Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Activating signal cointegrator 1  

UniProtKB / Swiss-Prot ID :  TRIP4_HUMAN

Gene Name (Synonyms) : 
TRIP4  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, centrosome. Note=Cytoplasmic under conditions of serum deprivation. Co-localizes with NEK6 in the centrosome. 

Protein Function :  Transcription coactivator of nuclear receptors which functions in conjunction with CBP-p300 and SRC-1 and may play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF- kappa-B. Plays a role in androgen receptor transactivation and in testicular function (By similarity). 

Protein Sequence MAVAGAVSGEPLVHWCTQQLRKTFGLDVSEEIIQYVLSIESAEEIREYVTDLLQGNEGKKGQFIEELITK...
Predicted Secondary Structure CCCCCCCCCCHHHHHHHHHHHHHHCCCHHHHHHHHHHHCCCHHHHHHHHHHHHCCCCCCCCCHHHHHHHH...
Protein Variant -
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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
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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
2N-acetylalanine.---MAVAGA
---CCCCCC
10.40UniProtKB
Link-
135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FDLAKAQEN
HHHHHHHHC
58.88Phosphositeplus
Link-
209PhosphothreonineTLVCTHEEQ
CCCCCCHHH
25.50Phosphositeplus
Link-
245Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DISTKDLLP
CCHHHHHCC
39.32Phosphositeplus
Link-
289PhosphotyrosineDESDYFASD
CHHCCCCCC
15.43HPRD
Link-
289PhosphotyrosineDESDYFASD
CHHCCCCCC
15.43PhosphoELM
Link-
289PhosphotyrosineDESDYFASD
CHHCCCCCC
15.43Phosphositeplus
Link-
289Phosphotyrosine.DESDYFASD
CHHCCCCCC
15.43UniProtKB
Link-
300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QWLSKLERE
HHHHHHHHH
52.80Phosphositeplus
Link-
345PhosphotyrosineSLAEYHSRL
HHHHHHHHH
10.25Phosphositeplus
Link-
367Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QPLTKLDRS
CHHHHHHCC
56.95Phosphositeplus
Link-
385PhosphotyrosineNPNMYQSPP
CCCCCCCCH
16.69HPRD
Link-
385PhosphotyrosineNPNMYQSPP
CCCCCCCCH
16.69PhosphoELM
Link-
406PhosphoserineKAFRSSGFG
HHHHHCCCC
28.49HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ESR1_HUMANin vitro
in vivo
HPRD:05140HPRD10454579
JUN_HUMANin vivoHPRD:05140HPRD12077347
NFKB1_HUMANin vitroHPRD:05140HPRD12077347
TF65_HUMANin vitroHPRD:05140HPRD12077347
RXRA_HUMANyeast 2-hybridHPRD:05140HPRD7776974
TF2AA_HUMANin vitroHPRD:05140HPRD10454579
TBP_HUMANin vitroHPRD:05140HPRD10454579
CBP_HUMANin vitro
yeast 2-hybrid
HPRD:05140HPRD10454579
NCOA1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:05140HPRD10454579
EP300_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:05140HPRD10454579
TRIP4_HUMANin vitro
in vivo
HPRD:05140HPRD10567404
ANDR_HUMANin vitro
yeast 2-hybrid
HPRD:05140HPRD12390891
THB_HUMANENSP00000261884STRING
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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
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-289, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures