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Q9Y4A5

- TRRAP_HUMAN

UniProt

Q9Y4A5 - TRRAP_HUMAN

Protein

Transformation/transcription domain-associated protein

Gene

TRRAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      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. Also involved in transcription activation mediated by the adenovirus E1A, a viral oncoprotein that deregulates transcription of key genes. 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.8 Publications

    GO - Molecular functioni

    1. phosphotransferase activity, alcohol group as acceptor Source: InterPro
    2. protein binding Source: UniProtKB
    3. transcription coactivator activity Source: Ensembl
    4. transcription cofactor activity Source: UniProtKB

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone acetylation Source: UniProtKB
    3. histone deubiquitination Source: UniProtKB
    4. histone H2A acetylation Source: UniProtKB
    5. histone H4 acetylation Source: UniProtKB
    6. mitotic cell cycle checkpoint Source: Ensembl
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transformation/transcription domain-associated protein
    Alternative name(s):
    350/400 kDa PCAF-associated factor
    Short name:
    PAF350/400
    STAF40
    Tra1 homolog
    Gene namesi
    Name:TRRAP
    Synonyms:PAF400
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:12347. TRRAP.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. NuA4 histone acetyltransferase complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. PCAF complex Source: UniProtKB
    5. STAGA complex Source: UniProtKB
    6. Swr1 complex Source: UniProtKB
    7. transcription factor TFTC complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    TRRAP mutation Phe-722 has been frequently found in cutaneous malignant melanoma, suggesting that TRRAP may play a role in the pathogenesis of melanoma.1 Publication

    Organism-specific databases

    PharmGKBiPA37020.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 38593858Transformation/transcription domain-associated proteinPRO_0000088851Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei2051 – 20511Phosphoserine2 Publications
    Modified residuei2077 – 20771Phosphoserine1 Publication
    Modified residuei3078 – 30781N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y4A5.
    PaxDbiQ9Y4A5.
    PRIDEiQ9Y4A5.

    PTM databases

    PhosphoSiteiQ9Y4A5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y4A5.
    BgeeiQ9Y4A5.
    CleanExiHS_TRRAP.
    GenevestigatoriQ9Y4A5.

    Organism-specific databases

    HPAiHPA038203.

    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. Interaction with TELO2 AND TTI1. Component of a SWR1-like complex.14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN7O152656EBI-399128,EBI-708350
    BRCA1P383988EBI-399128,EBI-349905
    ESRRAP114743EBI-399128,EBI-372412
    MYCP011064EBI-399128,EBI-447544

    Protein-protein interaction databases

    BioGridi113900. 75 interactions.
    DIPiDIP-28149N.
    IntActiQ9Y4A5. 26 interactions.
    MINTiMINT-1955478.
    STRINGi9606.ENSP00000347733.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y4A5.
    SMRiQ9Y4A5. Positions 113-139, 2195-2220, 3828-3858.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2704 – 3275572FATPROSITE-ProRule annotationAdd
    BLAST
    Domaini3528 – 3826299PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST
    Domaini3827 – 385933FATCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2010 – 2388379Interaction with TP53Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2047 – 206216Bipartite nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi485 – 52642Pro-richAdd
    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.1 Publication

    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

    Phylogenomic databases

    eggNOGiCOG5032.
    HOGENOMiHOG000252997.
    HOVERGENiHBG079283.
    InParanoidiQ9Y4A5.
    KOiK08874.
    OMAiETWVERH.
    PhylomeDBiQ9Y4A5.
    TreeFamiTF106414.

    Family and domain databases

    Gene3Di1.10.1070.11. 1 hit.
    1.25.10.10. 3 hits.
    1.25.40.10. 3 hits.
    InterProiIPR011989. ARM-like.
    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]
    PfamiPF02259. FAT. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    [Graphical view]
    SMARTiSM00146. PI3Kc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 13 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEiPS51189. FAT. 1 hit.
    PS51190. FATC. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y4A5-1) [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

    MAFVATQGAT VVDQTTLMKK YLQFVAALTD VNTPDETKLK MMQEVSENFE     50
    NVTSSPQYST FLEHIIPRFL TFLQDGEVQF LQEKPAQQLR KLVLEIIHRI 100
    PTNEHLRPHT KNVLSVMFRF LETENEENVL ICLRIIIELH KQFRPPITQE 150
    IHHFLDFVKQ IYKELPKVVN RYFENPQVIP ENTVPPPEMV GMITTIAVKV 200
    NPEREDSETR THSIIPRGSL SLKVLAELPI IVVLMYQLYK LNIHNVVAEF 250
    VPLIMNTIAI QVSAQARQHK LYNKELYADF IAAQIKTLSF LAYIIRIYQE 300
    LVTKYSQQMV KGMLQLLSNC PAETAHLRKE LLIAAKHILT TELRNQFIPC 350
    MDKLFDESIL IGSGYTARET LRPLAYSTLA DLVHHVRQHL PLSDLSLAVQ 400
    LFAKNIDDES LPSSIQTMSC KLLLNLVDCI RSKSEQESGN GRDVLMRMLE 450
    VFVLKFHTIA RYQLSAIFKK CKPQSELGAV EAALPGVPTA PAAPGPAPSP 500
    APVPAPPPPP PPPPPATPVT PAPVPPFEKQ GEKDKEDKQT FQVTDCRSLV 550
    KTLVCGVKTI TWGITSCKAP GEAQFIPNKQ LQPKETQIYI KLVKYAMQAL 600
    DIYQVQIAGN GQTYIRVANC QTVRMKEEKE VLEHFAGVFT MMNPLTFKEI 650
    FQTTVPYMVE RISKNYALQI VANSFLANPT TSALFATILV EYLLDRLPEM 700
    GSNVELSNLY LKLFKLVFGS VSLFAAENEQ MLKPHLHKIV NSSMELAQTA 750
    KEPYNYFLLL RALFRSIGGG SHDLLYQEFL PLLPNLLQGL NMLQSGLHKQ 800
    HMKDLFVELC LTVPVRLSSL LPYLPMLMDP LVSALNGSQT LVSQGLRTLE 850
    LCVDNLQPDF LYDHIQPVRA ELMQALWRTL RNPADSISHV AYRVLGKFGG 900
    SNRKMLKESQ KLHYVVTEVQ GPSITVEFSD CKASLQLPME KAIETALDCL 950
    KSANTEPYYR RQAWEVIKCF LVAMMSLEDN KHALYQLLAH PNFTEKTIPN 1000
    VIISHRYKAQ DTPARKTFEQ ALTGAFMSAV IKDLRPSALP FVASLIRHYT 1050
    MVAVAQQCGP FLLPCYQVGS QPSTAMFHSE ENGSKGMDPL VLIDAIAICM 1100
    AYEEKELCKI GEVALAVIFD VASIILGSKE RACQLPLFSY IVERLCACCY 1150
    EQAWYAKLGG VVSIKFLMER LPLTWVLQNQ QTFLKALLFV MMDLTGEVSN 1200
    GAVAMAKTTL EQLLMRCATP LKDEERAEEI VAAQEKSFHH VTHDLVREVT 1250
    SPNSTVRKQA MHSLQVLAQV TGKSVTVIME PHKEVLQDMV PPKKHLLRHQ 1300
    PANAQIGLME GNTFCTTLQP RLFTMDLNVV EHKVFYTELL NLCEAEDSAL 1350
    TKLPCYKSLP SLVPLRIAAL NALAACNYLP QSREKIIAAL FKALNSTNSE 1400
    LQEAGEACMR KFLEGATIEV DQIHTHMRPL LMMLGDYRSL TLNVVNRLTS 1450
    VTRLFPNSFN DKFCDQMMQH LRKWMEVVVI THKGGQRSDG NESISECGRC 1500
    PLSPFCQFEE MKICSAIINL FHLIPAAPQT LVKPLLEVVM KTERAMLIEA 1550
    GSPFREPLIK FLTRHPSQTV ELFMMEATLN DPQWSRMFMS FLKHKDARPL 1600
    RDVLAANPNR FITLLLPGGA QTAVRPGSPS TSTMRLDLQF QAIKIISIIV 1650
    KNDDSWLASQ HSLVSQLRRV WVSENFQERH RKENMAATNW KEPKLLAYCL 1700
    LNYCKRNYGD IELLFQLLRA FTGRFLCNMT FLKEYMEEEI PKNYSIAQKR 1750
    ALFFRFVDFN DPNFGDELKA KVLQHILNPA FLYSFEKGEG EQLLGPPNPE 1800
    GDNPESITSV FITKVLDPEK QADMLDSLRI YLLQYATLLV EHAPHHIHDN 1850
    NKNRNSKLRR LMTFAWPCLL SKACVDPACK YSGHLLLAHI IAKFAIHKKI 1900
    VLQVFHSLLK AHAMEARAIV RQAMAILTPA VPARMEDGHQ MLTHWTRKII 1950
    VEEGHTVPQL VHILHLIVQH FKVYYPVRHH LVQHMVSAMQ RLGFTPSVTI 2000
    EQRRLAVDLS EVVIKWELQR IKDQQPDSDM DPNSSGEGVN SVSSSIKRGL 2050
    SVDSAQEVKR FRTATGAISA VFGRSQSLPG ADSLLAKPID KQHTDTVVNF 2100
    LIRVACQVND NTNTAGSPGE VLSRRCVNLL KTALRPDMWP KSELKLQWFD 2150
    KLLMTVEQPN QVNYGNICTG LEVLSFLLTV LQSPAILSSF KPLQRGIAAC 2200
    MTCGNTKVLR AVHSLLSRLM SIFPTEPSTS SVASKYEELE CLYAAVGKVI 2250
    YEGLTNYEKA TNANPSQLFG TLMILKSACS NNPSYIDRLI SVFMRSLQKM 2300
    VREHLNPQAA SGSTEATSGT SELVMLSLEL VKTRLAVMSM EMRKNFIQAI 2350
    LTSLIEKSPD AKILRAVVKI VEEWVKNNSP MAANQTPTLR EKSILLVKMM 2400
    TYIEKRFPED LELNAQFLDL VNYVYRDETL SGSELTAKLE PAFLSGLRCA 2450
    QPLIRAKFFE VFDNSMKRRV YERLLYVTCS QNWEAMGNHF WIKQCIELLL 2500
    AVCEKSTPIG TSCQGAMLPS ITNVINLADS HDRAAFAMVT HVKQEPRERE 2550
    NSESKEEDVE IDIELAPGDQ TSTPKTKELS EKDIGNQLHM LTNRHDKFLD 2600
    TLREVKTGAL LSAFVQLCHI STTLAEKTWV QLFPRLWKIL SDRQQHALAG 2650
    EISPFLCSGS HQVQRDCQPS ALNCFVEAMS QCVPPIPIRP CVLKYLGKTH 2700
    NLWFRSTLML EHQAFEKGLS LQIKPKQTTE FYEQESITPP QQEILDSLAE 2750
    LYSLLQEEDM WAGLWQKRCK YSETATAIAY EQHGFFEQAQ ESYEKAMDKA 2800
    KKEHERSNAS PAIFPEYQLW EDHWIRCSKE LNQWEALTEY GQSKGHINPY 2850
    LVLECAWRVS NWTAMKEALV QVEVSCPKEM AWKVNMYRGY LAICHPEEQQ 2900
    LSFIERLVEM ASSLAIREWR RLPHVVSHVH TPLLQAAQQI IELQEAAQIN 2950
    AGLQPTNLGR NNSLHDMKTV VKTWRNRLPI VSDDLSHWSS IFMWRQHHYQ 3000
    GKPTWSGMHS SSIVTAYENS SQHDPSSNNA MLGVHASASA IIQYGKIARK 3050
    QGLVNVALDI LSRIHTIPTV PIVDCFQKIR QQVKCYLQLA GVMGKNECMQ 3100
    GLEVIESTNL KYFTKEMTAE FYALKGMFLA QINKSEEANK AFSAAVQMHD 3150
    VLVKAWAMWG DYLENIFVKE RQLHLGVSAI TCYLHACRHQ NESKSRKYLA 3200
    KVLWLLSFDD DKNTLADAVD KYCIGVPPIQ WLAWIPQLLT CLVGSEGKLL 3250
    LNLISQVGRV YPQAVYFPIR TLYLTLKIEQ RERYKSDPGP IRATAPMWRC 3300
    SRIMHMQREL HPTLLSSLEG IVDQMVWFRE NWHEEVLRQL QQGLAKCYSV 3350
    AFEKSGAVSD AKITPHTLNF VKKLVSTFGV GLENVSNVST MFSSAASESL 3400
    ARRAQATAQD PVFQKLKGQF TTDFDFSVPG SMKLHNLISK LKKWIKILEA 3450
    KTKQLPKFFL IEEKCRFLSN FSAQTAEVEI PGEFLMPKPT HYYIKIARFM 3500
    PRVEIVQKHN TAARRLYIRG HNGKIYPYLV MNDACLTESR REERVLQLLR 3550
    LLNPCLEKRK ETTKRHLFFT VPRVVAVSPQ MRLVEDNPSS LSLVEIYKQR 3600
    CAKKGIEHDN PISRYYDRLA TVQARGTQAS HQVLRDILKE VQSNMVPRSM 3650
    LKEWALHTFP NATDYWTFRK MFTIQLALIG FAEFVLHLNR LNPEMLQIAQ 3700
    DTGKLNVAYF RFDINDATGD LDANRPVPFR LTPNISEFLT TIGVSGPLTA 3750
    SMIAVARCFA QPNFKVDGIL KTVLRDEIIA WHKKTQEDTS SPLSAAGQPE 3800
    NMDSQQLVSL VQKAVTAIMT RLHNLAQFEG GESKVNTLVA AANSLDNLCR 3850
    MDPAWHPWL 3859
    Length:3,859
    Mass (Da):437,600
    Last modified:October 17, 2006 - v3
    Checksum:i391E467C0047B00B
    GO
    Isoform 2 (identifier: Q9Y4A5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1492-1509: Missing.
         3001-3012: GKPTWSGMHSSS → A

