Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Transformation/transcription domain-associated protein  

UniProtKB / Swiss-Prot ID :  TRRAP_HUMAN

Gene Name (Synonyms) : 
TRRAP, PAF400  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein 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. 

Protein Sequence MAFVATQGATVVDQTTLMKKYLQFVAALTDVNTPDETKLKMMQEVSENFENVTSSPQYSTFLEHIIPRFL...
Predicted Secondary Structure CCEEECCCCHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHCCCCHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
722S -> F (found in a cutaneous malignantmelanoma sample; somatic mutation;
878R -> L (in dbSNP:rs17161510). VAR_028359
893R -> C (in an ovarian serous carcinomasample; somatic mutation).
1070S -> G (in dbSNP:rs55920979). VAR_041659
1669R -> H (in a colorectal adenocarcinomasample; somatic mutation).
1724R -> H (in a gastric adenocarcinomasample; somatic mutation).
1925A -> V. VAR_041662
1932P -> L (in a colorectal adenocarcinomasample; somatic mutation).
1947R -> L (in an ovarian mucinous carcinomasample; somatic mutation).
2139W -> G. VAR_041665
2302R -> W (in a colorectal adenocarcinomasample; somatic mutation).
2433S -> G. VAR_041667
2690P -> L (in a lung large cell carcinomasample; somatic mutation).
2750E -> D. VAR_041669
2801K -> E. VAR_041670
2931T -> M (in a colorectal adenocarcinomasample; somatic mutation).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
84Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FLQEKPAQQ
HHHCCCHHH
32.46Phosphositeplus
Link-
579Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FIPNKQLQP
CCCCCCCCC
47.21Phosphositeplus
Link-
897Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RVLGKFGGS
HHHHHHCCC
36.35Phosphositeplus
Link-
1441PhosphothreonineYRSLTLNVV
CCEECHHHH
19.96HPRD
Link-
1552PhosphoserineIEAGSPFRE
HHCCCHHHH
28.10Phosphositeplus
Link-
1628PhosphoserineVRPGSPSTS
EEECCCCHH
20.54Phosphositeplus
Link-
1628PhosphoserineVRPGSPSTS
EEECCCCHH
20.54SysPTM
Link-
1628Phosphoserine.VRPGSPSTS
EEECCCCHH
20.54UniProtKB
Link-
1769Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GDELKAKVL
HHHHHHHHH
44.08Phosphositeplus
Link-
2022Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LQRIKDQQP
HHHHCCCCC
52.23Phosphositeplus
Link-
2034PhosphoserineMDPNSSGEG
CCCCCCCHH
45.14PhosphoELM
Link-
2047Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SSSIKRGLS
HHHHHHCCC
42.22Phosphositeplus
Link-
2051PhosphoserineKRGLSVDSA
HHCCCCCCH
27.05PhosphoELM
Link-
2051PhosphoserineKRGLSVDSA
HHCCCCCCH
27.05Phosphositeplus
Link-
2051PhosphoserineKRGLSVDSA
HHCCCCCCH
27.05SysPTM
Link-
2051Phosphoserine.KRGLSVDSA
HHCCCCCCH
27.05UniProtKB
Link-
2063PhosphothreonineKRFRTATGA
CCHHCCCCC
26.34Phosphositeplus
Link-
2069PhosphoserineTGAISAVFG
CCCEEEHHC
20.18Phosphositeplus
Link-
2075PhosphoserineVFGRSQSLP
HHCCCCCCC
25.21PhosphoELM
Link-
2077PhosphoserineGRSQSLPGA
CCCCCCCCC
37.47PhosphoELM
Link-
2077PhosphoserineGRSQSLPGA
CCCCCCCCC
37.47Phosphositeplus
Link-
2077PhosphoserineGRSQSLPGA
CCCCCCCCC
37.47SysPTM
Link-
2077Phosphoserine.GRSQSLPGA
CCCCCCCCC
37.47UniProtKB
Link-
2114PhosphothreonineDNTNTAGSP
CCCCCCCCC
30.29HPRD
Link-
2132PhosphothreonineNLLKTALRP
HHHHHHHCC
30.78Phosphositeplus
Link-
2333PhosphothreonineELVKTRLAV
HHHHHHHHH
24.36Phosphositeplus
Link-
2333PhosphothreonineELVKTRLAV
HHHHHHHHH
24.36SysPTM
Link-
2333Phosphothreonine.ELVKTRLAV
HHHHHHHHH
24.36UniProtKB
Link-
2438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ELTAKLEPA
CEEEEECHH
48.42Phosphositeplus
Link-
2543N6-acetyllysineVTHVKQEPR
CCHHHHCCC
41.14Phosphositeplus
