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Protein

Myosin-11

Gene

MYH11

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Muscle contraction.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi177 – 184ATP8

GO - Molecular functioni

  • actin binding Source: CAFA
  • actin-dependent ATPase activity Source: CAFA
  • ADP binding Source: CAFA
  • ATP binding Source: CAFA
  • calmodulin binding Source: UniProtKB-KW
  • magnesium ion binding Source: CAFA
  • microfilament motor activity Source: CAFA
  • myosin II binding Source: CAFA
  • myosin light chain binding Source: CAFA
  • protein heterodimerization activity Source: CAFA
  • structural constituent of muscle Source: CAFA

GO - Biological processi

Keywordsi

Molecular functionActin-binding, Calmodulin-binding, Motor protein, Muscle protein, Myosin
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-GGA-445355. Smooth Muscle Contraction.
R-GGA-5627123. RHO GTPases activate PAKs.
SABIO-RKiP10587.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-11
Alternative name(s):
Myosin heavy chain 11
Myosin heavy chain, gizzard smooth muscle
Gene namesi
Name:MYH11
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 14

Subcellular locationi

GO - Cellular componenti

  • muscle myosin complex Source: CAFA
  • myofibril Source: UniProtKB-SubCell
  • myosin filament Source: UniProtKB-KW

Keywords - Cellular componenti

Cytoplasm, Thick filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001234292 – 1979Myosin-11Add BLAST1978

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2Blocked amino end (Ser)1 Publication1
Modified residuei128N6,N6,N6-trimethyllysine1 Publication1

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP10587.
PRIDEiP10587.

Expressioni

Gene expression databases

ExpressionAtlasiP10587. baseline.

Interactioni

Subunit structurei

Muscle 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).

Binary interactionsi

WithEntry#Exp.IntActNotes
MYL6P026072EBI-1027098,EBI-1027073

GO - Molecular functioni

  • actin binding Source: CAFA
  • calmodulin binding Source: UniProtKB-KW
  • myosin II binding Source: CAFA
  • myosin light chain binding Source: CAFA
  • protein heterodimerization activity Source: CAFA

Protein-protein interaction databases

IntActiP10587. 1 interactor.
STRINGi9031.ENSGALP00000032964.

Structurei

Secondary structure

11979
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Helixi23 – 28Combined sources6
Beta strandi34 – 39Combined sources6
Turni40 – 42Combined sources3
Beta strandi43 – 53Combined sources11
Beta strandi56 – 61Combined sources6
Turni62 – 64Combined sources3
Beta strandi67 – 71Combined sources5
Helixi72 – 74Combined sources3
Helixi81 – 83Combined sources3
Helixi89 – 91Combined sources3
Helixi97 – 109Combined sources13
Beta strandi114 – 116Combined sources3
Beta strandi118 – 124Combined sources7
Helixi131 – 133Combined sources3
Helixi135 – 141Combined sources7
Helixi146 – 148Combined sources3
Helixi153 – 167Combined sources15
Beta strandi171 – 176Combined sources6
Helixi183 – 197Combined sources15
Helixi219 – 224Combined sources6
Helixi227 – 235Combined sources9
Beta strandi236 – 239Combined sources4
Beta strandi245 – 256Combined sources12
Beta strandi258 – 260Combined sources3
Beta strandi262 – 270Combined sources9
Helixi274 – 277Combined sources4
Helixi288 – 296Combined sources9
Helixi299 – 304Combined sources6
Helixi310 – 312Combined sources3
Helixi328 – 342Combined sources15
Helixi346 – 362Combined sources17
Turni371 – 373Combined sources3
Beta strandi375 – 377Combined sources3
Helixi382 – 391Combined sources10
Helixi395 – 403Combined sources9
Beta strandi406 – 408Combined sources3
Beta strandi410 – 414Combined sources5
Helixi420 – 450Combined sources31
Turni451 – 453Combined sources3
Beta strandi458 – 465Combined sources8
Beta strandi473 – 475Combined sources3
Helixi477 – 506Combined sources30
Helixi517 – 521Combined sources5
Helixi522 – 529Combined sources8
Beta strandi532 – 534Combined sources3
Helixi537 – 545Combined sources9
Helixi552 – 563Combined sources12
Beta strandi569 – 571Combined sources3
Turni576 – 578Combined sources3
Beta strandi580 – 585Combined sources6
Beta strandi588 – 593Combined sources6
Helixi597 – 602Combined sources6
Helixi607 – 614Combined sources8
Helixi619 – 624Combined sources6
Helixi659 – 675Combined sources17
Beta strandi677 – 685Combined sources9
Helixi698 – 707Combined sources10
Helixi710 – 718Combined sources9
Beta strandi723 – 726Combined sources4
Helixi727 – 734Combined sources8
Turni735 – 737Combined sources3
Beta strandi740 – 742Combined sources3
Helixi749 – 758Combined sources10
Turni759 – 761Combined sources3
Beta strandi766 – 769Combined sources4
Beta strandi771 – 776Combined sources6
Turni778 – 784Combined sources7
Helixi793 – 819Combined sources27