    Show »
    Length:3,830
    Mass (Da):434,414
    Checksum:i5740D4E21629560B
    GO

    Sequence cautioni

    The sequence AAC62433.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti660 – 6601E → D in AAD04629. (PubMed:9885574)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti722 – 7221S → F Found in a cutaneous malignant melanoma sample; somatic mutation; induces cell transformation and confers resistance to apoptosis. 1 Publication
    VAR_067754
    Natural varianti878 – 8781R → L.
    Corresponds to variant rs17161510 [ dbSNP | Ensembl ].
    VAR_028359
    Natural varianti893 – 8931R → C in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
    VAR_041658
    Natural varianti1070 – 10701S → G.1 Publication
    Corresponds to variant rs55920979 [ dbSNP | Ensembl ].
    VAR_041659
    Natural varianti1669 – 16691R → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041660
    Natural varianti1724 – 17241R → H in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041661
    Natural varianti1925 – 19251A → V.1 Publication
    VAR_041662
    Natural varianti1932 – 19321P → L in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041663
    Natural varianti1947 – 19471R → L in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_041664
    Natural varianti2139 – 21391W → G.1 Publication
    VAR_041665
    Natural varianti2302 – 23021R → W in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041666
    Natural varianti2433 – 24331S → G.1 Publication
    VAR_041667
    Natural varianti2690 – 26901P → L in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041668
    Natural varianti2750 – 27501E → D.1 Publication
    Corresponds to variant rs55755466 [ dbSNP | Ensembl ].
    VAR_041669
    Natural varianti2801 – 28011K → E.1 Publication
    VAR_041670
    Natural varianti2931 – 29311T → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041671

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1492 – 150918Missing in isoform 2. 1 PublicationVSP_009102Add
    BLAST
    Alternative sequencei3001 – 301212GKPTW…MHSSS → A in isoform 2. 1 PublicationVSP_009103Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076974 mRNA. Translation: AAD09420.1.
    AF110377 mRNA. Translation: AAD04629.1.
    AC004893 Genomic DNA. Translation: AAC62433.1. Sequence problems.
    AC004991 Genomic DNA. Translation: AAC27675.2.
    CH471091 Genomic DNA. Translation: EAW76694.1.
    CH236956 Genomic DNA. Translation: EAL23887.1.
    CCDSiCCDS5659.1. [Q9Y4A5-2]
    CCDS59066.1. [Q9Y4A5-1]
    PIRiT02632.
    RefSeqiNP_001231509.1. NM_001244580.1. [Q9Y4A5-1]
    NP_003487.1. NM_003496.3. [Q9Y4A5-2]
    UniGeneiHs.203952.

    Genome annotation databases

    EnsembliENST00000355540; ENSP00000347733; ENSG00000196367. [Q9Y4A5-2]
    ENST00000359863; ENSP00000352925; ENSG00000196367. [Q9Y4A5-1]
    GeneIDi8295.
    KEGGihsa:8295.
    UCSCiuc003upp.3. human. [Q9Y4A5-1]
    uc011kis.2. human. [Q9Y4A5-2]

    Polymorphism databases

    DMDMi116242829.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076974 mRNA. Translation: AAD09420.1 .
    AF110377 mRNA. Translation: AAD04629.1 .
    AC004893 Genomic DNA. Translation: AAC62433.1 . Sequence problems.
    AC004991 Genomic DNA. Translation: AAC27675.2 .
    CH471091 Genomic DNA. Translation: EAW76694.1 .
    CH236956 Genomic DNA. Translation: EAL23887.1 .
    CCDSi CCDS5659.1. [Q9Y4A5-2 ]
    CCDS59066.1. [Q9Y4A5-1 ]
    PIRi T02632.
    RefSeqi NP_001231509.1. NM_001244580.1. [Q9Y4A5-1 ]
    NP_003487.1. NM_003496.3. [Q9Y4A5-2 ]
    UniGenei Hs.203952.

    3D structure databases

    ProteinModelPortali Q9Y4A5.
    SMRi Q9Y4A5. Positions 113-139, 2195-2220, 3828-3858.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113900. 75 interactions.
    DIPi DIP-28149N.
    IntActi Q9Y4A5. 26 interactions.
    MINTi MINT-1955478.
    STRINGi 9606.ENSP00000347733.

    PTM databases

    PhosphoSitei Q9Y4A5.

    Polymorphism databases

    DMDMi 116242829.

    Proteomic databases

    MaxQBi Q9Y4A5.
    PaxDbi Q9Y4A5.
    PRIDEi Q9Y4A5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355540 ; ENSP00000347733 ; ENSG00000196367 . [Q9Y4A5-2 ]
    ENST00000359863 ; ENSP00000352925 ; ENSG00000196367 . [Q9Y4A5-1 ]
    GeneIDi 8295.
    KEGGi hsa:8295.
    UCSCi uc003upp.3. human. [Q9Y4A5-1 ]
    uc011kis.2. human. [Q9Y4A5-2 ]

    Organism-specific databases

    CTDi 8295.
    GeneCardsi GC07P098475.
    HGNCi HGNC:12347. TRRAP.
    HPAi HPA038203.
    MIMi 603015. gene.
    neXtProti NX_Q9Y4A5.
    PharmGKBi PA37020.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5032.
    HOGENOMi HOG000252997.
    HOVERGENi HBG079283.
    InParanoidi Q9Y4A5.
    KOi K08874.
    OMAi ETWVERH.
    PhylomeDBi Q9Y4A5.
    TreeFami TF106414.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.

    Miscellaneous databases

    ChiTaRSi TRRAP. human.
    GenomeRNAii 8295.
    NextBioi 31097.
    PROi Q9Y4A5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y4A5.
    Bgeei Q9Y4A5.
    CleanExi HS_TRRAP.
    Genevestigatori Q9Y4A5.

    Family and domain databases

    Gene3Di 1.10.1070.11. 1 hit.
    1.25.10.10. 3 hits.
    1.25.40.10. 3 hits.
    InterProi IPR011989. ARM-like.
    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. 13 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 novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins."
      McMahon S.B., Van Buskirk H.A., Dugan K.A., Copeland T.D., Cole M.D.
      Cell 94:363-374(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYC AND E2F1.
      Tissue: Cervix carcinoma.
    2. "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily."
      Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J., Nakatani Y.
      Mol. Cell 2:869-875(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 41-90; 337-344; 369-387; 879-892; 997-1005; 1171-1184; 1237-1247; 1545-1560; 1815-1820; 1922-1934; 2211-2218; 2260-2275; 2534-2547; 2583-2594; 2706-2726; 2830-2844; 3567-3573; 3583-3598; 3604-3614; 3712-3730 AND 3822-3834, IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; TAF6L; TAF10; SUPT3H; TAF12 AND TAF9.
      Tissue: Fetal heart.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo."
      Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G.
      Mol. Cell. Biol. 21:6782-6795(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; GCN5L2; KIAA0764; TAF5L; TAF6L; TADA3L; TAF10; TAF12 AND TAF9, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction."
      Brand M., Yamamoto K., Staub A., Tora L.
      J. Biol. Chem. 274:18285-18289(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; TAF2; TAF4; TAF5; GCN5L2 AND TAF10.
    8. "Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis."
      Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., Scully R., Qin J., Nakatani Y.
      Cell 102:463-473(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TIP60 HAT COMPLEX WITH KAT5; RUVBL1 AND RUVBL2.
    9. "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc."
      McMahon S.B., Wood M.A., Cole M.D.
      Mol. Cell. Biol. 20:556-562(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GCN5L2.
    10. "E2F transcriptional activation requires TRRAP and GCN5 cofactors."
      Lang S.E., McMahon S.B., Cole M.D., Hearing P.
      J. Biol. Chem. 276:32627-32634(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH E2F1 AND E2F4, FUNCTION.
    11. "The ATM-related domain of TRRAP is required for histone acetyltransferase recruitment and Myc-dependent oncogenesis."
      Park J., Kunjibettu S., McMahon S.B., Cole M.D.
      Genes Dev. 15:1619-1624(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    12. "Transcriptional regulation of the mdm2 oncogene by p53 requires TRRAP acetyltransferase complexes."
      Ard P.G., Chatterjee C., Kunjibettu S., Adside L.R., Gralinski L.E., McMahon S.B.
      Mol. Cell. Biol. 22:5650-5661(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53.
    13. "BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation."
      Park J., Wood M.A., Cole M.D.
      Mol. Cell. Biol. 22:1307-1316(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND SMARCA4.
    14. "The adenovirus E1A oncoprotein recruits the cellular TRRAP/GCN5 histone acetyltransferase complex."
      Lang S.E., Hearing P.
      Oncogene 22:2836-2841(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation."
      Liu X., Tesfai J., Evrard Y.A., Dent S.Y.R., Martinez E.
      J. Biol. Chem. 278:20405-20412(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
      Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
      Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 COMPLEX.
    17. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
      Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
      Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN STAGA COMPLEX.
    18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2051, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Transcriptional activation of histone genes requires NPAT-dependent recruitment of TRRAP-Tip60 complex to histone promoters during the G1/S phase transition."
      DeRan M., Pulvino M., Greene E., Su C., Zhao J.
      Mol. Cell. Biol. 28:435-447(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NPAT.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2051 AND SER-2077, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3078, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly."
      Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., Iemura S., Natsume T., Mizushima N.
      J. Biol. Chem. 285:20109-20116(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TELO2 AND TTI1.
    23. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: PROBABLE INVOLVEMENT IN MELANOMA, VARIANT PHE-722, CHARACTERIZATION OF VARIANT PHE-722.
    26. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
    27. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    28. "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] CYS-893; GLY-1070; HIS-1669; HIS-1724; VAL-1925; LEU-1932; LEU-1947; GLY-2139; TRP-2302; GLY-2433; LEU-2690; ASP-2750; GLU-2801 AND MET-2931.

    Entry informationi

    Entry nameiTRRAP_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4A5
    Secondary accession number(s): A4D265
    , O75218, Q9Y631, Q9Y6H4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3