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Q92614 (MY18A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-XVIIIa
Alternative name(s):
Molecule associated with JAK3 N-terminus
Short name=MAJN
Myosin containing a PDZ domain
Gene names
Name:MYO18A
Synonyms:KIAA0216, MYSPDZ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2054 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.14 Ref.20

Subunit structure

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. Ref.5 Ref.7 Ref.9 Ref.14 Ref.19 Ref.20

Subcellular location

Isoform 1: Endoplasmic reticulum-Golgi intermediate compartment By similarity. Cytoplasmcytoskeleton. Note: Colocalizes with actin. Ref.7 Ref.14

Isoform 2: Cytoplasm. Note: Lacks the PDZ domain. Diffusely localized in the cytoplasm. Ref.7 Ref.14

Golgi apparatus. Golgi apparatustrans-Golgi network. Note: Recruited to the Golgi apparatus by GOLPH3. Ref.7 Ref.14

Domain

The myosin head-like domain binds ADP and ATP but has no intrinsic ATPase activity. Mediates ADP-dependent binding to actin (Ref.19). Ref.19

Sequence similarities

Contains 1 IQ domain.

Contains 1 myosin head-like domain.

Contains 1 PDZ (DHR) domain.

Caution

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

Sequence caution

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

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

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Golgi apparatus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA metabolic process

Inferred from electronic annotation. Source: InterPro

Golgi organization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

Golgi vesicle budding

Inferred from mutant phenotype Ref.14. Source: UniProtKB

actomyosin structure organization

Inferred from mutant phenotype Ref.9. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.9. Source: UniProtKB

negative regulation of apoptotic process

Traceable author statement PubMed 9918798. Source: ProtInc

positive regulation of protein secretion

Inferred from mutant phenotype Ref.20. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from mutant phenotype Ref.14. Source: GOC

actomyosin

Inferred from direct assay Ref.9. Source: UniProtKB

endoplasmic reticulum-Golgi intermediate compartment

Inferred from electronic annotation. Source: UniProtKB-SubCell

myosin complex

Inferred from electronic annotation. Source: UniProtKB-KW

trans-Golgi network

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionADP binding

Inferred from direct assay Ref.19. Source: UniProtKB

ATP binding

Inferred from direct assay Ref.19. Source: UniProtKB

DNA binding

Inferred from electronic annotation. Source: InterPro

actin filament binding

Inferred from direct assay Ref.19. Source: UniProtKB

motor activity

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GOLPH3Q9H4A64EBI-949059,EBI-2465479

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92614-1)

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.
Isoform 2 (identifier: Q92614-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-331: Missing.
     332-333: SD → MR
Isoform 3 (identifier: Q92614-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1571-1607: Missing.
     1952-1966: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q92614-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1952-1966: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q92614-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20542054Unconventional myosin-XVIIIa
PRO_0000123476

Regions

Domain220 – 31192PDZ
Domain420 – 1186767Myosin head-like
Domain1188 – 121730IQ
Nucleotide binding498 – 5058ATP Potential
Region1 – 398398Mediates nucleotide-independent binding to F-actin and interaction with GOLPH3
Coiled coil1246 – 1971726 Potential
Motif114 – 1185Interaction with actin
Compositional bias6 – 2520Lys-rich

Amino acid modifications

Modified residue721Phosphoserine By similarity
Modified residue831Phosphoserine Ref.16
Modified residue1401Phosphoserine Ref.16 Ref.18
Modified residue1641Phosphoserine By similarity
Modified residue10701Phosphoserine Ref.12
Modified residue19701Phosphoserine Ref.8 Ref.13 Ref.18
Modified residue19741Phosphoserine Ref.8 Ref.13
Modified residue19981Phosphoserine Ref.12
Modified residue20021Phosphoserine Ref.12
Modified residue20071Phosphoserine Ref.18
Modified residue20201Phosphoserine Ref.11 Ref.12
Modified residue20411Phosphoserine Ref.12 Ref.15 Ref.16 Ref.18
Modified residue20431Phosphoserine Ref.12 Ref.15 Ref.16 Ref.18
Modified residue20451Phosphothreonine Ref.12

Natural variations

Alternative sequence1 – 458458Missing in isoform 5.
VSP_023058
Alternative sequence1 – 331331Missing in isoform 2.
VSP_007869
Alternative sequence332 – 3332SD → MR in isoform 2.
VSP_007870
Alternative sequence1571 – 160737Missing in isoform 3.
VSP_007871
Alternative sequence1952 – 196615Missing in isoform 3, isoform 4 and isoform 5.
VSP_007872
Natural variant9581A → V. Ref.2 Ref.4
Corresponds to variant rs8076604 [ dbSNP | Ensembl ].
VAR_030585

Experimental info

Mutagenesis114 – 1152RG → AA: No effect on interaction with actin. Ref.7
Mutagenesis117 – 1182VL → AA: Abolishes interaction with actin. Ref.7
Sequence conflict10141A → V in BAD66838. Ref.1
Sequence conflict10201S → P in CAI45931. Ref.3
Sequence conflict17571E → K in CAI45931. Ref.3
Sequence conflict18891E → G in CAI45931. Ref.3

Sequences

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

Last modified July 25, 2003. Version 3.
Checksum: 52BFA0AA273E18F7

FASTA2,054233,115
        10         20         30         40         50         60 
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS LRRGFFNLNR SSKRESKTRL 

        70         80         90        100        110        120 
EISNPIPIKV ASGSDLHLTD IDSDSNRGSV ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR 

       130        140        150        160        170        180 
AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLVQHP 

       190        200        210        220        230        240 
GPGIPRPGHR SRAPELVTKK FPVDLRLPPV VPLPPPTLRE LELQRRPTGD FGFSLRRTTM 

       250        260        270        280        290        300 
LDRGPEGQAC RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GHNVESKSRD EIVEMIRQSG 

       310        320        330        340        350        360 
DSVRLKVQPI PELSELSRSW LRSGEGPRRE PSDAKTEEQI AAEEAWNETE KVWLVHRDGF 

       370        380        390        400        410        420 
SLASQLKSEE LNLPEGKVRV KLDHDGAILD VDEDDVEKAN APSCDRLEDL ASLVYLNESS 

       430        440        450        460        470        480 
VLHTLRQRYG ASLLHTYAGP SLLVLGPRGA PAVYSEKVMH MFKGCRREDM APHIYAVAQT 

       490        500        510        520        530        540 
AYRAMLMSRQ DQSIILLGSS GSGKTTSCQH LVQYLATIAG ISGNKVFSVE KWQALYTLLE 

       550        560        570        580        590        600 
AFGNSPTIIN GNATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA SEATFNVFYY 

       610        620        630        640        650        660 
LLACGDGTLR TELHLNHLAE NNVFGIVPLA KPEEKQKAAQ QFSKLQAAMK VLGISPDEQK 

       670        680        690        700        710        720 
ACWFILAAIY HLGAAGATKE AAEAGRKQFA RHEWAQKAAY LLGCSLEELS SAIFKHQHKG 

       730        740        750        760        770        780 
GTLQRSTSFR QGPEESGLGD GTGPKLSALE CLEGMAAGLY SELFTLLVSL VNRALKSSQH 

       790        800        810        820        830        840 
SLCSMMIVDT PGFQNPEQGG SARGASFEEL CHNYTQDRLQ RLFHERTFVQ ELERYKEENI 

       850        860        870        880        890        900 
ELAFDDLEPP TDDSVAAVDQ ASHQSLVRSL ARTDEARGLL WLLEEEALVP GASEDTLLER 

       910        920        930        940        950        960 
LFSYYGPQEG DKKGQSPLLH SSKPHHFLLG HSHGTNWVEY NVTGWLNYTK QNPATQNAPR 

       970        980        990       1000       1010       1020 
LLQDSQKKII SNLFLGRAGS ATVLSGSIAG LEGGSQLALR RATSMRKTFT TGMAAVKKKS 

      1030       1040       1050       1060       1070       1080 
LCIQMKLQVD ALIDTIKKSK LHFVHCFLPV AEGWAGEPRS ASSRRVSSSS ELDLPSGDHC 

      1090       1100       1110       1120       1130       1140 
EAGLLQLDVP LLRTQLRGSR LLDAMRMYRQ GYPDHMVFSE FRRRFDVLAP HLTKKHGRNY 

      1150       1160       1170       1180       1190       1200 
IVVDERRAVE ELLECLDLEK SSCCMGLSRV FFRAGTLARL EEQRDEQTSR NLTLFQAACR 

      1210       1220       1230       1240       1250       1260 
GYLARQHFKK RKIQDLAIRC VQKNIKKNKG VKDWPWWKLF TTVRPLIEVQ LSEEQIRNKD 

      1270       1280       1290       1300       1310       1320 
EEIQQLRSKL EKAEKERNEL RLNSDRLESR ISELTSELTD ERNTGESASQ LLDAETAERL 

      1330       1340       1350       1360       1370       1380 
RAEKEMKELQ TQYDALKKQM EVMEMEVMEA RLIRAAEING EVDDDDAGGE WRLKYERAVR 

      1390       1400       1410       1420       1430       1440 
EVDFTKKRLQ QEFEDKLEVE QQNKRQLERR LGDLQADSEE SQRALQQLKK KCQRLTAELQ 

      1450       1460       1470       1480       1490       1500 
DTKLHLEGQQ VRNHELEKKQ RRFDSELSQA HEEAQREKLQ REKLQREKDM LLAEAFSLKQ 

      1510       1520       1530       1540       1550       1560 
QLEEKDMDIA GFTQKVVSLE AELQDISSQE SKDEASLAKV KKQLRDLEAK VKDQEEELDE 

      1570       1580       1590       1600       1610       1620 
QAGTIQMLEQ AKLRLEMEME RMRQTHSKEM ESRDEEVEEA RQSCQKKLKQ MEVQLEEEYE 

      1630       1640       1650       1660       1670       1680 
DKQKVLREKR ELEGKLATLS DQVNRRDFES EKRLRKDLKR TKALLADAQL MLDHLKNSAP 

      1690       1700       1710       1720       1730       1740 
SKREIAQLKN QLEESEFTCA AAVKARKAME VEIEDLHLQI DDIAKAKTAL EEQLSRLQRE 

      1750       1760       1770       1780       1790       1800 
KNEIQNRLEE DQEDMNELMK KHKAAVAQAS RDLAQINDLQ AQLEEANKEK QELQEKLQAL 

      1810       1820       1830       1840       1850       1860 
QSQVEFLEQS MVDKSLVSRQ EAKIRELETR LEFERTQVKR LESLASRLKE NMEKLTEERD 

      1870       1880       1890       1900       1910       1920 
QRIAAENREK EQNKRLQRQL RDTKEEMGEL ARKEAEASRK KHELEMDLES LEAANQSLQA 

      1930       1940       1950       1960       1970       1980 
DLKLAFKRIG DLQAAIEDEM ESDENEDLIN SLQDMVTKYQ KRKNKLEGDS DVDSELEDRV 

      1990       2000       2010       2020       2030       2040 
DGVKSWLSKN KGPSKAASDD GSLKSSSPTS YWKSLAPDRS DDEHDPLDNT SRPRYSHSYL 

      2050 
SDSDTEAKLT ETNA 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: A0764A2A6D54D6EC
Show »

FASTA1,723196,438
Isoform 3 [UniParc].

Checksum: 89350E07C2CF8B03
Show »

FASTA2,002226,690
Isoform 4 [UniParc].

Checksum: 70DDB5F30E54B9C3
Show »

FASTA2,039231,240
Isoform 5 [UniParc].

Checksum: DDE7EF34D1A7E515
Show »

FASTA1,581180,495

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2020, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[12]"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: 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]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_510880.2. NM_078471.3.
NP_976063.1. NM_203318.1.
UniGeneHs.462590.

3D structure databases

ProteinModelPortalQ92614.
SMRQ92614. Positions 223-307, 342-1247.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid134384. 7 interactions.
IntActQ92614. 17 interactions.
STRING9606.ENSP00000346291.

PTM databases

PhosphoSiteQ92614.

Polymorphism databases

DMDM33301318.

Proteomic databases

PaxDbQ92614.
PRIDEQ92614.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000527372; ENSP00000437073; ENSG00000196535. [Q92614-1]
ENST00000531253; ENSP00000434228; ENSG00000196535. [Q92614-4]
ENST00000533112; ENSP00000435932; ENSG00000196535. [Q92614-3]
GeneID399687.
KEGGhsa:399687.
UCSCuc002hds.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

CTD399687.
GeneCardsGC17M027400.
HGNCHGNC:31104. MYO18A.
HPAHPA019646.
HPA021121.
MIM609517. gene.
610067. gene.
neXtProtNX_Q92614.
PharmGKBPA134978348.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000113701.
HOVERGENHBG052543.
InParanoidQ92614.
KOK10362.
PhylomeDBQ92614.
TreeFamTF339614.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressQ92614.
BgeeQ92614.
CleanExHS_MYO18A.
GenevestigatorQ92614.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
4.10.270.10. 1 hit.
InterProIPR000048. IQ_motif_EF-hand-BS.
IPR028561. MYO18A/B.
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]
PANTHERPTHR13140:SF14. PTHR13140:SF14. 1 hit.
PfamPF00063. Myosin_head. 2 hits.
PF01576. Myosin_tail_1. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 3 hits.
PROSITEPS50096. IQ. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO18A. human.
GeneWikiMYO18A.
GenomeRNAi399687.
NextBio105494.
PROQ92614.
SOURCESearch...

Entry information

Entry nameMY18A_HUMAN
AccessionPrimary (citable) accession number: Q92614
Secondary accession number(s): Q5H9U3 expand/collapse secondary AC list , Q5W9F9, Q5W9G1, Q8IXP8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: July 25, 2003
Last modified: April 16, 2014
This is version 142 of the entry and version 3 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM