Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y4I1

- MYO5A_HUMAN

UniProt

Q9Y4I1 - MYO5A_HUMAN

Protein

Unconventional myosin-Va

Gene

MYO5A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi163 – 1708ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: Ensembl
    3. microfilament motor activity Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. actin filament-based movement Source: UniProtKB
    2. anagen Source: Ensembl
    3. cellular protein metabolic process Source: Reactome
    4. cellular response to insulin stimulus Source: UniProtKB
    5. endoplasmic reticulum localization Source: Ensembl
    6. exocytosis Source: Ensembl
    7. insulin secretion Source: Ensembl
    8. locomotion involved in locomotory behavior Source: Ensembl
    9. long-chain fatty acid biosynthetic process Source: Ensembl
    10. melanin biosynthetic process Source: Ensembl
    11. melanocyte differentiation Source: Ensembl
    12. melanosome transport Source: Ensembl
    13. membrane organization Source: Reactome
    14. myelination Source: Ensembl
    15. odontogenesis Source: Ensembl
    16. protein localization to plasma membrane Source: UniProtKB
    17. protein transport Source: UniProtKB-KW
    18. regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: Ensembl
    19. secretory granule localization Source: Ensembl
    20. synapse organization Source: Ensembl
    21. synaptic transmission Source: Ensembl
    22. transport Source: UniProtKB
    23. vesicle-mediated transport Source: UniProtKB
    24. visual perception Source: Ensembl

    Keywords - Molecular functioni

    Motor protein, Myosin

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_15550. Insulin processing.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Unconventional myosin-Va
    Alternative name(s):
    Dilute myosin heavy chain, non-muscle
    Myosin heavy chain 12
    Myosin-12
    Myoxin
    Gene namesi
    Name:MYO5A
    Synonyms:MYH12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:7602. MYO5A.

    Subcellular locationi

    GO - Cellular componenti

    1. actomyosin Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. Golgi apparatus Source: Ensembl
    4. growth cone Source: UniProtKB
    5. insulin-responsive compartment Source: UniProtKB
    6. intermediate filament Source: Ensembl
    7. melanosome Source: Ensembl
    8. membrane Source: UniProtKB
    9. microtubule plus-end Source: Ensembl
    10. myosin complex Source: UniProtKB-KW
    11. neuronal cell body Source: Ensembl
    12. neuron projection Source: UniProtKB
    13. photoreceptor outer segment Source: Ensembl
    14. ruffle Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Griscelli syndrome 1 (GS1) [MIM:214450]: Rare autosomal recessive disorder that results in pigmentary dilution of the skin and hair, the presence of large clumps of pigment in hair shafts, silvery-gray hair and accumulation of melanosomes in melanocytes. GS1 patients show developmental delay, hypotonia and mental retardation, without apparent immune abnormalities.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Griscelli syndrome 3 (GS3) [MIM:609227]: Rare autosomal recessive disorder characterized by pigmentary dilution of the skin and hair, the presence of large clumps of pigment in hair shafts, and an accumulation of melanosomes in melanocytes, without other clinical manifestations.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Elejalde syndrome (ELEJAS) [MIM:256710]: Autosomal recessive condition characterized by skin hypopigmentation, the presence of large clumps of pigment in hair shafts, silvery-gray hair, accumulation of melanosomes in melanocytes and primary neurological abnormalities. Elejalde syndrome may be the same entity as Griscelli syndrome type I.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi214450. phenotype.
    256710. phenotype.
    609227. phenotype.
    Orphaneti79476. Griscelli disease type 1.
    79478. Griscelli disease type 3.
    33445. Neuroectodermal melanolysosomal disease.
    PharmGKBiPA31407.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 18551854Unconventional myosin-VaPRO_0000123456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei600 – 6001PhosphoserineBy similarity
    Modified residuei1032 – 10321PhosphothreonineBy similarity
    Modified residuei1452 – 14521Phosphoserine1 Publication
    Modified residuei1760 – 17601PhosphothreonineSequence Analysis

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y4I1.
    PaxDbiQ9Y4I1.
    PRIDEiQ9Y4I1.

    PTM databases

    PhosphoSiteiQ9Y4I1.

    Expressioni

    Tissue specificityi

    Detected in melanocytes.

    Gene expression databases

    ArrayExpressiQ9Y4I1.
    BgeeiQ9Y4I1.
    CleanExiHS_MYO5A.
    GenevestigatoriQ9Y4I1.

    Organism-specific databases

    HPAiHPA001356.

    Interactioni

    Subunit structurei

    May be a homodimer, which associates with multiple calmodulin or myosin light chains. Interacts with SYTL4, MLPH and MYRIP. Interacts with RIPL2, the interaction is required for its role in dendrite formation By similarity. Interacts with RAB10; mediates the transport to the plasma membrane of SLC2A4/GLUT4 storage vesicles.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi110728. 18 interactions.
    IntActiQ9Y4I1. 4 interactions.
    MINTiMINT-3388025.
    STRINGi9606.ENSP00000382177.

    Structurei

    Secondary structure

    1
    1855
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1475 – 14784
    Helixi1481 – 14833
    Helixi1484 – 14918
    Turni1492 – 14943
    Helixi1500 – 15023
    Turni1505 – 15073
    Helixi1508 – 152215
    Helixi1526 – 154722
    Helixi1551 – 157020
    Helixi1575 – 15773
    Helixi1583 – 15864
    Beta strandi1591 – 15944
    Helixi1596 – 162126
    Helixi1622 – 16243
    Helixi1625 – 16295
    Helixi1661 – 167717
    Helixi1682 – 170625
    Beta strandi1708 – 17103
    Helixi1713 – 173220
    Helixi1740 – 17434
    Helixi1745 – 175511
    Helixi1761 – 177010
    Helixi1776 – 178510
    Turni1790 – 17923
    Helixi1798 – 180710
    Turni1808 – 18103
    Helixi1838 – 18403
    Helixi1845 – 18473
    Beta strandi1852 – 18554

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4J5LX-ray2.20A/B1448-1855[»]
    4LLIX-ray2.20A/B1467-1855[»]
    4LX1X-ray1.87A/B1464-1855[»]
    4LX2X-ray1.50A1464-1855[»]
    ProteinModelPortaliQ9Y4I1.
    SMRiQ9Y4I1. Positions 2-819, 860-900, 1473-1855.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini69 – 763695Myosin motorAdd
    BLAST
    Domaini766 – 78823IQ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini789 – 81830IQ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini814 – 83623IQ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini837 – 86125IQ 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini862 – 88322IQ 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini885 – 91430IQ 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1534 – 1810277DilutePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni643 – 66523Actin-bindingSequence AnalysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili914 – 1237324Sequence AnalysisAdd
    BLAST
    Coiled coili1338 – 1445108Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 dilute domain.PROSITE-ProRule annotation
    Contains 6 IQ domains.PROSITE-ProRule annotation
    Contains 1 myosin motor domain.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5022.
    HOVERGENiHBG052556.
    KOiK10357.
    OrthoDBiEOG7PK8XT.
    PhylomeDBiQ9Y4I1.
    TreeFamiTF328771.

    Family and domain databases

    InterProiIPR018444. Dil_domain.
    IPR002710. Dilute.
    IPR000048. IQ_motif_EF-hand-BS.
    IPR001609. Myosin_head_motor_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF01843. DIL. 1 hit.
    PF00612. IQ. 6 hits.
    PF00063. Myosin_head. 1 hit.
    [Graphical view]
    PRINTSiPR00193. MYOSINHEAVY.
    SMARTiSM00015. IQ. 6 hits.
    SM00242. MYSc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    PROSITEiPS51126. DILUTE. 1 hit.
    PS50096. IQ. 6 hits.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y4I1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' 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

    MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY     50
    HLDPKTKELP HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY 100
    TYCGIVLVAI NPYEQLPIYG EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM 150
    ARDERNQSII VSGESGAGKT VSAKYAMRYF ATVSGSASEA NVEEKVLASN 200
    PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR TYLLEKSRVV 250
    FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADNFNYTKQ GGSPVIEGVD 300
    DAKEMAHTRQ ACTLLGISES HQMGIFRILA GILHLGNVGF TSRDADSCTI 350
    PPKHEPLCIF CELMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR 400
    DALAKHIYAK LFNWIVDNVN QALHSAVKQH SFIGVLDIYG FETFEINSFE 450
    QFCINYANEK LQQQFNMHVF KLEQEEYMKE QIPWTLIDFY DNQPCINLIE 500
    SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK PRLSNKAFII 550
    QHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS 600
    PTSATSSGRT PLTRTPAKPT KGRPGQMAKE HKKTVGHQFR NSLHLLMETL 650
    NATTPHYVRC IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR 700
    WTYQEFFSRY RVLMKQKDVL SDRKQTCKNV LEKLILDKDK YQFGKTKIFF 750
    RAGQVAYLEK LRADKLRAAC IRIQKTIRGW LLRKKYLRMR KAAITMQRYV 800
    RGYQARCYAK FLRRTKAATI IQKYWRMYVV RRRYKIRRAA TIVLQSYLRG 850
    FLARNRYRKI LREHKAVIIQ KRVRGWLART HYKRSMHAII YLQCCFRRMM 900
    AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLVEKL 950
    TNLEGIYNSE TEKLRSDLER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE 1000
    QTRSEKKCIE EHADRYKQET EQLVSNLKEE NTLLKQEKEA LNHRIVQQAK 1050
    EMTETMEKKL VEETKQLELD LNDERLRYQN LLNEFSRLEE RYDDLKEEMT 1100
    LMVHVPKPGH KRTDSTHSSN ESEYIFSSEI AEMEDIPSRT EEPSEKKVPL 1150
    DMSLFLKLQK RVTELEQEKQ VMQDELDRKE EQVLRSKAKE EERPQIRGAE 1200
    LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME 1250
    QLTSVSEELD VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ 1300
    KMKDKGEIAQ AYIGLKETNR SSALDYHELN EDGELWLVYE GLKQANRLLE 1350
    SQLQSQKRSH ENEAEALRGE IQSLKEENNR QQQLLAQNLQ LPPEARIEAS 1400
    LQHEITRLTN ENLDLMEQLE KQDKTVRKLK KQLKVFAKKI GELEVGQMEN 1450
    ISPGQIIDEP IRPVNIPRKE KDFQGMLEYK KEDEQKLVKN LILELKPRGV 1500
    AVNLIPGLPA YILFMCVRHA DYLNDDQKVR SLLTSTINSI KKVLKKRGDD 1550
    FETVSFWLSN TCRFLHCLKQ YSGEEGFMKH NTSRQNEHCL TNFDLAEYRQ 1600
    VLSDLAIQIY QQLVRVLENI LQPMIVSGML EHETIQGVSG VKPTGLRKRT 1650
    SSIADEGTYT LDSILRQLNS FHSVMCQHGM DPELIKQVVK QMFYIIGAIT 1700
    LNNLLLRKDM CSWSKGMQIR YNVSQLEEWL RDKNLMNSGA KETLEPLIQA 1750
    AQLLQVKKKT DDDAEAICSM CNALTTAQIV KVLNLYTPVN EFEERVSVSF 1800
    IRTIQMRLRD RKDSPQLLMD AKHIFPVTFP FNPSSLALET IQIPASLGLG 1850
    FISRV 1855
    Length:1,855
    Mass (Da):215,405
    Last modified:May 18, 2010 - v2
    Checksum:i78FD3B1D08D90A0A
    GO
    Isoform 2 (identifier: Q9Y4I1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1321-1347: Missing.

    Show »
    Length:1,828
    Mass (Da):212,273
    Checksum:i6C1F609CE0FAC368
    GO
    Isoform 3 (identifier: Q9Y4I1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1413-1413: L → LYFEELYADDPKKYQSYRISLYKRMI

    Show »
    Length:1,880
    Mass (Da):218,608
    Checksum:i86CCDF8124408640
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti198 – 1981A → T in CAA69035. 1 PublicationCurated
    Sequence conflicti198 – 1981A → T in CAA69036. 1 PublicationCurated
    Sequence conflicti198 – 1981A → T in AAD00702. (PubMed:9207796)Curated
    Sequence conflicti362 – 3621E → D in CAA69035. 1 PublicationCurated
    Sequence conflicti362 – 3621E → D in CAA69036. 1 PublicationCurated
    Sequence conflicti362 – 3621E → D in AAD00702. (PubMed:9207796)Curated
    Sequence conflicti668 – 6681F → L in CAA69035. 1 PublicationCurated
    Sequence conflicti668 – 6681F → L in CAA69036. 1 PublicationCurated
    Sequence conflicti833 – 8331Missing in CAA80533. (PubMed:8188282)Curated
    Sequence conflicti863 – 8631E → G in CAA69035. 1 PublicationCurated
    Sequence conflicti863 – 8631E → G in CAA69036. 1 PublicationCurated
    Sequence conflicti922 – 9221H → R in CAA69035. 1 PublicationCurated
    Sequence conflicti922 – 9221H → R in CAA69036. 1 PublicationCurated
    Sequence conflicti1061 – 10611V → L in AAB33211. (PubMed:7835087)Curated
    Sequence conflicti1089 – 10891E → Q in CAA80533. (PubMed:8188282)Curated
    Sequence conflicti1177 – 11771D → E in AAB33211. (PubMed:7835087)Curated
    Sequence conflicti1465 – 147713NIPRK…FQGML → SVLCACCVSVTVR in CAA80533. (PubMed:8188282)CuratedAdd
    BLAST
    Sequence conflicti1471 – 14711K → N in AAB33211. (PubMed:7835087)Curated
    Sequence conflicti1484 – 14841E → D in AAB33211. (PubMed:7835087)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti627 – 6271M → T.
    Corresponds to variant rs16964944 [ dbSNP | Ensembl ].
    VAR_056180
    Natural varianti1246 – 12461R → C.2 Publications
    Corresponds to variant rs1058219 [ dbSNP | Ensembl ].
    VAR_010645
    Natural varianti1673 – 16731S → L.
    Corresponds to variant rs9282796 [ dbSNP | Ensembl ].
    VAR_056181

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1321 – 134727Missing in isoform 2. 3 PublicationsVSP_003351Add
    BLAST
    Alternative sequencei1413 – 14131L → LYFEELYADDPKKYQSYRIS LYKRMI in isoform 3. 1 PublicationVSP_003352

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07759 mRNA. Translation: CAA69035.1.
    Y07759 mRNA. Translation: CAA69036.1.
    U90942 mRNA. Translation: AAD00702.1.
    AC010674 Genomic DNA. No translation available.
    AC018902 Genomic DNA. No translation available.
    AC025917 Genomic DNA. No translation available.
    Z22957 mRNA. Translation: CAA80533.1.
    S74799 mRNA. Translation: AAB33211.1.
    AF055459 mRNA. Translation: AAC14188.1.
    CCDSiCCDS42037.1. [Q9Y4I1-1]
    CCDS45262.1. [Q9Y4I1-2]
    PIRiA53016.
    A59254.
    B59254.
    I52966.
    RefSeqiNP_000250.3. NM_000259.3.
    XP_005254454.1. XM_005254397.2. [Q9Y4I1-3]
    UniGeneiHs.21213.
    Hs.596221.

    Genome annotation databases

    EnsembliENST00000356338; ENSP00000348693; ENSG00000197535. [Q9Y4I1-2]
    ENST00000399231; ENSP00000382177; ENSG00000197535. [Q9Y4I1-1]
    GeneIDi4644.
    KEGGihsa:4644.
    UCSCiuc002aby.2. human. [Q9Y4I1-1]
    uc010uge.1. human. [Q9Y4I1-2]

    Polymorphism databases

    DMDMi296439234.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    MYO5Abase

    MYO5A mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07759 mRNA. Translation: CAA69035.1 .
    Y07759 mRNA. Translation: CAA69036.1 .
    U90942 mRNA. Translation: AAD00702.1 .
    AC010674 Genomic DNA. No translation available.
    AC018902 Genomic DNA. No translation available.
    AC025917 Genomic DNA. No translation available.
    Z22957 mRNA. Translation: CAA80533.1 .
    S74799 mRNA. Translation: AAB33211.1 .
    AF055459 mRNA. Translation: AAC14188.1 .
    CCDSi CCDS42037.1. [Q9Y4I1-1 ]
    CCDS45262.1. [Q9Y4I1-2 ]
    PIRi A53016.
    A59254.
    B59254.
    I52966.
    RefSeqi NP_000250.3. NM_000259.3.
    XP_005254454.1. XM_005254397.2. [Q9Y4I1-3 ]
    UniGenei Hs.21213.
    Hs.596221.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4J5L X-ray 2.20 A/B 1448-1855 [» ]
    4LLI X-ray 2.20 A/B 1467-1855 [» ]
    4LX1 X-ray 1.87 A/B 1464-1855 [» ]
    4LX2 X-ray 1.50 A 1464-1855 [» ]
    ProteinModelPortali Q9Y4I1.
    SMRi Q9Y4I1. Positions 2-819, 860-900, 1473-1855.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110728. 18 interactions.
    IntActi Q9Y4I1. 4 interactions.
    MINTi MINT-3388025.
    STRINGi 9606.ENSP00000382177.

    PTM databases

    PhosphoSitei Q9Y4I1.

    Polymorphism databases

    DMDMi 296439234.

    Proteomic databases

    MaxQBi Q9Y4I1.
    PaxDbi Q9Y4I1.
    PRIDEi Q9Y4I1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356338 ; ENSP00000348693 ; ENSG00000197535 . [Q9Y4I1-2 ]
    ENST00000399231 ; ENSP00000382177 ; ENSG00000197535 . [Q9Y4I1-1 ]
    GeneIDi 4644.
    KEGGi hsa:4644.
    UCSCi uc002aby.2. human. [Q9Y4I1-1 ]
    uc010uge.1. human. [Q9Y4I1-2 ]

    Organism-specific databases

    CTDi 4644.
    GeneCardsi GC15M052599.
    HGNCi HGNC:7602. MYO5A.
    HPAi HPA001356.
    MIMi 160777. gene.
    214450. phenotype.
    256710. phenotype.
    609227. phenotype.
    neXtProti NX_Q9Y4I1.
    Orphaneti 79476. Griscelli disease type 1.
    79478. Griscelli disease type 3.
    33445. Neuroectodermal melanolysosomal disease.
    PharmGKBi PA31407.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5022.
    HOVERGENi HBG052556.
    KOi K10357.
    OrthoDBi EOG7PK8XT.
    PhylomeDBi Q9Y4I1.
    TreeFami TF328771.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_15550. Insulin processing.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    ChiTaRSi MYO5A. human.
    GeneWikii MYO5A.
    GenomeRNAii 4644.
    NextBioi 17896.
    PROi Q9Y4I1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y4I1.
    Bgeei Q9Y4I1.
    CleanExi HS_MYO5A.
    Genevestigatori Q9Y4I1.

    Family and domain databases

    InterProi IPR018444. Dil_domain.
    IPR002710. Dilute.
    IPR000048. IQ_motif_EF-hand-BS.
    IPR001609. Myosin_head_motor_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF01843. DIL. 1 hit.
    PF00612. IQ. 6 hits.
    PF00063. Myosin_head. 1 hit.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    SMARTi SM00015. IQ. 6 hits.
    SM00242. MYSc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51126. DILUTE. 1 hit.
    PS50096. IQ. 6 hits.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete cDNA for human myosin heavy chain 12, a class V myosin."
      Meurers B.H., Zimmermann R., Vosberg H.P.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Skin.
    2. "Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene."
      Pastural E., Barrat F.J., Dufourcq-Lagelouse R., Certain S., Sanal O., Jabado N., Seger R., Griscelli C., Fischer A., de Saint Basile G.
      Nat. Genet. 16:289-292(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-1246.
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Cloning, analysis, and chromosomal localization of myoxin (MYH12), the human homologue to the mouse dilute gene."
      Engle L.J., Kennett R.H.
      Genomics 19:407-416(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 638-1477 (ISOFORM 2).
      Tissue: Fetal brain.
    5. "Cloning and regional assignment of the human myosin heavy chain 12 (MYH12) gene to chromosome band 15q21."
      Moore K.J., Testa J.R., Francke U., Milatovich A., Copeland N.G., Jenkins N.A.
      Cytogenet. Cell Genet. 69:53-58(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1061-1498 (ISOFORM 2).
      Tissue: Brain.
    6. "Inhibition of dendrite formation in melanocytes transiently transfected with antisense DNA to myosin V."
      Edgar A.J., Bennett J.P.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1358-1460 (ISOFORM 3).
    7. Cited for: FUNCTION.
    8. "Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions."
      Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T., Izumi T.
      FEBS Lett. 517:233-238(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLPH.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes."
      Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J.
      J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB10.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Arg-Cys substitution at codon 1246 of the human myosin Va gene is not associated with Griscelli syndrome."
      Lambert J., Naeyaert J.-M., De Paepe A., Van Coster R., Ferster A., Song M., Messiaen L.
      J. Invest. Dermatol. 114:731-733(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CYS-1246.
    17. Cited for: INVOLVEMENT IN GS1.
    18. "Evidence that Griscelli syndrome with neurological involvement is caused by mutations in RAB27A, not MYO5A."
      Anikster Y., Huizing M., Anderson P.D., Fitzpatrick D.L., Klar A., Gross-Kieselstein E., Berkun Y., Shazberg G., Gahl W.A., Hurvitz H.
      Am. J. Hum. Genet. 71:407-414(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN ELEJAS.
    19. "Griscelli syndrome restricted to hypopigmentation results from a melanophilin defect (GS3) or a MYO5A F-exon deletion (GS1)."
      Menasche G., Ho C.H., Sanal O., Feldmann J., Tezcan I., Ersoy F., Houdusse A., Fischer A., de Saint Basile G.
      J. Clin. Invest. 112:450-456(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN GS3.

    Entry informationi

    Entry nameiMYO5A_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4I1
    Secondary accession number(s): A8MZC5
    , O60653, Q07902, Q16249, Q9UE30, Q9UE31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3