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P36006

- MYO3_YEAST

UniProt

P36006 - MYO3_YEAST

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Protein

Myosin-3

Gene

MYO3

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 STE2.7 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi129 – 1368ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. microfilament motor activity Source: SGD
  3. myosin binding Source: UniProtKB

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. response to osmotic 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-31910-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-3
Alternative name(s):
Actin-dependent myosin-I MYO3
Class I unconventional myosin MYO3
Type I myosin MYO3
Gene namesi
Name:MYO3
Ordered Locus Names:YKL129C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

SGDiS000001612. MYO3.

Subcellular locationi

Cytoplasmcytoskeletonactin patch 1 Publication
Note: Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth.

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
Mutagenesisi132 – 1321G → R: Loss of function. 1 Publication
Mutagenesisi357 – 3571S → A: Loss of function. 2 Publications
Mutagenesisi357 – 3571S → D: Has a constitutive higher activity in actin assembly. 2 Publications
Mutagenesisi1158 – 11581W → S: Abolishes interaction with LAS17 and causes severe mislocalization of the protein.
Mutagenesisi1272 – 12721Missing: Abolishes interaction with ARC40.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12721272Myosin-3PRO_0000123490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei357 – 3571Phosphoserine4 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 (By similarity). Ser-357 is phosphorylated by CLA4 and STE20 in vitro.By similarity4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36006.
PaxDbiP36006.
PeptideAtlasiP36006.

Expressioni

Gene expression databases

GenevestigatoriP36006.

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIM21P405633EBI-11670,EBI-25376
BBC1P470685EBI-11670,EBI-3437
BCK1Q013896EBI-11670,EBI-3470
BNI1P418323EBI-11670,EBI-3692
BNR1P404506EBI-11670,EBI-3711
LAS17Q124463EBI-11670,EBI-10022
OSH2Q124513EBI-11670,EBI-12621
PRP8P333344EBI-11670,EBI-465
SAP1P399553EBI-11670,EBI-16463
STE20Q034973EBI-11670,EBI-18285
UBP7P404533EBI-11670,EBI-19857
VRP1P3737011EBI-11670,EBI-20502
YOR389WQ089122EBI-11670,EBI-38289

Protein-protein interaction databases

BioGridi34006. 67 interactions.
DIPiDIP-2221N.
IntActiP36006. 57 interactions.
MINTiMINT-382399.
STRINGi4932.YKL129C.

Structurei

Secondary structure

1
1272
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1123 – 11297
Beta strandi1137 – 11393
Beta strandi1147 – 11537
Beta strandi1157 – 11637
Beta strandi1169 – 11735
Helixi1174 – 11763
Beta strandi1177 – 11793

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RUWX-ray1.80A1121-1189[»]
1VA7X-ray2.90A/B/C/D1121-1189[»]
2BTTNMR-A1121-1189[»]
ProteinModelPortaliP36006.
SMRiP36006. Positions 37-745, 1121-1189.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36006.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 715680Myosin motorAdd
BLAST
Domaini719 – 73921IQ 1Add
BLAST
Domaini740 – 76526IQ 2Add
BLAST
Domaini759 – 960202Myosin tailSequence AnalysisAdd
BLAST
Domaini1120 – 118263SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni404 – 48683Actin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1003 – 1123121Ala/Pro-richAdd
BLAST
Compositional biasi1109 – 11168Poly-Pro
Compositional biasi1259 – 127113Asp-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 myosin tail domain (also named 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.Curated
Contains 1 myosin motor domain.Curated
Contains 1 myosin tail domain.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00760000120106.
HOGENOMiHOG000260265.
InParanoidiP36006.
KOiK10356.
OMAiAGAPMMK.
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.

