SGD DescriptionNegative regulator of actin nucleation-promoting factor activity; interacts with Las17p, a homolog of human Wiskott-Aldrich Syndrome protein (WASP), via an N-terminal SH3 domain, and along with LSB1 cooperatively inhibits the nucleation of actin filaments; short-lived protein whose levels increase in response to thermal stress; induces the formation of the [PIN+] and [RNQ+] prions when overproduced; PIN3 has a paralog, LSB1, that arose from the whole genome duplication|Negative regulator of actin nucleation-promoting factor activity; interacts with Las17p, a homolog of human Wiskott-Aldrich Syndrome protein (WASP), via an N-terminal SH3 domain, and along with PIN3 cooperatively inhibits the nucleation of actin filaments; overexpression blocks receptor-mediated endocytosis; protein increases in abundance and forms nuclear foci in response to DNA replication stress; LSB1 has a paralog, PIN3, that arose from the whole genome duplication
PomBase DescriptionWiskott-Aldrich syndrome homolog binding protein Lsb1 (predicted)
AspGD DescriptionOrtholog(s) have role in negative regulation of Arp2/3 complex-mediated actin nucleation and actin cortical patch, nucleus localization
References
Rieger KJ, et al. (1999 Jul). Chemotyping of yeast mutants using robotics.
Madania A, et al. (1999 Oct). The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex.
Derkatch IL, et al. (2001 Jul 27). Prions affect the appearance of other prions: the story of [PIN(+)].
Peng J, et al. (2003 Aug). A proteomics approach to understanding protein ubiquitination.
Hitchcock AL, et al. (2003 Oct 28). A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.
Gupta R, et al. (2007). Ubiquitination screen using protein microarrays for comprehensive identification of Rsp5 substrates in yeast.
Chi A, et al. (2007 Feb 13). Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.
Calvo IA, et al. (2009 Aug 12). Genome-wide screen of genes required for caffeine tolerance in fission yeast.
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Starita LM, et al. (2012 Jan). Sites of ubiquitin attachment in Saccharomyces cerevisiae.
Kawashima SA, et al. (2012 Jul 27). Analyzing fission yeast multidrug resistance mechanisms to develop a genetically tractable model system for chemical biology.
Van Damme P, et al. (2012 Jul 31). N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
Pan X, et al. (2012 Nov 23). Identification of novel genes involved in DNA damage response by screening a genome-wide Schizosaccharomyces pombe deletion library.
Chen Z, et al. (2012 Oct). A genetic screen to discover pathways affecting cohesin function in Schizosaccharomyces pombe identifies chromatin effectors.
Das J, et al. (2013 May 21). Cross-species protein interactome mapping reveals species-specific wiring of stress response pathways.
Carpy A, et al. (2014 Aug). Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (Fission Yeast).
Encinar del Dedo J, et al. (2014 Oct). Eng2 is a component of a dynamic protein complex required for endocytic uptake in fission yeast.
Beckley JR, et al. (2015 Dec). A Degenerate Cohort of Yeast Membrane Trafficking DUBs Mediates Cell Polarity and Survival.
Yamamoto T, et al. (2015 Dec). Identification and characterization of Csh3 as an SH3 protein that interacts with fission yeast Cap1.
Petrini E, et al. (2015 Oct 15). A new phosphate-starvation response in fission yeast requires the endocytic function of myosin I.
SGD DescriptionSubunit of the endosomal Vps27p-Hse1p complex; complex is required for sorting of ubiquitinated membrane proteins into intralumenal vesicles prior to vacuolar degradation, as well as for recycling of Golgi proteins and formation of lumenal membranes
PomBase DescriptionSTAM like protein Hse1
AspGD DescriptionOrtholog(s) have role in ascospore-type prospore assembly, protein targeting to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway
References
Bilodeau PS, et al. (2002 Jul). The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting.
Bilodeau PS, et al. (2003 Oct 27). Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome.
Bowers K, et al. (2004 Mar). Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae.
Ren J, et al. (2007 Jan). Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies.
Van Damme P, et al. (2012 Jul 31). N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.