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Q9Y4A5

- TRRAP_HUMAN

UniProt

Q9Y4A5 - TRRAP_HUMAN

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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

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. transcription coactivator activity Source: Ensembl
  3. 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_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

BgeeiQ9Y4A5.
CleanExiHS_TRRAP.
ExpressionAtlasiQ9Y4A5. baseline and differential.
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. 83 interactions.
DIPiDIP-28149N.
IntActiQ9Y4A5. 26 interactions.
MINTiMINT-1955478.
STRINGi9606.ENSP00000347733.

Structurei

3D structure databases

ProteinModelPortaliQ9Y4A5.
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.
GeneTreeiENSGT00390000017961.
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_dom.
[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

        10         20         30         40         50
MAFVATQGAT VVDQTTLMKK YLQFVAALTD VNTPDETKLK MMQEVSENFE
60 70 80 90 100
NVTSSPQYST FLEHIIPRFL TFLQDGEVQF LQEKPAQQLR KLVLEIIHRI
110 120 130 140 150
PTNEHLRPHT KNVLSVMFRF LETENEENVL ICLRIIIELH KQFRPPITQE
160 170 180 190 200
IHHFLDFVKQ IYKELPKVVN RYFENPQVIP ENTVPPPEMV GMITTIAVKV
210 220 230 240 250
NPEREDSETR THSIIPRGSL SLKVLAELPI IVVLMYQLYK LNIHNVVAEF
260 270 280 290 300
VPLIMNTIAI QVSAQARQHK LYNKELYADF IAAQIKTLSF LAYIIRIYQE
310 320 330 340 350
LVTKYSQQMV KGMLQLLSNC PAETAHLRKE LLIAAKHILT TELRNQFIPC
360 370 380 390 400
MDKLFDESIL IGSGYTARET LRPLAYSTLA DLVHHVRQHL PLSDLSLAVQ
410 420 430 440 450
LFAKNIDDES LPSSIQTMSC KLLLNLVDCI RSKSEQESGN GRDVLMRMLE
460 470 480 490 500
VFVLKFHTIA RYQLSAIFKK CKPQSELGAV EAALPGVPTA PAAPGPAPSP
510 520 530 540 550
APVPAPPPPP PPPPPATPVT PAPVPPFEKQ GEKDKEDKQT FQVTDCRSLV
560 570 580 590 600
KTLVCGVKTI TWGITSCKAP GEAQFIPNKQ LQPKETQIYI KLVKYAMQAL
610 620 630 640 650
DIYQVQIAGN GQTYIRVANC QTVRMKEEKE VLEHFAGVFT MMNPLTFKEI
660 670 680 690 700
FQTTVPYMVE RISKNYALQI VANSFLANPT TSALFATILV EYLLDRLPEM
710 720 730 740 750
GSNVELSNLY LKLFKLVFGS VSLFAAENEQ MLKPHLHKIV NSSMELAQTA
760 770 780 790 800
KEPYNYFLLL RALFRSIGGG SHDLLYQEFL PLLPNLLQGL NMLQSGLHKQ
810 820 830 840 850
HMKDLFVELC LTVPVRLSSL LPYLPMLMDP LVSALNGSQT LVSQGLRTLE
860 870 880 890 900
LCVDNLQPDF LYDHIQPVRA ELMQALWRTL RNPADSISHV AYRVLGKFGG
910 920 930 940 950
SNRKMLKESQ KLHYVVTEVQ GPSITVEFSD CKASLQLPME KAIETALDCL
960 970 980 990 1000
KSANTEPYYR RQAWEVIKCF LVAMMSLEDN KHALYQLLAH PNFTEKTIPN
1010 1020 1030 1040 1050
VIISHRYKAQ DTPARKTFEQ ALTGAFMSAV IKDLRPSALP FVASLIRHYT
