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Q9Y4A5

- TRRAP_HUMAN

UniProt

Q9Y4A5 - TRRAP_HUMAN

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Protein

Transformation/transcription domain-associated protein

Gene
TRRAP, PAF400
Organism
Homo sapiens (Human)
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. 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
Complete GO annotation...

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
Complete GO annotation...

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2704 – 3275572FATAdd
BLAST
Domaini3528 – 3826299PI3K/PI4KAdd
BLAST
Domaini3827 – 385933FATCAdd
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2047 – 206216Bipartite nuclear localization signal Reviewed predictionAdd
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

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

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.

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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.

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. VSP_009102Add
BLAST
Alternative sequencei3001 – 301212GKPTW…MHSSS → A in isoform 2. VSP_009103Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti660 – 6601E → D in AAD04629. 1 Publication

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]
ENST00000562259; ENSP00000454503; ENSG00000261023. [Q9Y4A5-2]
ENST00000565218; ENSP00000457834; ENSG00000261023. [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 ]
ENST00000562259 ; ENSP00000454503 ; ENSG00000261023 . [Q9Y4A5-2 ]
ENST00000565218 ; ENSP00000457834 ; ENSG00000261023 . [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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 143 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

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