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Q9Y4A5 (TRRAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transformation/transcription domain-associated protein
Alternative name(s):
350/400 kDa PCAF-associated factor
Short name=PAF350/400
STAF40
Tra1 homolog
Gene names
Name:TRRAP
Synonyms:PAF400
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3859 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.19 Ref.26

Subunit structure

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. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.16 Ref.17 Ref.19 Ref.22 Ref.26

Subcellular location

Nucleus Ref.1 Ref.6.

Domain

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. Ref.11

Involvement in disease

TRRAP mutation Phe-722 has been frequently found in cutaneous malignant melanoma, suggesting that TRRAP may play a role in the pathogenesis of melanoma (Ref.25).

Sequence similarities

Belongs to the PI3/PI4-kinase family. TRA1 subfamily.

Contains 1 FAT domain.

Contains 1 FATC domain.

Contains 1 PI3K/PI4K domain.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionActivator
Chromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

histone H2A acetylation

Inferred from direct assay Ref.16. Source: UniProtKB

histone H4 acetylation

Inferred from direct assay Ref.16. Source: UniProtKB

histone acetylation

Non-traceable author statement Ref.8. Source: UniProtKB

histone deubiquitination

Inferred from direct assay Ref.17. Source: UniProtKB

mitotic cell cycle checkpoint

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuA4 histone acetyltransferase complex

Inferred from direct assay Ref.8Ref.16. Source: UniProtKB

PCAF complex

Non-traceable author statement Ref.2. Source: UniProtKB

STAGA complex

Inferred from direct assay Ref.6. Source: UniProtKB

Swr1 complex

Inferred from direct assay Ref.26. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

transcription factor TFTC complex

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionphosphotransferase activity, alcohol group as acceptor

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

transcription cofactor activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y4A5-1)

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.
Isoform 2 (identifier: Q9Y4A5-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.27
Chain2 – 38593858Transformation/transcription domain-associated protein
PRO_0000088851

Regions

Domain2704 – 3275572FAT
Domain3528 – 3826299PI3K/PI4K
Domain3827 – 385933FATC
Region2010 – 2388379Interaction with TP53
Motif2047 – 206216Bipartite nuclear localization signal Potential
Compositional bias485 – 52642Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.27
Modified residue20511Phosphoserine Ref.18 Ref.20
Modified residue20771Phosphoserine Ref.20
Modified residue30781N6-acetyllysine Ref.21

Natural variations

Alternative sequence1492 – 150918Missing in isoform 2.
VSP_009102
Alternative sequence3001 – 301212GKPTW…MHSSS → A in isoform 2.
VSP_009103
Natural variant7221S → F Found in a cutaneous malignant melanoma sample; somatic mutation; induces cell transformation and confers resistance to apoptosis. Ref.25
VAR_067754
Natural variant8781R → L.
Corresponds to variant rs17161510 [ dbSNP | Ensembl ].
VAR_028359
Natural variant8931R → C in an ovarian serous carcinoma sample; somatic mutation. Ref.28
VAR_041658
Natural variant10701S → G. Ref.28
Corresponds to variant rs55920979 [ dbSNP | Ensembl ].
VAR_041659
Natural variant16691R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.28
VAR_041660
Natural variant17241R → H in a gastric adenocarcinoma sample; somatic mutation. Ref.28
VAR_041661
Natural variant19251A → V. Ref.28
VAR_041662
Natural variant19321P → L in a colorectal adenocarcinoma sample; somatic mutation. Ref.28
VAR_041663
Natural variant19471R → L in an ovarian mucinous carcinoma sample; somatic mutation. Ref.28
VAR_041664
Natural variant21391W → G. Ref.28
VAR_041665
Natural variant23021R → W in a colorectal adenocarcinoma sample; somatic mutation. Ref.28
VAR_041666
Natural variant24331S → G. Ref.28
VAR_041667
Natural variant26901P → L in a lung large cell carcinoma sample; somatic mutation. Ref.28
VAR_041668
Natural variant27501E → D. Ref.28
Corresponds to variant rs55755466 [ dbSNP | Ensembl ].
VAR_041669
Natural variant28011K → E. Ref.28
VAR_041670
Natural variant29311T → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.28
VAR_041671

