NIT3/YLR351C Summary

NIT3 BASIC INFORMATION

Standard Name	NIT3
Systematic Name	YLR351C
Feature Type	ORF, Verified
Description	Nit protein, one of two proteins in S. cerevisiae with similarity to the Nit domain of NitFhit from fly and worm and to the mouse and human Nit protein which interacts with the Fhit tumor suppressor; nitrilase superfamily member (1)
Name Description	NITrilase superfamily 2

GO Annotations	All NIT3 GO evidence and references
	View Computational GO annotations for NIT3
Molecular Function
Manually curated	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds (ISS)
Biological Process
Manually curated	biological_process unknown (ND)
Cellular Component
High-throughput	cytoplasm (IDA) mitochondrion (IDA)

Mutant Phenotype	All NIT3 Phenotype details and references
Large-scale survey
null	polyphosphate accumulation: abnormal viable

Interactions	NIT3 All interactions details and references
	2 total interaction(s) for 1 unique genes/features.
Physical Interactions	Co-crystal Structure: 1 Reconstituted Complex: 1

Sequence Information

ChrXII:830363 to 829488 | |

Note: this feature is encoded on the Crick strand.

Last Update

Coordinates: 2004-02-05 | Sequence: 1996-07-31

Subfeature details

	Relative Coordinates	Chromosomal Coordinates	Most Recent Updates
	Relative Coordinates	Chromosomal Coordinates	Coordinates	Sequence
CDS	1..876	830363..829488	2004-02-05	1996-07-31

External Links	All Associated Seq \| E.C. \| Entrez Gene \| Entrez RefSeq Protein \| MIPS \| UniProtKB

Primary SGDID	S000004343

NIT3 RESOURCES

Click on map for expanded view

SGD ORF map	GBrowse

Click on histogram for expression summary
Expression Summary

ADDITIONAL INFORMATION for NIT3

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for NIT3]

1)	Pace HC and Brenner C (2001) The nitrilase superfamily: classification, structure and function. Genome Biol 2(1):REVIEWS0001
2)	Pace HC, et al. (2000) Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers. Curr Biol 10(15):907-17

SGD^tm pages Database Copyright © 1997-2010 The Board of Trustees of Leland Stanford Junior University. Permission to use the information contained in this database was given by the researchers/institutes who contributed or published the information. Users of the database are solely responsible for compliance with any copyright restrictions, including those applying to the author abstracts. Documents from this server are provided "AS-IS" without any warranty, expressed or implied. The SGD project at Stanford University is supported by a Genome Research Resource Grant from the US National Human Genome Research Institute, part of the US National Institutes of Health.