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Q04439

- MYO5_YEAST

UniProt

Q04439 - MYO5_YEAST

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Protein
Myosin-5
Gene
MYO5, YMR109W, YM9718.08
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.9 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi129 – 1368ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. microfilament motor activity Source: SGD
  4. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. actin cortical patch localization Source: SGD
  2. bipolar cellular bud site selection Source: SGD
  3. endocytosis Source: SGD
  4. exocytosis Source: SGD
  5. fungal-type cell wall organization Source: SGD
  6. metabolic process Source: GOC
  7. receptor-mediated endocytosis Source: SGD
  8. response to osmotic stress Source: SGD
  9. response to salt stress Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Motor protein, Myosin

Keywords - Ligandi

Actin-binding, ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32805-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-5
Alternative name(s):
Actin-dependent myosin-I MYO5
Class I unconventional myosin MYO5
Type I myosin MYO5
Gene namesi
Name:MYO5
Ordered Locus Names:YMR109W
ORF Names:YM9718.08
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR109w.
SGDiS000004715. MYO5.

Subcellular locationi

Cytoplasmcytoskeletonactin patch
Note: Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth.4 Publications

GO - Cellular componenti

  1. actin cortical patch Source: SGD
  2. myosin complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi164 – 1641V → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication
Mutagenesisi168 – 1681N → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication
Mutagenesisi209 – 2091N → S: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication
Mutagenesisi357 – 3571S → A: Leads to a depolarized actin cytoskeleton and a strong defect in the capacity to internalize STE2. 1 Publication
Mutagenesisi357 – 3571S → E: No growth defect, but leads to a partially depolarized actin cytoskeleton. Accelerates the constitutive internalization of STE2. 1 Publication
Mutagenesisi377 – 3771K → M: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication
Mutagenesisi472 – 4721E → K in MYO5-1; temperature sensitive loss of function. 1 Publication
Mutagenesisi1123 – 11231W → S: Abolishes interaction with BBC1 and VRP1. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12191219Myosin-5
PRO_0000123492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei357 – 3571Phosphoserine4 Publications
Modified residuei359 – 3591Phosphotyrosine1 Publication
Modified residuei777 – 7771Phosphoserine1 Publication
Modified residuei992 – 9921Phosphoserine1 Publication
Modified residuei1205 – 12051Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase activity. Ser-357 is phosphorylated by YPK2 in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04439.
PaxDbiQ04439.
PeptideAtlasiQ04439.

Expressioni

Gene expression databases

GenevestigatoriQ04439.

Interactioni

Subunit structurei

Interacts (via myosin motor domain) with SHE4; this interaction is important for proper localization and may regulate the interaction of the motor domain with actin. Interacts (via SH3 domain) with VRP1; this interaction is required for localization to sites of polarized growth and may regulate the interaction of the tail domain with actin. Interacts (via SH3 domain) with PAN1; this interaction is important for late stages of endocytopsis. Interacts (via SH3 domain) with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19 and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits. Interacts with BZZ1, PKH1, PKH2, YPK1 and YPK2.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-11687,EBI-11687
AIM21P405632EBI-11687,EBI-25376
APP1P539332EBI-11687,EBI-28798
ARC40P383283EBI-11687,EBI-2777
BBC1P470686EBI-11687,EBI-3437
BCK1Q013896EBI-11687,EBI-3470
BNR1P404507EBI-11687,EBI-3711
BZZ1P388225EBI-11687,EBI-3889
CDC55Q003624EBI-11687,EBI-1942
CLA4P485623EBI-11687,EBI-4750
CMD1P067877EBI-11687,EBI-3976
LAS17Q124467EBI-11687,EBI-10022
OSH2Q124516EBI-11687,EBI-12621
PAN1P325212EBI-11687,EBI-12875
PKH3Q033062EBI-11687,EBI-37683
PRP8P333344EBI-11687,EBI-465
RVS167P397433EBI-11687,EBI-14500
SAP1P399554EBI-11687,EBI-16463
STE20Q034974EBI-11687,EBI-18285
UBP7P404534EBI-11687,EBI-19857
VRP1P3737019EBI-11687,EBI-20502
YOR389WQ089122EBI-11687,EBI-38289
ZRG8P400212EBI-11687,EBI-22484

Protein-protein interaction databases

BioGridi35285. 116 interactions.
DIPiDIP-2222N.
IntActiQ04439. 99 interactions.
MINTiMINT-593586.
STRINGi4932.YMR109W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1089 – 10946
Beta strandi1112 – 11187
Beta strandi1122 – 11309
Beta strandi1134 – 11385
Helixi1139 – 11413
Beta strandi1142 – 11443

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YP5X-ray1.68A1088-1145[»]
1ZUYX-ray1.39A/B1088-1145[»]
ProteinModelPortaliQ04439.
SMRiQ04439. Positions 37-715, 1088-1145.

Miscellaneous databases

EvolutionaryTraceiQ04439.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 715680Myosin motor
Add
BLAST
Domaini719 – 73921IQ 1
Add
BLAST
Domaini740 – 76526IQ 2
Add
BLAST
Domaini1085 – 114763SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni404 – 48683Actin-binding By similarity
Add
BLAST
Regioni766 – 961196Basic, putative membrane-binding region
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1000 – 108889Ala/Pro-rich
Add
BLAST
Compositional biasi1011 – 10166Poly-Pro
Compositional biasi1060 – 10634Poly-Ala
Compositional biasi1073 – 10819Poly-Pro
Compositional biasi1204 – 121815Asp/Glu-rich (acidic)
Add
BLAST

Domaini

The myosin motor domain displays actin-stimulated ATPase activity and generates a mechanochemical force.
The tail domain participates in molecular interactions that specify the role of the motor domain. It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding domain (TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).

Sequence similaritiesi

Contains 2 IQ domains.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00750000117868.
HOGENOMiHOG000260265.
KOiK10356.
OMAiLFRVINT.
OrthoDBiEOG7VDXXK.

Family and domain databases

InterProiIPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04439-1 [UniParc]FASTAAdd to Basket

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MAILKRGARK KVHQEPAKRS ANIKKATFDS SKKKEVGVSD LTLLSKISDE     50
AINENLKKRF LNATIYTYIG HVLISVNPFR DLGIYTDAVM NEYKGKNRLE 100
VPPHVFAIAE SMYYNMKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS 150
STHTESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNNQF 200
EPCAGNITNY LLEKQRVVSQ IKNERNFHIF YQFTKGASDA YRQTFGVQKP 250
EQYVYTAAAG CISAETIDDL QDYQETLKAM RVIGLGQEEQ DQIFRMLAAI 300
LWIGNVSFIE NEEGNAQVRD TSVTDFVAYL LQIDSQLLIK SLVERIMETN 350
HGMKRGSVYH VPLNIVQADA VRDALAKAIY NNLFDWIVSR VNKSLQAFPG 400
AEKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKSEQETYE 450
REKIQWTPIK YFDNKVVCDL IEARRPPGIF AAMNDSVATA HADSNAADQA 500
FAQRLNLFTT NPHFDLRSNK FVIKHYAGDV TYDIDGITDK NKDQLQKDLV 550
ELIGTTTNTF LATIFPDTVD RESKRRPPTA GDKIIKSAND LVETLSKAQP 600
SYIRTIKPNE TKSPNDYDDR QVLHQIKYLG LQENVRIRRA GFAYRQVFEK 650
FVERFYLLSP HCSYAGDYTW QGDTLDAVKY ILQDSSIPQQ EYQLGVTSVF 700
IKTPETLFAL EHMRDRYWHN MAARIQRAWR RFLQRRIDAA TKIQRTIRER 750
KEGNKYEKLR DYGTKVLGGR KERRSMSLLG YRAFMGDYLS CNESKSKGAY 800
IKRQVSIKEK VIFSIHGEAL HTKFGRSAQR LKKTFLLTPT TLYIVGQTLV 850
QNAMTYTQDY KIDVRNIQAV SLTNLQDDWV AIKLASSGQP DPLINTYFKT 900
ELITHLKRLN DKIQIKIGSA IEYQKKPGKL HSVKCQINES APKYGDIYKS 950
STISVRRGNP PNSQVHKKPR KKSSISSGYH ASSSQATRRP VSIAAAQHVP 1000
TAPASRHSKK PAPPPPGMQN KAATRRSVPN PASTLTASQS NARPSPPTAA 1050
TRATPAATPA AAAMGSGRQA NIPPPPPPPP PSSKPKEPMF EAAYDFPGSG 1100
SPSELPLKKG DVIYITREEP SGWSLGKLLD GSKEGWVPTA YMKPHSGNNN 1150
IPTPPQNRDV PKPVLNSVQH DNTSANVIPA AAQASLGDGL ANALAARANK 1200
MRLESDDEEA NEDEEEDDW 1219
Length:1,219
Mass (Da):136,899
Last modified:November 1, 1997 - v1
Checksum:iDFFB9EC16B61CD29
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49702 Genomic DNA. Translation: CAA89745.1.
BK006946 Genomic DNA. Translation: DAA10006.1.
PIRiS54570.
RefSeqiNP_013827.1. NM_001182609.1.

Genome annotation databases

EnsemblFungiiYMR109W; YMR109W; YMR109W.
GeneIDi855136.
KEGGisce:YMR109W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49702 Genomic DNA. Translation: CAA89745.1 .
BK006946 Genomic DNA. Translation: DAA10006.1 .
PIRi S54570.
RefSeqi NP_013827.1. NM_001182609.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YP5 X-ray 1.68 A 1088-1145 [» ]
1ZUY X-ray 1.39 A/B 1088-1145 [» ]
ProteinModelPortali Q04439.
SMRi Q04439. Positions 37-715, 1088-1145.
ModBasei Search...

