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Protein

Myosin-5

Gene

MYO5

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 STE2.9 Publications

Miscellaneous

Present with 2280 molecules/cell in log phase SD medium.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 – 136ATPSequence analysis8

<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
  • identical protein binding Source: IntAct
  • microfilament motor activity Source: SGD

GO - Biological processi

  • actin cortical patch localization Source: SGD
  • bipolar cellular bud site selection Source: SGD
  • endocytosis Source: SGD
  • exocytosis Source: SGD
  • fungal-type cell wall organization Source: SGD
  • positive regulation of Arp2/3 complex-mediated actin nucleation Source: SGD
  • receptor-mediated endocytosis Source: SGD
  • response to osmotic stress Source: SGD
  • response to salt stress Source: SGD

<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-32805-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-194840 Rho GTPase cycle
R-SCE-8985586 SLIT2:ROBO1 increases RHOA activity

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
Q04439 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-5
Alternative name(s):
Actin-dependent myosin-I MYO5
Class I unconventional myosin MYO5
Type I myosin MYO5
<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:MYO5
Ordered Locus Names:YMR109W
ORF Names:YM9718.08
<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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000004715 MYO5

<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; 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>Mutagenesisi164V → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication1
Mutagenesisi168N → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication1
Mutagenesisi209N → S: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication1
Mutagenesisi357S → A: Leads to a depolarized actin cytoskeleton and a strong defect in the capacity to internalize STE2. 1 Publication1
Mutagenesisi357S → E: No growth defect, but leads to a partially depolarized actin cytoskeleton. Accelerates the constitutive internalization of STE2. 1 Publication1
Mutagenesisi377K → M: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication1
Mutagenesisi472E → K in MYO5-1; temperature sensitive loss of function. 1 Publication1
Mutagenesisi1123W → S: Abolishes interaction with BBC1 and VRP1. 2 Publications1

<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_00001234921 – 1219Myosin-5Add BLAST1219

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
Modified residuei359PhosphotyrosineCombined sources1
Modified residuei777Phosphoserine1 Publication1
Modified residuei992PhosphoserineCombined sources1
Modified residuei1205PhosphoserineCombined sources1

<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 activity. Ser-357 is phosphorylated by YPK2 in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q04439

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

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PaxDbi
Q04439

PRoteomics IDEntifications database

More...
PRIDEi
Q04439

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
Q04439

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q04439

<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. Interacts with BZZ1, PKH1, PKH2, YPK1 and YPK2.10 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
35285, 239 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1470 Myosin class I complex, MYO5 variant

Database of interacting proteins

More...
DIPi
DIP-2222N

Protein interaction database and analysis system

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IntActi
Q04439, 99 interactors

Molecular INTeraction database

More...
MINTi
Q04439

STRING: functional protein association networks

More...
STRINGi
4932.YMR109W

<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

11219
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YP5X-ray1.68A1088-1145[»]
1ZUYX-ray1.39A/B1088-1145[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q04439

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

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SMRi
Q04439

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q04439

<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
Domaini1085 – 1147SH3PROSITE-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>Regioni404 – 486Actin-bindingBy similarityAdd BLAST83

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 biasi1000 – 1088Ala/Pro-richAdd BLAST89
Compositional biasi1011 – 1016Poly-Pro6
Compositional biasi1060 – 1063Poly-Ala4
Compositional biasi1073 – 1081Poly-Pro9
Compositional biasi1204 – 1218Asp/Glu-rich (acidic)Add BLAST15

<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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000170976

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000260265

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q04439

KEGG Orthology (KO)

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KOi
K10356

Identification of Orthologs from Complete Genome Data

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OMAi
HQGFGDL

Family and domain databases

Conserved Domains Database

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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

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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

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

Superfamily database of structural and functional annotation

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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>.<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.