P36006-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGISD LTLLSKISDE
60 70 80 90 100
SINENLKKRF KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE
110 120 130 140 150
VPPHVFAIAE SMYYNLKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS
160 170 180 190 200
NSHSESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNSQF
210 220 230 240 250
EPCAGNITNY LLEKQRVVGQ IKNERNFHIF YQFTKGASDT YKQMFGVQMP
260 270 280 290 300
EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI
310 320 330 340 350
LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS
360 370 380 390 400
HGMKRGSVYH VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG
410 420 430 440 450
ADKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKAEQETYE
460 470 480 490 500
REKIKWTPIK YFDNKVVCDL IEAKNPPGIL AAMNDSIATA HADSNAADQA
510 520 530 540 550
FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK NKDQLQKDLI
560 570 580 590 600
ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP
610 620 630 640 650
SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK
660 670 680 690 700
FVERFYLLSP DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF
710 720 730 740 750
IKTPESLFAL EDMRDKYWYN MAARIQRAWR RFLQRRIDAA IKIQRTIREK
760 770 780 790 800
KGGNKYVKLR DYGTKLLAGK KERRSMSLLG YRAFMGDYLS CNESKTKGSY
810 820 830 840 850
IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK TFYIIGQTRE
860 870 880 890 900
QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQS DPLINTPFKT
910 920 930 940 950
ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS
960 970 980 990 1000
STIYVRRGHP ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH
1010 1020 1030 1040 1050
RDAAKKQPLP SQKPVNPLSL AATAAQAAYN PKPDKTVPIK SSAIPAAKVS
1060 1070 1080 1090 1100
SKHSSKPSSK EKVAVKKASS SHKSSSAKQN QVSMPPSKGV EKNKEPLKET
1110 1120 1130 1140 1150
TATATANIPI PPPPPPMGQP KDPKFEAAYD FPGSGSSSEL PLKKGDIVFI
1160 1170 1180 1190 1200
SRDEPSGWSL AKLLDGSKEG WVPTAYMTPY KDTRNTVPVA ATGAVNDVTN
1210 1220 1230 1240 1250
QKSSQIDNTI SSAQEGVQFG SATVGPTSDN QSNPVGTFSD GLASALAARA
1260 1270
NKMRAESADD DDNDDGDDDD DW
Length:1,272
Mass (Da):142,451
Last modified:September 21, 2011 - v4
Checksum:i6CB13AD3CD669600
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951G → RK in AAB34124. (PubMed:7728870)Curated
Sequence conflicti168 – 1692NP → T in AAB34124. (PubMed:7728870)Curated
Sequence conflicti263 – 2708TADTIDDV → SADQLMR in CAA81970. (PubMed:8196765)Curated
Sequence conflicti917 – 9182VG → RLV in AAB34124. (PubMed:7728870)Curated
Sequence conflicti1021 – 10211A → R in CAA81970. (PubMed:8196765)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S76960 Genomic DNA. Translation: AAB34124.1.
Z28129 Genomic DNA. Translation: CAA81970.1.
BK006944 Genomic DNA. Translation: DAA09032.2.
PIRiS37958.
RefSeqiNP_012793.2. NM_001179695.2.

Genome annotation databases

EnsemblFungiiYKL129C; YKL129C; YKL129C.
GeneIDi853729.
KEGGisce:YKL129C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S76960 Genomic DNA. Translation: AAB34124.1 .
Z28129 Genomic DNA. Translation: CAA81970.1 .
BK006944 Genomic DNA. Translation: DAA09032.2 .
PIRi S37958.
RefSeqi NP_012793.2. NM_001179695.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RUW X-ray 1.80 A 1121-1189 [» ]
1VA7 X-ray 2.90 A/B/C/D 1121-1189 [» ]
2BTT NMR - A 1121-1189 [» ]
ProteinModelPortali P36006.
SMRi P36006. Positions 37-745, 1121-1189.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34006. 67 interactions.
DIPi DIP-2221N.
IntActi P36006. 57 interactions.
MINTi MINT-382399.
STRINGi 4932.YKL129C.

Proteomic databases

MaxQBi P36006.
PaxDbi P36006.
PeptideAtlasi P36006.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL129C ; YKL129C ; YKL129C .
GeneIDi 853729.
KEGGi sce:YKL129C.

Organism-specific databases

SGDi S000001612. MYO3.

Phylogenomic databases

eggNOGi COG5022.
GeneTreei ENSGT00760000120106.
HOGENOMi HOG000260265.
InParanoidi P36006.
KOi K10356.
OMAi AGAPMMK.
OrthoDBi EOG7VDXXK.

Enzyme and pathway databases

BioCyci YEAST:G3O-31910-MONOMER.

Miscellaneous databases

EvolutionaryTracei P36006.
NextBioi 974764.

Gene expression databases

Genevestigatori P36006.

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. "Identification and molecular characterization of a yeast myosin I."
    Goodson H.V., Spudich J.A.
    Cell Motil. Cytoskeleton 30:73-84(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CRY3.
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 263-270 AND 1021.
    Strain: ATCC 204508 / S288c.
  4. "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: FUNCTION IN ACTIN CYTOSKELETON ORGANIZATION.
  5. "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.
  6. "The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast."
    Wu C., Lytvyn V., Thomas D.Y., Leberer E.
    J. Biol. Chem. 272:30623-30626(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-357 BY CLA4 AND STE20, MUTAGENESIS OF SER-357.
  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; ARC40; LAS17 AND VRP1.
  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 ARP2 AND LAS17, MUTAGENESIS OF GLY-132 AND SER-357.
  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.
  10. "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.
  11. "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.
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  14. "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.
  15. "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].
  16. "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-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S.cerevisiae."
    Musi V., Birdsall B., Fernandez-Ballester G., Guerrini R., Salvatori S., Serrano L., Pastore A.
    Protein Sci. 15:795-807(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1123-1191.
  18. "Crystal structure of the SH3 domain from S.cerevisiae Myo3."
    Kursula P., Kursula I., Lehmann F., Song Y.H., Wilmanns M.
    Submitted (MAR-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1123-1191.
  19. "High-throughput structural genomics of yeast SH3 domains."
    Kursula P., Lehmann F., Song Y.H., Wilmanns M.
    Submitted (JUN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1123-1191.

Entry informationi

Entry nameiMYO3_YEAST
AccessioniPrimary (citable) accession number: P36006
Secondary accession number(s): D6VX66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: September 21, 2011
Last modified: October 29, 2014
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 155 molecules/cell in log phase SD medium.1 Publication

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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3