CIN1/YOR349W Summary Help

Standard Name CIN1 1
Systematic Name YOR349W
Feature Type ORF, Verified
Description Tubulin folding factor D involved in beta-tubulin (Tub2p) folding; isolated as mutant with increased chromosome loss and sensitivity to benomyl (1, 2, 3 and see Summary Paragraph)
Name Description Chromosome INstability 1
Chromosomal Location
ChrXV:989789 to 992833 | ORF Map | GBrowse
Genetic position: 215 cM
Gene Ontology Annotations All CIN1 GO evidence and references
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 14 genes
Classical genetics
reduction of function
Large-scale survey
346 total interaction(s) for 146 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 5
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 2

Genetic Interactions
  • Dosage Lethality: 3
  • Dosage Rescue: 4
  • Negative Genetic: 201
  • Phenotypic Enhancement: 2
  • Positive Genetic: 12
  • Synthetic Growth Defect: 50
  • Synthetic Lethality: 63
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 1,014
Molecular Weight (Da) 116,647
Isoelectric Point (pI) 8.18
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXV:989789 to 992833 | ORF Map | GBrowse
Genetic position: 215 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..3045 989789..992833 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005876

Microtubules are conserved cytoskeletal elements that form by the polymerization of alpha- and beta-tubulin heterodimers. The formation of polymerization-competent tubulin heterodimers requires that alpha-tubulin and beta-tubulin are properly folded. Specific cofactors are required for the folding of alpha- and beta-tubulin in vitro and homologs of these cofactors have been found in many organisms, including S.cerevisiae (reviewed in 4).

In S.cerevisiae, CIN1 is a non-essential gene that encodes the homolog of mammalian cofactor D 4, 1, 2, 3. In vitro, cofactor D acts in the beta-tubulin folding pathway and forms a quaternary complex with cofactor E (Pac2p), and alpha- and beta-tubulin, to make polymerization-competent tubulin heterodimers 3. Consistent with the in vitro studies, Cin1p has been shown to physically interact with Pac2p 5 and beta-tubulin (encoded by the TUB2 gene) 6. Overexpression of CIN1 can suppress the benomyl (a microtubule-depolymerizing drug) sensitivity of a pac2 null mutant 5 and cin1 mutants have allele-specific synthetic phenotypes in combination with tubulin mutants 7, 1.

CIN1 was isolated in a genetic screen for mutants that displayed super-sensitivity to benomyl 1, and independently isolated in a genetic screen for elevated chromosome loss 2. cin1 null mutants are cold-sensitive and have defects in nuclear migration and nuclear fusion 1, 2.

Last updated: 2003-08-27 Contact SGD

References cited on this page View Complete Literature Guide for CIN1
1) Stearns T, et al.  (1990) Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function. Genetics 124(2):251-62
2) Hoyt MA, et al.  (1990) Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes. Mol Cell Biol 10(1):223-34
3) Tian G, et al.  (1996) Pathway leading to correctly folded beta-tubulin. Cell 86(2):287-96
4) Lopez-Fanarraga M, et al.  (2001) Review: postchaperonin tubulin folding cofactors and their role in microtubule dynamics. J Struct Biol 135(2):219-29
5) Hoyt MA, et al.  (1997) Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability. Genetics 146(3):849-57
6) Feierbach B, et al.  (1999) Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin. J Cell Biol 144(1):113-24
7) Fleming JA, et al.  (2000) Function of tubulin binding proteins in vivo. Genetics 156(1):69-80