Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Unconventional myosin-XVIIIa

Gene

MYO18A

Organism
Homo sapiens (Human)
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.3 Publications

Regions

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

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • ADP binding Source: UniProtKB
  • ATP binding Source: UniProtKB
  • DNA binding Source: InterPro
  • motor activity Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • actomyosin structure organization Source: UniProtKB
  • asymmetric Golgi ribbon formation Source: CACAO
  • cell migration Source: UniProtKB
  • DNA metabolic process Source: InterPro
  • Golgi organization Source: UniProtKB
  • Golgi ribbon formation Source: CACAO
  • Golgi vesicle budding Source: UniProtKB
  • negative regulation of apoptotic process Source: CACAO
  • positive regulation of protein secretion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_121141. Signaling by FGFR1 fusion mutants.

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:KIAA0216, MYSPDZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:31104. MYO18A.

Subcellular locationi

Isoform 2 :
  • Cytoplasm

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

GO - Cellular componenti

  • actomyosin Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  • Golgi membrane Source: GOC
  • membrane Source: UniProtKB
  • myosin complex Source: UniProtKB-KW
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1152RG → AA: No effect on interaction with actin. 1 Publication
Mutagenesisi117 – 1182VL → AA: Abolishes interaction with actin. 1 Publication

Organism-specific databases

PharmGKBiPA134978348.

Polymorphism and mutation databases

BioMutaiMYO18A.
DMDMi33301318.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20542054Unconventional myosin-XVIIIaPRO_0000123476Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721PhosphoserineBy similarity
Modified residuei79 – 791Phosphothreonine1 Publication
Modified residuei83 – 831Phosphoserine1 Publication
Modified residuei98 – 981Phosphoserine1 Publication
Modified residuei99 – 991Phosphothreonine1 Publication
Modified residuei103 – 1031Phosphoserine1 Publication
Modified residuei140 – 1401Phosphoserine3 Publications
Modified residuei164 – 1641PhosphoserineBy similarity
Modified residuei234 – 2341Phosphoserine1 Publication
Modified residuei1067 – 10671Phosphoserine1 Publication
Modified residuei1068 – 10681Phosphoserine1 Publication
Modified residuei1070 – 10701Phosphoserine1 Publication
Modified residuei1640 – 16401Phosphoserine1 Publication
Modified residuei1942 – 19421Phosphoserine1 Publication
Modified residuei1970 – 19701Phosphoserine4 Publications
Modified residuei1974 – 19741Phosphoserine3 Publications
Modified residuei1998 – 19981Phosphoserine2 Publications
Modified residuei2002 – 20021Phosphoserine2 Publications
Modified residuei2006 – 20061Phosphoserine1 Publication
Modified residuei2007 – 20071Phosphoserine1 Publication
Modified residuei2014 – 20141Phosphoserine1 Publication
Modified residuei2020 – 20201Phosphoserine3 Publications
Modified residuei2035 – 20351Phosphotyrosine1 Publication
Modified residuei2041 – 20411Phosphoserine5 Publications
Modified residuei2043 – 20431Phosphoserine5 Publications
Modified residuei2045 – 20451Phosphothreonine1 Publication
Isoform 5 (identifier: Q92614-5)
Modified residuei1501 – 15011Phosphoserine1 Publication
Isoform 3 (identifier: Q92614-3)
Modified residuei1922 – 19221Phosphoserine1 Publication
Isoform 4 (identifier: Q92614-4)
Modified residuei1959 – 19591Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92614.
PaxDbiQ92614.
PRIDEiQ92614.

PTM databases

PhosphoSiteiQ92614.

Expressioni

Gene expression databases

BgeeiQ92614.
CleanExiHS_MYO18A.
ExpressionAtlasiQ92614. baseline.
GenevisibleiQ92614. HS.

Organism-specific databases

HPAiHPA019646.
HPA021121.

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 JAK3.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLPH3Q9H4A66EBI-949059,EBI-2465479

Protein-protein interaction databases

BioGridi134384. 26 interactions.
IntActiQ92614. 17 interactions.
STRINGi9606.ENSP00000437073.

Structurei

3D structure databases

ProteinModelPortaliQ92614.
SMRiQ92614. Positions 223-307, 342-1247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini220 – 31192PDZPROSITE-ProRule annotationAdd
BLAST
Domaini405 – 1185781Myosin motorAdd
BLAST
Domaini1188 – 121730IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 398398Mediates nucleotide-independent binding to F-actin and interaction with GOLPH3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1246 – 1971726Sequence AnalysisAdd
BLAST

Motif

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

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 (PubMed:23990465).1 Publication

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

eggNOGiCOG5022.
GeneTreeiENSGT00650000093350.
HOGENOMiHOG000113701.
HOVERGENiHBG052543.
InParanoidiQ92614.
KOiK10362.
OMAiFKHQPKG.
PhylomeDBiQ92614.
TreeFamiTF339614.

Family and domain databases

Gene3Di2.30.42.10. 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.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERiPTHR13140:SF293. PTHR13140:SF293. 1 hit.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92614-1) [UniParc]FASTAAdd to basket

Also known as: Alpha

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 LRRGFFNLNR
60 70 80 90 100
SSKRESKTRL EISNPIPIKV ASGSDLHLTD IDSDSNRGSV ILDSGHLSTA
110 120 130 140 150
SSSDDLKGEE GSFRGSVLQR AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA
160 170 180 190 200
SETSTPSEHS AAPSPQVEVR TLEGQLVQHP GPGIPRPGHR SRAPELVTKK
210 220 230 240 250
FPVDLRLPPV VPLPPPTLRE LELQRRPTGD FGFSLRRTTM LDRGPEGQAC
260 270 280 290 300
RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GHNVESKSRD EIVEMIRQSG
310 320 330 340 350
DSVRLKVQPI PELSELSRSW LRSGEGPRRE PSDAKTEEQI AAEEAWNETE
360 370 380 390 400
KVWLVHRDGF SLASQLKSEE LNLPEGKVRV KLDHDGAILD VDEDDVEKAN
410 420 430 440 450
APSCDRLEDL ASLVYLNESS VLHTLRQRYG ASLLHTYAGP SLLVLGPRGA
460 470 480 490 500
PAVYSEKVMH MFKGCRREDM APHIYAVAQT AYRAMLMSRQ DQSIILLGSS
510 520 530 540 550
GSGKTTSCQH LVQYLATIAG ISGNKVFSVE KWQALYTLLE AFGNSPTIIN
560 570 580 590 600
GNATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA SEATFNVFYY
610 620 630 640 650
LLACGDGTLR TELHLNHLAE NNVFGIVPLA KPEEKQKAAQ QFSKLQAAMK
660 670 680 690 700
VLGISPDEQK ACWFILAAIY HLGAAGATKE AAEAGRKQFA RHEWAQKAAY
710 720 730 740 750
LLGCSLEELS SAIFKHQHKG GTLQRSTSFR QGPEESGLGD GTGPKLSALE
760 770 780 790 800
CLEGMAAGLY SELFTLLVSL VNRALKSSQH SLCSMMIVDT PGFQNPEQGG
810 820 830 840 850
SARGASFEEL CHNYTQDRLQ RLFHERTFVQ ELERYKEENI ELAFDDLEPP
860 870 880 890 900
TDDSVAAVDQ ASHQSLVRSL ARTDEARGLL WLLEEEALVP GASEDTLLER
910 920 930 940 950
LFSYYGPQEG DKKGQSPLLH SSKPHHFLLG HSHGTNWVEY NVTGWLNYTK
960 970 980 990 1000
QNPATQNAPR LLQDSQKKII SNLFLGRAGS ATVLSGSIAG LEGGSQLALR
1010 1020 1030 1040 1050
RATSMRKTFT TGMAAVKKKS LCIQMKLQVD ALIDTIKKSK LHFVHCFLPV
1060 1070 1080 1090 1100
AEGWAGEPRS ASSRRVSSSS ELDLPSGDHC EAGLLQLDVP LLRTQLRGSR
1110 1120 1130 1140 1150
LLDAMRMYRQ GYPDHMVFSE FRRRFDVLAP HLTKKHGRNY IVVDERRAVE
1160 1170 1180 1190 1200
ELLECLDLEK SSCCMGLSRV FFRAGTLARL EEQRDEQTSR NLTLFQAACR
1210 1220 1230 1240 1250
GYLARQHFKK RKIQDLAIRC VQKNIKKNKG VKDWPWWKLF TTVRPLIEVQ
1260 1270 1280 1290 1300
LSEEQIRNKD EEIQQLRSKL EKAEKERNEL RLNSDRLESR ISELTSELTD
1310 1320 1330 1340 1350
ERNTGESASQ LLDAETAERL RAEKEMKELQ TQYDALKKQM EVMEMEVMEA
1360 1370 1380 1390 1400
RLIRAAEING EVDDDDAGGE WRLKYERAVR EVDFTKKRLQ QEFEDKLEVE
1410 1420 1430 1440 1450
QQNKRQLERR LGDLQADSEE SQRALQQLKK KCQRLTAELQ DTKLHLEGQQ
1460 1470 1480 1490 1500
VRNHELEKKQ RRFDSELSQA HEEAQREKLQ REKLQREKDM LLAEAFSLKQ
1510 1520 1530 1540 1550
QLEEKDMDIA GFTQKVVSLE AELQDISSQE SKDEASLAKV KKQLRDLEAK
1560 1570 1580 1590 1600
VKDQEEELDE QAGTIQMLEQ AKLRLEMEME RMRQTHSKEM ESRDEEVEEA
1610 1620 1630 1640 1650
RQSCQKKLKQ MEVQLEEEYE DKQKVLREKR ELEGKLATLS DQVNRRDFES
1660 1670 1680 1690 1700
EKRLRKDLKR TKALLADAQL MLDHLKNSAP SKREIAQLKN QLEESEFTCA
1710 1720 1730 1740 1750
AAVKARKAME VEIEDLHLQI DDIAKAKTAL EEQLSRLQRE KNEIQNRLEE
1760 1770 1780 1790 1800
DQEDMNELMK KHKAAVAQAS RDLAQINDLQ AQLEEANKEK QELQEKLQAL
1810 1820 1830 1840 1850
QSQVEFLEQS MVDKSLVSRQ EAKIRELETR LEFERTQVKR LESLASRLKE
1860 1870 1880 1890 1900
NMEKLTEERD QRIAAENREK EQNKRLQRQL RDTKEEMGEL ARKEAEASRK
1910 1920 1930 1940 1950
KHELEMDLES LEAANQSLQA DLKLAFKRIG DLQAAIEDEM ESDENEDLIN
1960 1970 1980 1990 2000
SLQDMVTKYQ KRKNKLEGDS DVDSELEDRV DGVKSWLSKN KGPSKAASDD
2010 2020 2030 2040 2050
GSLKSSSPTS YWKSLAPDRS DDEHDPLDNT SRPRYSHSYL SDSDTEAKLT

ETNA
Length:2,054
Mass (Da):233,115
Last modified:July 25, 2003 - v3
Checksum:i52BFA0AA273E18F7
GO
Isoform 2 (identifier: Q92614-2) [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: SD → MR

Show »
Length:1,723
Mass (Da):196,438
Checksum:iA0764A2A6D54D6EC
GO
Isoform 3 (identifier: Q92614-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1571-1607: Missing.
     1952-1966: Missing.

Note: No experimental confirmation available.1 Publication
Show »
Length:2,002
Mass (Da):226,690
Checksum:i89350E07C2CF8B03
GO
Isoform 4 (identifier: Q92614-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1952-1966: Missing.

Note: No experimental confirmation available.1 Publication
Show »
Length:2,039
Mass (Da):231,240
Checksum:i70DDB5F30E54B9C3
GO
Isoform 5 (identifier: Q92614-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-458: Missing.
     1952-1966: Missing.

Show »
Length:1,581
Mass (Da):180,495
Checksum:iDDE7EF34D1A7E515
GO

Sequence cautioni

The sequence BAA13206.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD66838.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1014 – 10141A → V in BAD66838 (PubMed:15491607).Curated
Sequence conflicti1020 – 10201S → P in CAI45931 (PubMed:17974005).Curated
Sequence conflicti1757 – 17571E → K in CAI45931 (PubMed:17974005).Curated
Sequence conflicti1889 – 18891E → G in CAI45931 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti958 – 9581A → V.2 Publications
Corresponds to variant rs8076604 [ dbSNP | Ensembl ].
VAR_030585

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 458458Missing in isoform 5. 1 PublicationVSP_023058Add
BLAST
Alternative sequencei1 – 331331Missing in isoform 2. CuratedVSP_007869Add
BLAST
Alternative sequencei332 – 3332SD → MR in isoform 2. CuratedVSP_007870
Alternative sequencei1571 – 160737Missing in isoform 3. 1 PublicationVSP_007871Add
BLAST
Alternative sequencei1952 – 196615Missing in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_007872Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB177858 mRNA. Translation: BAD66836.1.
AB177860 mRNA. Translation: BAD66838.1. Different initiation.
D86970 mRNA. Translation: BAA13206.2. Different initiation.
CR933614 mRNA. Translation: CAI45931.1.
BC039612 mRNA. Translation: AAH39612.1.
CCDSiCCDS45641.1. [Q92614-4]
CCDS45642.1. [Q92614-1]
RefSeqiNP_510880.2. NM_078471.3. [Q92614-1]
NP_976063.1. NM_203318.1. [Q92614-4]
UniGeneiHs.462590.

Genome annotation databases

EnsembliENST00000527372; ENSP00000437073; ENSG00000196535.
ENST00000533112; ENSP00000435932; ENSG00000196535. [Q92614-3]
GeneIDi399687.
KEGGihsa:399687.
UCSCiuc002hds.2. human. [Q92614-5]
uc002hdt.1. human. [Q92614-1]
uc002hdu.1. human. [Q92614-4]
uc010csa.1. human. [Q92614-3]
uc010wbd.1. human. [Q92614-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB177858 mRNA. Translation: BAD66836.1.
AB177860 mRNA. Translation: BAD66838.1. Different initiation.
D86970 mRNA. Translation: BAA13206.2. Different initiation.
CR933614 mRNA. Translation: CAI45931.1.
BC039612 mRNA. Translation: AAH39612.1.
CCDSiCCDS45641.1. [Q92614-4]
CCDS45642.1. [Q92614-1]
RefSeqiNP_510880.2. NM_078471.3. [Q92614-1]
NP_976063.1. NM_203318.1. [Q92614-4]
UniGeneiHs.462590.

3D structure databases

ProteinModelPortaliQ92614.
SMRiQ92614. Positions 223-307, 342-1247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi134384. 26 interactions.
IntActiQ92614. 17 interactions.
STRINGi9606.ENSP00000437073.

PTM databases

PhosphoSiteiQ92614.

Polymorphism and mutation databases

BioMutaiMYO18A.
DMDMi33301318.

Proteomic databases

MaxQBiQ92614.
PaxDbiQ92614.
PRIDEiQ92614.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000527372; ENSP00000437073; ENSG00000196535.
ENST00000533112; ENSP00000435932; ENSG00000196535. [Q92614-3]
GeneIDi399687.
KEGGihsa:399687.
UCSCiuc002hds.2. human. [Q92614-5]
uc002hdt.1. human. [Q92614-1]
uc002hdu.1. human. [Q92614-4]
uc010csa.1. human. [Q92614-3]
uc010wbd.1. human. [Q92614-2]

Organism-specific databases

CTDi399687.
GeneCardsiGC17M027400.
HGNCiHGNC:31104. MYO18A.
HPAiHPA019646.
HPA021121.
MIMi609517. gene.
610067. gene.
neXtProtiNX_Q92614.
PharmGKBiPA134978348.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00650000093350.
HOGENOMiHOG000113701.
HOVERGENiHBG052543.
InParanoidiQ92614.
KOiK10362.
OMAiFKHQPKG.
PhylomeDBiQ92614.
TreeFamiTF339614.

Enzyme and pathway databases

ReactomeiREACT_121141. Signaling by FGFR1 fusion mutants.

Miscellaneous databases

ChiTaRSiMYO18A. human.
GeneWikiiMYO18A.
GenomeRNAii399687.
NextBioi105494.
PROiQ92614.
SOURCEiSearch...

Gene expression databases

BgeeiQ92614.
CleanExiHS_MYO18A.
ExpressionAtlasiQ92614. baseline.
GenevisibleiQ92614. HS.

Family and domain databases

Gene3Di2.30.42.10. 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.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERiPTHR13140:SF293. PTHR13140:SF293. 1 hit.
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

« Hide 'large scale' publications
  1. "Alternative splice variants encoding unstable protein domains exist in the human brain."
    Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.
    J. Mol. Biol. 343:1207-1220(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 9-2054 (ISOFORM 1).
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-958.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Amygdala.
  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] (ISOFORM 3), VARIANT VAL-958.
    Tissue: Testis.
  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).
  7. "The N-terminal domain of MYO18A has an ATP-insensitive actin-binding site."
    Isogawa Y., Kon T., Inoue T., Ohkura R., Yamakawa H., Ohara O., Sutoh K.
    Biochemistry 44:6190-6196(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, HOMODIMERIZATION, INTERACTION WITH ACTIN, MUTAGENESIS OF 114-ARG-GLY-115 AND 117-VAL-LEU-118.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1970 AND SER-1974, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow."
    Tan I., Yong J., Dong J.M., Lim L., Leung T.
    Cell 135:123-136(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH LURAP1 AND CDC42BPA/CDC42BPB.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2020, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1070; SER-1998; SER-2002; SER-2020; SER-2041; SER-2043 AND THR-2045, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1970 AND SER-1974, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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 MEMBRANE BUDDING, INTERACTION WITH GOLPH3, SUBCELLULAR LOCATION.
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2041 AND SER-2043, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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-83; SER-140; SER-2041 AND SER-2043, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-1970; SER-2007; SER-2041 AND SER-2043, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Functional Characterization of Human Myosin-18A and its Interaction with F-actin and GOLPH3."
    Taft M.H., Behrmann E., Munske-Weidemann L.C., Thiel C., Raunser S., Manstein D.J.
    J. Biol. Chem. 288:30029-30041(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GOLPH3, F-ACTIN-BINDING, NUCLEOTIDE-BINDING, DOMAIN.
  20. "GOLPH3L antagonizes GOLPH3 to determine Golgi morphology."
    Ng M.M., Dippold H.C., Buschman M.D., Noakes C.J., Field S.J.
    Mol. Biol. Cell 24:796-808(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GOLPH3.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79; SER-98; THR-99; SER-103; SER-140; SER-234; SER-1067; SER-1068; SER-1640; SER-1942; SER-1970; SER-1974; SER-1998; SER-2002; SER-2006; SER-2014; SER-2020; TYR-2035; SER-2041 AND SER-2043, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1922 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1959 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1501 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMY18A_HUMAN
AccessioniPrimary (citable) accession number: Q92614
Secondary accession number(s): Q5H9U3
, Q5W9F9, Q5W9G1, Q8IXP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: July 25, 2003
Last modified: July 22, 2015
This is version 155 of the entry and version 3 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

Caution

The TIAF1 protein is coded in the 3'-UTR region of MYO18A.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.