Link-
2543N6-acetyllysine.VTHVKQEPR
CCHHHHCCC
41.14UniProtKB
Link-
2597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NRHDKFLDT
HHHHHHHHH
41.52Phosphositeplus
Link-
2601PhosphothreonineKFLDTLREV
HHHHHHHCC
29.84Phosphositeplus
Link-
2601PhosphothreonineKFLDTLREV
HHHHHHHCC
29.84SysPTM
Link-
2601Phosphothreonine.KFLDTLREV
HHHHHHHCC
29.84UniProtKB
Link-
2638Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PRLWKILSD
CHHEECCCH
38.06Phosphositeplus
Link-
2972Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KTVVKTWRN
HHHHHHHHH
37.73Phosphositeplus
Link-
3050Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KIARKQGLV
HHHHHCCCH
39.43Phosphositeplus
Link-
3078N6-acetyllysineDCFQKIRQQ
HHHHHHHHH
21.43Phosphositeplus
Link-
3078N6-acetyllysine.DCFQKIRQQ
HHHHHHHHH
21.43UniProtKB
Link-
3122PhosphotyrosineTAEFYALKG
HHHHHHHHH
11.52Phosphositeplus
Link-
3255PhosphoserineLNLISQVGR
HHHHHHHHH
23.21Phosphositeplus
Link-
3372Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LNFVKKLVS
HHHHHHHHH
35.93Phosphositeplus
Link-
3415Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PVFQKLKGQ
HHHHHHHHH
40.47Phosphositeplus
Link-
3598Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VEIYKQRCA
HHHHHHHHH
36.61Phosphositeplus
Link-
3639Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RDILKEVQS
HHHHHHHHH
57.06Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MAX_HUMANphysical interaction
physical interaction
DIP:56672EDIP12660246
9708738
TAF10_HUMANphysical interaction
physical interaction
EBI-708415
EBI-708555
intact15115762
15115762
GCNL2_HUMANphysical interaction
physical interaction
physical interaction
EBI-708415
EBI-708555
EBI-896
intact15115762
15115762
16260778
ERR1_HUMANdirect interaction
physical interaction
physical interaction
EBI-896538
EBI-896407
EBI-896
intact16260778
16260778
16260778
E2F4_HUMANphysical interactionEBI-448954
intact11418595
ESR1_HUMANin vitroHPRD:04310HPRD11931763
16260778
MAX_HUMANin vitroHPRD:04310HPRD10611234
E2F1_HUMANin vivoHPRD:04310HPRD9708738
MYC_HUMANin vitro
in vivo
HPRD:04310HPRD9708738
E2F4_HUMANin vivoHPRD:04310HPRD11418595
BRD8_HUMANin vitro
in vivo
HPRD:04310HPRD12963728
TAF9_HUMANENSP00000352925STRING
RUVB2_HUMANENSP00000352925STRING
RUVB2_HUMANENSP00000352925STRING
TAD2L_HUMANENSP00000352925STRING
GCNL2_HUMANENSP00000352925STRING
TBP_HUMANENSP00000352925STRING
YETS4_HUMANENSP00000352925STRING
TAF4_HUMANENSP00000352925STRING
BRD8_HUMANENSP00000352925STRING
TAF5L_HUMANENSP00000352925STRING
ACL6A_HUMANENSP00000352925STRING
EPC1_HUMANENSP00000352925STRING
PCAF_HUMANENSP00000352925STRING
TAF12_HUMANENSP00000352925STRING
TM11D_HUMANENSP00000352925STRING
TAF6L_HUMANENSP00000352925STRING
TAF10_HUMANENSP00000352925STRING
SF3B3_HUMANENSP00000352925STRING
SUPT3_HUMANENSP00000352925STRING
TAD3L_HUMANENSP00000352925STRING
DMAP1_HUMANENSP00000352925STRING
RUVB1_HUMANENSP00000352925STRING
ING3_HUMANENSP00000352925STRING
MO4L1_HUMANENSP00000352925STRING
MORF4_HUMANENSP00000352925STRING
MO4L2_HUMANENSP00000352925STRING
E2F1_HUMANENSP00000352925STRING
MAX_HUMANENSP00000352925STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2543 AND LYS-3078, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2051, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1628; SER-2051;SER-2077; THR-2333 AND THR-2601, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2051 AND SER-2077, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1628, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2051, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures