Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Nucleotide bindingi174 – 181ATPSequence analysis8

GO - Molecular functioni

  • actin binding Source: RGD
  • actin-dependent ATPase activity Source: RGD
  • actin filament binding Source: UniProtKB
  • ADP binding Source: RGD
  • ATPase activity Source: UniProtKB
  • ATP binding Source: RGD
  • cadherin binding Source: RGD
  • calmodulin binding Source: UniProtKB-KW
  • follicle-stimulating hormone receptor binding Source: RGD
  • G-protein alpha-subunit binding Source: RGD
  • identical protein binding Source: RGD
  • microfilament motor activity Source: UniProtKB
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: RGD
  • protein membrane anchor Source: UniProtKB
  • RNA binding Source: RGD
  • scaffold protein binding Source: RGD
  • sodium:potassium-exchanging ATPase activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: RGD
  • actin filament-based movement Source: UniProtKB
  • actin filament bundle assembly Source: RGD
  • actin filament bundle distribution Source: RGD
  • actomyosin structure organization Source: RGD
  • angiogenesis Source: UniProtKB
  • blood vessel endothelial cell migration Source: UniProtKB
  • cell adhesion Source: RGD
  • cell-cell adhesion Source: RGD
  • cell morphogenesis involved in differentiation Source: RGD
  • cellular response to mechanical stimulus Source: RGD
  • cellular response to platelet-derived growth factor stimulus Source: RGD
  • cytokinetic process Source: UniProtKB
  • establishment of meiotic spindle localization Source: RGD
  • establishment of T cell polarity Source: RGD
  • follicle-stimulating hormone signaling pathway Source: RGD
  • in utero embryonic development Source: RGD
  • meiotic spindle organization Source: RGD
  • membrane protein ectodomain proteolysis Source: UniProtKB
  • monocyte differentiation Source: UniProtKB
  • myoblast fusion Source: RGD
  • negative regulation of actin filament severing Source: RGD
  • negative regulation of vascular associated smooth muscle cell migration Source: RGD
  • phagocytosis, engulfment Source: RGD
  • platelet aggregation Source: RGD
  • platelet formation Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: RGD
  • positive regulation of endocytosis Source: RGD
  • positive regulation of ERK1 and ERK2 cascade Source: RGD
  • positive regulation of focal adhesion assembly Source: RGD
  • positive regulation of G-protein coupled receptor protein signaling pathway Source: RGD
  • positive regulation of inositol trisphosphate biosynthetic process Source: RGD
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: RGD
  • positive regulation of phagocytosis Source: RGD
  • positive regulation of protein processing in phagocytic vesicle Source: RGD
  • protein transport Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • uropod organization Source: RGD

Keywordsi

Molecular functionActin-binding, Calmodulin-binding, Motor protein, Myosin
Biological processCell adhesion, Cell shape
LigandATP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3140. Myh9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001234182 – 1961Myosin-9Add BLAST1960

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei8N6-acetyllysineBy similarity1
Modified residuei11PhosphotyrosineBy similarity1
Modified residuei102N6-acetyllysineBy similarity1
Modified residuei299N6-acetyllysineBy similarity1
Modified residuei435N6-acetyllysineBy similarity1
Modified residuei613N6-acetyllysineBy similarity1
Modified residuei628PhosphoserineBy similarity1
Modified residuei754PhosphotyrosineCombined sources1
Modified residuei850N6-succinyllysineBy similarity1
Modified residuei860N6-acetyllysineBy similarity1
Modified residuei975N6-acetyllysineBy similarity1
Modified residuei1024N6-acetyllysineBy similarity1
Modified residuei1114PhosphoserineCombined sources1
Modified residuei1234N6-acetyllysineBy similarity1
Modified residuei1249N6-acetyllysineBy similarity1
Modified residuei1358N6-acetyllysineBy similarity1
Modified residuei1393N6-acetyllysineBy similarity1
Modified residuei1405N6-acetyllysineBy similarity1
Modified residuei1411N6-acetyllysineBy similarity1
Modified residuei1460N6-acetyllysineBy similarity1
Modified residuei1639N6-acetyllysineBy similarity1
Modified residuei1670N6-succinyllysineBy similarity1
Modified residuei1715PhosphoserineCombined sources1
Modified residuei1794N6-acetyllysineBy similarity1
Modified residuei1803N6-acetyllysineBy similarity1
Modified residuei1846N6-acetyllysineBy similarity1
Modified residuei1924Omega-N-methylarginineBy similarity1
Modified residuei1944PhosphoserineCombined sources1

Post-translational modificationi

ISGylated.By similarity
Ubiquitination.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ62812.
PRIDEiQ62812.

PTM databases

iPTMnetiQ62812.
PhosphoSitePlusiQ62812.
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 RASIP1 (By similarity). Interacts with DDR1 (By similarity). Interacts with SLC6A4 (PubMed:12944413). Interacts with PDLIM2 (PubMed:15505042). Interacts with SVIL (By similarity). Interacts with HTRA3 (By similarity). Interacts with Myo7a (By similarity). Interacts with C9orf135 homolog (By similarity).By similarity2 Publications

GO - Molecular functioni

  • actin binding Source: RGD
  • actin filament binding Source: UniProtKB
  • cadherin binding Source: RGD
  • calmodulin binding Source: UniProtKB-KW
  • follicle-stimulating hormone receptor binding Source: RGD
  • G-protein alpha-subunit binding Source: RGD
  • identical protein binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: RGD
  • protein membrane anchor Source: UniProtKB
  • scaffold protein binding Source: RGD

Protein-protein interaction databases

BioGridi247773. 3 interactors.
CORUMiQ62812.
IntActiQ62812. 4 interactors.
MINTiMINT-2778870.
STRINGi10116.ENSRNOP00000035440.

Structurei

3D structure databases

ProteinModelPortaliQ62812.
SMRiQ62812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 77Myosin N-terminal SH3-likePROSITE-ProRule annotationAdd BLAST51
Domaini81 – 776Myosin motorPROSITE-ProRule annotationAdd BLAST696
Domaini779 – 808IQPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni654 – 676Actin-bindingAdd BLAST23

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili841 – 1927Sequence analysisAdd BLAST1087

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

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

Family and domain databases

Gene3Di2.30.30.360. 1 hit.
InterProiView protein in InterPro
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR008989. Myosin_S1_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
PfamiView protein in Pfam
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
PRINTSiPR00193. MYOSINHEAVY.
SMARTiView protein in SMART
SM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiView protein in PROSITE
PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
PS51844. SH3_LIKE. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiMYH9_RAT
AccessioniPrimary (citable) accession number: Q62812
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 147 of the entry and version 3 of the sequence. See 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