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Entry version 184 (18 Sep 2019)
Sequence version 4 (21 Sep 2011)
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Protein

Myosin-3

Gene

MYO3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi129 – 136ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • actin binding Source: UniProtKB-KW
  • ATP binding Source: UniProtKB-KW
  • microfilament motor activity Source: SGD
  • myosin binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActin-binding, Hydrolase, Motor protein, Myosin
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31910-MONOMER

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
P36006 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Myosin-3
Alternative name(s):
Actin-dependent myosin-I MYO3
Class I unconventional myosin MYO3
Type I myosin MYO3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MYO3
Ordered Locus Names:YKL129C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YKL129C

Saccharomyces Genome Database

More...
SGDi
S000001612 MYO3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi132G → R: Loss of function. 1 Publication1
Mutagenesisi357S → A: Loss of function. 2 Publications1
Mutagenesisi357S → D: Has a constitutive higher activity in actin assembly. 2 Publications1
Mutagenesisi1158W → S: Abolishes interaction with LAS17 and causes severe mislocalization of the protein. 1 Publication1
Mutagenesisi1272Missing : Abolishes interaction with ARC40. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001234901 – 1272Myosin-3Add BLAST1272

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei357PhosphoserineCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P36006

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P36006

PRoteomics IDEntifications database

More...
PRIDEi
P36006

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P36006

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34006, 104 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1500 Myosin class I complex, MYO3 variant

Database of interacting proteins

More...
DIPi
DIP-2221N

Protein interaction database and analysis system

More...
IntActi
P36006, 57 interactors

Molecular INTeraction database

More...
MINTi
P36006

STRING: functional protein association networks

More...
STRINGi
4932.YKL129C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11272
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P36006

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P36006

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini36 – 715Myosin motorPROSITE-ProRule annotationAdd BLAST680
Domaini719 – 739IQ 1Add BLAST21
Domaini740 – 765IQ 2Add BLAST26
Domaini771 – 961TH1PROSITE-ProRule annotationAdd BLAST191
Domaini1120 – 1182SH3PROSITE-ProRule annotationAdd BLAST63

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni588 – 610Actin-bindingPROSITE-ProRule annotationAdd BLAST23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1003 – 1123Ala/Pro-richAdd BLAST121
Compositional biasi1109 – 1116Poly-Pro8
Compositional biasi1259 – 1271Asp-rich (acidic)Add BLAST13

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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).

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000260265

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P36006

KEGG Orthology (KO)

More...
KOi
K10356

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01378 MYSc_Myo1, 1 hit
cd11858 SH3_Myosin-I_fungi, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.850.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035535 Fungal_myosin-I_SH3
IPR036961 Kinesin_motor_dom_sf
IPR001609 Myosin_head_motor_dom
IPR010926 Myosin_TH1
IPR036072 MYSc_Myo1
IPR027417 P-loop_NTPase
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00063 Myosin_head, 1 hit
PF06017 Myosin_TH1, 1 hit
PF00018 SH3_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00193 MYOSINHEAVY

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00242 MYSc, 1 hit
SM00326 SH3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50044 SSF50044, 1 hit
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51456 MYOSIN_MOTOR, 1 hit
PS50002 SH3, 1 hit
PS51757 TH1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6CB13AD3CD669600
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti95G → RK in AAB34124 (PubMed:7728870).Curated1
Sequence conflicti168 – 169NP → T in AAB34124 (PubMed:7728870).Curated2
Sequence conflicti263 – 270TADTIDDV → SADQLMR in CAA81970 (PubMed:8196765).Curated8
Sequence conflicti917 – 918VG → RLV in AAB34124 (PubMed:7728870).Curated2
Sequence conflicti1021A → R in CAA81970 (PubMed:8196765).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
S76960 Genomic DNA Translation: AAB34124.1
Z28129 Genomic DNA Translation: CAA81970.1
BK006944 Genomic DNA Translation: DAA09032.2

Protein sequence database of the Protein Information Resource

More...
PIRi
S37958

NCBI Reference Sequences

More...
RefSeqi
NP_012793.2, NM_001179695.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YKL129C_mRNA; YKL129C; YKL129C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853729

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKL129C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RUWX-ray1.80A1121-1189[»]
1VA7X-ray2.90A/B/C/D1121-1189[»]
2BTTNMR-A1121-1189[»]
SMRiP36006
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi34006, 104 interactors
ComplexPortaliCPX-1500 Myosin class I complex, MYO3 variant
DIPiDIP-2221N
IntActiP36006, 57 interactors
MINTiP36006
STRINGi4932.YKL129C

Protein family/group databases

MoonDBiP36006 Predicted

PTM databases

iPTMnetiP36006

Proteomic databases

MaxQBiP36006
PaxDbiP36006
PRIDEiP36006

Genome annotation databases

EnsemblFungiiYKL129C_mRNA; YKL129C; YKL129C
GeneIDi853729
KEGGisce:YKL129C

Organism-specific databases

EuPathDBiFungiDB:YKL129C
SGDiS000001612 MYO3

Phylogenomic databases

HOGENOMiHOG000260265
InParanoidiP36006
KOiK10356

Enzyme and pathway databases

BioCyciYEAST:G3O-31910-MONOMER

Miscellaneous databases

EvolutionaryTraceiP36006

Protein Ontology

More...
PROi
PR:P36006

Family and domain databases

CDDicd01378 MYSc_Myo1, 1 hit
cd11858 SH3_Myosin-I_fungi, 1 hit
Gene3Di3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR035535 Fungal_myosin-I_SH3
IPR036961 Kinesin_motor_dom_sf
IPR001609 Myosin_head_motor_dom
IPR010926 Myosin_TH1
IPR036072 MYSc_Myo1
IPR027417 P-loop_NTPase
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
PfamiView protein in Pfam
PF00063 Myosin_head, 1 hit
PF06017 Myosin_TH1, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00193 MYOSINHEAVY
SMARTiView protein in SMART
SM00242 MYSc, 1 hit
SM00326 SH3, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51456 MYOSIN_MOTOR, 1 hit
PS50002 SH3, 1 hit
PS51757 TH1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMYO3_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P36006
Secondary accession number(s): D6VX66
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: September 21, 2011
Last modified: September 18, 2019
This is version 184 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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