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Q80YV3

- TRRAP_MOUSE

UniProt

Q80YV3 - TRRAP_MOUSE

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Protein

Transformation/transcription domain-associated protein

Gene
Trrap
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. phosphotransferase activity, alcohol group as acceptor Source: InterPro
  2. protein binding Source: IntAct
  3. transcription coactivator activity Source: MGI

GO - Biological processi

  1. histone H2A acetylation Source: UniProtKB
  2. histone H4 acetylation Source: UniProtKB
  3. mitotic cell cycle checkpoint Source: MGI
  4. regulation of transcription, DNA-templated Source: MGI
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Transformation/transcription domain-associated protein
Alternative name(s):
Tra1 homolog
Gene namesi
Name:Trrap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2153272. Trrap.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. histone acetyltransferase complex Source: MGI
  2. NuA4 histone acetyltransferase complex Source: UniProtKB
  3. Swr1 complex Source: UniProtKB
  4. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25652565Transformation/transcription domain-associated proteinPRO_0000088852Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei749 – 7491Phosphoserine By similarity
Modified residuei775 – 7751Phosphoserine By similarity
Modified residuei1766 – 17661N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ80YV3.
PRIDEiQ80YV3.

PTM databases

PhosphoSiteiQ80YV3.

Expressioni

Gene expression databases

GenevestigatoriQ80YV3.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
Kat2aQ9JHD23EBI-2942477,EBI-2943116

Protein-protein interaction databases

DIPiDIP-29177N.
IntActiQ80YV3. 23 interactions.
MINTiMINT-2568321.

Structurei

3D structure databases

ProteinModelPortaliQ80YV3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1403 – 1963561FATAdd
BLAST
Domaini2234 – 2532299PI3K/PI4KAdd
BLAST
Domaini2533 – 256533FATCAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni710 – 1087378Interaction with TP53 By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi745 – 76016Bipartite nuclear localization signal Reviewed predictionAdd
BLAST

Domaini

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 similaritiesi

Contains 1 FAT domain.
Contains 1 FATC domain.
Contains 1 PI3K/PI4K domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5032.
HOVERGENiHBG079283.
PhylomeDBiQ80YV3.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.10. 3 hits.
InterProiIPR016024. 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]
PfamiPF02259. FAT. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 7 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80YV3-1 [UniParc]FASTAAdd to Basket

