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Entry version 210 (03 Jul 2019)
Sequence version 1 (01 Feb 1991)
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Protein

Myosin-2

Gene

MYO2

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

Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Essential for the delivery of secretory vesicles to sites of active growth during bud emergence and cytokinesis. Required for segregation and inheritance of peroxisomes, late Golgi compartments, mitochondria and the vacuole to the daughter cell during cell division. Also required for correct alignment of the spindle during mitosis.8 Publications

Miscellaneous

Present with 4339 molecules/cell in log phase SD medium.1 Publication
Moves with an average velocity of 3 um/s along actin cables.

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 bindingi164 – 171ATPBy similarity8

<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

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, Calmodulin-binding, Motor protein, Myosin
Biological processCell cycle, Cell division, Protein transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33803-MONOMER

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-SCE-190873 Gap junction degradation

<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-2
Alternative name(s):
Cell division control protein 66
Class V unconventional myosin MYO2
Type V myosin heavy chain MYO2
Short name:
Myosin V MYO2
<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:MYO2
Synonyms:CDC66
Ordered Locus Names:YOR326W
ORF Names:O6167
<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 XV

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
FungiDB:YOR326W

Saccharomyces Genome Database

More...
SGDi
S000005853 MYO2

<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

<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>Mutagenesisi511E → K in MYO2-66; disrupts actin binding. 1 Publication1
Mutagenesisi1189V → A in MYO2-573; causes a mitochondria inheritance defect; when associated with G-1288; M-1500; S-1529; G-1546 and R-1559. 1 Publication1
Mutagenesisi1247S → G: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1248G → D in MYO2-2; causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1262V → A: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1264F → S: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1268S → P: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1274T → M: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1275F → S: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1288V → A: Intragenic suppressor of MYO2-2. 2 Publications1
Mutagenesisi1288V → G in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; M-1500; S-1529; G-1546 and R-1559. 2 Publications1
Mutagenesisi1297D → G, N or V: Causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1301L → P: Causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1304N → D or S: Causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1307N → D: Causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1474L → S in MYO2-338; abolishes interaction with YPT11; when associated with G-1484 and G-1511. 1 Publication1
Mutagenesisi1484E → G in MYO2-338; abolishes interaction with YPT11; when associated with S-1474 and G-1511. 1 Publication1
Mutagenesisi1500K → M in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; S-1529; G-1546 and R-1559. 1 Publication1
Mutagenesisi1511D → G in MYO2-338; abolishes interaction with YPT11; when associated with S-1474 and G-1484. 1 Publication1
Mutagenesisi1529P → S in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; G-1546 and R-1559. 1 Publication1
Mutagenesisi1546E → G in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; S-1529 and R-1559. 1 Publication1
Mutagenesisi1559K → R in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; S-1529 and G-1546. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001234892 – 1574Myosin-2Add BLAST1573

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 residuei2N-acetylserineCombined sources1
Modified residuei1097PhosphothreonineCombined sources1
Modified residuei1121PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P19524

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

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PaxDbi
P19524

PRoteomics IDEntifications database

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PRIDEi
P19524

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P19524

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P19524

<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

Homodimer.

Interacts with calmodulin (CMD1) and the myosin light chain MLC1 through its IQ repeats. Binds to the membrane receptors SEC4 and VAC17 to transport secretory vesicles and the vacuole, respectively. Binds to KAR9, which transports BIM1-coated cytoplasmic microtubules that are attached to the spindle pole body into the emerging bud, thereby correctly orienting the mitotic spindle.

Interacts with YPT11 and MMR1 to accelerate mitochondrial distribution to the bud.

Interacts with SHE4 and localizes it to the bud tip.

Interacts with RHO3 and SMY1, putative regulators of MYO2 function.

Interacts with SRO7.

14 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)

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BioGridi
34711, 665 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1304 MYO2-VAC17-VAC8 transport complex
CPX-2225 Myosin class V complex, MYO2 variant

Database of interacting proteins

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DIPi
DIP-2308N

Protein interaction database and analysis system

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IntActi
P19524, 50 interactors

Molecular INTeraction database

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MINTi
P19524

STRING: functional protein association networks

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STRINGi
4932.YOR326W

<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

11574
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

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SMRi
P19524

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P19524

<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>Domaini4 – 57Myosin N-terminal SH3-likePROSITE-ProRule annotationAdd BLAST54
Domaini70 – 781Myosin motorPROSITE-ProRule annotationAdd BLAST712
Domaini784 – 806IQ 1PROSITE-ProRule annotationAdd BLAST23
Domaini807 – 831IQ 2PROSITE-ProRule annotationAdd BLAST25
Domaini832 – 855IQ 3PROSITE-ProRule annotationAdd BLAST24
Domaini856 – 879IQ 4PROSITE-ProRule annotationAdd BLAST24
Domaini880 – 902IQ 5PROSITE-ProRule annotationAdd BLAST23
Domaini903 – 932IQ 6PROSITE-ProRule annotationAdd BLAST30
Domaini1226 – 1501DilutePROSITE-ProRule annotationAdd BLAST276

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>Regioni443 – 523Actin-bindingBy similarityAdd BLAST81
Regioni1087 – 1574Non alpha-helical, tail domainAdd BLAST488

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili933 – 1088Add BLAST156

<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 binds to actin.
The IQ domains provide the interaction surface for the myosin light chain MLC1.
The coiled-coiled domain is necessary for dimerization.
The tail domain is a globular cargo-binding domain involved in vectorial vesicle transport.

