Myosin-9 - Mus musculus (Mouse)

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Q8VDD5 (MYH9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Myosin-9

Alternative name(s):
Cellular myosin heavy chain, type A
Myosin heavy chain 9
Myosin heavy chain, non-muscle IIa
Non-muscle myosin heavy chain A
Short name=NMMHC-A
Non-muscle myosin heavy chain IIa
Short name=NMMHC II-a
Short name=NMMHC-IIA

Gene names

Name:

Myh9

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1960 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Plays a role in cell spreading and cell migration. Ref.16
Subunit structure	Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with SVIL, HTRA3 and SLC6A4 By similarity. Interacts with PDLIM2. Interacts with RASIP1. Interacts with DDR1. Ref.16 Ref.18
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cell cortex. Note: Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells. Ref.16
Domain	The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.
Post-translational modification	ISGylated. Ref.7
Sequence similarities	Contains 1 IQ domain. Contains 1 myosin head-like domain.
Sequence caution	The sequence BAE27768.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell shape
Cellular component	Cytoplasm Cytoskeleton
Domain	Coiled coil
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton reorganization Inferred from sequence or structural similarity. Source: UniProtKB actin filament-based movement Inferred from sequence or structural similarity. Source: UniProtKB angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB blood vessel endothelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB cell-cell adhesion Inferred from mutant phenotype PubMed 15292239. Source: MGI cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB establishment of T cell polarity Inferred from mutant phenotype PubMed 15064761. Source: MGI establishment of meiotic spindle localization Inferred from direct assay PubMed 9725909. Source: MGI in utero embryonic development Inferred from mutant phenotype PubMed 15555549 PubMed 16630581. Source: MGI meiotic metaphase I Inferred from direct assay PubMed 9725909. Source: MGI meiotic spindle organization Inferred from direct assay PubMed 9725909. Source: MGI membrane protein ectodomain proteolysis Inferred from sequence or structural similarity. Source: UniProtKB monocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB myoblast fusion Inferred from mutant phenotype PubMed 16895968. Source: MGI platelet formation Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB uropod organization Inferred from mutant phenotype PubMed 15064761. Source: MGI
Cellular_component	actomyosin contractile ring Inferred from sequence or structural similarity. Source: UniProtKB cell-cell adherens junction Inferred from direct assay PubMed 15292239. Source: MGI cleavage furrow Inferred from sequence or structural similarity. Source: UniProtKB cortical cytoskeleton Inferred from direct assay PubMed 12893741. Source: MGI cytosol Inferred from sequence or structural similarity. Source: UniProtKB integrin complex Inferred from electronic annotation. Source: Compara myosin II complex Inferred from direct assay PubMed 21126233. Source: MGI nucleus Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB ruffle Inferred from sequence or structural similarity. Source: UniProtKB signalosome Inferred from electronic annotation. Source: Compara stress fiber Inferred from sequence or structural similarity. Source: UniProtKB uropod Inferred from direct assay PubMed 15064761. Source: MGI
Molecular_function	ADP binding Inferred from electronic annotation. Source: Compara ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB actin filament binding Inferred from sequence or structural similarity. Source: UniProtKB actin-dependent ATPase activity Inferred from electronic annotation. Source: Compara microfilament motor activity Inferred from sequence or structural similarity. Source: UniProtKB protein anchor Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 1960

1959

Myosin-9

PRO_0000123417

Regions

Domain

2 – 778

777

Myosin head-like

Domain

779 – 808

Nucleotide binding

174 – 181

ATP Potential

Region

654 – 676

Actin-binding

Coiled coil

841 – 1926

1086

Potential

Amino acid modifications

Modified residue

N-acetylalanine Ref.4

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

102

N6-acetyllysine By similarity

Modified residue

181

Phosphothreonine Ref.10

Modified residue

299

N6-acetyllysine By similarity

Modified residue

638

Phosphothreonine By similarity

Modified residue

754

Phosphotyrosine Ref.9

Modified residue

1024

N6-acetyllysine By similarity

Modified residue

1357

N6-acetyllysine By similarity

Modified residue

1392

N6-acetyllysine By similarity

Modified residue

1404

N6-acetyllysine By similarity

Modified residue

1410

N6-acetyllysine By similarity

Modified residue

1459

N6-acetyllysine By similarity

Modified residue

1638

N6-acetyllysine By similarity

Modified residue

1714

Phosphoserine By similarity

Modified residue

1799

Phosphoserine By similarity

Modified residue

1939

Phosphothreonine Ref.12 Ref.14 Ref.17

Modified residue

1943

Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Experimental info

Sequence conflict

1733

Q → L in CAC85955. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q8VDD5 [UniParc].

Last modified September 2, 2008. Version 4.
Checksum: AAAC0E83A0A4F24A
Show »

FASTA

1,960

226,372

        10         20         30         40         50         60 
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSSKNG FEPASLKEEV GEEAIVELVE 

        70         80         90        100        110        120 
NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKERYYSGLI YTYSGLFCVV 

       130        140        150        160        170        180 
INPYKNLPIY SEEIVEMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK 

       190        200        210        220        230        240 
TENTKKVIQY LAHVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR 

       250        260        270        280        290        300 
INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY 

       310        320        330        340        350        360 
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEDEQMGLL RVISGVLQLG NIAFKKERNT 

       370        380        390        400        410        420 
DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA 

       430        440        450        460        470        480 
TYERMFRWLV LRINKALDKT KRQGASFIGI LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF 

       490        500        510        520        530        540 
NHTMFILEQE EYQREGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK 

       550        560        570        580        590        600 
SFVEKVVQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL 

       610        620        630        640        650        660 
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT 

       670        680        690        700        710        720 
LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR 

       730        740        750        760        770        780 
YEILTPNSIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRAGVLAH LEEERDLKIT 

       790        800        810        820        830        840 
DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL RLRNWQWWRL FTKVKPLLNS 

       850        860        870        880        890        900 
IRHEDELLAK EAELTKVREK HLAAENRLTE METMQSQLMA EKLQLQEQLQ AETELCAEAE 

       910        920        930        940        950        960 
ELRARLTAKK QELEEICHDL EARVEEEEER CQYLQAEKKK MQQNIQELEE QLEEEESARQ 

       970        980        990       1000       1010       1020 
KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR VAEFTTNLME EEEKSKSLAK 

      1030       1040       1050       1060       1070       1080 
LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSTDL SDQIAELQAQ IAELKMQLAK 

      1090       1100       1110       1120       1130       1140 
KEEELQAALA RVEEEAAQKN MALKKIRELE TQISELQEDL ESERASRNKA EKQKRDLGEE 

      1150       1160       1170       1180       1190       1200 
LEALKTELED TLDSTAAQQE LRSKREQEVS ILKKTLEDEA KTHEAQIQEM RQKHSQAVEE 

      1210       1220       1230       1240       1250       1260 
LADQLEQTKR VKATLEKAKQ TLENERGELA NEVKALLQGK GDSEHKRKKV EAQLQELQVK 

      1270       1280       1290       1300       1310       1320 
FSEGERVRTE LADKVTKLQV ELDSVTGLLS QSDSKSSKLT KDFSALESQL QDTQELLQEE 

      1330       1340       1350       1360       1370       1380 
NRQKLSLSTK LKQMEDEKNS FREQLEEEEE AKRNLEKQIA TLHAQVTDMK KKMEDGVGCL 

      1390       1400       1410       1420       1430       1440 
ETAEEAKRRL QKDLEGLSQR LEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSVSNLE 

      1450       1460       1470       1480       1490       1500 
KKQKKFDQLL AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK 

      1510       1520       1530       1540       1550       1560 
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA TEDAKLRLEV 

      1570       1580       1590       1600       1610       1620 
NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED ERKQRSMAMA ARKKLEMDLK 

      1630       1640       1650       1660       1670       1680 
DLEAHIDTAN KNREEAIKQL RKLQAQMKDC MRELDDTRAS REEILAQAKE NEKKLKSMEA 

      1690       1700       1710       1720       1730       1740 
EMIQLQEELA AAERAKRQAQ QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE 

      1750       1760       1770       1780       1790       1800 
EQGNTELIND RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KAKLQEMESA 

      1810       1820       1830       1840       1850       1860 
VKSKYKASIA ALEAKIAQLE EQLDNETKER QAASKQVRRT EKKLKDVLLQ VEDERRNAEQ 

      1870       1880       1890       1900       1910       1920 
FKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL EDATETADAM NREVSSLKNK 

      1930       1940       1950       1960 
LRRGDLPFVV TRRIVRKGTG DCSDEEVDGK ADGADAKAAE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the murine non-muscle myosin heavy chain IIA gene ortholog of human MYH9 responsible for May-Hegglin, Sebastian, Fechtner, and Epstein syndromes." D'Apolito M., Guarnieri V., Boncristiano M., Zelante L., Savoia A. Gene 286:215-222(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Amnion, Brain, Embryo, Embryonic liver and Placenta.
[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. 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]	Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-64; 83-102; 126-139; 144-159; 186-199; 210-225; 241-261; 273-299; 302-355; 374-387; 408-419; 476-494; 518-536; 564-613; 618-637; 645-651; 663-678; 683-702; 712-731; 738-755; 765-775; 802-810; 815-821; 834-850; 910-923; 931-938; 941-959; 975-989; 1001-1014; 1023-1035; 1052-1075; 1081-1091; 1106-1124; 1136-1162; 1166-1174; 1182-1191; 1194-1210; 1227-1234; 1249-1260; 1278-1295; 1302-1322; 1343-1353; 1358-1370; 1393-1400; 1405-1413; 1418-1441; 1445-1454; 1484-1492; 1504-1518; 1529-1566; 1593-1602; 1614-1620; 1659-1669; 1677-1694; 1698-1724; 1731-1751; 1754-1770; 1792-1802; 1807-1828; 1844-1855; 1857-1867; 1877-1888; 1899-1912 AND 1923-1932, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[5]	"Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H. DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 626-1960. Strain: ICR. Tissue: Embryonic tail.
[6]	"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 1066-1960. Strain: FVB/N. Tissue: Mammary tumor.
[7]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ISGYLATION.
[8]	"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-1943, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754, MASS SPECTROMETRY. Tissue: Mast cell.
[10]	"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 THR-181 AND SER-1943, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Liver.
[12]	"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 THR-1939 AND SER-1943, MASS SPECTROMETRY. Tissue: Liver.
[13]	"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-1943, MASS SPECTROMETRY. Tissue: Liver.
[14]	"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 THR-1939 AND SER-1943, MASS SPECTROMETRY. Tissue: Melanoma.
[15]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, MASS SPECTROMETRY. Tissue: Macrophage.
[16]	"The collagen receptor DDR1 regulates cell spreading and motility by associating with myosin IIA." Huang Y., Arora P., McCulloch C.A., Vogel W.F. J. Cell Sci. 122:1637-1646(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DDR1, MASS SPECTROMETRY.
[17]	"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 THR-1939 AND SER-1943, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[18]	"Blood vessel tubulogenesis requires Rasip1 regulation of GTPase signaling." Xu K., Sacharidou A., Fu S., Chong D.C., Skaug B., Chen Z.J., Davis G.E., Cleaver O. Dev. Cell 20:526-539(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RASIP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ312390 mRNA. Translation: CAC85955.1. AK147203 mRNA. Translation: BAE27761.1. AK147206 mRNA. Translation: BAE27763.1. AK147208 mRNA. Translation: BAE27765.1. AK147209 mRNA. Translation: BAE27766.1. AK147210 mRNA. Translation: BAE27767.1. AK147211 mRNA. Translation: BAE27768.1. Different initiation. AK147215 mRNA. Translation: BAE27772.1. AK147216 mRNA. Translation: BAE27773.1. AK147221 mRNA. Translation: BAE27776.1. AK147222 mRNA. Translation: BAE27777.1. AK147223 mRNA. Translation: BAE27778.1. AK147233 mRNA. Translation: BAE27783.1. AK147235 mRNA. Translation: BAE27785.1. AK147296 mRNA. Translation: BAE27829.1. AK147407 mRNA. Translation: BAE27894.1. AK147430 mRNA. Translation: BAE27906.1. AL583886 Genomic DNA. Translation: CAM23428.1. AK131171 mRNA. Translation: BAD21421.1. BC044834 mRNA. Translation: AAH44834.1.
IPI	IPI00123181.
RefSeq	NP_071855.2. NM_022410.2.
UniGene	Mm.29677.
3D structure databases
ProteinModelPortal	Q8VDD5.
SMR	Q8VDD5. Positions 7-897, 1894-1934.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29546N.
IntAct	Q8VDD5. 8 interactions.
MINT	MINT-2524850.
PTM databases
PhosphoSite	Q8VDD5.
Proteomic databases
PaxDb	Q8VDD5.
PRIDE	Q8VDD5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000016771; ENSMUSP00000016771; ENSMUSG00000022443.
GeneID	17886.
KEGG	mmu:17886.
UCSC	uc007woc.1. mouse.
Organism-specific databases
CTD	4627.
MGI	MGI:107717. Myh9.
Phylogenomic databases
eggNOG	COG5022.
GeneTree	ENSGT00650000092896.
HOGENOM	HOG000173958.
HOVERGEN	HBG004704.
InParanoid	Q8VDD5.
KO	K10352.
OMA	EMRQKHS.
OrthoDB	EOG4TXBR1.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane. REACT_88307. Membrane Trafficking.
Gene expression databases
ArrayExpress	Q8VDD5.
Bgee	Q8VDD5.
CleanEx	MM_MYH9.
Genevestigator	Q8VDD5.
GermOnline	ENSMUSG00000022443. Mus musculus.
Family and domain databases
InterPro	IPR000048. IQ_motif_EF-hand-BS. IPR001609. Myosin_head_motor_dom. IPR004009. Myosin_N. IPR002928. Myosin_tail. [Graphical view]
Pfam	PF00612. IQ. 1 hit. PF00063. Myosin_head. 1 hit. PF02736. Myosin_N. 1 hit. PF01576. Myosin_tail_1. 1 hit. [Graphical view]
PRINTS	PR00193. MYOSINHEAVY.
SMART	SM00015. IQ. 1 hit. SM00242. MYSc. 1 hit. [Graphical view]
PROSITE	PS50096. IQ. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MYH9. mouse.
NextBio	292701.
SOURCE	Search...

Entry information

Entry name

MYH9_MOUSE

Accession

Primary (citable) accession number: Q8VDD5
Secondary accession number(s): Q3UHT9

Q811I2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	September 2, 2008
Last modified:	May 1, 2013
This is version 102 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents