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Protein

Myosin-10

Gene

Myh10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9 (By similarity). Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi178 – 1858ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • actin filament-based movement Source: MGI
  • actomyosin structure organization Source: MGI
  • adult heart development Source: MGI
  • aorta development Source: MGI
  • axon guidance Source: MGI
  • axonogenesis Source: MGI
  • brain development Source: MGI
  • cardiac myofibril assembly Source: MGI
  • cardiac septum development Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • cell proliferation Source: MGI
  • cerebellar Purkinje cell layer development Source: MGI
  • coronary vasculature development Source: MGI
  • exocytosis Source: MGI
  • fourth ventricle development Source: MGI
  • heart development Source: MGI
  • in utero embryonic development Source: MGI
  • lateral ventricle development Source: MGI
  • mitotic cytokinesis Source: MGI
  • myofibril assembly Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • neuron migration Source: MGI
  • neuron projection development Source: MGI
  • nuclear migration Source: MGI
  • plasma membrane repair Source: MGI
  • regulation of cell shape Source: MGI
  • retina development in camera-type eye Source: MGI
  • substrate-dependent cell migration, cell extension Source: MGI
  • third ventricle development Source: MGI
  • ventricular cardiac muscle cell development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Cell adhesion, Cell shape

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5627123. RHO GTPases activate PAKs.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-10
Alternative name(s):
Cellular myosin heavy chain, type B
Myosin heavy chain 10
Myosin heavy chain, non-muscle IIb
Non-muscle myosin heavy chain B
Short name:
NMMHC-B
Non-muscle myosin heavy chain IIb
Short name:
NMMHC II-b
Short name:
NMMHC-IIB
Gene namesi
Name:Myh10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1930780. Myh10.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • actomyosin Source: MGI
  • axon Source: MGI
  • brush border Source: UniProtKB
  • cell cortex Source: MGI
  • cleavage furrow Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • dendritic spine Source: MGI
  • extracellular exosome Source: MGI
  • growth cone Source: MGI
  • lamellipodium Source: UniProtKB-SubCell
  • midbody Source: MGI
  • mitochondrion Source: MGI
  • myosin complex Source: MGI
  • myosin II complex Source: MGI
  • myosin II filament Source: MGI
  • neuronal cell body Source: MGI
  • neuron projection Source: MGI
  • nucleus Source: MGI
  • stress fiber Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19761976Myosin-10PRO_0000123422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei442 – 4421N6-acetyllysineBy similarity
Modified residuei1145 – 11451PhosphoserineBy similarity
Modified residuei1241 – 12411N6-acetyllysineCombined sources
Modified residuei1301 – 13011N6-acetyllysineCombined sources
Modified residuei1645 – 16451N6-acetyllysineBy similarity
Modified residuei1935 – 19351PhosphoserineBy similarity
Modified residuei1938 – 19381PhosphoserineBy similarity
Modified residuei1939 – 19391PhosphoserineCombined sources
Modified residuei1952 – 19521PhosphoserineCombined sources
Modified residuei1956 – 19561PhosphoserineCombined sources
Modified residuei1960 – 19601PhosphothreonineBy similarity
Modified residuei1962 – 19621PhosphoserineBy similarity
Modified residuei1965 – 19651PhosphoserineBy similarity
Modified residuei1975 – 19751PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by ABL2.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ61879.
MaxQBiQ61879.
PaxDbiQ61879.
PRIDEiQ61879.

PTM databases

iPTMnetiQ61879.
PhosphoSiteiQ61879.
SwissPalmiQ61879.

Expressioni

Tissue specificityi

In newborn kidney, expressed in the mesenchyme and ureteric buds.1 Publication

Gene expression databases

BgeeiQ61879.
CleanExiMM_MYH10.
ExpressionAtlasiQ61879. baseline and differential.
GenevisibleiQ61879. MM.

Interactioni

Subunit structurei

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 PLEKHG6 (By similarity). Interacts with ECM29 (By similarity). Interacts with LARP6 (By similarity). Interacts with MCC (By similarity). Interacts with KIF26B.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi218774. 147 interactions.
DIPiDIP-31956N.
IntActiQ61879. 152 interactions.
MINTiMINT-4102674.
STRINGi10090.ENSMUSP00000099671.

Structurei

3D structure databases

ProteinModelPortaliQ61879.
SMRiQ61879. Positions 7-963.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 783699Myosin motorAdd
BLAST
Domaini786 – 81530IQPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili845 – 19761132Sequence analysisAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 IQ domain.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0160. Eukaryota.
KOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiQ61879.
KOiK10352.
OrthoDBiEOG71CFK3.
PhylomeDBiQ61879.
TreeFamiTF333601.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR008989. Myosin_S1_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI
60 70 80 90 100
KEERGDEVMV ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS
110 120 130 140 150
VLHNLKDRYY SGLIYTYSGL FCVVINPYKN LPIYSENIIE MYRGKKRHEM
160 170 180 190 200
PPHIYAISES AYRCMLQDRE DQSILCTGES GAGKTENTKK VIQYLAHVAS
210 220 230 240 250
SHKGRKDHNI PGELERQLLQ ANPILESFGN AKTVKNDNSS RFGKFIRINF
260 270 280 290 300
DVTGYIVGAN IETYLLEKSR AVRQAKDERT FHIFYQLLSG AGEHLKSDLL
310 320 330 340 350
LEGFNNYRFL SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV
360 370 380 390 400
SSVLQFGNIS FKKERNTDQA SMPENTVAQK LCHLLGMNVM EFTRAILTPR
410 420 430 440 450
IKVGRDYVQK AQTKEQADFA VEALAKATYE RLFRWLVHRI NKALDRTKRQ
460 470 480 490 500
GASFIGILDI AGFEIFELNS FEQLCINYTN EKLQQLFNHT MFILEQEEYQ
510 520 530 540 550
REGIEWNFID FGLDLQPCID LIERPANPPG VLALLDEECW FPKATDKTFV
560 570 580 590 600
EKLVQEQGSH SKFQKPRQLK DKADFCIIHY AGKVDYKADE WLMKNMDPLN
610 620 630 640 650
DNVATLLHQS SDRFVAELWK DVDRIVGLDQ VTGMTETAFG SAYKTKKGMF
660 670 680 690 700
RTVGQLYKES LTKLMATLRN TNPNFVRCII PNHEKRAGKL DPHLVLDQLR
710 720 730 740 750
CNGVLEGIRI CRQGFPNRIV FQEFRQRYEI LTPNAIPKGF MDGKQACERM
760 770 780 790 800
IRALELDPNL YRIGQSKIFF RAGVLAHLEE ERDLKITDII IFFQAVCRGY
810 820 830 840 850
LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR HWQWWRVFTK VKPLLQVTRQ
860 870 880 890 900
EEELQAKDEE LLKVKEKQTK VEGELEEMER KHQQLLEEKN ILAEQLQAET
910 920 930 940 950
ELFAEAEEMR ARLAAKKQEL EEILHDLESR VEEEEERNQI LQNEKKKMQA
960 970 980 990 1000
HIQDLEEQLD EEEGARQKLQ LEKVTAEAKI KKMEEEVLLL EDQNSKFIKE
1010 1020 1030 1040 1050
KKLMEDRIAE CSSQLAEEEE KAKNLAKIRN KQEVMISDLE ERLKKEEKTR
1060 1070 1080 1090 1100
QELEKAKRKL DGETTDLQDQ IAELQAQVDE LKVQLTKKEE ELQGALARGD
1110 1120 1130 1140 1150
DETLHKNNAL KVARELQAQI AELQEDFESE KASRNKAEKQ KRDLSEELEA
1160 1170 1180 1190 1200
LKTELEDTLD TTAAQQELRT KREQEVAELK KALEDETKNH EAQIQDMRQR
1210 1220 1230 1240 1250
HATALEELSE QLEQAKRFKA NLEKNKQGLE TDNKELACEV KVLQQVKAES
1260 1270 1280 1290 1300
EHKRKKLDAQ VQELHAKVSE GDRLRVELAE KANKLQNELD NVSTLLEEAE
1310 1320 1330 1340 1350
KKGIKFAKDA AGLESQLQDT QELLQEETRQ KLNLSSRIRQ LEEEKNSLQE
1360 1370 1380 1390 1400
QQEEEEEARK NLEKQVLALQ SQLADTKKKV DDDLGTIESL EEAKKKLLKD
1410 1420 1430 1440 1450
VEALSQRLEE KVLAYDKLEK TKNRLQQELD DLTVDLDHQR QIVSNLEKKQ
1460 1470 1480 1490 1500
KKFDQLLAEE KGISARYAEE RDRAEAEARE KETKALSLAR ALEEALEAKE
1510 1520 1530 1540 1550
EFERQNKQLR ADMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE
1560 1570 1580 1590 1600
LEDELQATED AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK KRLLLKQVRE
1610 1620 1630 1640 1650
LEAELEDERK QRALAVASKK KMEIDLKDLE AQIEAANKAR DEVIKQLRKL
1660 1670 1680 1690 1700
QAQMKDYQRE LEEARASRDE IFAQSKESEK KLKSLEAEIL QLQEELASSE
1710 1720 1730 1740 1750
RARRHAEQER DELADEIANS ASGKSALLDE KRRLEARIAQ LEEELEEEQS
1760 1770 1780 1790 1800
NMELLNDRFR KTTLQVDTLN TELAAERSAA QKSDNARQQL ERQNKELKAK
1810 1820 1830 1840 1850
LQELEGAVKS KFKATISALE AKIGQLEEQL EQEAKERAAA NKLVRRTEKK
1860 1870 1880 1890 1900
LKEIFMQVED ERRHADQYKE QMEKANARMK QLKRQLEEAE EEATRANASR
1910 1920 1930 1940 1950
RKLQRELDDA TEANEGLSRE VSTLKNRLRR GGPISFSSSR SGRRQLHIEG
1960 1970
ASLELSDDDT ESKTSDVNDT QPPQSE
Length:1,976
Mass (Da):228,996
Last modified:July 19, 2005 - v2
Checksum:iD00F922EB6682AEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL645644, AL603662 Genomic DNA. Translation: CAI25576.1.
AL603662, AL645644 Genomic DNA. Translation: CAI25528.1.
BC089011 mRNA. Translation: AAH89011.1.
AH003264 Genomic DNA. Translation: AAA84879.1.
CCDSiCCDS24869.1.
RefSeqiNP_780469.1. NM_175260.2.
UniGeneiMm.218233.

Genome annotation databases

EnsembliENSMUST00000102611; ENSMUSP00000099671; ENSMUSG00000020900.
GeneIDi77579.
KEGGimmu:77579.
UCSCiuc007jny.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL645644, AL603662 Genomic DNA. Translation: CAI25576.1.
AL603662, AL645644 Genomic DNA. Translation: CAI25528.1.
BC089011 mRNA. Translation: AAH89011.1.
AH003264 Genomic DNA. Translation: AAA84879.1.
CCDSiCCDS24869.1.
RefSeqiNP_780469.1. NM_175260.2.
UniGeneiMm.218233.

3D structure databases

ProteinModelPortaliQ61879.
SMRiQ61879. Positions 7-963.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218774. 147 interactions.
DIPiDIP-31956N.
IntActiQ61879. 152 interactions.
MINTiMINT-4102674.
STRINGi10090.ENSMUSP00000099671.

PTM databases

iPTMnetiQ61879.
PhosphoSiteiQ61879.
SwissPalmiQ61879.

Proteomic databases

EPDiQ61879.
MaxQBiQ61879.
PaxDbiQ61879.
PRIDEiQ61879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102611; ENSMUSP00000099671; ENSMUSG00000020900.
GeneIDi77579.
KEGGimmu:77579.
UCSCiuc007jny.1. mouse.

Organism-specific databases

CTDi4628.
MGIiMGI:1930780. Myh10.

Phylogenomic databases

eggNOGiKOG0160. Eukaryota.
KOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiQ61879.
KOiK10352.
OrthoDBiEOG71CFK3.
PhylomeDBiQ61879.
TreeFamiTF333601.

Enzyme and pathway databases

ReactomeiR-MMU-5627123. RHO GTPases activate PAKs.

Miscellaneous databases

NextBioi347140.
PROiQ61879.
SOURCEiSearch...

Gene expression databases

BgeeiQ61879.
CleanExiMM_MYH10.
ExpressionAtlasiQ61879. baseline and differential.
GenevisibleiQ61879. MM.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR008989. Myosin_S1_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Characterization of the nonmuscle myosin heavy chain IIB promoter: regulation by E2F."
    Weir L., Chen D.
    Gene Expr. 6:45-57(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
  4. "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-1952 AND SER-1956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Use of a chemical genetic technique to identify myosin IIb as a substrate of the Abl-related gene (Arg) tyrosine kinase."
    Boyle S.N., Koleske A.J.
    Biochemistry 46:11614-11620(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1952 AND SER-1956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "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-1956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND SER-1956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. Cited for: INTERACTION WITH KIF26B, TISSUE SPECIFICITY.
  10. "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 LYS-1241 AND LYS-1301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiMYH10_MOUSE
AccessioniPrimary (citable) accession number: Q61879
Secondary accession number(s): Q5SV63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 19, 2005
Last modified: April 13, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Represents a conventional non-muscle myosin. This protein should not be confused with the unconventional myosin-10 (MYO10).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.