« Hide

MTRKFVKRSI FLHLLRHQPA NAQIGLMEGN TFCTTLQPRL FTMDLNVVEH     50
KVFYTELLNL CEAEDSALTK LPCYKSLPSL VPLRIAALNA LAACNYLPQS 100
REKIIAALFK ALNSTNSELQ EAGEACMRKF LEGATIEVDQ IHTHMRPLLM 150
MLGDYRSLTL NVVNRLTSVT RLFPNSFNDK FCDQMMQHLR KWMEVVVITH 200
KGGQRSDGNE MKICSAIINL FHLIPAAPQT LVKPPLEVVM ETERAMLIEA 250
GSPFREPLIK FLTRHPSQTV ELFMMGATLN DPQWSRMFMS FLKHKDARPL 300
RDVLAANPNR FITLLLPGGA QTAVRPGSSS TSNMRLDLQF QAIKIISIIV 350
KNDDAWLASQ HSLVSQLRRV WVSETFQERH RKENMAATNW KEPKLLAFCL 400
LNYCKRNYGD IELLFQLLRA FTGRFLCNMT FLKEYMEEEI PKNYSIAQKR 450
ALFFRFVEFN DPNFGDELKA KVLQHILNPA FLYSFEKGEG EQLLGPPNPE 500
GDNPESITSV FITKVLDPEK QADMLDSLRI YLLQYATLLV EHAPHHIHDN 550
NKNRNSKLRR LMTFAWPCLL SKACVDPACR YSGHLLLAHI IAKFAIHKKI 600
VLQVFHSLLK AHAMEARAIV RQAMAILTPA VPARMEDGHQ MLTHWTRKII 650
VEEGHTVPQL VHILHPIVQH FKVYYPVRHH LVQHMVSAMQ RLGFTPSVTI 700
EQRRLAVDLS EVVIKWELQR IKDQQPDSDM DPNSSGEGVN SVSIKRGLSV 750
DSAQEVKRFR AATGAISAVF GRSQSLPGAD SLLAKPIDKQ HTDTVVNFLI 800
RVACQVNDNT NTAGSPGEVL SRRCVNLLKT ALRPDMWCKS ELKLQWFDKL 850
LMTVEQPNQV NYGNICTGLE VLNFLLTVLQ SPAILSSFKP LQRGIAACMT 900
CGNTKVLRAV HSLLSRLMSI FPTEPSTSSV ASKYEELECL YAAVGKVIYE 950
GLTNYEKATS ANPSQLFGTL MIHKSACCNN PSYIDRLISV FMRSLQKMVR 1000
EHLNPQTASG STEATAAGTS ELVMLSLDLV KTRLAVMSME MRKNFIQTIL 1050
TSLIEKSPDA KILRAVVKIV EEWVKNNSPM AANQTPTLRE KSILLVKMMT 1100
YIEKRFPEDL ELNAQFLDLV NYVYRDEALS GSELTAKLEP AFLSGLRCAQ 1150
PLIRAKFFEV FDNSMKRRVY ERLLYVTCSQ NWEAMGSHFW IKQCIELLLA 1200
VCEKSTAIGT SCQGAMLPSI TNVINLADSH DRAAFAMVTH VKQEPREREN 1250
SESKEEDVEI DIELAPGDQT STPKTKELSE KDIGNQLHML TNRHDKFLDT 1300
LREVKTGALL SAFVQLCHIS TTLAEKTWVQ LFPRLWKILS DRQQHALAGE 1350
ISPFLCSGSH QVQRDCQPSA LNCFVEAMSQ CVPPIPMRPC VLKYLGKTHN 1400
LWFRSTLMLE HQAFEKGLSL PIKPKQTTEF YEQESITPPQ QEILDSLAEL 1450
YSLLQEEDMW AGLWQKRCKF SETATAIAYE QHGFFEQAQE SYEKAMDKAK 1500
KEHERSNASP AIFPEYQLWE DHWIRCSKEL NQWEALTEFG QSKGHINPYL 1550
VLECAWRVSN WTAMKEALVQ VEVSCPKEMA WKVNMYRGYL AICHPEEQQL 1600
SFIERLVEMA SSLAIREWRR LPHVVSHVHT PLLQAAQQII ELQEAAQINA 1650
GLQPTNLGRN NSLHDMKTVV KTWRNRLPIV SDDLSHWSSV FMWRQHHYQA 1700
IVTAYENSSH HDPSSNNAML GVHASASAII QYGKIARKQG LVNVALDILS 1750
RIHTIPTVPI VDCFQKIRQQ VKCYLQLAGV MGKNECMQGL EVIESTNLKY 1800
FTKEMTAEFY ALKGMFLAQI NKSEEANKAF SAAVQMHDVL VKAWAMWGDY 1850
LESIFVKERQ LHLGVSAITC YLHACRHQNE SKSRKYLAKV LWLLSFDDDK 1900
NTLADAVDKY CIGVPPIQWL AWIPQLLTCL VGSEGKLLLN LISQVGRVYP 1950
QAVYFPIRTL YLTLKIEQRE RYKSDSGQQQ PSSAGNQSHS ASDPGPIRAT 2000
APMWRCSRIM HMQRELHPTL LSSLEGIVDQ MVWFRENWHE EVLRQLQQGL 2050
AKCYSVAFEK SGAVSDAKIT PHTLNFVKKL VSTFGVGLEN VSNVSTMFSS 2100
AASESLARRA QATAQDPVFQ KLKGQFTTDF DFSVPGSMKL HNLISKLKKW 2150
IKILEAKTKQ LPKFFLIEEK CRFLSNFSAQ TAEVEIPGEF LMPKPTHYYI 2200
KIARFMPRVE IVQKHNTAAR RLHIRGHNGK IYPYLVMNDA CLTESRREER 2250
VLQLLRLLNP CLEKRKETTK RHLFFTVPRV VAVSPQMRLV EDNPSSLSLV 2300
EIYKQRCAKK GIEHDNPISR YYDRLATVQA RGTQASHQVL RDILKEVQSN 2350
MVPRSMLKEW ALHTFPNATD YWTFRKMFTI QLALIGFAEF VLHLNRLNPE 2400
MLQIAQDTGK LNVAYFRFDI NDATGDLDAN RPVPFRLTPN ISEFLTTIGV 2450
SGPLTASMIA VARCFAQPNF KVDGVLKTVL RDEIIAWHKK TQEDTSSPLS 2500
AAGQPENMDS QQLVSLVQKA VTAIMTRLHN LAQFDGGESK VNTLVAAANS 2550
LDNLCRMDPA WHPWL 2565
Length:2,565
Mass (Da):291,557
Last modified:November 28, 2003 - v2
Checksum:i702138B3F2642B21
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC029023 mRNA. Translation: AAH29023.1.
BC050105 mRNA. Translation: AAH50105.1.
AK029388 mRNA. Translation: BAC26431.1.
UniGeneiMm.273570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC029023 mRNA. Translation: AAH29023.1 .
BC050105 mRNA. Translation: AAH50105.1 .
AK029388 mRNA. Translation: BAC26431.1 .
UniGenei Mm.273570.

3D structure databases

ProteinModelPortali Q80YV3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29177N.
IntActi Q80YV3. 23 interactions.
MINTi MINT-2568321.

PTM databases

PhosphoSitei Q80YV3.

Proteomic databases

PaxDbi Q80YV3.
PRIDEi Q80YV3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:2153272. Trrap.

Phylogenomic databases

eggNOGi COG5032.
HOVERGENi HBG079283.
PhylomeDBi Q80YV3.

Miscellaneous databases

PROi Q80YV3.
SOURCEi Search...

Gene expression databases

Genevestigatori Q80YV3.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
1.25.40.10. 3 hits.
InterProi IPR016024. 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 ]
Pfami PF02259. FAT. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 7 hits.
SSF56112. SSF56112. 2 hits.
PROSITEi PS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTRRAP_MOUSE
AccessioniPrimary (citable) accession number: Q80YV3
Secondary accession number(s): Q8C0Z5, Q8K104
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: June 11, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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