Version 5.4
Bos taurus Protein: ATIC
Summary
InnateDB Protein IDBP-696222.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ATIC
Protein Name Bifunctional purine biosynthesis protein PURHPhosphoribosylaminoimidazolecarboxamide formyltransferaseIMP cyclohydrolase
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000025662
InnateDB Gene IDBG-643650 (ATIC)
Protein Structure
UniProt Annotation
Function Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis. {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 25 interaction(s) predicted by orthology.
Predicted by orthology
Total 25 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0003937 IMP cyclohydrolase activity
GO:0004643 phosphoribosylaminoimidazolecarboxamide formyltransferase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0008152 metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0016020 membrane
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR002695 AICARFT/IMPCHase bienzyme
IPR011607 Methylglyoxal synthase-like domain
IPR016193 Cytidine deaminase-like
PFAM PF01808
PF02142
PRINTS
PIRSF PIRSF000414
SMART SM00798
SM00851
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q0VCK0
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 506343
UniGene Bt.61076
RefSeq NP_001068722
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC120131
GenPept AAI20132

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca