KTI11 Kti11p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: KTI11
Gene description: Kti11p
Primary source: SGD:S000007587
Locus tag: YBL071W-A
See related: AllianceGenome:SGD:S000007587
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: DPH3
Summary: Enables iron ion binding activity; oxidoreductase activity, acting on iron-sulfur proteins as donors; and zinc ion binding activity. Involved in peptidyl-diphthamide biosynthetic process from peptidyl-histidine and tRNA wobble uridine modification. Located in cytoplasm and nucleus. Orthologous to several human genes including DPH3 (diphthamide biosynthesis 3). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (89978..90226)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to Transform a [3Fe-4S] to a [4Fe-4S] Cluster in Dph1-Dph2.
Title: Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to Transform a [3Fe-4S] to a [4Fe-4S] Cluster in Dph1-Dph2.
The Diphthamide and the tRNA wobble uridine modifications both require diphthamide biosynthesis 3 (Dph3) protein as an electron donor for the iron-sulfur clusters in their biosynthetic enzymes.
Title: Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification.
Insight into the molecular mechanisms that allow the Kti11/Kti13 heterodimer to coregulate two consecutive steps in ribosomal protein synthesis.
Title: Structure of the Kti11/Kti13 heterodimer and its double role in modifications of tRNA and eukaryotic elongation factor 2.
Kti11 forms a stable 1 : 1 complex with Kti13.In the complex, Kti13 orients Kti11 and restricts access to its electron-carrying iron atom, constraining the electron transfer capacity of Kti11.
Title: Structure of the Elongator cofactor complex Kti11/Kti13 provides insight into the role of Kti13 in Elongator-dependent tRNA modification.
Kti11/Dph3 is involved in tRNA modification, tRNA suppression and prevents ADP-ribosylation of eEF2 by diphthamide.
Title: A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3.
Chemical and stereo structural information around the Zn ion in Kti11p was obtained high-spatial resolution technique MXAN.
Title: 3D local structure around Zn in Kti11p as a representative Zn-(Cys)4 motif as obtained by MXAN.
Kti13 and Kti11 support Elongator functions and they both share Elongator-independent roles that are important for cell viability.
Title: Yeast alpha-tubulin suppressor Ats1/Kti13 relates to the Elongator complex and interacts with Elongator partner protein Kti11.
Solution structure of the Kti11 protein using NMR. Provides the first structure of the CSL-class zinc-binding protein family.
Title: Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables iron ion binding	IDA Inferred from Direct Assay more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity, acting on iron-sulfur proteins as donors	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in protein histidyl modification to diphthamide	IDA Inferred from Direct Assay more info	PubMed
involved_in protein histidyl modification to diphthamide	IEA Inferred from Electronic Annotation more info
involved_in protein histidyl modification to diphthamide	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in tRNA processing	IEA Inferred from Electronic Annotation more info
involved_in tRNA wobble uridine modification	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	HDA more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Kti11p

NP_660100.1

Zn-ribbon protein that co-purifies with Dph1 and Dph2; forms a complex required for synthesis of diphthamide on translation factor eEF2 and with Elongator subunits Iki3p, Elp2p, and Elp3p; involved in modification of wobble nucleosides in tRNAs; forms a stable heterodimer with Ats1p