1060 1070 1080 1090 1100
MVAVAQQCGP FLLPCYQVGS QPSTAMFHSE ENGSKGMDPL VLIDAIAICM
1110 1120 1130 1140 1150
AYEEKELCKI GEVALAVIFD VASIILGSKE RACQLPLFSY IVERLCACCY
1160 1170 1180 1190 1200
EQAWYAKLGG VVSIKFLMER LPLTWVLQNQ QTFLKALLFV MMDLTGEVSN
1210 1220 1230 1240 1250
GAVAMAKTTL EQLLMRCATP LKDEERAEEI VAAQEKSFHH VTHDLVREVT
1260 1270 1280 1290 1300
SPNSTVRKQA MHSLQVLAQV TGKSVTVIME PHKEVLQDMV PPKKHLLRHQ
1310 1320 1330 1340 1350
PANAQIGLME GNTFCTTLQP RLFTMDLNVV EHKVFYTELL NLCEAEDSAL
1360 1370 1380 1390 1400
TKLPCYKSLP SLVPLRIAAL NALAACNYLP QSREKIIAAL FKALNSTNSE
1410 1420 1430 1440 1450
LQEAGEACMR KFLEGATIEV DQIHTHMRPL LMMLGDYRSL TLNVVNRLTS
1460 1470 1480 1490 1500
VTRLFPNSFN DKFCDQMMQH LRKWMEVVVI THKGGQRSDG NESISECGRC
1510 1520 1530 1540 1550
PLSPFCQFEE MKICSAIINL FHLIPAAPQT LVKPLLEVVM KTERAMLIEA
1560 1570 1580 1590 1600
GSPFREPLIK FLTRHPSQTV ELFMMEATLN DPQWSRMFMS FLKHKDARPL
1610 1620 1630 1640 1650
RDVLAANPNR FITLLLPGGA QTAVRPGSPS TSTMRLDLQF QAIKIISIIV
1660 1670 1680 1690 1700
KNDDSWLASQ HSLVSQLRRV WVSENFQERH RKENMAATNW KEPKLLAYCL
1710 1720 1730 1740 1750
LNYCKRNYGD IELLFQLLRA FTGRFLCNMT FLKEYMEEEI PKNYSIAQKR
1760 1770 1780 1790 1800
ALFFRFVDFN DPNFGDELKA KVLQHILNPA FLYSFEKGEG EQLLGPPNPE
1810 1820 1830 1840 1850
GDNPESITSV FITKVLDPEK QADMLDSLRI YLLQYATLLV EHAPHHIHDN
1860 1870 1880 1890 1900
NKNRNSKLRR LMTFAWPCLL SKACVDPACK YSGHLLLAHI IAKFAIHKKI
1910 1920 1930 1940 1950
VLQVFHSLLK AHAMEARAIV RQAMAILTPA VPARMEDGHQ MLTHWTRKII
1960 1970 1980 1990 2000
VEEGHTVPQL VHILHLIVQH FKVYYPVRHH LVQHMVSAMQ RLGFTPSVTI
2010 2020 2030 2040 2050
EQRRLAVDLS EVVIKWELQR IKDQQPDSDM DPNSSGEGVN SVSSSIKRGL
2060 2070 2080 2090 2100
SVDSAQEVKR FRTATGAISA VFGRSQSLPG ADSLLAKPID KQHTDTVVNF
2110 2120 2130 2140 2150
LIRVACQVND NTNTAGSPGE VLSRRCVNLL KTALRPDMWP KSELKLQWFD
2160 2170 2180 2190 2200
KLLMTVEQPN QVNYGNICTG LEVLSFLLTV LQSPAILSSF KPLQRGIAAC
2210 2220 2230 2240 2250
MTCGNTKVLR AVHSLLSRLM SIFPTEPSTS SVASKYEELE CLYAAVGKVI
2260 2270 2280 2290 2300
YEGLTNYEKA TNANPSQLFG TLMILKSACS NNPSYIDRLI SVFMRSLQKM
2310 2320 2330 2340 2350
VREHLNPQAA SGSTEATSGT SELVMLSLEL VKTRLAVMSM EMRKNFIQAI
2360 2370 2380 2390 2400
LTSLIEKSPD AKILRAVVKI VEEWVKNNSP MAANQTPTLR EKSILLVKMM
2410 2420 2430 2440 2450
TYIEKRFPED LELNAQFLDL VNYVYRDETL SGSELTAKLE PAFLSGLRCA
2460 2470 2480 2490 2500
QPLIRAKFFE VFDNSMKRRV YERLLYVTCS QNWEAMGNHF WIKQCIELLL
2510 2520 2530 2540 2550
AVCEKSTPIG TSCQGAMLPS ITNVINLADS HDRAAFAMVT HVKQEPRERE
2560 2570 2580 2590 2600
NSESKEEDVE IDIELAPGDQ TSTPKTKELS EKDIGNQLHM LTNRHDKFLD
2610 2620 2630 2640 2650
TLREVKTGAL LSAFVQLCHI STTLAEKTWV QLFPRLWKIL SDRQQHALAG
2660 2670 2680 2690 2700
EISPFLCSGS HQVQRDCQPS ALNCFVEAMS QCVPPIPIRP CVLKYLGKTH
2710 2720 2730 2740 2750
NLWFRSTLML EHQAFEKGLS LQIKPKQTTE FYEQESITPP QQEILDSLAE
2760 2770 2780 2790 2800
LYSLLQEEDM WAGLWQKRCK YSETATAIAY EQHGFFEQAQ ESYEKAMDKA
2810 2820 2830 2840 2850
KKEHERSNAS PAIFPEYQLW EDHWIRCSKE LNQWEALTEY GQSKGHINPY
2860 2870 2880 2890 2900
LVLECAWRVS NWTAMKEALV QVEVSCPKEM AWKVNMYRGY LAICHPEEQQ
2910 2920 2930 2940 2950
LSFIERLVEM ASSLAIREWR RLPHVVSHVH TPLLQAAQQI IELQEAAQIN
2960 2970 2980 2990 3000
AGLQPTNLGR NNSLHDMKTV VKTWRNRLPI VSDDLSHWSS IFMWRQHHYQ
3010 3020 3030 3040 3050
GKPTWSGMHS SSIVTAYENS SQHDPSSNNA MLGVHASASA IIQYGKIARK
3060 3070 3080 3090 3100
QGLVNVALDI LSRIHTIPTV PIVDCFQKIR QQVKCYLQLA GVMGKNECMQ
3110 3120 3130 3140 3150
GLEVIESTNL KYFTKEMTAE FYALKGMFLA QINKSEEANK AFSAAVQMHD
3160 3170 3180 3190 3200
VLVKAWAMWG DYLENIFVKE RQLHLGVSAI TCYLHACRHQ NESKSRKYLA
3210 3220 3230 3240 3250
KVLWLLSFDD DKNTLADAVD KYCIGVPPIQ WLAWIPQLLT CLVGSEGKLL
3260 3270 3280 3290 3300
LNLISQVGRV YPQAVYFPIR TLYLTLKIEQ RERYKSDPGP IRATAPMWRC
3310 3320 3330 3340 3350
SRIMHMQREL HPTLLSSLEG IVDQMVWFRE NWHEEVLRQL QQGLAKCYSV
3360 3370 3380 3390 3400
AFEKSGAVSD AKITPHTLNF VKKLVSTFGV GLENVSNVST MFSSAASESL
3410 3420 3430 3440 3450
ARRAQATAQD PVFQKLKGQF TTDFDFSVPG SMKLHNLISK LKKWIKILEA
3460 3470 3480 3490 3500
KTKQLPKFFL IEEKCRFLSN FSAQTAEVEI PGEFLMPKPT HYYIKIARFM
3510 3520 3530 3540 3550
PRVEIVQKHN TAARRLYIRG HNGKIYPYLV MNDACLTESR REERVLQLLR
3560 3570 3580 3590 3600
LLNPCLEKRK ETTKRHLFFT VPRVVAVSPQ MRLVEDNPSS LSLVEIYKQR
3610 3620 3630 3640 3650
CAKKGIEHDN PISRYYDRLA TVQARGTQAS HQVLRDILKE VQSNMVPRSM
3660 3670 3680 3690 3700
LKEWALHTFP NATDYWTFRK MFTIQLALIG FAEFVLHLNR LNPEMLQIAQ
3710 3720 3730 3740 3750
DTGKLNVAYF RFDINDATGD LDANRPVPFR LTPNISEFLT TIGVSGPLTA
3760 3770 3780 3790 3800
SMIAVARCFA QPNFKVDGIL KTVLRDEIIA WHKKTQEDTS SPLSAAGQPE
3810 3820 3830 3840 3850
NMDSQQLVSL VQKAVTAIMT RLHNLAQFEG GESKVNTLVA AANSLDNLCR

MDPAWHPWL
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113900. 83 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.
GeneTreei ENSGT00390000017961.
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_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

Bgeei Q9Y4A5.
CleanExi HS_TRRAP.
ExpressionAtlasi Q9Y4A5. baseline and differential.
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_dom.
[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: November 26, 2014
This is version 146 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

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