1810       1820       1830       1840       1850       1860 
FTKEMTAEFY ALKGMFLAQI NKSEEANKAF SAAVQMHDVL VKAWAMWGDY LESIFVKERQ 

      1870       1880       1890       1900       1910       1920 
LHLGVSAITC YLHACRHQNE SKSRKYLAKV LWLLSFDDDK NTLADAVDKY CIGVPPIQWL 

      1930       1940       1950       1960       1970       1980 
AWIPQLLTCL VGSEGKLLLN LISQVGRVYP QAVYFPIRTL YLTLKIEQRE RYKSDSGQQQ 

      1990       2000       2010       2020       2030       2040 
PSSAGNQSHS ASDPGPIRAT APMWRCSRIM HMQRELHPTL LSSLEGIVDQ MVWFRENWHE 

      2050       2060       2070       2080       2090       2100 
EVLRQLQQGL AKCYSVAFEK SGAVSDAKIT PHTLNFVKKL VSTFGVGLEN VSNVSTMFSS 

      2110       2120       2130       2140       2150       2160 
AASESLARRA QATAQDPVFQ KLKGQFTTDF DFSVPGSMKL HNLISKLKKW IKILEAKTKQ 

      2170       2180       2190       2200       2210       2220 
LPKFFLIEEK CRFLSNFSAQ TAEVEIPGEF LMPKPTHYYI KIARFMPRVE IVQKHNTAAR 

      2230       2240       2250       2260       2270       2280 
RLHIRGHNGK IYPYLVMNDA CLTESRREER VLQLLRLLNP CLEKRKETTK RHLFFTVPRV 

      2290       2300       2310       2320       2330       2340 
VAVSPQMRLV EDNPSSLSLV EIYKQRCAKK GIEHDNPISR YYDRLATVQA RGTQASHQVL 

      2350       2360       2370       2380       2390       2400 
RDILKEVQSN MVPRSMLKEW ALHTFPNATD YWTFRKMFTI QLALIGFAEF VLHLNRLNPE 

      2410       2420       2430       2440       2450       2460 
MLQIAQDTGK LNVAYFRFDI NDATGDLDAN RPVPFRLTPN ISEFLTTIGV SGPLTASMIA 

      2470       2480       2490       2500       2510       2520 
VARCFAQPNF KVDGVLKTVL RDEIIAWHKK TQEDTSSPLS AAGQPENMDS QQLVSLVQKA 

      2530       2540       2550       2560 
VTAIMTRLHN LAQFDGGESK VNTLVAAANS LDNLCRMDPA WHPWL 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Kidney.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2211-2565.
Strain: C57BL/6J.
Tissue: Head.
[3]"Disruption of Trrap causes early embryonic lethality and defects in cell cycle progression."
Herceg Z., Hulla W., Gell D., Cuenin C., Lleonart M., Jackson S., Wang Z.-Q.
Nat. Genet. 29:206-211(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC029023 mRNA. Translation: AAH29023.1.
BC050105 mRNA. Translation: AAH50105.1.
AK029388 mRNA. Translation: BAC26431.1.
UniGeneMm.273570.

3D structure databases

ProteinModelPortalQ80YV3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29177N.
IntActQ80YV3. 23 interactions.
MINTMINT-2568321.

PTM databases

PhosphoSiteQ80YV3.

Proteomic databases

PaxDbQ80YV3.
PRIDEQ80YV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:2153272. Trrap.

Phylogenomic databases

eggNOGCOG5032.
HOVERGENHBG079283.
PhylomeDBQ80YV3.

Gene expression databases

GenevestigatorQ80YV3.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.10. 3 hits.
InterProIPR016024. ARM-type_fold.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF02259. FAT. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 7 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ80YV3.
SOURCESearch...

Entry information

Entry nameTRRAP_MOUSE
AccessionPrimary (citable) accession number: Q80YV3
Secondary accession number(s): Q8C0Z5, Q8K104
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: April 16, 2014
This is version 103 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot