Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y4I1 (MYO5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-Va
Alternative name(s):
Dilute myosin heavy chain, non-muscle
Myosin heavy chain 12
Myosin-12
Myoxin
Gene names
Name:MYO5A
Synonyms:MYH12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1855 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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. Ref.9 Ref.15

Tissue specificity

Detected in melanocytes.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Contains 1 dilute domain.

Contains 6 IQ domains.

Contains 1 myosin motor domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament-based movement

Non-traceable author statement Ref.8. Source: UniProtKB

anagen

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum localization

Inferred from electronic annotation. Source: Ensembl

exocytosis

Inferred from electronic annotation. Source: Ensembl

insulin secretion

Inferred from electronic annotation. Source: Ensembl

locomotion involved in locomotory behavior

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

melanin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

melanocyte differentiation

Inferred from electronic annotation. Source: Ensembl

melanosome transport

Inferred from electronic annotation. Source: Ensembl

membrane organization

Traceable author statement. Source: Reactome

myelination

Inferred from electronic annotation. Source: Ensembl

odontogenesis

Inferred from electronic annotation. Source: Ensembl

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Inferred from electronic annotation. Source: Ensembl

secretory granule localization

Inferred from electronic annotation. Source: Ensembl

synapse organization

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Inferred from electronic annotation. Source: Ensembl

transport

Non-traceable author statement PubMed 11980908. Source: UniProtKB

vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

actomyosin

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 9852149. Source: UniProtKB

growth cone

Non-traceable author statement PubMed 10391919. Source: UniProtKB

insulin-responsive compartment

Inferred from sequence or structural similarity. Source: UniProtKB

intermediate filament

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: Ensembl

microtubule plus-end

Inferred from electronic annotation. Source: Ensembl

myosin complex

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Non-traceable author statement PubMed 10391919. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

photoreceptor outer segment

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from direct assay PubMed 9852149. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

microfilament motor activity

Non-traceable author statement Ref.8. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y4I1-1)

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.
Isoform 2 (identifier: Q9Y4I1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1321-1347: Missing.
Isoform 3 (identifier: Q9Y4I1-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 18551854Unconventional myosin-Va
PRO_0000123456

Regions

Domain69 – 763695Myosin motor
Domain766 – 78823IQ 1
Domain789 – 81830IQ 2
Domain814 – 83623IQ 3
Domain837 – 86125IQ 4
Domain862 – 88322IQ 5
Domain885 – 91430IQ 6
Domain1534 – 1810277Dilute
Nucleotide binding163 – 1708ATP Potential
Region643 – 66523Actin-binding Potential
Coiled coil914 – 1237324 Potential
Coiled coil1338 – 1445108 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.16
Modified residue6001Phosphoserine By similarity
Modified residue10321Phosphothreonine By similarity
Modified residue14521Phosphoserine Ref.13
Modified residue17601Phosphothreonine Potential

Natural variations

Alternative sequence1321 – 134727Missing in isoform 2.
VSP_003351
Alternative sequence14131L → LYFEELYADDPKKYQSYRIS LYKRMI in isoform 3.
VSP_003352
Natural variant6271M → T.
Corresponds to variant rs16964944 [ dbSNP | Ensembl ].
VAR_056180
Natural variant12461R → C. Ref.2 Ref.17
Corresponds to variant rs1058219 [ dbSNP | Ensembl ].
VAR_010645
Natural variant16731S → L.
Corresponds to variant rs9282796 [ dbSNP | Ensembl ].
VAR_056181

Experimental info

Sequence conflict1981A → T in CAA69035. Ref.1
Sequence conflict1981A → T in CAA69036. Ref.1
Sequence conflict1981A → T in AAD00702. Ref.2
Sequence conflict3621E → D in CAA69035. Ref.1
Sequence conflict3621E → D in CAA69036. Ref.1
Sequence conflict3621E → D in AAD00702. Ref.2
Sequence conflict6681F → L in CAA69035. Ref.1
Sequence conflict6681F → L in CAA69036. Ref.1
Sequence conflict8331Missing in CAA80533. Ref.5
Sequence conflict8631E → G in CAA69035. Ref.1
Sequence conflict8631E → G in CAA69036. Ref.1
Sequence conflict9221H → R in CAA69035. Ref.1
Sequence conflict9221H → R in CAA69036. Ref.1
Sequence conflict10611V → L in AAB33211. Ref.6
Sequence conflict10891E → Q in CAA80533. Ref.5
Sequence conflict11771D → E in AAB33211. Ref.6
Sequence conflict1465 – 147713NIPRK…FQGML → SVLCACCVSVTVR in CAA80533. Ref.5
Sequence conflict14711K → N in AAB33211. Ref.6
Sequence conflict14841E → D in AAB33211. Ref.6

Secondary structure

.................................................... 1855
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 78FD3B1D08D90A0A

FASTA1,855215,405
        10         20         30         40         50         60 
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY HLDPKTKELP 

        70         80         90        100        110        120 
HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY TYCGIVLVAI NPYEQLPIYG 

       130        140        150        160        170        180 
EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRYF 

       190        200        210        220        230        240 
ATVSGSASEA NVEEKVLASN PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR 

       250        260        270        280        290        300 
TYLLEKSRVV FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADNFNYTKQ GGSPVIEGVD 

       310        320        330        340        350        360 
DAKEMAHTRQ ACTLLGISES HQMGIFRILA GILHLGNVGF TSRDADSCTI PPKHEPLCIF 

       370        380        390        400        410        420 
CELMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR DALAKHIYAK LFNWIVDNVN 

       430        440        450        460        470        480 
QALHSAVKQH SFIGVLDIYG FETFEINSFE QFCINYANEK LQQQFNMHVF KLEQEEYMKE 

       490        500        510        520        530        540 
QIPWTLIDFY DNQPCINLIE SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK 

       550        560        570        580        590        600 
PRLSNKAFII QHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS 

       610        620        630        640        650        660 
PTSATSSGRT PLTRTPAKPT KGRPGQMAKE HKKTVGHQFR NSLHLLMETL NATTPHYVRC 

       670        680        690        700        710        720 
IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL 

       730        740        750        760        770        780 
SDRKQTCKNV LEKLILDKDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRGW 

       790        800        810        820        830        840 
LLRKKYLRMR KAAITMQRYV RGYQARCYAK FLRRTKAATI IQKYWRMYVV RRRYKIRRAA 

       850        860        870        880        890        900 
TIVLQSYLRG FLARNRYRKI LREHKAVIIQ KRVRGWLART HYKRSMHAII YLQCCFRRMM 

       910        920        930        940        950        960 
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLVEKL TNLEGIYNSE 

       970        980        990       1000       1010       1020 
TEKLRSDLER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE QTRSEKKCIE EHADRYKQET 

      1030       1040       1050       1060       1070       1080 
EQLVSNLKEE NTLLKQEKEA LNHRIVQQAK EMTETMEKKL VEETKQLELD LNDERLRYQN 

      1090       1100       1110       1120       1130       1140 
LLNEFSRLEE RYDDLKEEMT LMVHVPKPGH KRTDSTHSSN ESEYIFSSEI AEMEDIPSRT 

      1150       1160       1170       1180       1190       1200 
EEPSEKKVPL DMSLFLKLQK RVTELEQEKQ VMQDELDRKE EQVLRSKAKE EERPQIRGAE 

      1210       1220       1230       1240       1250       1260 
LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME QLTSVSEELD 

      1270       1280       1290       1300       1310       1320 
VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ KMKDKGEIAQ AYIGLKETNR 

      1330       1340       1350       1360       1370       1380 
SSALDYHELN EDGELWLVYE GLKQANRLLE SQLQSQKRSH ENEAEALRGE IQSLKEENNR 

      1390       1400       1410       1420       1430       1440 
QQQLLAQNLQ LPPEARIEAS LQHEITRLTN ENLDLMEQLE KQDKTVRKLK KQLKVFAKKI 

      1450       1460       1470       1480       1490       1500 
GELEVGQMEN ISPGQIIDEP IRPVNIPRKE KDFQGMLEYK KEDEQKLVKN LILELKPRGV 

      1510       1520       1530       1540       1550       1560 
AVNLIPGLPA YILFMCVRHA DYLNDDQKVR SLLTSTINSI KKVLKKRGDD FETVSFWLSN 

      1570       1580       1590       1600       1610       1620 
TCRFLHCLKQ YSGEEGFMKH NTSRQNEHCL TNFDLAEYRQ VLSDLAIQIY QQLVRVLENI 

      1630       1640       1650       1660       1670       1680 
LQPMIVSGML EHETIQGVSG VKPTGLRKRT SSIADEGTYT LDSILRQLNS FHSVMCQHGM 

      1690       1700       1710       1720       1730       1740 
DPELIKQVVK QMFYIIGAIT LNNLLLRKDM CSWSKGMQIR YNVSQLEEWL RDKNLMNSGA 

      1750       1760       1770       1780       1790       1800 
KETLEPLIQA AQLLQVKKKT DDDAEAICSM CNALTTAQIV KVLNLYTPVN EFEERVSVSF 

      1810       1820       1830       1840       1850 
IRTIQMRLRD RKDSPQLLMD AKHIFPVTFP FNPSSLALET IQIPASLGLG FISRV 

« Hide

Isoform 2 [UniParc].

Checksum: 6C1F609CE0FAC368
Show »

FASTA1,828212,273
Isoform 3 [UniParc].

Checksum: 86CCDF8124408640
Show »

FASTA1,880218,608

References

« Hide 'large scale' references
[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]Erratum
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. 23:373-373(1999)
[4]"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. expand/collapse author list , 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].
[5]"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.
[6]"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.
[7]"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).
[8]"Myosin-V is a processive actin-based motor."
Mehta A.D., Rock R.S., Rief M., Spudich J.A., Mooseker M.S., Cheney R.E.
Nature 400:590-593(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"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.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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.
[13]"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.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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.
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[17]"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.
[18]"Two genes are responsible for Griscelli syndrome at the same 15q21 locus."
Pastural E., Ersoy F., Yalman N., Wulffraat N., Grillo E., Ozkinay F., Tezcan I., Gedikoglu G., Philippe N., Fischer A., de Saint Basile G.
Genomics 63:299-306(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GS1.
[19]"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.
[20]Erratum
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. 71:1007-1007(2002)
[21]"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.
+Additional computationally mapped references.

Web resources

MYO5Abase

MYO5A mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS42037.1. [Q9Y4I1-1]
CCDS45262.1. [Q9Y4I1-2]
PIRA53016.
A59254.
B59254.
I52966.
RefSeqNP_000250.3. NM_000259.3.
XP_005254454.1. XM_005254397.2. [Q9Y4I1-3]
UniGeneHs.21213.
Hs.596221.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4J5LX-ray2.20A/B1448-1855[»]
4LLIX-ray2.20A/B1467-1855[»]
4LX1X-ray1.87A/B1464-1855[»]
4LX2X-ray1.50A1464-1855[»]
ProteinModelPortalQ9Y4I1.
SMRQ9Y4I1. Positions 2-819, 860-900, 1473-1855.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110728. 18 interactions.
IntActQ9Y4I1. 4 interactions.
MINTMINT-3388025.
STRING9606.ENSP00000382177.

PTM databases

PhosphoSiteQ9Y4I1.

Polymorphism databases

DMDM296439234.

Proteomic databases

MaxQBQ9Y4I1.
PaxDbQ9Y4I1.
PRIDEQ9Y4I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356338; ENSP00000348693; ENSG00000197535. [Q9Y4I1-2]
ENST00000399231; ENSP00000382177; ENSG00000197535. [Q9Y4I1-1]
GeneID4644.
KEGGhsa:4644.
UCSCuc002aby.2. human. [Q9Y4I1-1]
uc010uge.1. human. [Q9Y4I1-2]

Organism-specific databases

CTD4644.
GeneCardsGC15M052599.
HGNCHGNC:7602. MYO5A.
HPAHPA001356.
MIM160777. gene.
214450. phenotype.
256710. phenotype.
609227. phenotype.
neXtProtNX_Q9Y4I1.
Orphanet79476. Griscelli disease type 1.
79478. Griscelli disease type 3.
33445. Neuroectodermal melanolysosomal disease.
PharmGKBPA31407.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOVERGENHBG052556.
KOK10357.
OrthoDBEOG7PK8XT.
PhylomeDBQ9Y4I1.
TreeFamTF328771.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9Y4I1.
BgeeQ9Y4I1.
CleanExHS_MYO5A.
GenevestigatorQ9Y4I1.

Family and domain databases

InterProIPR018444. Dil_domain.
IPR002710. Dilute.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01843. DIL. 1 hit.
PF00612. IQ. 6 hits.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 6 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
PROSITEPS51126. DILUTE. 1 hit.
PS50096. IQ. 6 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO5A. human.
GeneWikiMYO5A.
GenomeRNAi4644.
NextBio17896.
PROQ9Y4I1.
SOURCESearch...

Entry information

Entry nameMYO5A_HUMAN
AccessionPrimary (citable) accession number: Q9Y4I1
Secondary accession number(s): A8MZC5 expand/collapse secondary AC list , O60653, Q07902, Q16249, Q9UE30, Q9UE31
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM