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YEAST:MYO5

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) MYO5
Protein Name(s) Myosin-5

Actin-dependent myosin-I MYO5 Class I unconventional myosin MYO5 Type I myosin MYO5

External Links
UniProt Q04439
EMBL Z49702
BK006946
PIR S54570
RefSeq NP_013827.1
PDB 1YP5
1ZUY
PDBsum 1YP5
1ZUY
ProteinModelPortal Q04439
SMR Q04439
BioGrid 35285
DIP DIP-2222N
IntAct Q04439
MINT MINT-593586
STRING 4932.YMR109W
MaxQB Q04439
PaxDb Q04439
PeptideAtlas Q04439
EnsemblFungi [example_ID YMR109W]
GeneID 855136
KEGG sce:YMR109W
CYGD YMR109w
SGD S000004715
eggNOG COG5022
GeneTree ENSGT00760000118956
HOGENOM HOG000260265
InParanoid Q04439
KO K10356
OMA HVILESN
OrthoDB EOG7VDXXK
BioCyc YEAST:G3O-32805-MONOMER
EvolutionaryTrace Q04439
NextBio 978516
Proteomes UP000002311
Genevestigator Q04439
GO GO:0030479
GO:0016459
GO:0005524
GO:0042802
GO:0000146
GO:0051666
GO:0007121
GO:0006897
GO:0006887
GO:0031505
GO:0008152
GO:0006898
GO:0006970
GO:0009651
InterPro IPR001609
IPR010926
IPR027417
IPR001452
Pfam PF00063
PF06017
PF00018
PRINTS PR00193
SMART SM00242
SM00326
SUPFAM SSF50044
SSF52540
PROSITE PS51456
PS50002

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005933

cellular bud

PMID:26928762[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0071944

cell periphery

PMID:26928762[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0043332

mating projection tip

PMID:19053807[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:2000601

positive regulation of Arp2/3 complex-mediated actin nucleation

PMID:16824951[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2000601

positive regulation of Arp2/3 complex-mediated actin nucleation

PMID:16824951[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051666

actin cortical patch localization

PMID:18177206[4]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000001612
SGD:S000005707

P

Seeded From UniProt

complete

involved_in

GO:0051666

actin cortical patch localization

PMID:18177206[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0030479

actin cortical patch

PMID:16824951[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030479

actin cortical patch

PMID:20647997[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009651

response to salt stress

PMID:12391157[6]

ECO:0000353

physical interaction evidence used in manual assertion

SGD:S000001156

P

Seeded From UniProt

complete

involved_in

GO:0009651

response to salt stress

PMID:12391157[6]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000001156

P

Seeded From UniProt

complete

involved_in

GO:0006898

receptor-mediated endocytosis

PMID:8614799[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006897

endocytosis

PMID:16824951[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0000146

microfilament motor activity

PMID:16824951[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:9628892[8]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q04439

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:20647997[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q04439

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19841731[9]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q04439

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18467557[10]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q04439

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:11743162[11]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q04439

F

Seeded From UniProt

complete

enables

GO:0003774

motor activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001609
InterPro:IPR010926

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001609

F

Seeded From UniProt

complete

part_of

GO:0016459

myosin complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001609
InterPro:IPR010926

C

Seeded From UniProt

complete

involved_in

GO:0031505

fungal-type cell wall organization

PMID:10652251[12]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007121

bipolar cellular bud site selection

PMID:10652251[12]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006970

response to osmotic stress

PMID:10652251[12]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006887

exocytosis

PMID:10652251[12]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003779

actin binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0009

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0206

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0016459

myosin complex

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0518

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

part_of

GO:0030479

actin cortical patch

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0008

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Yofe, I et al. (2016) One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Nat. Methods 13 371-378 PubMed GONUTS page
  2. Narayanaswamy, R et al. (2009) Systematic definition of protein constituents along the major polarization axis reveals an adaptive reuse of the polarization machinery in pheromone-treated budding yeast. J. Proteome Res. 8 6-19 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Sun, Y et al. (2006) Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity. Dev. Cell 11 33-46 PubMed GONUTS page
  4. 4.0 4.1 Galletta, BJ et al. (2008) Distinct roles for Arp2/3 regulators in actin assembly and endocytosis. PLoS Biol. 6 e1 PubMed GONUTS page
  5. 5.0 5.1 Grötsch, H et al. (2010) Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites. EMBO J. 29 2899-914 PubMed GONUTS page
  6. 6.0 6.1 Soulard, A et al. (2002) Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro. Mol. Cell. Biol. 22 7889-906 PubMed GONUTS page
  7. Geli, MI & Riezman, H (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272 533-5 PubMed GONUTS page
  8. Anderson, BL et al. (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J. Cell Biol. 141 1357-70 PubMed GONUTS page
  9. Tonikian, R et al. (2009) Bayesian modeling of the yeast SH3 domain interactome predicts spatiotemporal dynamics of endocytosis proteins. PLoS Biol. 7 e1000218 PubMed GONUTS page
  10. Tarassov, K et al. (2008) An in vivo map of the yeast protein interactome. Science 320 1465-70 PubMed GONUTS page
  11. Tong, AH et al. (2002) A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 295 321-4 PubMed GONUTS page
  12. 12.0 12.1 12.2 12.3 Pruyne, D & Bretscher, A (2000) Polarization of cell growth in yeast. J. Cell. Sci. 113 ( Pt 4) 571-85 PubMed GONUTS page