Q04439-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAILKRGARK KVHQEPAKRS ANIKKATFDS SKKKEVGVSD LTLLSKISDE
60 70 80 90 100
AINENLKKRF LNATIYTYIG HVLISVNPFR DLGIYTDAVM NEYKGKNRLE
110 120 130 140 150
VPPHVFAIAE SMYYNMKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS
160 170 180 190 200
STHTESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNNQF
210 220 230 240 250
EPCAGNITNY LLEKQRVVSQ IKNERNFHIF YQFTKGASDA YRQTFGVQKP
260 270 280 290 300
EQYVYTAAAG CISAETIDDL QDYQETLKAM RVIGLGQEEQ DQIFRMLAAI
310 320 330 340 350
LWIGNVSFIE NEEGNAQVRD TSVTDFVAYL LQIDSQLLIK SLVERIMETN
360 370 380 390 400
HGMKRGSVYH VPLNIVQADA VRDALAKAIY NNLFDWIVSR VNKSLQAFPG
410 420 430 440 450
AEKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKSEQETYE
460 470 480 490 500
REKIQWTPIK YFDNKVVCDL IEARRPPGIF AAMNDSVATA HADSNAADQA
510 520 530 540 550
FAQRLNLFTT NPHFDLRSNK FVIKHYAGDV TYDIDGITDK NKDQLQKDLV
560 570 580 590 600
ELIGTTTNTF LATIFPDTVD RESKRRPPTA GDKIIKSAND LVETLSKAQP
610 620 630 640 650
SYIRTIKPNE TKSPNDYDDR QVLHQIKYLG LQENVRIRRA GFAYRQVFEK
660 670 680 690 700
FVERFYLLSP HCSYAGDYTW QGDTLDAVKY ILQDSSIPQQ EYQLGVTSVF
710 720 730 740 750
IKTPETLFAL EHMRDRYWHN MAARIQRAWR RFLQRRIDAA TKIQRTIRER
760 770 780 790 800
KEGNKYEKLR DYGTKVLGGR KERRSMSLLG YRAFMGDYLS CNESKSKGAY
810 820 830 840 850
IKRQVSIKEK VIFSIHGEAL HTKFGRSAQR LKKTFLLTPT TLYIVGQTLV
860 870 880 890 900
QNAMTYTQDY KIDVRNIQAV SLTNLQDDWV AIKLASSGQP DPLINTYFKT
910 920 930 940 950
ELITHLKRLN DKIQIKIGSA IEYQKKPGKL HSVKCQINES APKYGDIYKS
960 970 980 990 1000
STISVRRGNP PNSQVHKKPR KKSSISSGYH ASSSQATRRP VSIAAAQHVP
1010 1020 1030 1040 1050
TAPASRHSKK PAPPPPGMQN KAATRRSVPN PASTLTASQS NARPSPPTAA
1060 1070 1080 1090 1100
TRATPAATPA AAAMGSGRQA NIPPPPPPPP PSSKPKEPMF EAAYDFPGSG
1110 1120 1130 1140 1150
SPSELPLKKG DVIYITREEP SGWSLGKLLD GSKEGWVPTA YMKPHSGNNN
1160 1170 1180 1190 1200
IPTPPQNRDV PKPVLNSVQH DNTSANVIPA AAQASLGDGL ANALAARANK
1210
MRLESDDEEA NEDEEEDDW
Length:1,219
Mass (Da):136,899
Last modified:November 1, 1997 - v1
<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:iDFFB9EC16B61CD29
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z49702 Genomic DNA Translation: CAA89745.1
BK006946 Genomic DNA Translation: DAA10006.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S54570

NCBI Reference Sequences

More...
RefSeqi
NP_013827.1, NM_001182609.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YMR109W_mRNA; YMR109W_mRNA; YMR109W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855136

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YMR109W

<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
Z49702 Genomic DNA Translation: CAA89745.1
BK006946 Genomic DNA Translation: DAA10006.1
PIRiS54570
RefSeqiNP_013827.1, NM_001182609.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YP5X-ray1.68A1088-1145[»]
1ZUYX-ray1.39A/B1088-1145[»]
ProteinModelPortaliQ04439
SMRiQ04439
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35285, 239 interactors
ComplexPortaliCPX-1470 Myosin class I complex, MYO5 variant
DIPiDIP-2222N
IntActiQ04439, 99 interactors
MINTiQ04439
STRINGi4932.YMR109W

Protein family/group databases

MoonDBiQ04439 Predicted

PTM databases

CarbonylDBiQ04439
iPTMnetiQ04439

Proteomic databases

MaxQBiQ04439
PaxDbiQ04439
PRIDEiQ04439

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR109W_mRNA; YMR109W_mRNA; YMR109W
GeneIDi855136
KEGGisce:YMR109W

Organism-specific databases

SGDiS000004715 MYO5

Phylogenomic databases

GeneTreeiENSGT00940000170976
HOGENOMiHOG000260265
InParanoidiQ04439
KOiK10356
OMAiHQGFGDL

Enzyme and pathway databases

BioCyciYEAST:G3O-32805-MONOMER
ReactomeiR-SCE-194840 Rho GTPase cycle
R-SCE-8985586 SLIT2:ROBO1 increases RHOA activity

Miscellaneous databases

EvolutionaryTraceiQ04439

Protein Ontology

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PROi
PR:Q04439

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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<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 nameiMYO5_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: Q04439
Secondary accession number(s): D6VZT2
<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: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 16, 2019
This is version 185 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
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