<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

Coiled coil, Repeat

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00940000170389

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000171839

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P19524

KEGG Orthology (KO)

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KOi
K10357

Identification of Orthologs from Complete Genome Data

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OMAi
AESDMLQ

Family and domain databases

Conserved Domains Database

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CDDi
cd01380 MYSc_Myo5, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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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
IPR002710 Dilute_dom
IPR000048 IQ_motif_EF-hand-BS
IPR036961 Kinesin_motor_dom_sf
IPR001609 Myosin_head_motor_dom
IPR004009 Myosin_N
IPR008989 Myosin_S1_N
IPR036103 MYSc_Myo5
IPR027417 P-loop_NTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01843 DIL, 1 hit
PF00063 Myosin_head, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00193 MYOSINHEAVY

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01132 DIL, 1 hit
SM00015 IQ, 4 hits
SM00242 MYSc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50084 SSF50084, 1 hit
SSF52540 SSF52540, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51126 DILUTE, 1 hit
PS50096 IQ, 1 hit
PS51456 MYOSIN_MOTOR, 1 hit
PS51844 SH3_LIKE, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P19524-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFEVGTRCW YPHKELGWIG AEVIKNEFND GKYHLELQLE DDEIVSVDTK
60 70 80 90 100
DLNNDKDQSL PLLRNPPILE ATEDLTSLSY LNEPAVLHAI KQRYSQLNIY
110 120 130 140 150
TYSGIVLIAT NPFDRVDQLY TQDMIQAYAG KRRGELEPHL FAIAEEAYRL
160 170 180 190 200
MKNDKQNQTI VVSGESGAGK TVSAKYIMRY FASVEEENSA TVQHQVEMSE
210 220 230 240 250
TEQKILATNP IMEAFGNAKT TRNDNSSRFG KYLEILFDKD TSIIGARIRT
260 270 280 290 300
YLLERSRLVY QPPIERNYHI FYQLMAGLPA QTKEELHLTD ASDYFYMNQG
310 320 330 340 350
GDTKINGIDD AKEYKITVDA LTLVGITKET QHQIFKILAA LLHIGNIEIK
360 370 380 390 400
KTRNDASLSA DEPNLKLACE LLGIDAYNFA KWVTKKQIIT RSEKIVSNLN
410 420 430 440 450
YSQALVAKDS VAKFIYSALF DWLVENINTV LCNPAVNDQI SSFIGVLDIY
460 470 480 490 500
GFEHFEKNSF EQFCINYANE KLQQEFNQHV FKLEQEEYVK EEIEWSFIEF
510 520 530 540 550
NDNQPCIDLI ENKLGILSLL DEESRLPAGS DESWTQKLYQ TLDKSPTNKV
560 570 580 590 600
FSKPRFGQTK FIVSHYALDV AYDVEGFIEK NRDTVSDGHL EVLKASTNET
610 620 630 640 650
LINILEGLEK AAKKLEEAKK LELEQAGSKK PGPIRTVNRK PTLGSMFKQS
660 670 680 690 700
LIELMNTINS TNVHYIRCIK PNADKEAWQF DNLMVLSQLR ACGVLETIRI
710 720 730 740 750
SCAGFPSRWT FEEFVLRYYI LIPHEQWDLI FKKKETTEED IISVVKMILD
760 770 780 790 800
ATVKDKSKYQ IGNTKIFFKA GMLAYLEKLR SNKMHNSIVM IQKKIRAKYY
810 820 830 840 850
RKQYLQISQA IKYLQNNIKG FIIRQRVNDE MKVNCATLLQ AAYRGHSIRA
860 870 880 890 900
NVFSVLRTIT NLQKKIRKEL KQRQLKQEHE YNAAVTIQSK VRTFEPRSRF
910 920 930 940 950
LRTKKDTVVV QSLIRRRAAQ RKLKQLKADA KSVNHLKEVS YKLENKVIEL
960 970 980 990 1000
TQNLASKVKE NKEMTERIKE LQVQVEESAK LQETLENMKK EHLIDIDNQK
1010 1020 1030 1040 1050
SKDMELQKTI ENNLQSTEQT LKDAQLELED MVKQHDELKE ESKKQLEELE
1060 1070 1080 1090 1100
QTKKTLVEYQ TLNGDLQNEV KSLKEEIARL QTAMSLGTVT TSVLPQTPLK
1110 1120 1130 1140 1150
DVMGGGASNF NNMMLENSDL SPNDLNLKSR STPSSGNNHI DSLSVDRENG
1160 1170 1180 1190 1200
VNATQINEEL YRLLEDTEIL NQEITEGLLK GFEVPDAGVA IQLSKRDVVY
1210 1220 1230 1240 1250
PARILIIVLS EMWRFGLTKQ SESFLAQVLT TIQKVVTQLK GNDLIPSGVF
1260 1270 1280 1290 1300
WLANVRELYS FVVFALNSIL TEETFKNGMT DEEYKEYVSL VTELKDDFEA
1310 1320 1330 1340 1350
LSYNIYNIWL KKLQKQLQKK AINAVVISES LPGFSAGETS GFLNKIFANT
1360 1370 1380 1390 1400
EEYTMDDILT FFNSIYWCMK SFHIENEVFH AVVTTLLNYV DAICFNELIM
1410 1420 1430 1440 1450
KRNFLSWKRG LQLNYNVTRL EEWCKTHGLT DGTECLQHLI QTAKLLQVRK
1460 1470 1480 1490 1500
YTIEDIDILR GICYSLTPAQ LQKLISQYQV ADYESPIPQE ILRYVADIVK
1510 1520 1530 1540 1550
KEAALSSSGN DSKGHEHSSS IFITPETGPF TDPFSLIKTR KFDQVEAYIP
1560 1570
AWLSLPSTKR IVDLVAQQVV QDGH
Length:1,574
Mass (Da):180,680
Last modified:February 1, 1991 - 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:i1F7E2887C1E59D54
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M35532 Genomic DNA Translation: AAA34810.1
Z75234 Genomic DNA Translation: CAA99646.1
Z75235 Genomic DNA Translation: CAA99648.1
X90565 Genomic DNA Translation: CAA62184.1
Z49821 Genomic DNA Translation: CAA89973.1
BK006948 Genomic DNA Translation: DAA11089.1

Protein sequence database of the Protein Information Resource

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PIRi
A38454

NCBI Reference Sequences

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RefSeqi
NP_014971.1, NM_001183746.1

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YOR326W_mRNA; YOR326W_mRNA; YOR326W

Database of genes from NCBI RefSeq genomes

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GeneIDi
854504

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YOR326W

<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
M35532 Genomic DNA Translation: AAA34810.1
Z75234 Genomic DNA Translation: CAA99646.1
Z75235 Genomic DNA Translation: CAA99648.1
X90565 Genomic DNA Translation: CAA62184.1
Z49821 Genomic DNA Translation: CAA89973.1
BK006948 Genomic DNA Translation: DAA11089.1
PIRiA38454
RefSeqiNP_014971.1, NM_001183746.1

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
1M45X-ray1.65B806-830[»]
1M46X-ray2.10B854-878[»]
1N2DX-ray2.00C806-853[»]
2F6HX-ray2.25X1152-1570[»]
6EYWX-ray2.88X1150-1574[»]
6IXOX-ray1.90A1152-1574[»]
6IXPX-ray2.73A/D1152-1574[»]
6IXQX-ray3.06A1152-1574[»]
6IXRX-ray2.85A1152-1574[»]
SMRiP19524
ModBaseiSearch...

Protein-protein interaction databases

BioGridi34711, 665 interactors
ComplexPortaliCPX-1304 MYO2-VAC17-VAC8 transport complex
CPX-2225 Myosin class V complex, MYO2 variant
DIPiDIP-2308N
IntActiP19524, 50 interactors
MINTiP19524
STRINGi4932.YOR326W

PTM databases

CarbonylDBiP19524
iPTMnetiP19524

Proteomic databases

MaxQBiP19524
PaxDbiP19524
PRIDEiP19524

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR326W_mRNA; YOR326W_mRNA; YOR326W
GeneIDi854504
KEGGisce:YOR326W

Organism-specific databases

EuPathDBiFungiDB:YOR326W
SGDiS000005853 MYO2

Phylogenomic databases

GeneTreeiENSGT00940000170389
HOGENOMiHOG000171839
InParanoidiP19524
KOiK10357
OMAiAESDMLQ

Enzyme and pathway databases

BioCyciYEAST:G3O-33803-MONOMER
ReactomeiR-SCE-190873 Gap junction degradation

Miscellaneous databases

EvolutionaryTraceiP19524

Protein Ontology

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PROi
PR:P19524

Family and domain databases

CDDicd01380 MYSc_Myo5, 1 hit
Gene3Di3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR002710 Dilute_dom
IPR000048 IQ_motif_EF-hand-BS
IPR036961 Kinesin_motor_dom_sf
IPR001609 Myosin_head_motor_dom
IPR004009 Myosin_N
IPR008989 Myosin_S1_N
IPR036103 MYSc_Myo5
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF01843 DIL, 1 hit
PF00063 Myosin_head, 1 hit
PRINTSiPR00193 MYOSINHEAVY
SMARTiView protein in SMART
SM01132 DIL, 1 hit
SM00015 IQ, 4 hits
SM00242 MYSc, 1 hit
SUPFAMiSSF50084 SSF50084, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51126 DILUTE, 1 hit
PS50096 IQ, 1 hit
PS51456 MYOSIN_MOTOR, 1 hit
PS51844 SH3_LIKE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

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 nameiMYO2_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: P19524
Secondary accession number(s): D6W323
<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: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 3, 2019
This is version 210 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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