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Q9JMH9 (MY18A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:Myspdz
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2050 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the maintenance of the stromal cell architecture required for cell to cell contact. Isoform 1 may be related to adherence and/or some other functions of mature macrophages. In concert with LURAP1 and CDC42BPA/CDC42BPB, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration By similarity.

Subunit structure

Homodimer. Interacts with JAK3 and actin. Forms a tripartite complex with CDC42BPA/CDC42BPB and LURAP1 with the latter acting as an adapter connecting CDC42BPA/CDC42BPB and MYO18A By similarity. Ref.5 Ref.8

Subcellular location

Isoform 1: Endoplasmic reticulum-Golgi intermediate compartment. Cytoplasmcytoskeleton. Note: Colocalizes with actin. Ref.8

Isoform 2: Cytoplasm. Note: Lacks the PDZ domain. Diffusely localized in the cytoplasm. Ref.8

Tissue specificity

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

Post-translational modification

Phosphorylated on tyrosine upon CSF1R activation. Isoform 6 is phosphorylated on Ser-340. Ref.7

Sequence similarities

Contains 1 IQ domain.

Contains 1 myosin head-like domain.

Contains 1 PDZ (DHR) domain.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q9JMH9-3)

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 1 (identifier: Q9JMH9-1)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1948-1962: Missing.
Isoform 2 (identifier: Q9JMH9-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-331: Missing.
     332-333: AD → ML
Isoform 4 (identifier: Q9JMH9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1567-1603: Missing.
     1948-1962: Missing.
Isoform 5 (identifier: Q9JMH9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-331: Missing.
     332-333: AD → ML
     1948-1962: Missing.
Isoform 6 (identifier: Q9JMH9-6)

The sequence of this isoform differs from the canonical sequence as follows:
     333-333: D → DLDPEAASPAYSQ
Note: Phosphorylated at position 340.
Isoform 7 (identifier: Q9JMH9-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20502050Unconventional myosin-XVIIIa
PRO_0000123477

Regions

Domain220 – 31192PDZ
Domain407 – 1169763Myosin head-like
Domain1184 – 121330IQ
Nucleotide binding498 – 5058ATP Potential
Coiled coil1242 – 1967726 Potential
Motif114 – 1185Interaction with actin By similarity

Amino acid modifications

Modified residue721Phosphoserine Ref.11
Modified residue741Phosphoserine Ref.11
Modified residue831Phosphoserine Ref.11 Ref.12
Modified residue1021Phosphoserine Ref.11
Modified residue1401Phosphoserine By similarity
Modified residue1641Phosphoserine Ref.11
Modified residue10661Phosphoserine By similarity
Modified residue19661Phosphoserine Ref.9 Ref.11 Ref.12 Ref.13
Modified residue19701Phosphoserine Ref.9 Ref.12 Ref.13
Modified residue19941Phosphoserine By similarity
Modified residue19981Phosphoserine By similarity
Modified residue20031Phosphoserine By similarity
Modified residue20161Phosphoserine Ref.12
Modified residue20321Phosphoserine Ref.11
Modified residue20371Phosphoserine Ref.11 Ref.12
Modified residue20391Phosphoserine Ref.11 Ref.12
Modified residue20411Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 331331Missing in isoform 2, isoform 5 and isoform 7.
VSP_007873
Alternative sequence332 – 3332AD → ML in isoform 2 and isoform 5.
VSP_007874
Alternative sequence332 – 3332AD → MLLDPEAASPAYSQ in isoform 7.
VSP_023059
Alternative sequence3331D → DLDPEAASPAYSQ in isoform 6.
VSP_023060
Alternative sequence1567 – 160337Missing in isoform 4.
VSP_023061
Alternative sequence1948 – 196215Missing in isoform 1, isoform 4, isoform 5 and isoform 7.
VSP_023062

Experimental info

Sequence conflict3991A → T in BAE28009. Ref.2
Sequence conflict4661R → Q in BAE42402. Ref.2
Sequence conflict680 – 6834Missing in BAE42402. Ref.2
Sequence conflict6801E → EPLEEQD in BAE28009. Ref.2
Sequence conflict7981G → D in BAE42402. Ref.2
Sequence conflict13621D → N in BAE42402. Ref.2
Sequence conflict16551K → R in BAE28009. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: 3D82B901F03D73B4

FASTA2,050232,755
        10         20         30         40         50         60 
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS MRRGFFNLNR SSKRESKTRL 

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

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

       190        200        210        220        230        240 
GLGIPRPGPR SRVPELVTKR FPADLRLPAL VPPPPPALRE LELQRRPTGD FGFSLRRTTM 

       250        260        270        280        290        300 
LDRAPEGQAY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GQNVENKSRD EIVEMIRQSG 

       310        320        330        340        350        360 
DSVRLKVQPI PELSELSRSW LRTGEGHRRE PADAKTEEQI AAEEAWYETE KVWLVHRDGF 

       370        380        390        400        410        420 
SLASQLKSEE LSLPEGKARV KLDHDGAILD VDEDDIEKAN APSCDRLEDL ASLVYLNESS 

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

       490        500        510        520        530        540 
AYRAMLMSRQ DQSIVLLGSS GSGKTTSFQH LVQYLATIAG TSGTKVFSVE KWQALSTLLE 

       550        560        570        580        590        600 
AFGNSPTIMN GSATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA SEATFNVFYY 

       610        620        630        640        650        660 
LLACGDATLR TELHLNHLAE NNVFGIVPLS KPEEKQKAAQ QFSKLQAAMK VLAISPEEQK 

       670        680        690        700        710        720 
TCWLILASIY HLGAAGATKE AAEAGRKQFA RHEWAQKAAY LLGCSLEELS SAIFKHQLKG 

       730        740        750        760        770        780 
GTLQRSTSFR QGPEESGLGE GTKLSALECL EGMASGLYSE LFTLLISLVN RALKSSQHSL 

       790        800        810        820        830        840 
CSMMIVDTPG FQNPEWGGSA RGASFEELCH NYAQDRLQRL FHERTFLQEL ERYKEDNIEL 

       850        860        870        880        890        900 
AFDDLEPVAD DSVAAVDQAS HLVRSLAHAD EARGLLWLLE EEALVPGATE DALLDRLFSY 

       910        920        930        940        950        960 
YGPQEGDKKG QSPLLRSSKP RHFLLGHSHG TNWVEYNVAG WLNYTKQNPA TQNAPRLLQD 

       970        980        990       1000       1010       1020 
SQKKIISNLF LGRAGSATVL SGSIAGLEGG SQLALRRATS MRKTFTTGMA AVKKKSLCIQ 

      1030       1040       1050       1060       1070       1080 
IKLQVDALID TIKRSKMHFV HCFLPVAEGW PGEPRSASSR RVSSSSELDL PPGDPCEAGL 

      1090       1100       1110       1120       1130       1140 
LQLDVSLLRA QLRGSRLLDA MRMYRQGYPD HMVFSEFRRR FDVLAPHLTK KHGRNYIVVD 

      1150       1160       1170       1180       1190       1200 
EKRAVEELLE SLDLEKSSCC LGLSRVFFRA GTLARLEEQR DEQTSRHLTL FQAACRGYLA 

      1210       1220       1230       1240       1250       1260 
RQHFKKRKIQ DLAIRCVQKN IKKNKGVKDW PWWKLFTTVR PLIQVQLSEE QIRNKDEEIQ 

      1270       1280       1290       1300       1310       1320 
QLRSKLEKVE KERNELRLSS DRLETRISEL TSELTDERNT GESASQLLDA ETAERLRTEK 

      1330       1340       1350       1360       1370       1380 
EMKELQTQYD ALKKQMEVME MEVMEARLIR AAEINGEVDD DDAGGEWRLK YERAVREVDF 

      1390       1400       1410       1420       1430       1440 
TKKRLQQELE DKMEVEQQSR RQLERRLGDL QADSDESQRA LQQLKKKCQR LTAELQDTKL 

      1450       1460       1470       1480       1490       1500 
HLEGQQVRNH ELEKKQRRFD SELSQAHEET QREKLQREKL QREKDMLLAE AFSLKQQMEE 

      1510       1520       1530       1540       1550       1560 
KDLDIAGFTQ KVVSLEAELQ DISSQESKDE ASLAKVKKQL RDLEAKVKDQ EEELDEQAGS 

      1570       1580       1590       1600       1610       1620 
IQMLEQAKLR LEMEMERMRQ THSKEMESRD EEVEEARQSC QKKLKQMEVQ LEEEYEDKQK 

      1630       1640       1650       1660       1670       1680 
ALREKRELES KLSTLSDQVN QRDFESEKRL RKDLKRTKAL LADAQIMLDH LKNNAPSKRE 

      1690       1700       1710       1720       1730       1740 
IAQLKNQLEE SEFTCAAAVK ARKAMEVEME DLHLQIDDIA KAKTALEEQL SRLQREKNEI 

      1750       1760       1770       1780       1790       1800 
QNRLEEDQED MNELMKKHKA AVAQASRDMA QMNDLQAQIE ESNKEKQELQ EKLQALQSQV 

      1810       1820       1830       1840       1850       1860 
EFLEQSMVDK SLVSRQEAKI RELETRLEFE KTQVKRLENL ASRLKETMEK LTEERDQRAA 

      1870       1880       1890       1900       1910       1920 
AENREKEQNK RLQRQLRDTK EEMSELARKE AEASRKKHEL EMDLESLEAA NQSLQADLKL 

      1930       1940       1950       1960       1970       1980 
AFKRIGDLQA AIEDEMESDE NEDLINSLQD MVTKYQKKKN KLEGDSDVDS ELEDRVDGVK 

      1990       2000       2010       2020       2030       2040 
SWLSKNKGPS KAPSDDGSLK SSSPTSHWKP LAPDPSDDEH DPVDSISRPR FSHSYLSDSD 

      2050 
TEAKLTETSA 

« Hide

Isoform 1 (Alpha) [UniParc].

Checksum: C5CE4BB053475119
Show »

FASTA2,035230,908
Isoform 2 (Beta) [UniParc].

Checksum: F533D2057E1E555A
Show »

FASTA1,719195,894
Isoform 4 [UniParc].

Checksum: 78A7FB6FF72A32D1
Show »

FASTA1,998226,357
Isoform 5 [UniParc].

Checksum: 494995EAC30B1C00
Show »

FASTA1,704194,047
Isoform 6 [UniParc].

Checksum: 823FB756634D16B9
Show »

FASTA2,062233,985
Isoform 7 [UniParc].

Checksum: 893846897B291215
Show »

FASTA1,716195,277

References

« Hide 'large scale' references
[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/6.
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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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, 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]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1966 AND SER-1970, MASS SPECTROMETRY.
Tissue: Liver.
[10]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 (ISOFORM 6), MASS SPECTROMETRY.
Tissue: Brain cortex.
[11]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-74; SER-83; SER-102; SER-164; SER-1966; SER-2032; SER-2037 AND SER-2039, MASS SPECTROMETRY.
Tissue: Liver.
[12]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-1966; SER-1970; SER-2016; SER-2037 AND SER-2039, MASS SPECTROMETRY.
Tissue: Melanoma.
[13]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1966 AND SER-1970, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00407425.
IPI00619995.
IPI00622556.
IPI00648918.
IPI00649326.
IPI00828545.
IPI00828766.
RefSeqNP_035716.1. NM_011586.2.
UniGeneMm.341248.
Mm.476162.

3D structure databases

ProteinModelPortalQ9JMH9.
SMRQ9JMH9. Positions 342-1243.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9JMH9. 3 interactions.

PTM databases

PhosphoSiteQ9JMH9.

Proteomic databases

PaxDbQ9JMH9.
PRIDEQ9JMH9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092884; ENSMUSP00000090560; ENSMUSG00000000631.
ENSMUST00000092887; ENSMUSP00000090563; ENSMUSG00000000631.
ENSMUST00000102488; ENSMUSP00000099546; ENSMUSG00000000631.
ENSMUST00000108375; ENSMUSP00000104012; ENSMUSG00000000631.
ENSMUST00000108376; ENSMUSP00000104013; ENSMUSG00000000631.
ENSMUST00000130305; ENSMUSP00000119574; ENSMUSG00000000631.
ENSMUST00000130627; ENSMUSP00000119839; ENSMUSG00000000631.
ENSMUST00000164334; ENSMUSP00000131771; ENSMUSG00000000631.
ENSMUST00000172303; ENSMUSP00000129098; ENSMUSG00000000631.
GeneID360013.
KEGGmmu:360013.
UCSCuc007khg.1. mouse.
uc007khh.1. mouse.
uc007khi.1. mouse.

Organism-specific databases

CTD399687.
MGIMGI:2667185. Myo18a.

Phylogenomic databases

eggNOGCOG5022.
GeneTreeENSGT00650000093350.
HOVERGENHBG052543.
KOK10362.

Gene expression databases

ArrayExpressQ9JMH9.
BgeeQ9JMH9.
CleanExMM_MYO18A.
GenevestigatorQ9JMH9.
GermOnlineENSMUSG00000000631. Mus musculus.

Family and domain databases

InterProIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR002928. Myosin_tail.
IPR001478. PDZ.
[Graphical view]
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. PDZ. 1 hit.
PROSITEPS50096. IQ. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO18A. mouse.
NextBio400702.
SOURCESearch...

Entry information

Entry nameMY18A_MOUSE
AccessionPrimary (citable) accession number: Q9JMH9
Secondary accession number(s): Q3TBB2 expand/collapse secondary AC list , Q3UH48, Q3UV60, Q5SYN8, Q5SYN9, Q5SYP0, Q5SYP1, Q811D7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families