Protein-protein interaction databases

BioGridi 35285. 116 interactions.
DIPi DIP-2222N.
IntActi Q04439. 99 interactions.
MINTi MINT-593586.
STRINGi 4932.YMR109W.

Proteomic databases

MaxQBi Q04439.
PaxDbi Q04439.
PeptideAtlasi Q04439.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YMR109W ; YMR109W ; YMR109W .
GeneIDi 855136.
KEGGi sce:YMR109W.

Organism-specific databases

CYGDi YMR109w.
SGDi S000004715. MYO5.

Phylogenomic databases

eggNOGi COG5022.
GeneTreei ENSGT00750000117868.
HOGENOMi HOG000260265.
KOi K10356.
OMAi LFRVINT.
OrthoDBi EOG7VDXXK.

Enzyme and pathway databases

BioCyci YEAST:G3O-32805-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q04439.
NextBioi 978516.

Gene expression databases

Genevestigatori Q04439.

Family and domain databases

InterProi IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00193. MYOSINHEAVY.
SMARTi SM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton."
    Goodson H.V., Anderson B.L., Warrick H.M., Pon L.A., Spudich J.A.
    J. Cell Biol. 133:1277-1291(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Role of type I myosins in receptor-mediated endocytosis in yeast."
    Geli M.I., Riezman H.
    Science 272:533-535(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECEPTOR ENDOCYTOSIS, MUTAGENESIS OF GLU-472.
  5. "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."
    Anderson B.L., Boldogh I., Evangelista M., Boone C., Greene L.A., Pon L.A.
    J. Cell Biol. 141:1357-1370(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VRP1, SUBCELLULAR LOCATION.
  6. "An intact SH3 domain is required for myosin I-induced actin polymerization."
    Geli M.I., Lombardi R., Schmelzl B., Riezman H.
    EMBO J. 19:4281-4291(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VRP1, MUTAGENESIS OF TRP-1123.
  7. "A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex."
    Evangelista M., Klebl B.M., Tong A.H.Y., Webb B.A., Leeuw T., Leberer E., Whiteway M., Thomas D.Y., Boone C.
    J. Cell Biol. 148:353-362(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARC19 AND ARC40.
  8. "Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization."
    Lechler T., Shevchenko A., Li R.
    J. Cell Biol. 148:363-373(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LAS17.
  9. "The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae."
    Mochida J., Yamamoto T., Fujimura-Kamada K., Tanaka K.
    Genetics 160:923-934(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BBC1, MUTAGENESIS OF TRP-1123.
  10. "Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro."
    Soulard A., Lechler T., Spiridonov V., Shevchenko A., Shevchenko A., Li R., Winsor B.
    Mol. Cell. Biol. 22:7889-7906(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BZZ1.
  11. "The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function."
    Wesche S., Arnold M., Jansen R.-P.
    Curr. Biol. 13:715-724(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SHE4.
  12. "She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae."
    Toi H., Fujimura-Kamada K., Irie K., Takai Y., Todo S., Tanaka K.
    Mol. Biol. Cell 14:2237-2249(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SHE4, MUTAGENESIS OF VAL-164; ASN-168; ASN-209 AND LYS-377.
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. "TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p."
    Grosshans B.L., Groetsch H., Mukhopadhyay D., Fernandez I.M., Pfannstiel J., Idrissi F.-Z., Lechner J., Riezman H., Geli M.I.
    J. Biol. Chem. 281:11104-11114(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-357 AND SER-777, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-357, SUBCELLULAR LOCATION, INTERACTION WITH PKH1; PKH2; YPK1 AND YPK2.
  15. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; TYR-359; SER-992 AND SER-1205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  16. "Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis."
    Barker S.L., Lee L., Pierce B.D., Maldonado-Baez L., Drubin D.G., Wendland B.
    Mol. Biol. Cell 18:2893-2903(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAN1, SUBCELLULAR LOCATION.
  17. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Yeast Myo5 SH3 domain, tetragonal crystal form."
    Gonfloni S., Kursula P., Sacco R., Cesareni G., Wilmanns M.
    Submitted (JAN-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1088-1145.
  21. "High-resolution structure of yeast Myo5 SH3 domain."
    Wilmanns M., Kursula P., Gonfloni S., Ferracuti S., Cesareni G.
    Submitted (OCT-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 1088-1145.

Entry informationi

Entry nameiMYO5_YEAST
AccessioniPrimary (citable) accession number: Q04439
Secondary accession number(s): D6VZT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2280 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3

Similar proteinsi