Experimental info

Sequence conflict6601E → D in AAD04629. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 391E467C0047B00B

FASTA3,859437,600
        10         20         30         40         50         60 
MAFVATQGAT VVDQTTLMKK YLQFVAALTD VNTPDETKLK MMQEVSENFE NVTSSPQYST 

        70         80         90        100        110        120 
FLEHIIPRFL TFLQDGEVQF LQEKPAQQLR KLVLEIIHRI PTNEHLRPHT KNVLSVMFRF 

       130        140        150        160        170        180 
LETENEENVL ICLRIIIELH KQFRPPITQE IHHFLDFVKQ IYKELPKVVN RYFENPQVIP 

       190        200        210        220        230        240 
ENTVPPPEMV GMITTIAVKV NPEREDSETR THSIIPRGSL SLKVLAELPI IVVLMYQLYK 

       250        260        270        280        290        300 
LNIHNVVAEF VPLIMNTIAI QVSAQARQHK LYNKELYADF IAAQIKTLSF LAYIIRIYQE 

       310        320        330        340        350        360 
LVTKYSQQMV KGMLQLLSNC PAETAHLRKE LLIAAKHILT TELRNQFIPC MDKLFDESIL 

       370        380        390        400        410        420 
IGSGYTARET LRPLAYSTLA DLVHHVRQHL PLSDLSLAVQ LFAKNIDDES LPSSIQTMSC 

       430        440        450        460        470        480 
KLLLNLVDCI RSKSEQESGN GRDVLMRMLE VFVLKFHTIA RYQLSAIFKK CKPQSELGAV 

       490        500        510        520        530        540 
EAALPGVPTA PAAPGPAPSP APVPAPPPPP PPPPPATPVT PAPVPPFEKQ GEKDKEDKQT 

       550        560        570        580        590        600 
FQVTDCRSLV KTLVCGVKTI TWGITSCKAP GEAQFIPNKQ LQPKETQIYI KLVKYAMQAL 

       610        620        630        640        650        660 
DIYQVQIAGN GQTYIRVANC QTVRMKEEKE VLEHFAGVFT MMNPLTFKEI FQTTVPYMVE 

       670        680        690        700        710        720 
RISKNYALQI VANSFLANPT TSALFATILV EYLLDRLPEM GSNVELSNLY LKLFKLVFGS 

       730        740        750        760        770        780 
VSLFAAENEQ MLKPHLHKIV NSSMELAQTA KEPYNYFLLL RALFRSIGGG SHDLLYQEFL 

       790        800        810        820        830        840 
PLLPNLLQGL NMLQSGLHKQ HMKDLFVELC LTVPVRLSSL LPYLPMLMDP LVSALNGSQT 

       850        860        870        880        890        900 
LVSQGLRTLE LCVDNLQPDF LYDHIQPVRA ELMQALWRTL RNPADSISHV AYRVLGKFGG 

       910        920        930        940        950        960 
SNRKMLKESQ KLHYVVTEVQ GPSITVEFSD CKASLQLPME KAIETALDCL KSANTEPYYR 

       970        980        990       1000       1010       1020 
RQAWEVIKCF LVAMMSLEDN KHALYQLLAH PNFTEKTIPN VIISHRYKAQ DTPARKTFEQ 

      1030       1040       1050       1060       1070       1080 
ALTGAFMSAV IKDLRPSALP FVASLIRHYT MVAVAQQCGP FLLPCYQVGS QPSTAMFHSE 

      1090       1100       1110       1120       1130       1140 
ENGSKGMDPL VLIDAIAICM AYEEKELCKI GEVALAVIFD VASIILGSKE RACQLPLFSY 

      1150       1160       1170       1180       1190       1200 
IVERLCACCY EQAWYAKLGG VVSIKFLMER LPLTWVLQNQ QTFLKALLFV MMDLTGEVSN 

      1210       1220       1230       1240       1250       1260 
GAVAMAKTTL EQLLMRCATP LKDEERAEEI VAAQEKSFHH VTHDLVREVT SPNSTVRKQA 

      1270       1280       1290       1300       1310       1320 
MHSLQVLAQV TGKSVTVIME PHKEVLQDMV PPKKHLLRHQ PANAQIGLME GNTFCTTLQP 

      1330       1340       1350       1360       1370       1380 
RLFTMDLNVV EHKVFYTELL NLCEAEDSAL TKLPCYKSLP SLVPLRIAAL NALAACNYLP 

      1390       1400       1410       1420       1430       1440 
QSREKIIAAL FKALNSTNSE LQEAGEACMR KFLEGATIEV DQIHTHMRPL LMMLGDYRSL 

      1450       1460       1470       1480       1490       1500 
TLNVVNRLTS VTRLFPNSFN DKFCDQMMQH LRKWMEVVVI THKGGQRSDG NESISECGRC 

      1510       1520       1530       1540       1550       1560 
PLSPFCQFEE MKICSAIINL FHLIPAAPQT LVKPLLEVVM KTERAMLIEA GSPFREPLIK 

      1570       1580       1590       1600       1610       1620 
FLTRHPSQTV ELFMMEATLN DPQWSRMFMS FLKHKDARPL RDVLAANPNR FITLLLPGGA 

      1630       1640       1650       1660       1670       1680 
QTAVRPGSPS TSTMRLDLQF QAIKIISIIV KNDDSWLASQ HSLVSQLRRV WVSENFQERH 

      1690       1700       1710       1720       1730       1740 
RKENMAATNW KEPKLLAYCL LNYCKRNYGD IELLFQLLRA FTGRFLCNMT FLKEYMEEEI 

      1750       1760       1770       1780       1790       1800 
PKNYSIAQKR ALFFRFVDFN DPNFGDELKA KVLQHILNPA FLYSFEKGEG EQLLGPPNPE 

      1810       1820       1830       1840       1850       1860 
GDNPESITSV FITKVLDPEK QADMLDSLRI YLLQYATLLV EHAPHHIHDN NKNRNSKLRR 

      1870       1880       1890       1900       1910       1920 
LMTFAWPCLL SKACVDPACK YSGHLLLAHI IAKFAIHKKI VLQVFHSLLK AHAMEARAIV 

      1930       1940       1950       1960       1970       1980 
RQAMAILTPA VPARMEDGHQ MLTHWTRKII VEEGHTVPQL VHILHLIVQH FKVYYPVRHH 

      1990       2000       2010       2020       2030       2040 
LVQHMVSAMQ RLGFTPSVTI EQRRLAVDLS EVVIKWELQR IKDQQPDSDM DPNSSGEGVN 

      2050       2060       2070       2080       2090       2100 
SVSSSIKRGL SVDSAQEVKR FRTATGAISA VFGRSQSLPG ADSLLAKPID KQHTDTVVNF 

      2110       2120       2130       2140       2150       2160 
LIRVACQVND NTNTAGSPGE VLSRRCVNLL KTALRPDMWP KSELKLQWFD KLLMTVEQPN 

      2170       2180       2190       2200       2210       2220 
QVNYGNICTG LEVLSFLLTV LQSPAILSSF KPLQRGIAAC MTCGNTKVLR AVHSLLSRLM 

      2230       2240       2250       2260       2270       2280 
SIFPTEPSTS SVASKYEELE CLYAAVGKVI YEGLTNYEKA TNANPSQLFG TLMILKSACS 

      2290       2300       2310       2320       2330       2340 
NNPSYIDRLI SVFMRSLQKM VREHLNPQAA SGSTEATSGT SELVMLSLEL VKTRLAVMSM 

      2350       2360       2370       2380       2390       2400 
EMRKNFIQAI LTSLIEKSPD AKILRAVVKI VEEWVKNNSP MAANQTPTLR EKSILLVKMM 

