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Protein

Myosin-9

Gene

Myh9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 1818ATPSequence analysis

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • follicle-stimulating hormone receptor binding Source: RGD
  • microfilament motor activity Source: UniProtKB
  • protein anchor Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: RGD
  • sodium:potassium-exchanging ATPase activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • actin filament-based movement Source: UniProtKB
  • angiogenesis Source: UniProtKB
  • ATP hydrolysis coupled transmembrane transport Source: GOC
  • blood vessel endothelial cell migration Source: UniProtKB
  • cell adhesion Source: UniProtKB-KW
  • cytokinesis Source: UniProtKB
  • establishment or maintenance of transmembrane electrochemical gradient Source: GOC
  • membrane protein ectodomain proteolysis Source: UniProtKB
  • monocyte differentiation Source: UniProtKB
  • platelet formation Source: UniProtKB
  • positive regulation of calcium ion transport into cytosol Source: RGD
  • positive regulation of endocytosis Source: RGD
  • positive regulation of phagocytosis Source: RGD
  • protein transport Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
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

Names & Taxonomyi

Protein namesi
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 namesi
Name:Myh9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3140. Myh9.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • actomyosin contractile ring Source: UniProtKB
  • cell leading edge Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • lateral plasma membrane Source: RGD
  • myosin complex Source: UniProtKB-KW
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • protein complex Source: UniProtKB
  • ruffle Source: UniProtKB
  • stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 19611960Myosin-9PRO_0000123418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei8 – 81N6-acetyllysineBy similarity
Modified residuei11 – 111PhosphotyrosineBy similarity
Modified residuei102 – 1021N6-acetyllysineBy similarity
Modified residuei299 – 2991N6-acetyllysineBy similarity
Modified residuei613 – 6131N6-acetyllysineBy similarity
Modified residuei628 – 6281PhosphoserineBy similarity
Modified residuei754 – 7541PhosphotyrosineCombined sources
Modified residuei850 – 8501N6-succinyllysineBy similarity
Modified residuei860 – 8601N6-acetyllysineBy similarity
Modified residuei975 – 9751N6-acetyllysineBy similarity
Modified residuei1024 – 10241N6-acetyllysineBy similarity
Modified residuei1114 – 11141PhosphoserineCombined sources
Modified residuei1249 – 12491N6-acetyllysineBy similarity
Modified residuei1358 – 13581N6-acetyllysineBy similarity
Modified residuei1393 – 13931N6-acetyllysineBy similarity
Modified residuei1405 – 14051N6-acetyllysineBy similarity
Modified residuei1411 – 14111N6-acetyllysineBy similarity
Modified residuei1460 – 14601N6-acetyllysineBy similarity
Modified residuei1639 – 16391N6-acetyllysineBy similarity
Modified residuei1670 – 16701N6-succinyllysineBy similarity
Modified residuei1715 – 17151PhosphoserineCombined sources
Modified residuei1794 – 17941N6-acetyllysineBy similarity
Modified residuei1803 – 18031N6-acetyllysineBy similarity
Modified residuei1846 – 18461N6-acetyllysineBy similarity
Modified residuei1940 – 19401PhosphothreonineBy similarity
Modified residuei1944 – 19441PhosphoserineCombined sources

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ62812.
PRIDEiQ62812.

PTM databases

iPTMnetiQ62812.
PhosphoSiteiQ62812.
SwissPalmiQ62812.

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 SVIL, RASIP1, HTRA3 and DDR1 (By similarity). Interacts with PDLIM2 AND SLC6A4.By similarity2 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • follicle-stimulating hormone receptor binding Source: RGD
  • protein anchor Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi247773. 2 interactions.
IntActiQ62812. 2 interactions.
MINTiMINT-2778870.
STRINGi10116.ENSRNOP00000035440.

Structurei

3D structure databases

ProteinModelPortaliQ62812.
SMRiQ62812. Positions 7-806.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 776696Myosin motorAdd
BLAST
Domaini779 – 80830IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni654 – 67623Actin-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili841 – 19271087Sequence 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

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiQ62812.
PhylomeDBiQ62812.

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.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00063. 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]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62812-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQQAADKYL YVDKNFINNP LAQADCGAKK LVWVPSTKNG FEPASLKEEV
60 70 80 90 100
GEEAIVELVE NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN
110 120 130 140 150
LKERYYSGLI YTYSGLFCVV INPYKNLPIY SEEIVDMYKG KKRHEMPPHI
160 170 180 190 200
YAITDTAYRS MMQDREDQSI LCTGESGAGK TENTKKVIQY LAHVASSHKS
210 220 230 240 250
KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR INFDVNGYIV
260 270 280 290 300
GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY
310 320 330 340 350
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEDEQMGLL RVISGVLQLG
360 370 380 390 400
NIVFKKERNT DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY
410 420 430 440 450
VQKAQTKEQA DFAIEALAKA TYERMFRWLV LRINKALDKT KRQGASFIGI
460 470 480 490 500
LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF NHTMFILEQE EYQREGIEWN
510 520 530 540 550
FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK SFVEKVVQEQ
560 570 580 590 600
GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL
610 620 630 640 650
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY
660 670 680 690 700
KEQLAKLMAT LRNTNPNFVC CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG
710 720 730 740 750
IRICRQGFPN RVVFQEFRQR YEILTPNSIP KGFMDGKQAC VLMIKALELD
760 770 780 790 800
SNLYRIGQSK VFFRSGVLAH LEEERDLKIT DVIIGFQACC RGYLARKAFA
810 820 830 840 850
KRQQQLTAMK VLQRNCAAYL RLRNWQWWRL FTKVKPLLNS IRHEDELLAK
860 870 880 890 900
EAELTKVREK HLAAENRLTE METMQSQLMA EKLQLQEQLQ AKTELCAEAE
910 920 930 940 950
ELRARLTAKK QELEEICHDL EARVEEEEER CQYLQAEKKK MQQNIQELEE
960 970 980 990 1000
QLEEEESARQ KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR
1010 1020 1030 1040 1050
VAEFTTDLME EEEKSKSLAK LKNKHEAMIT DLEERLRREE KQRQELEKTR
1060 1070 1080 1090 1100
RKLEGDSTDL SDQIAELQAQ IAELKMQLAK KEEELQAALA RVEEEAAQKN
1110 1120 1130 1140 1150
MALKKIRELE TQISELQEDL ESERACRNKA EKQKRDLGEE LEALKTELED
1160 1170 1180 1190 1200
TLDSTAAQQE LRSKREQEVS ILKKTLEDEA KTHEAQIQEM RQKHSQAVEE
1210 1220 1230 1240 1250
LAEQLEQTKR VKATLEKAKQ TLENERGELA NEVKALLQGK GDSEHKRKKV
1260 1270 1280 1290 1300
EAQLQELQVK FSEGERVRTE LADKVSKLQV ELDSVTGLLN QSDSKSSKLT
1310 1320 1330 1340 1350
KDFSALESQL QDTQELLQEE NRQKLSLSTK LKQMEDEKNS FREQLEEEEE
1360 1370 1380 1390 1400
EAKRNLEKQI ATLHAQVTDM KKKMEDGVGC LETAEEAKRR LQKDLEGLSQ
1410 1420 1430 1440 1450
RLEEKVAAYD KLEKTKTRLQ QELDDLLVDL DHQRQSVSNL EKKQKKFDQL
1460 1470 1480 1490 1500
LAEEKTISAK YAEERDRAEA EAREKETKAL SLARALEEAM EQKAELERLN
1510 1520 1530 1540 1550
KQFRTEMEDL MSSKDDVGKS VHELEKSNRA LEQQVEEMKT QLEELEDELQ
1560 1570 1580 1590 1600
ATEDAKLRLE VNLQAMKAQF ERDLQGRDEQ SEEKKKQLVR QVREMEAELE
1610 1620 1630 1640 1650
DERKQRSIAM AARKKLEMDL KDLEAHIDTA NKNREEAIKQ LRKLQAQMKD
1660 1670 1680 1690 1700
CMRDVDDTRA SREEILAQAK ENEKKLKSME AEMIQLQEEL AAAERAKRQA
1710 1720 1730 1740 1750
QQERDELADE IANSSGKGAL ALEEKRRLEA LIALLEEELE EEQGNTELIN
1760 1770 1780 1790 1800
DRLKKANLQI DQINTDLNLE RSHAQKNENA RQQLERQNKE LKAKLQEMES
1810 1820 1830 1840 1850
AVKSKYKASI AALEAKIAQL EEQLDNETKE RQAASKQVRR AEKKLKDVLL
1860 1870 1880 1890 1900
QVEDERRNAE QFKDQADKAS TRLKQLKRQL EEAEEEAQRA NASRRKLQRE
1910 1920 1930 1940 1950
LEDATETADA MNREVSSLKN KLRRGDMPFV VTRRIVRKGT GDCSDEEVDG
1960
KADGADAKAT E
Length:1,961
Mass (Da):226,338
Last modified:January 23, 2007 - v3
Checksum:i9B9876D9681FB19E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31463 mRNA. Translation: AAA74950.1.
UniGeneiRn.11385.
Rn.183891.

Genome annotation databases

UCSCiRGD:3140. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31463 mRNA. Translation: AAA74950.1.
UniGeneiRn.11385.
Rn.183891.

3D structure databases

ProteinModelPortaliQ62812.
SMRiQ62812. Positions 7-806.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247773. 2 interactions.
IntActiQ62812. 2 interactions.
MINTiMINT-2778870.
STRINGi10116.ENSRNOP00000035440.

PTM databases

iPTMnetiQ62812.
PhosphoSiteiQ62812.
SwissPalmiQ62812.

Proteomic databases

PaxDbiQ62812.
PRIDEiQ62812.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3140. rat.

Organism-specific databases

RGDi3140. Myh9.

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiQ62812.
PhylomeDBiQ62812.

Miscellaneous databases

PROiQ62812.

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.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00063. 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]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA encoding rat myosin heavy chain-A and evidence for the absence of myosin heavy chain-B in cultured rat mast (RBL-2H3) cells."
    Choi O.H., Park C., Itoh K., Adelstein R.S., Beaven M.A.
    J. Muscle Res. Cell Motil. 17:69-77(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 181-199; 546-555; 618-639; 1241-1248; 1402-1411; 1446-1455; 1474-1478; 1557-1567; 1605-1614; 1793-1803 AND 1925-1934, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Glycosyl modification facilitates homo- and hetero-oligomerization of the serotonin transporter. A specific role for sialic acid residues."
    Ozaslan D., Wang S., Ahmed B.A., Kocabas A.M., McCastlain J.C., Bene A., Kilic F.
    J. Biol. Chem. 278:43991-44000(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC6A4.
  4. "Pdlim2, a novel PDZ-LIM domain protein, interacts with alpha-actinins and filamin A."
    Torrado M., Senatorov V.V., Trivedi R., Fariss R.N., Tomarev S.I.
    Invest. Ophthalmol. Vis. Sci. 45:3955-3963(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDLIM2.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754; SER-1114; SER-1715 AND SER-1944, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMYH9_RAT
AccessioniPrimary (citable) accession number: Q62812
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.