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Entry version 116 (17 Jun 2020)
Sequence version 1 (01 Oct 2000)
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Protein

Unconventional myosin-VI

Gene

MYO6

Organism
Gallus gallus (Chicken)
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

Myosins are actin-based motor molecules with ATPase activity (By similarity). Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP binding (By similarity). Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway (By similarity). Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (By similarity). May act as a regulator of F-actin dynamics (By similarity). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Modulates RNA polymerase II-dependent transcription (By similarity).By similarity

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-6 (MYH6).Curated
Originally predicted to contain a coiled coil domain but generally accepted to contain a stable SAH domain instead.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi151 – 158ATPSequence 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

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 processEndocytosis, Hearing, Protein transport, Transport
LigandATP-binding, Nucleotide-binding

<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%5Fand%5Ftaxonomy%5Fsection">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:
Unconventional myosin-VI
Alternative name(s):
Unconventional myosin-6
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:MYO6
Synonyms:CMY6
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiGallus gallus (Chicken)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9031 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000539 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Coated pit, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Nucleus

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1088T → A: No effect on binding to OPTN; when associated with A-1091. 1 Publication1
Mutagenesisi1088T → E: Abolishes binding to OPTN; when associated with E-1091. 1 Publication1
Mutagenesisi1091T → A: No effect on binding to OPTN; when associated with A-1088. 1 Publication1
Mutagenesisi1091T → E: Abolishes binding to OPTN; when associated with E-1088. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002717471 – 1276Unconventional myosin-VIAdd BLAST1276

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 residuei405PhosphothreonineBy similarity1
Modified residuei1088Phosphothreonine1 Publication1
Modified residuei1091Phosphothreonine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 in the motor domain, induced by EGF, results in translocation of MYO6 from the cell surface to membrane ruffles. Phosphorylated in vitro by p21-activated kinase (PAK).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q9I8D1

PRoteomics IDEntifications database

More...
PRIDEi
Q9I8D1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9I8D1

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; dimerization seems to implicate the unfolding of the three-helix bundle region creating an additional calmodulin binding site, and cargo binding (By similarity). Able to function as a monomer under specific conditions in vitro (By similarity).

Forms a complex with CFTR and DAB2 in the apical membrane of epithelial cells (By similarity). Binding to calmodulin through a unique insert, not found in other myosins, located in the neck region between the motor domain and the IQ domain appears to contribute to the directionality reversal (By similarity). This interaction occurs only if the C-terminal lobe of calmodulin is occupied by calcium (By similarity). Interaction with F-actin/ACTN1 occurs only at the apical brush border domain of the proximal tubule cells (By similarity).

Interacts with DAB2 (By similarity). In vitro, the C-terminal globular tail binds a C-terminal region of DAB2 (By similarity).

Interacts with CFTR (By similarity).

Interacts with OPTN (PubMed:15837803).

Interacts with CABP5 (By similarity).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q9I8D1, 4 interactors

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000025573

<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

3D structure databases

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

More...
SMRi
Q9I8D1

Database of comparative protein structure models

More...
ModBasei
Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini2 – 53Myosin N-terminal SH3-likePROSITE-ProRule annotationAdd BLAST52
Domaini57 – 771Myosin motorPROSITE-ProRule annotationAdd BLAST715
Domaini813 – 842IQPROSITE-ProRule annotationAdd BLAST30

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>Regioni273 – 317Responsible for slow ATPase activityBy similarityAdd BLAST45
Regioni665 – 672Actin-bindingSequence analysis8
Regioni782 – 810Required for binding calmodulinBy similarityAdd BLAST29
Regioni835 – 916Three-helix bundleBy similarityAdd BLAST82
Regioni917 – 984SAHBy similarityAdd BLAST68
Regioni1107 – 1109Interaction with OPTN1 Publication3

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 biasi920 – 1027Glu-richAdd BLAST108

<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

Divided into three regions: a N-terminal motor (head) domain, followed by a neck domain consisting of a calmodulin-binding linker domain and a single IQ motif, and a C-terminal tail region with a three-helix bundle region, a SAH domain and a unique globular domain required for interaction with other proteins such as cargo-binding.By similarity
The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds (By similarity). Its contribution to the mechanism confering the myosin movement on actin filaments is debated (By similarity).By similarity

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0163 Eukaryota
COG5022 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9I8D1

KEGG Orthology (KO)

More...
KOi
K10358

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9I8D1

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01382 MYSc_Myo6, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.30.360, 1 hit
3.40.850.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000048 IQ_motif_EF-hand-BS
IPR036961 Kinesin_motor_dom_sf
IPR032412 Myosin-VI_CBD
IPR001609 Myosin_head_motor_dom
IPR004009 Myosin_N
IPR008989 Myosin_S1_N
IPR036114 MYSc_Myo6
IPR027417 P-loop_NTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16521 Myosin-VI_CBD, 1 hit
PF00063 Myosin_head, 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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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%5Flength">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>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9I8D1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEDGKPVWAP HPTDGFQMGM IVDIGTDYLT IEPLNQKGKT FQAAINQVFP
60 70 80 90 100
AEEDSKKDVE DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY
110 120 130 140 150
FDIPKFYSSD AIKKYQGRSL GTLPPHVFAI ADKAYRDMKV LKMSQSIIVS
160 170 180 190 200
GESGAGKTEN TKFVLRYLTE SYGTGQDIDD RIVEANPLLE AFGNAKTIRN
210 220 230 240 250
NNSSRFGKFV EIHFNEKNSV VGGFVSHYLL EKSRICVQGK EERNYHIFYR
260 270 280 290 300
LCAGAPEDIR EKLYLSSPDS FRYLNRGCTR YFATKETDKQ ILQNRKSPEY
310 320 330 340 350
LKAGSLKDPL LDDHGDFNRM CTAMKKIGLD DAEKLDLFRV VAGVLHLGNI
360 370 380 390 400
DFEEAGSTSG GCTLKAQSQP ALECCAALLG LDEEDLRVSL TTRVMLTTAG
410 420 430 440 450
GAKGTVIKVP LKVEQANNAR DALAKTVYSH LFDHVVNRVN QCFPFETSSF
460 470 480 490 500
FIGVLDIAGF EYFEHNSFEQ FCINYCNEKL QQFFNERILK EEQELYQKEG
510 520 530 540 550
LGVNEVRYVD NQDCIDLIEA KLIGVLDILD EENRLPQPSD QHFTSVVHQK
560 570 580 590 600
HKDHFRLSIP RKSKLAVHRN VRDDEGFIIR HFAGAVCYET TQFVEKNNDA
610 620 630 640 650
LHMSLESLIC ESKDKFVRQL FESNTNNNKD PKQKAGKLSF ISVGNKFKTQ
660 670 680 690 700
LNLLLEKLHS TGSSFIRCIF PNLKMTSHHF EGGQILSQLQ CSGMVSVLDL
710 720 730 740 750
MQGGFPSRAS FHELYNMYKK YLPEKLARLD PRLFCKALFK ALGLNEIDYK
760 770 780 790 800
FGLTKVFFRP GKFAEFDQIM KSDPDHLAEL VKRVNHWLIC SRWKKVQWCS
810 820 830 840 850
LSVIKLKNKI KYRASACIKI QKTIRMWLCK RKHKPRIDGL IKVRTLKKRL
860 870 880 890 900
DKFNEVVSAL KEGKAETSKQ IKELEYSIDA SMTKIKTTMM TREQIMKEYD
910 920 930 940 950
ALVRSSEQLL SALQKKKQQE EEAERLRRIQ EEMEKERKRR EEEEKRRRKE
960 970 980 990 1000
EEERRLKSEI EAKRKQEEEE RKKREEEEKR IQAEIEAQLA REREEETQHQ
1010 1020 1030 1040 1050
AILEQERRDR ELAMRIAQTG AELSTEETKL DVGLCRANGT KLQMTAEQMA
1060 1070 1080 1090 1100
KEMSEMLSRG PAVQATKAAA GAKKHDLSKW KYAELRDTIN TSCDIELLAA
1110 1120 1130 1140 1150
CREEFHRRLK VYHAWKSKNK KRNAETEQRA PKSVTDYAQQ NPTAQLPMRQ
1160 1170 1180 1190 1200
QEIEINRQQR YFRIPFIRPM DQYKDPQNKK KGWWYAHFDG PWIARQMELH
1210 1220 1230 1240 1250
PDKAPILLVA GKDDMDMCEL NLEETGLTRK RGAEILPRQF EEIWERCGGI
1260 1270
QYLQNAIESR QARPTYATAM LQNLLK
Length:1,276
Mass (Da):147,604
Last modified:October 1, 2000 - 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:i5F6AEE43A6FB260F
GO
Isoform 2 (identifier: Q9I8D1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1036-1058: Missing.

Show »
Length:1,253
Mass (Da):145,036
Checksum:iFDCA2D6B56BFB4D3
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0223311036 – 1058Missing in isoform 2. 1 PublicationAdd BLAST23

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
AJ278608 mRNA Translation: CAB96536.1

NCBI Reference Sequences

More...
RefSeqi
NP_990066.1, NM_204735.1 [Q9I8D1-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
395487

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gga:395487

Keywords - Coding sequence diversityi

Alternative splicing

<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
AJ278608 mRNA Translation: CAB96536.1
RefSeqiNP_990066.1, NM_204735.1 [Q9I8D1-1]

3D structure databases

SMRiQ9I8D1
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ9I8D1, 4 interactors
STRINGi9031.ENSGALP00000025573

PTM databases

iPTMnetiQ9I8D1

Proteomic databases

PaxDbiQ9I8D1
PRIDEiQ9I8D1

Genome annotation databases

GeneIDi395487
KEGGigga:395487

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4646

Phylogenomic databases

eggNOGiKOG0163 Eukaryota
COG5022 LUCA
InParanoidiQ9I8D1
KOiK10358
PhylomeDBiQ9I8D1

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9I8D1

Family and domain databases

CDDicd01382 MYSc_Myo6, 1 hit
Gene3Di2.30.30.360, 1 hit
3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR000048 IQ_motif_EF-hand-BS
IPR036961 Kinesin_motor_dom_sf
IPR032412 Myosin-VI_CBD
IPR001609 Myosin_head_motor_dom
IPR004009 Myosin_N
IPR008989 Myosin_S1_N
IPR036114 MYSc_Myo6
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF16521 Myosin-VI_CBD, 1 hit
PF00063 Myosin_head, 1 hit
PRINTSiPR00193 MYOSINHEAVY
SMARTiView protein in SMART
SM00242 MYSc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
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
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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 nameiMYO6_CHICK
<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: Q9I8D1
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 1, 2000
Last modified: June 17, 2020
This is version 116 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 programChordata 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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