      2410       2420       2430       2440       2450       2460 
TYIEKRFPED LELNAQFLDL VNYVYRDETL SGSELTAKLE PAFLSGLRCA QPLIRAKFFE 

      2470       2480       2490       2500       2510       2520 
VFDNSMKRRV YERLLYVTCS QNWEAMGNHF WIKQCIELLL AVCEKSTPIG TSCQGAMLPS 

      2530       2540       2550       2560       2570       2580 
ITNVINLADS HDRAAFAMVT HVKQEPRERE NSESKEEDVE IDIELAPGDQ TSTPKTKELS 

      2590       2600       2610       2620       2630       2640 
EKDIGNQLHM LTNRHDKFLD TLREVKTGAL LSAFVQLCHI STTLAEKTWV QLFPRLWKIL 

      2650       2660       2670       2680       2690       2700 
SDRQQHALAG EISPFLCSGS HQVQRDCQPS ALNCFVEAMS QCVPPIPIRP CVLKYLGKTH 

      2710       2720       2730       2740       2750       2760 
NLWFRSTLML EHQAFEKGLS LQIKPKQTTE FYEQESITPP QQEILDSLAE LYSLLQEEDM 

      2770       2780       2790       2800       2810       2820 
WAGLWQKRCK YSETATAIAY EQHGFFEQAQ ESYEKAMDKA KKEHERSNAS PAIFPEYQLW 

      2830       2840       2850       2860       2870       2880 
EDHWIRCSKE LNQWEALTEY GQSKGHINPY LVLECAWRVS NWTAMKEALV QVEVSCPKEM 

      2890       2900       2910       2920       2930       2940 
AWKVNMYRGY LAICHPEEQQ LSFIERLVEM ASSLAIREWR RLPHVVSHVH TPLLQAAQQI 

      2950       2960       2970       2980       2990       3000 
IELQEAAQIN AGLQPTNLGR NNSLHDMKTV VKTWRNRLPI VSDDLSHWSS IFMWRQHHYQ 

      3010       3020       3030       3040       3050       3060 
GKPTWSGMHS SSIVTAYENS SQHDPSSNNA MLGVHASASA IIQYGKIARK QGLVNVALDI 

      3070       3080       3090       3100       3110       3120 
LSRIHTIPTV PIVDCFQKIR QQVKCYLQLA GVMGKNECMQ GLEVIESTNL KYFTKEMTAE 

      3130       3140       3150       3160       3170       3180 
FYALKGMFLA QINKSEEANK AFSAAVQMHD VLVKAWAMWG DYLENIFVKE RQLHLGVSAI 

      3190       3200       3210       3220       3230       3240 
TCYLHACRHQ NESKSRKYLA KVLWLLSFDD DKNTLADAVD KYCIGVPPIQ WLAWIPQLLT 

      3250       3260       3270       3280       3290       3300 
CLVGSEGKLL LNLISQVGRV YPQAVYFPIR TLYLTLKIEQ RERYKSDPGP IRATAPMWRC 

      3310       3320       3330       3340       3350       3360 
SRIMHMQREL HPTLLSSLEG IVDQMVWFRE NWHEEVLRQL QQGLAKCYSV AFEKSGAVSD 

      3370       3380       3390       3400       3410       3420 
AKITPHTLNF VKKLVSTFGV GLENVSNVST MFSSAASESL ARRAQATAQD PVFQKLKGQF 

      3430       3440       3450       3460       3470       3480 
TTDFDFSVPG SMKLHNLISK LKKWIKILEA KTKQLPKFFL IEEKCRFLSN FSAQTAEVEI 

      3490       3500       3510       3520       3530       3540 
PGEFLMPKPT HYYIKIARFM PRVEIVQKHN TAARRLYIRG HNGKIYPYLV MNDACLTESR 

      3550       3560       3570       3580       3590       3600 
REERVLQLLR LLNPCLEKRK ETTKRHLFFT VPRVVAVSPQ MRLVEDNPSS LSLVEIYKQR 