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BR1X-ray3.50A/C/E/G3-819[»]
1BR2X-ray2.90A/B/C/D/E/F3-792[»]
1BR4X-ray3.62A/C/E/G3-819[»]
1I84electron microscopy20.00S/V2-1175[»]
3DTPelectron microscopy20.00A/B3-852[»]
3J04electron microscopy-A/D2-910[»]
5M05X-ray2.67A1-790[»]
5T45X-ray2.80A1-790[»]
DisProtiDP00102.
ProteinModelPortaliP10587.
SMRiP10587.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10587.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini84 – 789Myosin motorAdd BLAST706
Domaini792 – 821IQPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni667 – 689Actin-bindingAdd BLAST23
Regioni768 – 782Actin-bindingAdd BLAST15
Regioni850 – 1979Rodlike tail (S2 and LMM domains)Add BLAST1130

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili850 – 1979Sequence analysisAdd BLAST1130

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.
Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2).Curated

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiP10587.
PhylomeDBiP10587.
TreeFamiTF333601.

Family and domain databases

InterProiView protein in InterPro
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_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.

Sequencei

Sequence statusi: Complete.

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

P10587-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKPLSDDE KFLFVDKNFV NNPLAQADWS AKKLVWVPSE KHGFEAASIK
60 70 80 90 100
EEKGDEVTVE LQENGKKVTL SKDDIQKMNP PKFSKVEDMA ELTCLNEASV
110 120 130 140 150
LHNLRERYFS GLIYTYSGLF CVVINPYKQL PIYSEKIIDM YKGKKRHEMP
160 170 180 190 200
PHIYAIADTA YRSMLQDRED QSILCTGESG AGKTENTKKV IQYLAVVASS
210 220 230 240 250
HKGKKDTSIT QGPSFSYGEL EKQLLQANPI LEAFGNAKTV KNDNSSRFGK
260 270 280 290 300
FIRINFDVTG YIVGANIETY LLEKSRAIRQ AKDERTFHIF YYLIAGASEQ
310 320 330 340 350
MRNDLLLEGF NNYTFLSNGH VPIPAQQDDE MFQETLEAMT IMGFTEEEQT
360 370 380 390 400
SILRVVSSVL QLGNIVFKKE RNTDQASMPD NTAAQKVCHL MGINVTDFTR
410 420 430 440 450
SILTPRIKVG RDVVQKAQTK EQADFAIEAL AKAKFERLFR WILTRVNKAL
460 470 480 490 500
DKTKRQGASF LGILDIAGFE IFEINSFEQL CINYTNEKLQ QLFNHTMFIL
510 520 530 540 550
EQEEYQREGI EWNFIDFGLD LQPCIELIER PTNPPGVLAL LDEECWFPKA
560 570 580 590 600
TDTSFVEKLI QEQGNHAKFQ KSKQLKDKTE FCILHYAGKV TYNASAWLTK
610 620 630 640 650
NMDPLNDNVT SLLNQSSDKF VADLWKDVDR IVGLDQMAKM TESSLPSASK
660 670 680 690 700
TKKGMFRTVG QLYKEQLTKL MTTLRNTNPN FVRCIIPNHE KRAGKLDAHL
710 720 730 740 750
VLEQLRCNGV LEGIRICRQG FPNRIVFQEF RQRYEILAAN AIPKGFMDGK
760 770 780 790 800
QACILMIKAL ELDPNLYRIG QSKIFFRTGV LAHLEEERDL KITDVIIAFQ
810 820 830 840 850
AQCRGYLARK AFAKRQQQLT AMKVIQRNCA AYLKLRNWQW WRLFTKVKPL
860 870 880 890 900
LQVTRQEEEM QAKDEELQRT KERQQKAEAE LKELEQKHTQ LCEEKNLLQE
910 920 930 940 950
KLQAETELYA EAEEMRVRLA AKKQELEEIL HEMEARIEEE EERSQQLQAE
960 970 980 990 1000
KKKMQQQMLD LEEQLEEEEA ARQKLQLEKV TADGKIKKME DDILIMEDQN
1010 1020 1030 1040 1050
NKLTKERKLL EERVSDLTTN LAEEEEKAKN LTKLKNKHES MISELEVRLK
1060 1070 1080 1090 1100
KEEKSRQELE KIKRKLEGES SDLHEQIAEL QAQIAELKAQ LAKKEEELQA
1110 1120 1130 1140 1150
ALARLEDETS QKNNALKKIR ELESHISDLQ EDLESEKAAR NKAEKQKRDL
1160 1170 1180 1190 1200
SEELEALKTE LEDTLDTTAT QQELRAKREQ EVTVLKRALE EETRTHEAQV
1210 1220 1230 1240 1250
QEMRQKHTQA VEELTEQLEQ FKRAKANLDK TKQTLEKDNA DLANEIRSLS
1260 1270 1280 1290 1300
QAKQDVEHKK KKLEVQLQDL QSKYSDGERV RTELNEKVHK LQIEVENVTS
1310 1320 1330 1340 1350
LLNEAESKNI KLTKDVATLG SQLQDTQELL QEETRQKLNV TTKLRQLEDD
1360 1370 1380 1390 1400
KNSLQEQLDE EVEAKQNLER HISTLTIQLS DSKKKLQEFT ATVETMEEGK
1410 1420 1430 1440 1450
KKLQREIESL TQQFEEKAAS YDKLEKTKNR LQQELDDLVV DLDNQRQLVS
1460 1470 1480 1490 1500
NLEKKQKKFD QMLAEEKNIS SKYADERDRA EAEAREKETK ALSLARALEE
1510 1520 1530 1540 1550
ALEAKEELER TNKMLKAEME DLVSSKDDVG KNVHELEKSK RTLEQQVEEM
1560 1570 1580 1590 1600
KTQLEELEDE LQAAEDAKLR LEVNMQAMKS QFERDLQARD EQNEEKRRQL
1610 1620 1630 1640 1650
LKQLHEHETE LEDERKQRAL AAAAKKKLEV DVKDLESQVD SANKAREEAI
1660 1670 1680 1690 1700
KQLRKLQAQM KDYQRDLDDA RAAREEIFAT ARENEKKAKN LEAELIQLQE
1710 1720 1730 1740 1750
DLAAAERARK QADLEKEEMA EELASANSGR TSLQDEKRRL EARIAQLEEE
1760 1770 1780 1790 1800
LDEEHSNIET MSDRMRKAVQ QAEQLNNELA TERATAQKNE NARQQLERQN
1810 1820 1830 1840 1850
KELRSKLQEM EGAVKSKFKS TIAALEAKIA SLEEQLEQEA REKQAAAKTL
1860 1870 1880 1890 1900
RQKDKKLKDA LLQVEDERKQ AEQYKDQAEK GNLRLKQLKR QLEEAEEESQ
1910 1920 1930 1940 1950
RINANRRKLQ RELDEATESN DALGREVAAL KSKLRRGNEP VSFAPPRRSG
1960 1970
GRRVIENATD GGEEEIDGRD GDFNGKASE
Length:1,979
Mass (Da):228,796
Last modified:January 23, 2007 - v4
Checksum:i2F583CDDD4D9557D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti205 – 216KDTSI…GPSFS → RTPASLKVHLFP in CAA29793 (PubMed:2892941).CuratedAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06546 mRNA. Translation: CAA29793.1.
PIRiS03166.
UniGeneiGga.3225.

