CIN2/YPL241C Summary Help

Standard Name CIN2 1, 2
Systematic Name YPL241C
Feature Type ORF, Verified
Description GTPase-activating protein (GAP) for Cin4p; tubulin folding factor C involved in beta-tubulin (Tub2p) folding; mutants display increased chromosome loss and benomyl sensitivity; deletion complemented by human GAP, retinitis pigmentosa 2 (1, 3, 4, 5 and see Summary Paragraph)
Name Description Chromosome INstability 1
Chromosomal Location
ChrXVI:96258 to 95372 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -143 cM
Gene Ontology Annotations All CIN2 GO evidence and references
  View Computational GO annotations for CIN2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 16 genes
Classical genetics
Large-scale survey
275 total interaction(s) for 124 unique genes/features.
Physical Interactions
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Lethality: 1
  • Dosage Rescue: 3
  • Negative Genetic: 176
  • Phenotypic Enhancement: 1
  • Positive Genetic: 15
  • Synthetic Growth Defect: 27
  • Synthetic Lethality: 50

Expression Summary
Length (a.a.) 268
Molecular Weight (Da) 30,708
Isoelectric Point (pI) 7.01
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXVI:96258 to 95372 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -143 cM
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..25 96258..96234 1996-07-31 1996-07-31
Intron 26..105 96233..96154 1996-07-31 1996-07-31
CDS 106..887 96153..95372 1996-07-31 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 SGDIDS000006162

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 be 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 numerous organisms, including S. cerevisiae (reviewed in 6).

In S. cerevisiae, CIN2 is a non-essential gene that is homologus to tubulin cofactor C 1, 3, 4. Cofactor C acts in vitro to release the functional tubulin heterodimer from a quaternary tubulin folding complex containing alpha- and beta-tubulin, cofactor D (Cin1p) and cofactor E (Pac2p) 4. Consistent with the in vitro studies, CIN2 has been shown to genetically interact with specific tubulin mutants, and the tubulin cofactors CIN1, RBL2 and PAC2 1, 7, 8. Cin2p interacts in the two-hybrid assay with Cin4p 8, an arf-family GTPase and proposed regulator of the cofactor pathway 1, 3, 9.

CIN2 was isolated in a genetic screen for mutants that display benomyl (a microtubule-depolymerizing drug) super-sensitivity 1, and independently isolated in a genetic screen for elevated chromosome loss 3. cin2 null mutants are cold-sensitive and have defects in nuclear migration and nuclear fusion 1, 3.

Last updated: 2003-08-28 Contact SGD

References cited on this page View Complete Literature Guide for CIN2
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) Stearns, T. and Botstein, D.  (1989) Personal Communication, Mortimer Map Edition 10
3) 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
4) Tian G, et al.  (1996) Pathway leading to correctly folded beta-tubulin. Cell 86(2):287-96
5) Veltel S, et al.  (2008) The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3. Nat Struct Mol Biol 15(4):373-80
6) Lopez-Fanarraga M, et al.  (2001) Review: postchaperonin tubulin folding cofactors and their role in microtubule dynamics. J Struct Biol 135(2):219-29
7) Fleming JA, et al.  (2000) Function of tubulin binding proteins in vivo. Genetics 156(1):69-80
8) 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
9) Bhamidipati A, et al.  (2000) ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin. J Cell Biol 149(5):1087-96