      3610       3620       3630       3640       3650       3660 
CAKKGIEHDN PISRYYDRLA TVQARGTQAS HQVLRDILKE VQSNMVPRSM LKEWALHTFP 

      3670       3680       3690       3700       3710       3720 
NATDYWTFRK MFTIQLALIG FAEFVLHLNR LNPEMLQIAQ DTGKLNVAYF RFDINDATGD 

      3730       3740       3750       3760       3770       3780 
LDANRPVPFR LTPNISEFLT TIGVSGPLTA SMIAVARCFA QPNFKVDGIL KTVLRDEIIA 

      3790       3800       3810       3820       3830       3840 
WHKKTQEDTS SPLSAAGQPE NMDSQQLVSL VQKAVTAIMT RLHNLAQFEG GESKVNTLVA 

      3850 
AANSLDNLCR MDPAWHPWL 

« Hide

Isoform 2 [UniParc].

Checksum: 5740D4E21629560B
Show »

FASTA3,830434,414

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Exome sequencing identifies GRIN2A as frequently mutated in melanoma."
Wei X., Walia V., Lin J.C., Teer J.K., Prickett T.D., Gartner J., Davis S., Stemke-Hale K., Davies M.A., Gershenwald J.E., Robinson W., Robinson S., Rosenberg S.A., Samuels Y.
Nat. Genet. 43:442-446(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE INVOLVEMENT IN MELANOMA, VARIANT PHE-722, CHARACTERIZATION OF VARIANT PHE-722.
[26]"ANP32E is a histone chaperone that removes H2A.Z from chromatin."
Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M., Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C., Hamiche A.
Nature 505:648-653(2014) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT02632.
RefSeqNP_001231509.1. NM_001244580.1.
NP_003487.1. NM_003496.3.
UniGeneHs.203952.

3D structure databases

ProteinModelPortalQ9Y4A5.
SMRQ9Y4A5. Positions 113-139, 2195-2220, 3828-3858.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113900. 73 interactions.
DIPDIP-28149N.
IntActQ9Y4A5. 24 interactions.
MINTMINT-1955478.
STRING9606.ENSP00000347733.

PTM databases

PhosphoSiteQ9Y4A5.

Polymorphism databases

DMDM116242829.

Proteomic databases

PaxDbQ9Y4A5.
PRIDEQ9Y4A5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355540; ENSP00000347733; ENSG00000196367. [Q9Y4A5-2]
ENST00000359863; ENSP00000352925; ENSG00000196367. [Q9Y4A5-1]
ENST00000562259; ENSP00000454503; ENSG00000261023. [Q9Y4A5-2]
ENST00000565218; ENSP00000457834; ENSG00000261023. [Q9Y4A5-1]
GeneID8295.
KEGGhsa:8295.
UCSCuc003upp.3. human. [Q9Y4A5-1]
uc011kis.2. human. [Q9Y4A5-2]

Organism-specific databases

CTD8295.
GeneCardsGC07P098475.
HGNCHGNC:12347. TRRAP.
HPAHPA038203.
MIM603015. gene.
neXtProtNX_Q9Y4A5.
PharmGKBPA37020.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5032.
HOGENOMHOG000252997.
HOVERGENHBG079283.
InParanoidQ9Y4A5.
KOK08874.
OMAMEYGSSK.
PhylomeDBQ9Y4A5.
TreeFamTF106414.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.

Gene expression databases

ArrayExpressQ9Y4A5.
BgeeQ9Y4A5.
CleanExHS_TRRAP.
GenevestigatorQ9Y4A5.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.10.10. 3 hits.
1.25.40.10. 3 hits.
InterProIPR011989. 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]
PfamPF02259. FAT. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 13 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRRAP. human.
GenomeRNAi8295.
NextBio31097.
PROQ9Y4A5.
SOURCESearch...

Entry information

Entry nameTRRAP_HUMAN
AccessionPrimary (citable) accession number: Q9Y4A5
Secondary accession number(s): A4D265 expand/collapse secondary AC list , O75218, Q9Y631, Q9Y6H4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM