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Q80YV3

- TRRAP_MOUSE

UniProt

Q80YV3 - TRRAP_MOUSE

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
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (28 Nov 2003)
      Previous versions | rss
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    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

    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

    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 – 7491PhosphoserineBy similarity
    Modified residuei775 – 7751PhosphoserineBy similarity
    Modified residuei1766 – 17661N6-acetyllysineBy 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.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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1403 – 1963561FATPROSITE-ProRule annotationAdd
    BLAST
    Domaini2234 – 2532299PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST
    Domaini2533 – 256533FATCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni710 – 1087378Interaction with TP53By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi745 – 76016Bipartite nuclear localization signalSequence AnalysisAdd
    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.By similarity

    Sequence similaritiesi

    Belongs to the PI3/PI4-kinase family. TRA1 subfamily.Curated
    Contains 1 FAT domain.PROSITE-ProRule annotation
    Contains 1 FATC domain.PROSITE-ProRule annotation
    Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation

    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

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    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

    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: October 1, 2014
    This is version 105 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