Protein Domain and Function Prediction Resources

Biological information of protein primary structure is responsible for finding the protein function, extracting features and function of a protein in the biology lab is challenging and time-consuming. Identification of protein function provides essential information for the treatment of various diseases and drug design. Therefore, extracting the protein knowledge from primary structure alone has been a diverse field in the study of bioinformatics data mining and computational biology. This study aimed to function prediction of protein primary structure using the LSTM methods. PRNP(prion protein )most of the nervous system tissues express by prion protein, this is generally to protease-resistant from disease, due to this reasons, the human codon PRNP is most closely associated with Alzheimer disease. The PRNP protein data trained with Hemo sapiens PRNP selection, classification was implemented with network layer perceptron. The learning algorithms are frame by the nervous system. The training results observation indicate that the learning success of prion protein classification leads positively.

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The Structure, Expression, and Function Prediction of DAZAP2, A Down-Regulated Gene in Multiple Myeloma

Genomics Proteomics & Bioinformatics ◽

10.1016/s1672-0229(04)02007-8 ◽

2004 ◽

Vol 2 (1) ◽

pp. 47-54 ◽

Cited By ~ 10

Author(s):

Yiwu Shi ◽

Saiqun Luo ◽

Jianbin Peng ◽

Chenghan Huang ◽

Daren Tan ◽

...

Keyword(s):

Multiple Myeloma ◽

Function Prediction ◽

And Function

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Classification and Function Prediction of Proteins Using Diagnostic Amino Acid Patterns

Computer Analysis of Sequence Data ◽

10.1385/0-89603-276-0:295 ◽

1994 ◽

pp. 295-305

Author(s):

Aiala Reizer ◽

Milton H. Saier ◽

Jonathan Reizer

Keyword(s):

Amino Acid ◽

Function Prediction ◽

And Function

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Age- and Sex-Linked Bacterial Community Variation and Function Prediction from Insoles of Healthy Chinese Population

Indian Journal of Microbiology ◽

10.1007/s12088-020-00855-w ◽

2020 ◽

Vol 60 (2) ◽

pp. 222-229

Author(s):

Xiaojing Hu ◽

Licao Chang ◽

Zhenyu Wang ◽

Guosheng Liu ◽

Zongjie Hu ◽

...

Keyword(s):

Bacterial Community ◽

Chinese Population ◽

Function Prediction ◽

Community Variation ◽

Healthy Chinese ◽

And Function ◽

Age And Sex

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Inositol Pyrophosphate Pathways and Mechanisms: What Can We Learn from Plants?

Molecules ◽

10.3390/molecules25122789 ◽

2020 ◽

Vol 25 (12) ◽

pp. 2789 ◽

Cited By ~ 1

Author(s):

Caitlin Cridland ◽

Glenda Gillaspy

Keyword(s):

Inositol Phosphate ◽

Specific Protein ◽

Protein Domain ◽

Growth And Survival ◽

Inositol Pyrophosphate ◽

Protein Partners ◽

Inositol Pyrophosphates ◽

Energy Sensing ◽

And Function ◽

Complex Signaling

The ability of an organism to maintain homeostasis in changing conditions is crucial for growth and survival. Eukaryotes have developed complex signaling pathways to adapt to a readily changing environment, including the inositol phosphate (InsP) signaling pathway. In plants and humans the pyrophosphorylated inositol molecules, inositol pyrophosphates (PP-InsPs), have been implicated in phosphate and energy sensing. PP-InsPs are synthesized from the phosphorylation of InsP6, the most abundant InsP. The plant PP-InsP synthesis pathway is similar but distinct from that of the human, which may reflect differences in how molecules such as Ins(1,4,5)P3 and InsP6 function in plants vs. animals. In addition, PP-InsPs can potentially interact with several major signaling proteins in plants, suggesting PP-InsPs play unique signaling roles via binding to protein partners. In this review, we will compare the biosynthesis and role of PP-InsPs in animals and plants, focusing on three central themes: InsP6 synthesis pathways, synthesis and regulation of the PP-InsPs, and function of a specific protein domain called the Syg1, Pho1, Xpr1 (SPX ) domain in binding PP-InsPs and regulating inorganic phosphate (Pi) sensing. This review will provide novel insights into the biosynthetic pathway and bioactivity of these key signaling molecules in plant and human systems.

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