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Q8VDD5 (MYH9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1960 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 By similarity. Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Ref.13

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.13 Ref.15

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcell cortex. Note: Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells. Ref.13

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 processCell adhesion
Cell shape
   Cellular componentCytoplasm
Cytoskeleton
   DomainCoiled coil
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin 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 adhesion

Inferred from mutant phenotype PubMed 16407977. Source: MGI

cell morphogenesis involved in differentiation

Inferred from mutant phenotype PubMed 15292239. Source: MGI

cell-cell adhesion

Inferred from mutant phenotype PubMed 15292239. Source: MGI

cellular component movement

Inferred from mutant phenotype PubMed 15064761. 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 15555549PubMed 16630581. 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_componentCOP9 signalosome

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

actomyosin contractile ring

Inferred from sequence or structural similarity. Source: UniProtKB

cell cortex

Inferred from direct assay PubMed 16895968PubMed 9725909. Source: MGI

cell leading edge

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

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

integrin complex

Inferred from electronic annotation. Source: Ensembl

myosin II complex

Inferred from direct assay PubMed 21126233. Source: MGI

myosin complex

Inferred from direct assay PubMed 8482409PubMed 9356462PubMed 9725909. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

stress fiber

Inferred from sequence or structural similarity. Source: UniProtKB

uropod

Inferred from direct assay PubMed 15064761. Source: MGI

   Molecular_functionADP binding

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Trpm7Q923J13EBI-400906,EBI-8010314

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 19601959Myosin-9
PRO_0000123417

Regions

Domain2 – 778777Myosin head-like
Domain779 – 80830IQ
Nucleotide binding174 – 1818ATP Potential
Region654 – 67623Actin-binding
Coiled coil841 – 19261086 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.4 Ref.16
Modified residue81N6-acetyllysine Ref.16
Modified residue111Phosphotyrosine By similarity
Modified residue1021N6-acetyllysine By similarity
Modified residue2991N6-acetyllysine Ref.16
Modified residue6131N6-acetyllysine Ref.16
Modified residue7541Phosphotyrosine Ref.9
Modified residue8501N6-succinyllysine Ref.16
Modified residue8601N6-acetyllysine Ref.16
Modified residue9751N6-acetyllysine Ref.16
Modified residue10241N6-acetyllysine Ref.16
Modified residue12491N6-acetyllysine Ref.16
Modified residue13571N6-acetyllysine By similarity
Modified residue13921N6-acetyllysine By similarity
Modified residue14041N6-acetyllysine By similarity
Modified residue14101N6-acetyllysine By similarity
Modified residue14591N6-acetyllysine Ref.16
Modified residue16381N6-acetyllysine By similarity
Modified residue16691N6-succinyllysine Ref.16
Modified residue17141Phosphoserine By similarity
Modified residue17931N6-acetyllysine Ref.16
Modified residue18021N6-acetyllysine Ref.16
Modified residue18451N6-acetyllysine Ref.16
Modified residue19391Phosphothreonine Ref.10 Ref.14
Modified residue19431Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.14

Experimental info

Sequence conflict17331Q → L in CAC85955. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VDD5 [UniParc].

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

FASTA1,960226,372
        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' 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. 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].
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. 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]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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[15]"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.
[16]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-299; LYS-613; LYS-860; LYS-975; LYS-1024; LYS-1249; LYS-1459; LYS-1793; LYS-1802 AND LYS-1845, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-850 AND LYS-1669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+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.
RefSeqNP_071855.2. NM_022410.3.
UniGeneMm.29677.

3D structure databases

ProteinModelPortalQ8VDD5.
SMRQ8VDD5. Positions 7-958, 1894-1934.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201650. 12 interactions.
DIPDIP-29546N.
IntActQ8VDD5. 14 interactions.
MINTMINT-2524850.

PTM databases

PhosphoSiteQ8VDD5.

Proteomic databases

PaxDbQ8VDD5.
PRIDEQ8VDD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016771; ENSMUSP00000016771; ENSMUSG00000022443.
GeneID17886.
KEGGmmu:17886.
UCSCuc007woc.1. mouse.

Organism-specific databases

CTD4627.
MGIMGI:107717. Myh9.

Phylogenomic databases

eggNOGCOG5022.
GeneTreeENSGT00650000092896.
HOGENOMHOG000173958.
HOVERGENHBG004704.
InParanoidQ8VDD5.
KOK10352.
OMAMANSSGK.
OrthoDBEOG71CFK3.
PhylomeDBQ8VDD5.
TreeFamTF333601.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.

Gene expression databases

ArrayExpressQ8VDD5.
BgeeQ8VDD5.
CleanExMM_MYH9.
GenevestigatorQ8VDD5.

Family and domain databases

Gene3D4.10.270.10. 1 hit.
InterProIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS50096. IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYH9. mouse.
NextBio292701.
PROQ8VDD5.
SOURCESearch...

Entry information

Entry nameMYH9_MOUSE
AccessionPrimary (citable) accession number: Q8VDD5
Secondary accession number(s): Q3UHT9 expand/collapse secondary AC list , Q3UHU4, Q6KAN6, Q811I2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 112 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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