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Protein

Unconventional myosin-XVIIIa

Gene

Myo18a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. May be involved in the maintenance of the stromal cell architectures required for cell to cell contact.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi498 – 5058ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-XVIIIa
Alternative name(s):
Molecule associated with JAK3 N-terminus
Short name:
MAJN
Myosin containing a PDZ domain
Gene namesi
Name:Myo18a
Synonyms:Myspdz
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2667185. Myo18a.

Subcellular locationi

Isoform 2 :
  • Cytoplasm

  • Note: Lacks the PDZ domain. Diffusely localized in the cytoplasm.

GO - Cellular componenti

  • actomyosin Source: MGI
  • brush border Source: UniProtKB
  • cytoskeleton Source: MGI
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  • Golgi apparatus Source: MGI
  • Golgi membrane Source: MGI
  • membrane Source: MGI
  • myosin complex Source: UniProtKB-KW
  • nucleoplasm Source: MGI
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi503 – 5042GK → SA: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20502050Unconventional myosin-XVIIIaPRO_0000123477Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei72 – 721PhosphoserineCombined sources
Modified residuei74 – 741PhosphoserineBy similarity
Modified residuei79 – 791PhosphothreonineBy similarity
Modified residuei83 – 831PhosphoserineCombined sources
Modified residuei98 – 981PhosphoserineBy similarity
Modified residuei99 – 991PhosphothreonineBy similarity
Modified residuei102 – 1021PhosphoserineCombined sources
Modified residuei103 – 1031PhosphoserineCombined sources
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei145 – 1451PhosphoserineBy similarity
Modified residuei157 – 1571PhosphoserineCombined sources
Modified residuei160 – 1601PhosphoserineCombined sources
Modified residuei164 – 1641PhosphoserineCombined sources
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei983 – 9831PhosphoserineCombined sources
Modified residuei1063 – 10631PhosphoserineBy similarity
Modified residuei1064 – 10641PhosphoserineBy similarity
Modified residuei1066 – 10661PhosphoserineBy similarity
Modified residuei1636 – 16361PhosphoserineBy similarity
Modified residuei1938 – 19381PhosphoserineBy similarity
Modified residuei1966 – 19661PhosphoserineCombined sources
Modified residuei1970 – 19701PhosphoserineBy similarity
Modified residuei1994 – 19941PhosphoserineCombined sources
Modified residuei1998 – 19981PhosphoserineBy similarity
Modified residuei2002 – 20021PhosphoserineBy similarity
Modified residuei2003 – 20031PhosphoserineBy similarity
Modified residuei2016 – 20161PhosphoserineCombined sources
Modified residuei2032 – 20321PhosphoserineCombined sources
Modified residuei2037 – 20371PhosphoserineCombined sources
Modified residuei2039 – 20391PhosphoserineCombined sources
Modified residuei2041 – 20411PhosphothreonineCombined sources
Isoform 6 (identifier: Q9JMH9-6)
Modified residuei340 – 3401PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on tyrosine upon CSF1R activation. Isoform 6 is phosphorylated on Ser-340.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9JMH9.
MaxQBiQ9JMH9.
PaxDbiQ9JMH9.
PeptideAtlasiQ9JMH9.
PRIDEiQ9JMH9.

PTM databases

iPTMnetiQ9JMH9.
PhosphoSiteiQ9JMH9.

Expressioni

Tissue specificityi

Isoform 1 is expressed ubiquitously. Isoform 2 is specifically expressed in most hematopoietic cells.

Gene expression databases

BgeeiQ9JMH9.
CleanExiMM_MYO18A.
ExpressionAtlasiQ9JMH9. baseline and differential.
GenevisibleiQ9JMH9. MM.

