Q9Y4A5 (TRRAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3859 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.19
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. 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
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Activator Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	histone H2A acetylation Inferred from direct assay Ref.16. Source: UniProtKB histone H4 acetylation Inferred from direct assay Ref.16. Source: UniProtKB histone deubiquitination Inferred from direct assay Ref.17. Source: UniProtKB mitotic cell cycle checkpoint Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	NuA4 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 transcription factor TFTC complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro transcription coactivator activity Inferred from electronic annotation. Source: Compara transcription cofactor activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN7	O15265	6	EBI-399128,EBI-708350
BRCA1	P38398	8	EBI-399128,EBI-349905
ESRRA	P11474	3	EBI-399128,EBI-372412
MYC	P01106	4	EBI-399128,EBI-447544

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3859	3859	Transformation/transcription domain-associated protein		PRO_0000088851
Regions
	Domain	2704 – 3275	572	FAT
	Domain	3528 – 3826	299	PI3K/PI4K
	Domain	3827 – 3859	33	FATC
	Region	2010 – 2388	379	Interaction with TP53
	Motif	2047 – 2062	16	Bipartite nuclear localization signal Potential
	Compositional bias	485 – 526	42	Pro-rich
Amino acid modifications
	Modified residue	2051	1	Phosphoserine Ref.18 Ref.20
	Modified residue	2077	1	Phosphoserine Ref.20
	Modified residue	3078	1	N6-acetyllysine Ref.21
Natural variations
	Alternative sequence	1492 – 1509	18	Missing in isoform 2.		VSP_009102
	Alternative sequence	3001 – 3012	12	GKPTW…MHSSS → A in isoform 2.		VSP_009103
	Natural variant	722	1	S → F Found in a cutaneous malignant melanoma sample; somatic mutation; induces cell transformation and confers resistance to apoptosis. Ref.25		VAR_067754
	Natural variant	878	1	R → L. Corresponds to variant rs17161510 [ dbSNP | Ensembl ].		VAR_028359
	Natural variant	893	1	R → C in an ovarian serous carcinoma sample; somatic mutation. Ref.26		VAR_041658
	Natural variant	1070	1	S → G. Ref.26 Corresponds to variant rs55920979 [ dbSNP | Ensembl ].		VAR_041659
	Natural variant	1669	1	R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.26		VAR_041660
	Natural variant	1724	1	R → H in a gastric adenocarcinoma sample; somatic mutation. Ref.26		VAR_041661
	Natural variant	1925	1	A → V. Ref.26		VAR_041662
	Natural variant	1932	1	P → L in a colorectal adenocarcinoma sample; somatic mutation. Ref.26		VAR_041663
	Natural variant	1947	1	R → L in an ovarian mucinous carcinoma sample; somatic mutation. Ref.26		VAR_041664
	Natural variant	2139	1	W → G. Ref.26		VAR_041665
	Natural variant	2302	1	R → W in a colorectal adenocarcinoma sample; somatic mutation. Ref.26		VAR_041666
	Natural variant	2433	1	S → G. Ref.26		VAR_041667
	Natural variant	2690	1	P → L in a lung large cell carcinoma sample; somatic mutation. Ref.26		VAR_041668
	Natural variant	2750	1	E → D. Ref.26		VAR_041669
	Natural variant	2801	1	K → E. Ref.26		VAR_041670
	Natural variant	2931	1	T → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.26		VAR_041671
Experimental info
	Sequence conflict	660	1	E → D in AAD04629. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 391E467C0047B00B	FASTA	3,859	437,600
	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
	Isoform 2 [UniParc]. Checksum: 5740D4E21629560B	FASTA	3,830	434,414
	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 NEMKICSAII 1510 1520 1530 1540 1550 1560 NLFHLIPAAP QTLVKPLLEV VMKTERAMLI EAGSPFREPL IKFLTRHPSQ TVELFMMEAT 1570 1580 1590 1600 1610 1620 LNDPQWSRMF MSFLKHKDAR PLRDVLAANP NRFITLLLPG GAQTAVRPGS PSTSTMRLDL 1630 1640 1650 1660 1670 1680 QFQAIKIISI IVKNDDSWLA SQHSLVSQLR RVWVSENFQE RHRKENMAAT NWKEPKLLAY 1690 1700 1710 1720 1730 1740 CLLNYCKRNY GDIELLFQLL RAFTGRFLCN MTFLKEYMEE EIPKNYSIAQ KRALFFRFVD 1750 1760 1770 1780 1790 1800 FNDPNFGDEL KAKVLQHILN PAFLYSFEKG EGEQLLGPPN PEGDNPESIT SVFITKVLDP 1810 1820 1830 1840 1850 1860 EKQADMLDSL RIYLLQYATL LVEHAPHHIH DNNKNRNSKL RRLMTFAWPC LLSKACVDPA 1870 1880 1890 1900 1910 1920 CKYSGHLLLA HIIAKFAIHK KIVLQVFHSL LKAHAMEARA IVRQAMAILT PAVPARMEDG 1930 1940 1950 1960 1970 1980 HQMLTHWTRK IIVEEGHTVP QLVHILHLIV QHFKVYYPVR HHLVQHMVSA MQRLGFTPSV 1990 2000 2010 2020 2030 2040 TIEQRRLAVD LSEVVIKWEL QRIKDQQPDS DMDPNSSGEG VNSVSSSIKR GLSVDSAQEV 2050 2060 2070 2080 2090 2100 KRFRTATGAI SAVFGRSQSL PGADSLLAKP IDKQHTDTVV NFLIRVACQV NDNTNTAGSP 2110 2120 2130 2140 2150 2160 GEVLSRRCVN LLKTALRPDM WPKSELKLQW FDKLLMTVEQ PNQVNYGNIC TGLEVLSFLL 2170 2180 2190 2200 2210 2220 TVLQSPAILS SFKPLQRGIA ACMTCGNTKV LRAVHSLLSR LMSIFPTEPS TSSVASKYEE 2230 2240 2250 2260 2270 2280 LECLYAAVGK VIYEGLTNYE KATNANPSQL FGTLMILKSA CSNNPSYIDR LISVFMRSLQ 2290 2300 2310 2320 2330 2340 KMVREHLNPQ AASGSTEATS GTSELVMLSL ELVKTRLAVM SMEMRKNFIQ AILTSLIEKS 2350 2360 2370 2380 2390 2400 PDAKILRAVV KIVEEWVKNN SPMAANQTPT LREKSILLVK MMTYIEKRFP EDLELNAQFL 2410 2420 2430 2440 2450 2460 DLVNYVYRDE TLSGSELTAK LEPAFLSGLR CAQPLIRAKF FEVFDNSMKR RVYERLLYVT 2470 2480 2490 2500 2510 2520 CSQNWEAMGN HFWIKQCIEL LLAVCEKSTP IGTSCQGAML PSITNVINLA DSHDRAAFAM 2530 2540 2550 2560 2570 2580 VTHVKQEPRE RENSESKEED VEIDIELAPG DQTSTPKTKE LSEKDIGNQL HMLTNRHDKF 2590 2600 2610 2620 2630 2640 LDTLREVKTG ALLSAFVQLC HISTTLAEKT WVQLFPRLWK ILSDRQQHAL AGEISPFLCS 2650 2660 2670 2680 2690 2700 GSHQVQRDCQ PSALNCFVEA MSQCVPPIPI RPCVLKYLGK THNLWFRSTL MLEHQAFEKG 2710 2720 2730 2740 2750 2760 LSLQIKPKQT TEFYEQESIT PPQQEILDSL AELYSLLQEE DMWAGLWQKR CKYSETATAI 2770 2780 2790 2800 2810 2820 AYEQHGFFEQ AQESYEKAMD KAKKEHERSN ASPAIFPEYQ LWEDHWIRCS KELNQWEALT 2830 2840 2850 2860 2870 2880 EYGQSKGHIN PYLVLECAWR VSNWTAMKEA LVQVEVSCPK EMAWKVNMYR GYLAICHPEE 2890 2900 2910 2920 2930 2940 QQLSFIERLV EMASSLAIRE WRRLPHVVSH VHTPLLQAAQ QIIELQEAAQ INAGLQPTNL 2950 2960 2970 2980 2990 3000 GRNNSLHDMK TVVKTWRNRL PIVSDDLSHW SSIFMWRQHH YQAIVTAYEN SSQHDPSSNN 3010 3020 3030 3040 3050 3060 AMLGVHASAS AIIQYGKIAR KQGLVNVALD ILSRIHTIPT VPIVDCFQKI RQQVKCYLQL 3070 3080 3090 3100 3110 3120 AGVMGKNECM QGLEVIESTN LKYFTKEMTA EFYALKGMFL AQINKSEEAN KAFSAAVQMH 3130 3140 3150 3160 3170 3180 DVLVKAWAMW GDYLENIFVK ERQLHLGVSA ITCYLHACRH QNESKSRKYL AKVLWLLSFD 3190 3200 3210 3220 3230 3240 DDKNTLADAV DKYCIGVPPI QWLAWIPQLL TCLVGSEGKL LLNLISQVGR VYPQAVYFPI 3250 3260 3270 3280 3290 3300 RTLYLTLKIE QRERYKSDPG PIRATAPMWR CSRIMHMQRE LHPTLLSSLE GIVDQMVWFR 3310 3320 3330 3340 3350 3360 ENWHEEVLRQ LQQGLAKCYS VAFEKSGAVS DAKITPHTLN FVKKLVSTFG VGLENVSNVS 3370 3380 3390 3400 3410 3420 TMFSSAASES LARRAQATAQ DPVFQKLKGQ FTTDFDFSVP GSMKLHNLIS KLKKWIKILE 3430 3440 3450 3460 3470 3480 AKTKQLPKFF LIEEKCRFLS NFSAQTAEVE IPGEFLMPKP THYYIKIARF MPRVEIVQKH 3490 3500 3510 3520 3530 3540 NTAARRLYIR GHNGKIYPYL VMNDACLTES RREERVLQLL RLLNPCLEKR KETTKRHLFF 3550 3560 3570 3580 3590 3600 TVPRVVAVSP QMRLVEDNPS SLSLVEIYKQ RCAKKGIEHD NPISRYYDRL ATVQARGTQA 3610 3620 3630 3640 3650 3660 SHQVLRDILK EVQSNMVPRS MLKEWALHTF PNATDYWTFR KMFTIQLALI GFAEFVLHLN 3670 3680 3690 3700 3710 3720 RLNPEMLQIA QDTGKLNVAY FRFDINDATG DLDANRPVPF RLTPNISEFL TTIGVSGPLT 3730 3740 3750 3760 3770 3780 ASMIAVARCF AQPNFKVDGI LKTVLRDEII AWHKKTQEDT SSPLSAAGQP ENMDSQQLVS 3790 3800 3810 3820 3830 LVQKAVTAIM TRLHNLAQFE GGESKVNTLV AAANSLDNLC RMDPAWHPWL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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: MASS SPECTROMETRY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; GCN5L2; KIAA0764; TAF5L; TAF6L; TADA3L; TAF10; TAF12 AND TAF9.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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]	"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.
+	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.
IPI	IPI00069084. IPI00879277.
PIR	T02632.
RefSeq	NP_001231509.1. NM_001244580.1. NP_003487.1. NM_003496.3.
UniGene	Hs.203952. Hs.706926.
3D structure databases
ProteinModelPortal	Q9Y4A5.
SMR	Q9Y4A5. Positions 822-854, 2195-2221, 3119-3164, 3828-3858.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-28149N.
IntAct	Q9Y4A5. 16 interactions.
MINT	MINT-1955478.
STRING	9606.ENSP00000347733.
PTM databases
PhosphoSite	Q9Y4A5.
Polymorphism databases
DMDM	116242829.
Proteomic databases
PaxDb	Q9Y4A5.
PRIDE	Q9Y4A5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355540; ENSP00000347733; ENSG00000196367. ENST00000359863; ENSP00000352925; ENSG00000196367. ENST00000562259; ENSP00000454503; ENSG00000261023. ENST00000565218; ENSP00000457834; ENSG00000261023.
GeneID	8295.
KEGG	hsa:8295.
UCSC	uc003upp.3. human. uc011kis.2. human.
Organism-specific databases
CTD	8295.
GeneCards	GC07P098475.
HGNC	HGNC:12347. TRRAP.
HPA	HPA038203.
MIM	603015. gene.
neXtProt	NX_Q9Y4A5.
PharmGKB	PA37020.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5032.
HOGENOM	HOG000252997.
HOVERGEN	HBG079283.
InParanoid	Q9Y4A5.
KO	K08874.
OMA	TWVLQNQ.
OrthoDB	EOG4RR6GC.
PhylomeDB	Q9Y4A5.
Gene expression databases
ArrayExpress	Q9Y4A5.
Bgee	Q9Y4A5.
CleanEx	HS_TRRAP.
Genevestigator	Q9Y4A5.
GermOnline	ENSG00000196367. Homo sapiens.
Family and domain databases
Gene3D	1.10.1070.11. 1 hit. 1.25.10.10. 3 hits. 1.25.40.10. 3 hits.
InterPro	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]
Pfam	PF02259. FAT. 1 hit. PF00454. PI3_PI4_kinase. 1 hit. [Graphical view]
SMART	SM00146. PI3Kc. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 2 hits. SSF56112. Kinase_like. 1 hit.
PROSITE	PS51189. FAT. 1 hit. PS51190. FATC. 1 hit. PS00915. PI3_4_KINASE_1. False negative. PS00916. PI3_4_KINASE_2. False negative. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TRRAP. human.
GenomeRNAi	8295.
NextBio	31097.
SOURCE	Search...

Entry information

Entry name

TRRAP_HUMAN

Accession

Primary (citable) accession number: Q9Y4A5
Secondary accession number(s): A4D265 , O75218, Q9Y631, Q9Y6H4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.