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Protein

Myosin-9

Gene

MYH9

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. 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).By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

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):
Myosin heavy chain 9
Myosin heavy chain, non-muscle IIa
Non-muscle myosin heavy chain IIa
Short name:
NMMHC II-a
Short name:
NMMHC-IIA
Gene namesi
Name:MYH9
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 19601959Myosin-9PRO_0000274171Add
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 – 7541PhosphotyrosineBy similarity
Modified residuei850 – 8501N6-succinyllysineBy similarity
Modified residuei860 – 8601N6-acetyllysineBy similarity
Modified residuei975 – 9751N6-acetyllysineBy similarity
Modified residuei1024 – 10241N6-acetyllysineBy similarity
Modified residuei1114 – 11141PhosphoserineBy similarity
Modified residuei1249 – 12491N6-acetyllysineBy similarity
Modified residuei1357 – 13571N6-acetyllysineBy similarity
Modified residuei1392 – 13921N6-acetyllysineBy similarity
Modified residuei1404 – 14041N6-acetyllysineBy similarity
Modified residuei1410 – 14101N6-acetyllysineBy similarity
Modified residuei1459 – 14591N6-acetyllysineBy similarity
Modified residuei1638 – 16381N6-acetyllysineBy similarity
Modified residuei1669 – 16691N6-succinyllysineBy similarity
Modified residuei1714 – 17141PhosphoserineBy similarity
Modified residuei1793 – 17931N6-acetyllysineBy similarity
Modified residuei1802 – 18021N6-acetyllysineBy similarity
Modified residuei1845 – 18451N6-acetyllysineBy similarity
Modified residuei1943 – 19431PhosphoserineBy similarity

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ258K2.
PRIDEiQ258K2.

Interactioni

Subunit structurei

Interacts with PDLIM2 (By similarity). 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) (By similarity). Interacts with SVIL and SLC6A4 (By similarity). Interacts with RASIP1. Interacts with DDR1 and HTRA3 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000002455.

Structurei

3D structure databases

ProteinModelPortaliQ258K2.
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-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili837 – 19261090Sequence 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.
InParanoidiQ258K2.
KOiK10352.

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.
IPR016137. RGS.
[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]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF52540. 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.

Q258K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSDKSG FEPASLKEEV
60 70 80 90 100
GEEAIVELVE NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN
110 120 130 140 150
LKEXYYSGLI YTYSGLFCVV INPYKNLPIY SEEIVEMYKG 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 IPEEEQMGLL 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 LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG
710 720 730 740 750
IRICRQGFPN RVVFQEFRQR YEILTPNSIP KGFMDGKQAC VLMIKALELD
760 770 780 790 800
SNLYRIGQSK VFFRAGVLAH LEEERDLKIT DVIIGFQACC RGYLARKAFA
810 820 830 840 850
KRQQQLTAMK VLQRNCAAYL KLRNWQWWRL FTKVKPLLQV SRQEEEMMAK
860 870 880 890 900
EEELVKVREK QLAAENRLTE METLQSQLMA EKLQLQEQLQ AETELCAEAE
910 920 930 940 950
ELRARLTAKK QELEEICHDL EARVEEEEER CQHLQAEKKK MQQNIQELEE
960 970 980 990 1000
QLEEEESARQ KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR
1010 1020 1030 1040 1050
IAEFTTNLME EEEKSKSLAK LKNKHEAMIT DLEERLRREE KQRQELEKTR
1060 1070 1080 1090 1100
RKLEGDSTDL NDQIAELQAQ IAELKMQLAK KEEELQAALA RVEEEATQKN
1110 1120 1130 1140 1150
MALKKIRELE SQISELQEDL ESERASRNKA EKQKRDLGEE LEALKTELED
1160 1170 1180 1190 1200
TLDSTAAQQE LRSKREQEVN ILKKTLEEEA RTHEAQIQEM RQKHSQAVEE
1210 1220 1230 1240 1250
LAEQLEQTKR VKANLEKAKQ TLENERGELA NEVKVLQQGK GDSEHKRKKA
1260 1270 1280 1290 1300
EAQLQELQVK FTEGERVRTE LADKVTKLQV ELDNVMGLLT QSDSKSSKLT
1310 1320 1330 1340 1350
KDFSALESQL QDTQELLQEE NRQKLSLSTK LKQMEDEKNS FKEQLEEEEE
1360 1370 1380 1390 1400
AKRNLEKQIA TLHAQVTDMK KKMEDGVGCL ETAEEAKRKL QKDLEGLGQR
1410 1420 1430 1440 1450
YEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRRTASNLE KKQKKFDQLL
1460 1470 1480 1490 1500
AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK
1510 1520 1530 1540 1550
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA
1560 1570 1580 1590 1600
TEDAKLRLEV NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED
1610 1620 1630 1640 1650
EKKQRSMAVA ARKKLEMDLK DLEAHIDSAN KNRDEAIKQL RKLQAQMKDC
1660 1670 1680 1690 1700
VRELDDTRAS REEILAQAKE NEKKMKSMEA EMIQLQEELA AAERAKRQAQ
1710 1720 1730 1740 1750
QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE EQGNTELVND
1760 1770 1780 1790 1800
RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KVKLQEMEGT
1810 1820 1830 1840 1850
VKSKYKASIT ALEAKIAQLE EQLDNETKER QAACKQVRRA EKKLKDVLLQ
1860 1870 1880 1890 1900
VDDERRNAEQ FKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL
1910 1920 1930 1940 1950
EDATETADAM NREVSSLKNK LRRGDLPFVV PRRVARKGAG DCSDEEVDGK
1960
ADGAEAKAAE
Length:1,960
Mass (Da):226,469
Last modified:April 18, 2006 - v1
Checksum:i0D287FE27035D521
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM086385 mRNA. Translation: CAJ31056.1.
RefSeqiNP_001104237.1. NM_001110767.1.
UniGeneiCfa.12211.

Genome annotation databases

GeneIDi481280.
KEGGicfa:481280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM086385 mRNA. Translation: CAJ31056.1.
RefSeqiNP_001104237.1. NM_001110767.1.
UniGeneiCfa.12211.

3D structure databases

ProteinModelPortaliQ258K2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000002455.

Proteomic databases

PaxDbiQ258K2.
PRIDEiQ258K2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi481280.
KEGGicfa:481280.

Organism-specific databases

CTDi4627.

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiQ258K2.
KOiK10352.

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.
IPR016137. RGS.
[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]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterization of the canine myosin, heavy polypeptide 9, non-muscle (MYH9) gene on dog chromosome 10q23.2."
    Mieskes K., Wohlke A., Drogemuller C., Distl O.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiMYH9_CANLF
AccessioniPrimary (citable) accession number: Q258K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: April 18, 2006
Last modified: June 8, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.