Interactioni

Subunit structurei

Homodimer. Forms a tripartite complex with CDC42BPA/CDC42BPB and LURAP1 with the latter acting as an adapter connecting CDC42BPA/CDC42BPB and MYO18A. Binds F-actin; regulated by ADP and GOLPH3. Interacts with GOLPH3; the interaction is direct and may link Golgi membranes to the actin cytoskeleton. Interacts with JAK3.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi237427. 3 interactions.
IntActiQ9JMH9. 6 interactions.
MINTiMINT-1634736.
STRINGi10090.ENSMUSP00000090563.

Structurei

3D structure databases

ProteinModelPortaliQ9JMH9.
SMRiQ9JMH9. Positions 229-303, 337-1244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini220 – 31192PDZPROSITE-ProRule annotationAdd
BLAST
Domaini405 – 1181777Myosin motorAdd
BLAST
Domaini1184 – 121330IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 398398Mediates nucleotide-independent binding to F-actin and interaction with GOLPH3By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1242 – 1967726Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi114 – 1185Interaction with actinBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 2520Lys-richAdd
BLAST

Domaini

The myosin motor domain binds ADP and ATP but has no intrinsic ATPase activity. Mediates ADP-dependent binding to actin (By similarity).By similarity

Sequence similaritiesi

Contains 1 IQ domain.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129849.
HOVERGENiHBG052543.
InParanoidiQ9JMH9.
KOiK10362.
OrthoDBiEOG71P29W.
PhylomeDBiQ9JMH9.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
3.40.50.300. 1 hit.
4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR031244. MYO18A.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
[Graphical view]
PANTHERiPTHR13140:SF421. PTHR13140:SF421. 4 hits.
PfamiPF00063. Myosin_head. 2 hits.
PF01576. Myosin_tail_1. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 3 hits.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q9JMH9-3) [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
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS MRRGFFNLNR
60 70 80 90 100
SSKRESKTRL EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA
110 120 130 140 150
SSSDDLKGEE GSFRGSVLQR AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA
160 170 180 190 200
SETSTPSEHS AAPSPQVEVR TLEGQLMQHP GLGIPRPGPR SRVPELVTKR
210 220 230 240 250
FPADLRLPAL VPPPPPALRE LELQRRPTGD FGFSLRRTTM LDRAPEGQAY
260 270 280 290 300
RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GQNVENKSRD EIVEMIRQSG
310 320 330 340 350
DSVRLKVQPI PELSELSRSW LRTGEGHRRE PADAKTEEQI AAEEAWYETE
360 370 380 390 400
KVWLVHRDGF SLASQLKSEE LSLPEGKARV KLDHDGAILD VDEDDIEKAN
410 420 430 440 450
APSCDRLEDL ASLVYLNESS VLHTLRQRYG ASLLHTYAGP SLLVLSTRGA
460 470 480 490 500
PAVYSEKVMH MFKGCRREDM APHIYAVAQT AYRAMLMSRQ DQSIVLLGSS
510 520 530 540 550
GSGKTTSFQH LVQYLATIAG TSGTKVFSVE KWQALSTLLE AFGNSPTIMN
560 570 580 590 600
GSATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA SEATFNVFYY
610 620 630 640 650
LLACGDATLR TELHLNHLAE NNVFGIVPLS KPEEKQKAAQ QFSKLQAAMK
660 670 680 690 700
VLAISPEEQK TCWLILASIY HLGAAGATKE AAEAGRKQFA RHEWAQKAAY
710 720 730 740 750
LLGCSLEELS SAIFKHQLKG GTLQRSTSFR QGPEESGLGE GTKLSALECL
760 770 780 790 800
EGMASGLYSE LFTLLISLVN RALKSSQHSL CSMMIVDTPG FQNPEWGGSA
810 820 830 840 850
RGASFEELCH NYAQDRLQRL FHERTFLQEL ERYKEDNIEL AFDDLEPVAD
860 870 880 890 900
DSVAAVDQAS HLVRSLAHAD EARGLLWLLE EEALVPGATE DALLDRLFSY
910 920 930 940 950
YGPQEGDKKG QSPLLRSSKP RHFLLGHSHG TNWVEYNVAG WLNYTKQNPA
960 970 980 990 1000
TQNAPRLLQD SQKKIISNLF LGRAGSATVL SGSIAGLEGG SQLALRRATS
1010 1020 1030 1040 1050
MRKTFTTGMA AVKKKSLCIQ IKLQVDALID TIKRSKMHFV HCFLPVAEGW
1060 1070 1080 1090 1100
PGEPRSASSR RVSSSSELDL PPGDPCEAGL LQLDVSLLRA QLRGSRLLDA
1110 1120 1130 1140 1150
MRMYRQGYPD HMVFSEFRRR FDVLAPHLTK KHGRNYIVVD EKRAVEELLE
1160 1170 1180 1190 1200
SLDLEKSSCC LGLSRVFFRA GTLARLEEQR DEQTSRHLTL FQAACRGYLA
1210 1220 1230 1240 1250
RQHFKKRKIQ DLAIRCVQKN IKKNKGVKDW PWWKLFTTVR PLIQVQLSEE
1260 1270 1280 1290 1300
QIRNKDEEIQ QLRSKLEKVE KERNELRLSS DRLETRISEL TSELTDERNT
1310 1320 1330 1340 1350
GESASQLLDA ETAERLRTEK EMKELQTQYD ALKKQMEVME MEVMEARLIR
1360 1370 1380 1390 1400
AAEINGEVDD DDAGGEWRLK YERAVREVDF TKKRLQQELE DKMEVEQQSR
1410 1420 1430 1440 1450
RQLERRLGDL QADSDESQRA LQQLKKKCQR LTAELQDTKL HLEGQQVRNH
1460 1470 1480 1490 1500
ELEKKQRRFD SELSQAHEET QREKLQREKL QREKDMLLAE AFSLKQQMEE
1510 1520 1530 1540 1550
KDLDIAGFTQ KVVSLEAELQ DISSQESKDE ASLAKVKKQL RDLEAKVKDQ
1560 1570 1580 1590 1600
EEELDEQAGS IQMLEQAKLR LEMEMERMRQ THSKEMESRD EEVEEARQSC
1610 1620 1630 1640 1650
QKKLKQMEVQ LEEEYEDKQK ALREKRELES KLSTLSDQVN QRDFESEKRL
1660 1670 1680 1690 1700
RKDLKRTKAL LADAQIMLDH LKNNAPSKRE IAQLKNQLEE SEFTCAAAVK
1710 1720 1730 1740 1750
ARKAMEVEME DLHLQIDDIA KAKTALEEQL SRLQREKNEI QNRLEEDQED
1760 1770 1780 1790 1800
MNELMKKHKA AVAQASRDMA QMNDLQAQIE ESNKEKQELQ EKLQALQSQV
1810 1820 1830 1840 1850
EFLEQSMVDK SLVSRQEAKI RELETRLEFE KTQVKRLENL ASRLKETMEK
1860 1870 1880 1890 1900
LTEERDQRAA AENREKEQNK RLQRQLRDTK EEMSELARKE AEASRKKHEL
1910 1920 1930 1940 1950
EMDLESLEAA NQSLQADLKL AFKRIGDLQA AIEDEMESDE NEDLINSLQD
1960 1970 1980 1990 2000
MVTKYQKKKN KLEGDSDVDS ELEDRVDGVK SWLSKNKGPS KAPSDDGSLK
2010 2020 2030 2040 2050
SSSPTSHWKP LAPDPSDDEH DPVDSISRPR FSHSYLSDSD TEAKLTETSA
Length:2,050
Mass (Da):232,755
Last modified:February 6, 2007 - v2
Checksum:i3D82B901F03D73B4
GO
Isoform 1 (identifier: Q9JMH9-1) [UniParc]FASTAAdd to basket

Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     1948-1962: Missing.

Show »
Length:2,035
Mass (Da):230,908
Checksum:iC5CE4BB053475119
GO
Isoform 2 (identifier: Q9JMH9-2) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-331: Missing.
     332-333: AD → ML

Show »
Length:1,719
Mass (Da):195,894
Checksum:iF533D2057E1E555A
GO
Isoform 4 (identifier: Q9JMH9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1567-1603: Missing.
     1948-1962: Missing.

Show »
Length:1,998
Mass (Da):226,357
Checksum:i78A7FB6FF72A32D1
GO
Isoform 5 (identifier: Q9JMH9-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-331: Missing.
     332-333: AD → ML
     1948-1962: Missing.

Show »
Length:1,704
Mass (Da):194,047
Checksum:i494995EAC30B1C00
GO
Isoform 6 (identifier: Q9JMH9-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     333-333: D → DLDPEAASPAYSQ

Show »
Length:2,062
Mass (Da):233,985
Checksum:i823FB756634D16B9
GO
Isoform 7 (identifier: Q9JMH9-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-331: Missing.
     332-333: AD → MLLDPEAASPAYSQ
     1948-1962: Missing.

Show »
Length:1,716
Mass (Da):195,277
Checksum:i893846897B291215
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti399 – 3991A → T in BAE28009 (PubMed:16141072).Curated
Sequence conflicti466 – 4661R → Q in BAE42402 (PubMed:16141072).Curated
Sequence conflicti680 – 6834Missing in BAE42402 (PubMed:16141072).Curated
Sequence conflicti680 – 6801E → EPLEEQD in BAE28009 (PubMed:16141072).Curated
Sequence conflicti798 – 7981G → D in BAE42402 (PubMed:16141072).Curated
Sequence conflicti1362 – 13621D → N in BAE42402 (PubMed:16141072).Curated
Sequence conflicti1655 – 16551K → R in BAE28009 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 331331Missing in isoform 2, isoform 5 and isoform 7. 1 PublicationVSP_007873Add
BLAST
Alternative sequencei332 – 3332AD → ML in isoform 2 and isoform 5. 1 PublicationVSP_007874
Alternative sequencei332 – 3332AD → MLLDPEAASPAYSQ in isoform 7. CuratedVSP_023059
Alternative sequencei333 – 3331D → DLDPEAASPAYSQ in isoform 6. CuratedVSP_023060
Alternative sequencei1567 – 160337Missing in isoform 4. CuratedVSP_023061Add
BLAST
Alternative sequencei1948 – 196215Missing in isoform 1, isoform 4, isoform 5 and isoform 7. 3 PublicationsVSP_023062Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026497 mRNA. Translation: BAA93660.1.
AK137574 mRNA. Translation: BAE23413.1.
AK147584 mRNA. Translation: BAE28009.1.
AK171342 mRNA. Translation: BAE42402.1.
AL591065 Genomic DNA. Translation: CAI24424.1.
AL591065 Genomic DNA. Translation: CAI24425.1.
AL591065 Genomic DNA. Translation: CAI24426.1.
AL591065 Genomic DNA. Translation: CAI24427.1.
BC046638 mRNA. Translation: AAH46638.1.
CCDSiCCDS25085.1. [Q9JMH9-1]
RefSeqiNP_001278141.1. NM_001291212.1.
NP_001278142.1. NM_001291213.1.
NP_001278143.1. NM_001291214.1.
NP_001278144.1. NM_001291215.1.
NP_035716.1. NM_011586.3. [Q9JMH9-1]
XP_006533667.1. XM_006533604.2. [Q9JMH9-3]
XP_006533669.1. XM_006533606.2. [Q9JMH9-1]
XP_006533677.2. XM_006533614.2. [Q9JMH9-2]
UniGeneiMm.341248.
Mm.476162.

Genome annotation databases

EnsembliENSMUST00000092884; ENSMUSP00000090560; ENSMUSG00000000631. [Q9JMH9-5]
ENSMUST00000092887; ENSMUSP00000090563; ENSMUSG00000000631. [Q9JMH9-1]
ENSMUST00000102488; ENSMUSP00000099546; ENSMUSG00000000631. [Q9JMH9-1]
ENSMUST00000108375; ENSMUSP00000104012; ENSMUSG00000000631. [Q9JMH9-3]
ENSMUST00000108376; ENSMUSP00000104013; ENSMUSG00000000631. [Q9JMH9-4]
ENSMUST00000130305; ENSMUSP00000119574; ENSMUSG00000000631. [Q9JMH9-7]
ENSMUST00000130627; ENSMUSP00000119839; ENSMUSG00000000631. [Q9JMH9-6]
ENSMUST00000164334; ENSMUSP00000131771; ENSMUSG00000000631. [Q9JMH9-2]
GeneIDi360013.
KEGGimmu:360013.
UCSCiuc007khg.2. mouse. [Q9JMH9-1]
uc007khh.2. mouse. [Q9JMH9-5]
uc007khi.2. mouse. [Q9JMH9-7]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026497 mRNA. Translation: BAA93660.1.
AK137574 mRNA. Translation: BAE23413.1.
AK147584 mRNA. Translation: BAE28009.1.
AK171342 mRNA. Translation: BAE42402.1.
AL591065 Genomic DNA. Translation: CAI24424.1.
AL591065 Genomic DNA. Translation: CAI24425.1.
AL591065 Genomic DNA. Translation: CAI24426.1.
AL591065 Genomic DNA. Translation: CAI24427.1.
BC046638 mRNA. Translation: AAH46638.1.
CCDSiCCDS25085.1. [Q9JMH9-1]
RefSeqiNP_001278141.1. NM_001291212.1.
NP_001278142.1. NM_001291213.1.
NP_001278143.1. NM_001291214.1.
NP_001278144.1. NM_001291215.1.
NP_035716.1. NM_011586.3. [Q9JMH9-1]
XP_006533667.1. XM_006533604.2. [Q9JMH9-3]
XP_006533669.1. XM_006533606.2. [Q9JMH9-1]
XP_006533677.2. XM_006533614.2. [Q9JMH9-2]
UniGeneiMm.341248.
Mm.476162.

3D structure databases

ProteinModelPortaliQ9JMH9.
SMRiQ9JMH9. Positions 229-303, 337-1244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi237427. 3 interactions.
IntActiQ9JMH9. 6 interactions.
MINTiMINT-1634736.
STRINGi10090.ENSMUSP00000090563.

PTM databases

iPTMnetiQ9JMH9.
PhosphoSiteiQ9JMH9.

Proteomic databases

EPDiQ9JMH9.
MaxQBiQ9JMH9.
PaxDbiQ9JMH9.
PeptideAtlasiQ9JMH9.
PRIDEiQ9JMH9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092884; ENSMUSP00000090560; ENSMUSG00000000631. [Q9JMH9-5]
ENSMUST00000092887; ENSMUSP00000090563; ENSMUSG00000000631. [Q9JMH9-1]
ENSMUST00000102488; ENSMUSP00000099546; ENSMUSG00000000631. [Q9JMH9-1]
ENSMUST00000108375; ENSMUSP00000104012; ENSMUSG00000000631. [Q9JMH9-3]
ENSMUST00000108376; ENSMUSP00000104013; ENSMUSG00000000631. [Q9JMH9-4]
ENSMUST00000130305; ENSMUSP00000119574; ENSMUSG00000000631. [Q9JMH9-7]
ENSMUST00000130627; ENSMUSP00000119839; ENSMUSG00000000631. [Q9JMH9-6]
ENSMUST00000164334; ENSMUSP00000131771; ENSMUSG00000000631. [Q9JMH9-2]
GeneIDi360013.
KEGGimmu:360013.
UCSCiuc007khg.2. mouse. [Q9JMH9-1]
uc007khh.2. mouse. [Q9JMH9-5]
uc007khi.2. mouse. [Q9JMH9-7]

Organism-specific databases

CTDi399687.
MGIiMGI:2667185. Myo18a.

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129849.
HOVERGENiHBG052543.
InParanoidiQ9JMH9.
KOiK10362.
OrthoDBiEOG71P29W.
PhylomeDBiQ9JMH9.

Miscellaneous databases

ChiTaRSiMyo18a. mouse.
PROiQ9JMH9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JMH9.
CleanExiMM_MYO18A.
ExpressionAtlasiQ9JMH9. baseline and differential.
GenevisibleiQ9JMH9. MM.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
3.40.50.300. 1 hit.
4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR031244. MYO18A.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
[Graphical view]
PANTHERiPTHR13140:SF421. PTHR13140:SF421. 4 hits.
PfamiPF00063. Myosin_head. 2 hits.
PF01576. Myosin_tail_1. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 3 hits.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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  1. "Isolation of a novel PDZ-containing myosin from hematopoietic supportive bone marrow stromal cell lines."
    Furusawa T., Ikawa S., Yanai N., Obinata M.
    Biochem. Biophys. Res. Commun. 270:67-75(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Spleen.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-873 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Bone and Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1032-2050 (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Colon.
  5. "A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2 deprival."
    Ji H., Zhai Q., Zhu J., Yan M., Sun L., Liu X., Zheng Z.
    Biochem. Biophys. Res. Commun. 270:267-271(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JAK3.
  6. "Genome structure and differential expression of two isoforms of a novel PDZ-containing myosin (MysPDZ) (Myo18A)."
    Mori K., Furusawa T., Okubo T., Inoue T., Ikawa S., Yanai N., Mori K.J., Obinata M.
    J. Biochem. 133:405-413(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), DIFFERENTIAL EXPRESSION.
    Tissue: Spleen.
  7. "A novel 110 kDa form of myosin XVIIIA (MysPDZ) is tyrosine-phosphorylated after colony-stimulating factor-1 receptor signalling."
    Cross M., Csar X.F., Wilson N.J., Manes G., Addona T.A., Marks D.C., Whitty G.A., Ashman K., Hamilton J.A.
    Biochem. J. 380:243-253(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Subcellular localization and dynamics of MysPDZ (Myo18A) in live mammalian cells."
    Mori K., Matsuda K., Furusawa T., Kawata M., Inoue T., Obinata M.
    Biochem. Biophys. Res. Commun. 326:491-498(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMER, SUBCELLULAR LOCATION, INTERACTION WITH ACTIN.
  9. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 (ISOFORM 6), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-83; SER-164; SER-1966; SER-2037 AND SER-2039, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2037 AND SER-2039, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote budding."
    Dippold H.C., Ng M.M., Farber-Katz S.E., Lee S.K., Kerr M.L., Peterman M.C., Sim R., Wiharto P.A., Galbraith K.A., Madhavarapu S., Fuchs G.J., Meerloo T., Farquhar M.G., Zhou H., Field S.J.
    Cell 139:337-351(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GOLGI ORGANIZATION, MUTAGENESIS OF 503-GLY-LYS-504.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-83; SER-102; SER-103; SER-157; SER-160; SER-164; SER-983; SER-1966; SER-1994; SER-2016; SER-2032; SER-2037; SER-2039 AND THR-2041, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMY18A_MOUSE
AccessioniPrimary (citable) accession number: Q9JMH9
Secondary accession number(s): Q3TBB2
, Q3UH48, Q3UV60, Q5SYN8, Q5SYN9, Q5SYP0, Q5SYP1, Q811D7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: February 6, 2007
Last modified: July 6, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.