Genome annotation databases

EnsembliENSGALT00000010534; ENSGALP00000010520; ENSGALG00000006520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06546 mRNA. Translation: CAA29793.1.
PIRiS03166.
UniGeneiGga.3225.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BR1X-ray3.50A/C/E/G3-819[»]
1BR2X-ray2.90A/B/C/D/E/F3-792[»]
1BR4X-ray3.62A/C/E/G3-819[»]
1I84electron microscopy20.00S/V2-1175[»]
3DTPelectron microscopy20.00A/B3-852[»]
3J04electron microscopy-A/D2-910[»]
5M05X-ray2.67A1-790[»]
5T45X-ray2.80A1-790[»]
DisProtiDP00102.
ProteinModelPortaliP10587.
SMRiP10587.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP10587. 1 interactor.
STRINGi9031.ENSGALP00000032964.

Proteomic databases

PaxDbiP10587.
PRIDEiP10587.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000010534; ENSGALP00000010520; ENSGALG00000006520.

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiP10587.
PhylomeDBiP10587.
TreeFamiTF333601.

Enzyme and pathway databases

ReactomeiR-GGA-445355. Smooth Muscle Contraction.
R-GGA-5627123. RHO GTPases activate PAKs.
SABIO-RKiP10587.

Miscellaneous databases

EvolutionaryTraceiP10587.

Gene expression databases

ExpressionAtlasiP10587. baseline.

Family and domain databases

InterProiView protein in InterPro
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_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.
ProtoNetiSearch...

Entry informationi

Entry nameiMYH11_CHICK
AccessioniPrimary (citable) accession number: P10587
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 10, 2017
This is version 159 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.