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Q9Y4I1

- MYO5A_HUMAN

UniProt

Q9Y4I1 - MYO5A_HUMAN

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Protein

Unconventional myosin-Va

Gene

MYO5A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
  5. Rab GTPase 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. post-Golgi vesicle-mediated transport Source: UniProtKB
  17. protein localization to plasma membrane Source: UniProtKB
  18. protein transport Source: UniProtKB-KW
  19. regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: Ensembl
  20. secretory granule localization Source: Ensembl
  21. synapse organization Source: Ensembl
  22. synaptic transmission Source: Ensembl
  23. transport Source: UniProtKB
  24. vesicle-mediated transport Source: UniProtKB
  25. vesicle transport along actin filament Source: UniProtKB
  26. visual perception Source: Ensembl
Complete GO annotation...

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. cytosol Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. filopodium tip Source: UniProtKB
  6. Golgi apparatus Source: Ensembl
  7. growth cone Source: UniProtKB
  8. insulin-responsive compartment Source: UniProtKB
  9. intermediate filament Source: Ensembl
  10. melanosome Source: Ensembl
  11. membrane Source: UniProtKB
  12. microtubule plus-end Source: Ensembl
  13. myosin complex Source: UniProtKB-KW
  14. neuronal cell body Source: Ensembl
  15. neuron projection Source: UniProtKB
  16. photoreceptor outer segment Source: Ensembl
  17. ruffle Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9Y4I1.
CleanExiHS_MYO5A.
ExpressionAtlasiQ9Y4I1. baseline and differential.
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. 22 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, 840-883, 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.
GeneTreeiENSGT00760000119299.
HOVERGENiHBG052556.
InParanoidiQ9Y4I1.
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) [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

        10         20         30         40         50
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY
60 70 80 90 100
HLDPKTKELP HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY
110 120 130 140 150
TYCGIVLVAI NPYEQLPIYG EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM
160 170 180 190 200
ARDERNQSII VSGESGAGKT VSAKYAMRYF ATVSGSASEA NVEEKVLASN
210 220 230 240 250
PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR TYLLEKSRVV
260 270 280 290 300
FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADNFNYTKQ GGSPVIEGVD
310 320 330 340 350
DAKEMAHTRQ ACTLLGISES HQMGIFRILA GILHLGNVGF TSRDADSCTI
360 370 380 390 400
PPKHEPLCIF CELMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR
410 420 430 440 450
DALAKHIYAK LFNWIVDNVN QALHSAVKQH SFIGVLDIYG FETFEINSFE
460 470 480 490 500
QFCINYANEK LQQQFNMHVF KLEQEEYMKE QIPWTLIDFY DNQPCINLIE
510 520 530 540 550
SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK PRLSNKAFII
560 570 580 590 600
QHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS
610 620 630 640 650
PTSATSSGRT PLTRTPAKPT KGRPGQMAKE HKKTVGHQFR NSLHLLMETL
660 670 680 690 700
NATTPHYVRC IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR
710 720 730 740 750
WTYQEFFSRY RVLMKQKDVL SDRKQTCKNV LEKLILDKDK YQFGKTKIFF
760 770 780 790 800
RAGQVAYLEK LRADKLRAAC IRIQKTIRGW LLRKKYLRMR KAAITMQRYV
810 820 830 840 850
RGYQARCYAK FLRRTKAATI IQKYWRMYVV RRRYKIRRAA TIVLQSYLRG
860 870 880 890 900
FLARNRYRKI LREHKAVIIQ KRVRGWLART HYKRSMHAII YLQCCFRRMM
910 920 930 940 950
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLVEKL
960 970 980 990 1000
TNLEGIYNSE TEKLRSDLER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE
1010 1020 1030 1040 1050
QTRSEKKCIE EHADRYKQET EQLVSNLKEE NTLLKQEKEA LNHRIVQQAK
1060 1070 1080 1090 1100
EMTETMEKKL VEETKQLELD LNDERLRYQN LLNEFSRLEE RYDDLKEEMT
1110 1120 1130 1140 1150
LMVHVPKPGH KRTDSTHSSN ESEYIFSSEI AEMEDIPSRT EEPSEKKVPL
1160 1170 1180 1190 1200
DMSLFLKLQK RVTELEQEKQ VMQDELDRKE EQVLRSKAKE EERPQIRGAE
1210 1220 1230 1240 1250
LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME
1260 1270 1280 1290 1300
QLTSVSEELD VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ
1310 1320 1330 1340 1350
KMKDKGEIAQ AYIGLKETNR SSALDYHELN EDGELWLVYE GLKQANRLLE
1360 1370 1380 1390 1400
SQLQSQKRSH ENEAEALRGE IQSLKEENNR QQQLLAQNLQ LPPEARIEAS
1410 1420 1430 1440 1450
LQHEITRLTN ENLDLMEQLE KQDKTVRKLK KQLKVFAKKI GELEVGQMEN
1460 1470 1480 1490 1500
ISPGQIIDEP IRPVNIPRKE KDFQGMLEYK KEDEQKLVKN LILELKPRGV
1510 1520 1530 1540 1550
AVNLIPGLPA YILFMCVRHA DYLNDDQKVR SLLTSTINSI KKVLKKRGDD
1560 1570 1580 1590 1600
FETVSFWLSN TCRFLHCLKQ YSGEEGFMKH NTSRQNEHCL TNFDLAEYRQ
1610 1620 1630 1640 1650
VLSDLAIQIY QQLVRVLENI LQPMIVSGML EHETIQGVSG VKPTGLRKRT
1660 1670 1680 1690 1700
SSIADEGTYT LDSILRQLNS FHSVMCQHGM DPELIKQVVK QMFYIIGAIT
1710 1720 1730 1740 1750
LNNLLLRKDM CSWSKGMQIR YNVSQLEEWL RDKNLMNSGA KETLEPLIQA
1760 1770 1780 1790 1800
AQLLQVKKKT DDDAEAICSM CNALTTAQIV KVLNLYTPVN EFEERVSVSF
1810 1820 1830 1840 1850
IRTIQMRLRD RKDSPQLLMD AKHIFPVTFP FNPSSLALET IQIPASLGLG

FISRV
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, 840-883, 1473-1855.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110728. 22 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.
GeneTreei ENSGT00760000119299.
HOVERGENi HBG052556.
InParanoidi Q9Y4I1.
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

Bgeei Q9Y4I1.
CleanExi HS_MYO5A.
ExpressionAtlasi Q9Y4I1. baseline and differential.
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 ]
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Publicationsi

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  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 29, 2014
This is version 143 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

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